The Prion Chronicles: The Story Of Interferon


 

These are the continuing chronicles of prion disease, the reason for your own state of unease.

For past research and understanding of just what a prion is, see my previous research here:

Link–> http://realitybloger.wordpress.com/2012/11/11/xenotransplantation-creating-the-zombie-appocalypse/

Link–> http://realitybloger.wordpress.com/2013/02/20/the-prion-chronicles-prions-and-als/

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I wish to pose a question…

Is it possible that, in our efforts to create synthetic drugs (for profit) in order to artificially mimic or replace the body’s natural health and healing processes, even while suppressing the body’s immune response to those drugs so that they may fool the natural system, we have inadvertently created a permanent state of dis-ease as the average human condition?

Let’s take an obscene example.

Over half a century ago, while researching the efficiency of the vaccine for smallpox, Japanese virologists working for the Institute For Infectious Diseases at University of Tokyo published their findings (1954) that some “viral inhibitory factor” was inhibiting the growth of their purposefully induced viral infection of laboratory research rabbits. In other words, the tiny rabbit bodies were having the natural immune response they should, which interferes with the capability of a foreign zoological pathogen to propagate (grow and reproduce) after injection. But they also discovered through isolation of this unknown and naturally occurring preventative substance that it was not originated from antibodies. The desired immunization process of antibody stimulation through vaccination was being profoundly prevented.

Three years later, at the National Institute for medical Research in London, virologists discovered similar causal effects on the growth if influenza virus in chicken egg membranes. Something was again naturally interfering with the growth of the virus after purposeful (unnatural) injection. In their research paper they coined this viral inhibitory factor as “Interferon“.

At the same time, back at the University of Tokyo, those same Japanese virologists finally discovered the essense of what they originally coined as “Viral Inhibitory Factor (VIF)”,  and both research branches agreed that this anti-viral substance was caused by the same class of factors, and eventually these became officially known in medical science as “Interferon” (multiple types).

Further study revealed that these Interferon proteins reside in different human chromosomes, and a purification process of biologically active beta interferon was finally isolated in 1977. By the early 1980’s interferon protein types were isolated and cloned to show conclusive proof that indeed interferons were responsible for interfering with viral reproduction. Eventually, these interferon isolates were used as a treatment for viral infections.

So what are these naturally interfering produced factors, and why do pharmaceutical corporations hate them so much that they seek to interfere with their pre-programmed interference?

Clinically defined, Interferons (IFNs) are proteins (glycoproteins called cytokines) made and released by healthy host cells (naturally occurring cells in your body) in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. They literally act as communication devices traveling as RNA messengers, allowing cells to communicate with each other like micro text messages, creating a trigger effect to “interfere” with disease and viral replication by turning on the protective defensive structure of the immune system that is responsible for activating immune cells (natural killer cells, macrophages, etc.). Interferons also increase the ability of uninfected host cells in their ability to resist new infection by virus (an invading parasite to the host cell), and communicate the known presence of tumor cells to the immune system, up-regulating antigens to T lymphocytes.

A lymphocyte is one of 3 cells from the vertebrate’s immune system found in the lymphatic system called NK (natural killer) cells, B  cells, or T cells. There are currently identified 10 distinct interferons (IFN’s), 7 of which are found in humans. These are further broken down by classes (types 1, 2, and 3). All of these IFN’s are vital for the body’s defense against disease states and infections as well as prevention of tumor growth.

In layman’s terms, we could say that all of the body’s naturally healthy cells send out cell-phone calls in the form of amino acids (proteins), which float through the body as if upon a wirelessly fluid Ethernet, directly connecting to the body’s receiving phone-line like a 911 emergency call; thus literally summoning the body’s first responders in the form of the immune system to send out little firefighter cells (Natural Killer, B, and T-cell lymphocytes) to stop the spread of the fire caused by viral, bacterial, parasitic, or tumor causing pathogens that are invading the host cells.

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Those Pesky Little Interferons
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While interferons have been used in some cases as a breakthrough yet totally underutilized treatment for the slowing or halting of certain disease growth in humans, we find a much more sinister reason for such research and identification of interferons in modern medicine and vaccine production. You see, the original discovery of interferons was not an altruistic attempt to isolate and synthesize an amino acid compound that would treat disease. In fact, far from it…

Back in 1956, those Japanese and British virologists were not trying to cure disease. No, they were trying to induce disease within their animal subjects for research purposes and spread it into chicken eggs so as to grow the disease for vaccination and “other” purposes; chicken embryo substrates being the most popular method for disease culture growth. But as they learned through continuous interference from the host subjects, something kept getting in the way of their purposeful disease infection of those hosts – an at the time unknown intracellular function of the body as of yet unknown, later to be named as Interferon.

Please understand… in order to vaccinate against disease, these scientists believed that they had to stop the bodies own natural defense against the very disease these scientists were trying to purposefully infect their test subjects with. Some might call this a paradox… or just insanity. In order for their pseudo-science to supposedly work, those virologists had to figure out a way to cut the cell-phone signaling process (now known as interferon) caused by their purposeful inoculate infection of the hosts. They needed to cause the body to cease in its perfectly natural capacity to fight the very disease they were injecting into it, so as to grow the disease within that host body. This would seem to the average person to be, on the surface and rightly so, a counter-productive effort on their part. But then the average person could never comprehend what was happening behind the scenes, let alone the true purpose of funding such experimental “science” as medicine.

Let’s take the phenomenon known as Auto-Immune Deficiency Syndrome (AIDS) for example…

What are its symptoms?

Rare cancerous tumors, viral-like infection, wasting syndrome, and general immune-supression of the lymphatic system.

Sound familiar? Like maybe the body’s phone-lines are down?

The body works though a system of communication devices in bilogical form. When one part or system of the body needs to communicate with another, it does so through a highly advanced structure of expressive signaling and transduction; the release of various types of cells, proteins, and other substances that trigger each inter-dependent system to respond in kind. It is this body-wide platform of cellular communication that is being attacked and blocked by the introduction of inhibiting factors like infectious prions and other melevolent substances.

The body works just fine until it is stung and thus injected (vaccinated) with foreign proteins, DNA, RNA, and other ingreedients that in no other way would ever be able to insert themselves into the body of man (or rabbit).

The main issue with AIDS patients is the lack of the body’s immune response regarding the production of T Lymphocytes, commonly called T-cells. For some reason, despite the body’s many dis-ease states as symptoms of the AID-syndrome,  the body just isn’t getting the hint to produce the very thing that it needs to fight infection. It seems we have a failure to communicate here… For some reason the emergency 911 cell-phone lines seem to be cut, and the first responders (T-cells) are just not being called into action by the healthy cells that are under attack. Their chemical screams for help are going unheard. It’s as if the immune system labor union went on strike, and these “AIDS” symptoms are the resulting chaos and unrest that ensues throughout the body.

Not ironically, these are the same symptoms of what is known as Gulf War Syndrome, a known vaccine induced disease state thought by many researchers to be caused by vaccine adjuvants like squalene and other ingredients injected into the guinea pig soldiers of our military.

But what could possibly cause such a chain reaction throughout the body’s immune-supressive system?

What could possibly have been introduced within the body to prevent its ability to make a protein phone call, just like in those poor test-rabbits so many decades ago?

What is preventing interferon from interfering with the disease process, defeating its attempts to transmit its signal for help to the imune system?

Enter bioengineering and the novel prion…

http://i10.photobucket.com/albums/a123/Adrale/mailedD0.jpg

http://www.rense.com/general54/LexmarkAIOScan34.jpg

So how could this novel disease state be simultaniusly spread
throughout Africa and eventually the first world?

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Altering Gene Expression: Just A Little Pinprick
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.

“The genetic code is universal….
The complete word-for-word universality of the genetic dictionary is,
for the taxonomist, too much of a good thing.”

–Evolutionist Richard Dawkins, in his book,
‘The Blind Watchmaker’ (1986, p. 270)

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“It is recognized by molecular biologists that the genetic code is universal,
irrespective of how different living things are in their external appearances.”

–Creationist Robert Kautz, in his book,
‘The Origin of Living Things’ (1988, p. 44)

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“The construction and metabolism of a cell are thus dependent
upon its internal ‘handwriting’ in the genetic code.
Everything, even life itself, is regulated from a biological viewpoint
by the information contained in this genetic code.
All syntheses are directed by this information.”

–A.E. Wilder-Smith, United Nations scientist (1976, p. 254).

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“It may seem a platitude to say that the offspring of buttercups, sparrows and human beings are buttercups, sparrows and human beings… What then keeps them, and indeed living things in general, “on the right lines?” Why are there not pairs of sparrows, for instance, that beget robins, or some other species of bird: why indeed birds at all? Something must be handed on from parent to offspring which ensures conformity, not complete but in a high degree, and prevents such extreme departures. What is it, how does it work, what rules does it obey and why does it apparently allow only limited variation? Genetics is the science that endeavours to answer these questions, and much else besides. It is the study of organic inheritance and variation, if we must use more formal language.”

–British geneticist, E.B. Ford,
‘Understanding Genetics’ (1979, p. 13).

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“Tablets of stone prepared by the Babylonians some 6,000 years ago have been interpreted as showing pedigrees of several successive generations of horses, thus suggesting a conscious effort toward improvement. Other stone carvings of the same period illustrate artificial cross-pollination of the date palm as practiced by the early Babylonians. The early Chinese, many years before the Christian era, improved varieties of rice. Maize was cultivated and improved in the western hemisphere by the American Indians, beginning at an early period in their history. In another era, Hippocrates, Aristotle, and other Greek philosophers made observations and speculations suggesting genetic principles.”

–Eldon Gardner, ‘The History of Biology’ (1972, pp. 399-400)

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“And God said, let the earth put forth grass, the herb
yielding seed,  and the fruit tree yielding fruit after its kind,
wherein is the seed thereof upon the earth, and it was so.
And the earth brought forth grass, the herb yielding seed and
the fruit tree yielding fruit after its kind whose seed was in itself.”

–The Bible, Genesis 1:11-12

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“In the first chapter of Genesis, however, because it is a matter of the greatest religious importance, the Bible speaks clearly and finally on a matter of biology. After its kind is the statement of a biological principle that no human observation has ever known to fail. The most ancient human records engraved on stone or painted on the walls of caves bear witness to the fact that horses have ever been horses, bears have ever been bears, geese have ever been geese, reindeer have ever been reindeer. The most desperate and subtle efforts of man in modern times have been unable to alter this divine decree. The Bible teaches that from the beginning there have been a large number of types of living things, man included, which were so created as to remain true to their particular type throughout all generations…. The latest results of modern biological research, Mendel’s Laws, agree exactly with what was written by Moses three thousand years ago—and they also elucidate it…”

Byron Nelson, ‘After Its Kind’, (1967, pp. 3,103)

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“…once a fertilized, (a) single human cell begins to develop, the original plans are
faithfully copied each time the cell divides (a process called mitosis)
so that every one of the thousand million million cells in my body, and in yours,
contains a perfect replica of the original plans for the whole body”.

–Evolutionist John Gribbin (1981, p. 193)

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“The Nobel laureate, F.H. Crick has said that if one were to
translate the coded information on one human cell into book form,
one would require one thousand volumes each of five hundred pages to do so.
And yet the mechanism of a cell can copy faithfully at cell division
all this information of one thousand volumes each of
five hundred pages in just twenty minutes.”

–Dr. Wilder-Smith (1976, p. 258).

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“Every organism has in it a store of what is called genetic information… I will refer to an organism’s genetic information store as its Library…. Where is the Library in such a multicellular organism? The answer is everywhere. With a few exceptions every cell in a multicellular organism has a complete set of all the books in the Library. As such an organism grows its cells multiply and in the process the complete central Library gets copied again and again…. The human Library has 46 of these cord-like books in it. They are called chromosomes. They are not all of the same size, but an average one has the equivalent of about 20,000 pages…. Man’s Library, for example, consists of a set of construction and service manuals that run to the equivalent of about a million book-pages together.”

“It is an indication of the sheer complexity of E. coli
that its Library runs to a thousand page-equivalent”

–A.G. Cairns-Smith  (1985, pp. 9,10,11)

 

“The DNA in living cells contains coded information. It is not surprising that so many of the terms used in describing DNA and its functions are language terms. We speak of the genetic code. DNA is transcribed into RNA. RNA is translated into protein. Protein, in a sense, is coded in a foreign language from DNA. RNA could be said to be a dialect of DNA. Such designations are not simply convenient or just anthropomorphisms. They accurately describe the situation.”

–Lester and Bohlin (1984, pp. 85-86)

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Further, consider that human beings have learned to store information on
clay tablets, stone, papyrus, paper, film, cassettes, microchips, etc.
Yet ‘human technology has not yet advanced to the point of
storing information chemically as it is in the DNA molecule

http://apologeticspress.org/APContent.aspx?category=12&article=454

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“It is not possible for a code, of any kind, to arise by chance or accident.
The laws of chance or probability have been worked out by mathematics…
A code is the work of an intelligent mind. Even the cleverest dog or chimpanzee
could not  work out a code of any kind. It is obvious then that chance cannot do it…
This could no more have been the work of chance or accident than could the
“Moonlight Sonata” be played by mice running up and down the keyboard of my piano!
Codes do not arise from chaos”

–Professor Andrews (1978, pp. 28,29).

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Prions:
Infecting The World
Through Vaccination

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So what happens when man comes clumsily and irresponsibly into the age of molecular science, where he begins to intermix species through inoculation? How can man know if his limits truly are what is written in the ancient scriptures and philosophies of moral men unless he seeks the answers by destroying the perfection of nature’s mathematical equations of the biology of life? How can we know the limits of genetically altered life if we don’t push those limits to the very brink of extinction of species, including our own?

Ancient warnings are for pussies!!!

In my previous research, I have postulated the horrifyingly evidence-based theory that all modern disease states, from the dementia’s to cancer to AIDS, have been induced through the vaccination process via the direct bodily injection of foreign “infectious” proteins called prions. Further research has all but confirmed the reality of this notion, showing that the inherent protective foundation of these cellular proteins in cell health (before infection) are essential to life itself.

 

Prion protein aids bone marrow

New study findings point to possible stem cell role for normal form of protein

By Charles Choi | January 31, 2006

The normal form of prion protein (PrP) appears necessary for bone marrow stem cells to renew themselves, scientists reported online this week in the Proceedings of the National Academy of Sciences. These findings suggest a potential physiological function in stem cells for the normal form of the widely expressed protein. “Prior to this work there was no hint that PrP had a function in stem cell biology,” co-author Andrew Steele at the Whitehead Institute for Biomedical Research in Cambridge, Mass., told The Scientist. “We are now looking into PrP function in other adult stem cells, particularly neural stem cells.” Prions are infamous for being associated with transmissible spongiform encephalopathies (TSEs) such as mad cow disease, but the function of PrP — the normal, widespread and highly conserved form of prions — remains a mystery. In preliminary studies, co-author Cheng Cheng Zhang discovered 40% of adult mouse bone marrow cells expressed PrP on their surfaces. More than 80% of these PrP-marked cells were red blood cells or their developmental precursors, suggesting PrP might be a marker for long-term hematopoietic stem cells, which can give rise to the entire adult blood system. To determine if PrP was a marker for long-term hematopoietic stem cells, the researchers took bone marrow cells from wild-type mice and purified them into fractions, some of which expressed PrP. Six months after transplantation into lethally irradiated mice, the researchers saw both short- and long-term engraftment in mice that received PrP-containing cells, but only short-term engraftment activity in mice receiving non-PrP cells. While PrP is a marker for long-term hematopoietic stem cells in wild-type mice, PrP-knockout mice still possess these cells, as well as relatively normal levels of their derived progeny. To determine what function PrP might normally have in hematopoietic stem cells, the researchers carried out several rounds of bone marrow implantations. First they transplanted bone marrow from either wild-type mice or a PrP-null strain into lethally irradiated mice. When the engrafted marrow flourished and generated peripheral blood cells, the researchers implanted the newly reconstituted bone marrow into another lethally irradiated mouse group, then repeated the process a third time. In each round after the first, bone marrow originating from PrP-null mice experienced a dramatically reduced ability to renew itself, while cells from the wild-type mice did not. Retroviral infections that expressed PrP in recipients of PrP-null bone marrow rescued this defective process, suggesting PrP is necessary for hematopoietic stem cell self-renewal. Odile Kellerman at the Pasteur Institute in Paris, who did not participate in this study, noted prions often trigger neuron death in TSEs after long incubation periods,” similarly, PrP only impacted hematopoietic stem cells over the long term. “In both cases, PrP appears to contribute to the long-lasting adaptation of cells to injury,” she told The Scientist. Kellerman suggested that when PrP function is disrupted, cells try to adapt, “but in the long term, this turns out to be detrimental.” The exact mechanism behind how PrP might contribute to hematopoietic stem cell renewal remains unknown. Co-author Harvey Lodish speculated PrP might bond to and concentrate a hormone on the cell surface, or help stem cells adhere to neighboring cells or extracellular matrix. “It should prove fairly straightforward to see if it is adhering to other proteins or any known or unknown hormones,” he told The Scientist. William Stanford at the University of Toronto, who did not participate in this study, noted that PrP is tethered to cell membranes via a glycosylphosphatidylinositol (GPI) anchor, similar to hematopoietic stem cell marker Sca-1. “This suggests these GPI-anchored proteins, which have similar functions, may operate through a common mechanism,” Stanford told The Scientist. Future experiments could investigate whether overexpressing PrP in hematopoietic stem cells increases self-renewal, and rescues self-renewal defects such as in the Sca-1 deficient mouse, Stanford added — or if genetically substituting PrP with a different GPI-anchored protein rescues the self-renewal defect seen in PrP-null mice. cqchoi@nasw.org Links within this article C.C. Zhang et al. “Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal.” PNAS Early Edition.
Published online January 30, 2006. http://www.pnas.org B.A. Maher.
Sources:
“Prion hypothesis proven?” The Scientist, April 21, 2005. http://www.the-scientist.com/article/display/22653/
M. Fogarty. “Prions – The terminators.” The Scientist, July 28, 2003. http://www.the-scientist.com/article/display/13974/
M. Fogarty. “Researchers further define sources of adult blood stem cells.” The Scientist, September 16, 2002. http://www.the-scientist.com/article/display/13257/
J.U. Adams. “The tiniest of life’s rafts.” The Scientist, October 11, 2004 http://www.the-scientist.com/article/display/14978/

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Neurons and Astrocytes Respond to Prion Infection by Inducing Microglia Recruitment

Abstract

The accumulation and activation of microglial cells at sites of amyloid prion deposits or plaques have been documented extensively. Here, we investigate the in vivo recruitment of microglial cells soon after intraocular injection of scrapie-infected cell homogenate (hgtsc+) using immunohistochemistry on retinal sections. A population of CD11b/CD45-positive microglia was specifically detected within the ganglion and internal plexiform retinal cell layers by 2 d after intravitreal injection of hgtsc+. Whereas no chemotactism properties were ascribed to hgtsc+ alone, a massive migration of microglial cells was observed by incubating primary cultured neurons and astrocytes with hgtsc+ in a time- and concentration-dependent manner. hgtsc+ triggered the recruitment of microglial cells by interacting with both neurons and astrocytes by upregulation of the expression levels of a broad spectrum of neuronal and glial chemokines. We show that, in vitro and in vivo, the microglia migration is at least partly under the control of chemokine receptor-5 (CCR-5) activation, because highly specific CCR-5 antagonist TAK-779 significantly reduced the migration rate of microglia. Activated microglia recruited in the vicinity of prion may, in turn, cause neuronal cell damage by inducing apoptosis. These findings provide insight into the understanding of the cell-cell communication that takes place during the development of prion diseases.

Source–> http://www.jneurosci.org/content/24/3/620.full

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Prion hypothesis proven?

In vitro infectivity study in Cell stirs tempest in a test tube

By Brendan Maher (bmaher@the-scientist.com) | April 21, 2005

Protein aggregates generated in a test tube infected wildtype hamsters with a disease much like scrapie, according to an article appearing this week in Cell. Such a demonstration has, in the past, been called the gold standard of proof for the prion hypothesis, Stanley Prusiner’s Nobel-winning assertion that infectious, self-replicating protein isoforms are the culprit in transmissible spongiform encephalopathies (TSEs) like scrapie, Creutzfeldt-Jakob disease, and mad cow disease.

Study coauthor Claudio Soto, said that this demonstration, together with a paper published by Prusiner’s group last summer, should allay most doubts. “There is really little room for skepticism,” he told The Scientist.

But the study has done little to quiet prion hypothesis skeptics. “I’m not going to abandon alternative hypotheses for the time being,” said Robert A. Somerville of the Institute for Animal Health, Edinburgh.

While Prusiner’s group had successfully infected a mouse with a recombinant protein derived from bacteria, some argued that their use of transgenic mice susceptible to the disease undercut the power of the demonstration. In the new study, researchers at the University of Texas Medical Branch, Galveston, Universidad Autonoma, Madrid, and the University of Chile in Santiago fine-tuned a cyclical process for amplifying aggregated protein from an infected hamster brain. Through serial dilutions, they were able to infect a wildtype hamster with in vitro–produced aggregates without any traces of the original infectious brain. But skeptics, including a member of Prusiner’s group, argue that using material from a diseased hamster brain could have resulted in residual contamination.

Soto’s group has been using a process that they call protein misfolding cyclic amplification (PMCA), which aids the aggregation of the normal cellular protein PrPc into the misfolded, polymer-forming PrPres that is associated with TSE pathology. The process works in a fashion similar to polymerase chain reaction (PCR) amplification of oligonucleotides. After seeding PrPc with PrPres, the solution is incubated and sonicated. “Once the aggregates become long enough, we split them into smaller pieces so that in a new conversion, a new incubation, they are able to convert more and more of the normal protein,” Soto explained.

Crucially, however, the PrPres “seed” comes from infected hamster brain homogenate, while the normal PrPc comes from healthy hamster brain homogenate. “They actually started from infectious material, and we didn’t,” said Giuseppe Legname, of the University of California, San Francisco, and co-author on the Prusiner paper. “It’s an alternative approach to demonstrate that you might make prions, but to say that these are synthetic prions, it’s very difficult.”

Soto insisted that serial dilutions between rounds of PMCA reduce scrapie brain homogenate to an amount equivalent to a 10 to the minus 10th and a 10 to the minus 20th–fold dilution. Infectivity generally drops off after 10 to the minus 9th, according to the paper. “We’ve completely ruled out the possibility that the infectivity is still remaining from… the original brain,” Soto said...

Source–> http://www.the-scientist.com/?articles.view/articleNo/23325/title/Prion-hypothesis-proven-/

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While the article continues to criticize the control group results, which you may read at the link above, the important point here is that scientists are creating prions and making them purposefully more infectious. They are testing them in various substances and frequencies. And through the ultra-sound sonic vibration described above as protein misfolding cyclic amplification (PMCA), they are able to excite the growth factor of infectious prions so that they take over (mis-fold) healthy brain tissue much quicker. This PMCA process is used in autopsy to detect prion disease.

I have my own concerns that these ultra-sound frequencies are the same as used in cell-phone towers and in the process of ultra sound for unborn infants and other medical procedures, as well as other frequencies unknown via smart meters, radio waves, etc. We are playing with the fuel for the fire and there is virtually no escaping this permanent state of sonic bombardment…

It is also interesting to note that two men wsere cured of AIDS symptoms by receiving a bone marrow transfusion not so long ago…

(CBS News) Two men who’ve had HIV for years may now be free of the disease following bone marrow transplants, researchers at Brigham and Women’s Hospital in Boston announced Thursday.

The new research has some attendees at the XIX International AIDS Conference in Washington, D.C. hopeful for a cure.

Timothy Ray Brown, man thought to be first “cured” of AIDS, says he’s still cured
Man “cured” of AIDS: Timothy Ray Brown

Both patients were being treated for cases of cancer. One of the patients underwent a bone marrow transplant two years ago at the Dana-Farber/Brigham and Women’s Cancer Center in Boston, the other had the procedure done four years ago at the same hospital. NBCNews.com reports that one of the patients is in his 50s and has been infected since the early 1980s towards the beginning of the AIDS epidemic and the other man, in his 20s, was infected at birth.

Both stayed on their antiretroviral medication regimens, the standard treatment of HIV, following the transplants.

The researchers discovered that overtime as the patients’ cells were replaced by cells from the donor, evidence of HIV in the patients’ blood tests disappeared. The researchers also said both patients have no signs of HIV in their DNA or RNA and levels of their disease-fighting antibodies have also decreased. The researchers think the medications helped allow these cells to be replaced.

“This gives us some important information,” one of the researchers Dr. Daniel Kuritzkes, an infectious disease specialist at the hospital and Harvard Medical school said in a press release. “It suggests that under the cover of antiretroviral therapy, the cells that repopulated the patient’s immune system appear to be protected from becoming re-infected with HIV.”

The researchers themselves won’t call it a cure yet, saying they still need to check more tissues for traces of the disease. But they were surprised to see no signs of HIV beyond what’s seen in a blood test.

We expected HIV to vanish from the patients’ plasma, but it is surprising that we can’t find any traces of HIV in their cells,” said co-resarcher Dr. Timothy Henrich, also of BWH and Harvard. “The next step is to determine if there are any traces of HIV in their tissue.”

The researchers’ announcement comes days after Timothy Ray Brown, the man known as the “Berlin Patient,” held a press conference in Washington, D.C.,  to say he’s still cured of AIDS five years after undergoing a bone marrow blood transplant

Source–> http://www.cbsnews.com/news/bone-marrow-transplant-eliminates-hiv-traces-from-two-patients-dna-call-it-a-cure/

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It is important to note that the chemokine receptor-5 (CCR-5) antagonist prevents the cellular binding of the HIV-1 virus, as is explained in this video:

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And how do these prions effect disease states?

Let’s take for example Multiple Sclerosis:

“The etiology of Multiple Sclerosis (MS) is unknown. Existing epidemiologic data suggests that MS can be an infectious disease. MS used to be classified as one of the ‘slow infections‘–many of these are caused by prions. Prions are small, proteinaceous, infectious particles–distinguished from viruses by the absence of intrinsic nucleic acids. In a contrast to the ‘classic’ prional diseases (Kuru, Scrapie or Creutzfeldt-Jacob Disease) that in CNS affect primarily neurons, the ‘target’ cell in MS is an oligodendrocyte. This may explain differences in disease presentation. This paper presents a pathophysiological model of MS based on the assumption that MS is a prional disease. Processes leading to the demyelination in Multiple Sclerosis seem also to involve lymphocytes, astrocytes and macrophages as well as the interferon system…”

Source: http://www.ncbi.nlm.nih.gov/pubmed/8455467

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NOTE: The protein that prions are made of (PrP) is found throughout the body, even in healthy people and animals, and necessarily protects cells from infections. However, PrP found in infectious material has a different structure and is resistant to proteases, the enzymes (proteins) in the body that can normally break down other proteins. The normal form of the protein is called PrPC, while the infectious form is called PrPSc — the C refers to healthy ‘cellular‘ PrP, while the Sc refers to infectious ‘scrapie‘, the prototypic prion disease, occurring in sheep. The infectious isoform of PrP, known as PrPSc, is able to convert normal PrPC proteins in humans into this infectious isoform by changing their conformation, or shape. This, in turn, alters the way the proteins interconnect, creating symptoms like transmissible spongiform encephalopathy (holes in the human brain like mad cow disease). PrPSc always causes prion disease. In the end, no cellphone call can be made if the interferon protein is infected and mis-folded before it is able to reach its receiving protien that would activate T-Cells or other immune responses. Another word for mis-fold might be easier to understand as to misinform. The immune system is being lied to in a strange, chemically unbalanced way due to prion protein infections (mis-folding). Sheep blood (serum) is a popular vaccine substrate to grow vaccines for humans upon, and the protein and DNA cannot be filtered out of the final vaccine product. There are no other viable explanations why infectious prions from animals would intermingle within a human body (xenotransplantaion/xenografting).

A thorough and sourced description about prions can be found here: http://www.omim.org/entry/176640

This interference that infectious prions cause to interferon and other protein-based signaling and transcription cells is shown in the research studies below. For those with the gumption, let’s play a biological game of connect the dots.

Continued…

RESULTS

Prion infection is accelerated in (interferon type 3) IRF3-deficient mice…

The IRF3-dependent pathway is protective against prion infection in cell culture.

We tested whether over-expression of IRF3 (interferon) could affect the production of PrPSc (infectious/mis-folded prions) in the cell culture models. The level of PrPC (healthy prions) was not affected by the transient expression of the genes in uninfected N2a58 cells (data not shown). PrPSc was significantly decreased by overexpression of IRF3 in the 22L-N2a58 cells (Fig. 5A). We confirmed that the activated form of IRF3 (phosphorylated at Ser396 of IRF3) increases in a dose-dependent manner after transfection of the IRF3 gene in both 22L-N2a58 cells (Fig. 5A) and uninfected N2a58 cells (data not shown), indicating that the upregulation of IRF3 phosphorylation seen in the Fig. 5A is most likely due to an increase in the level of IRF3 protein after transfection.

To investigate the effect of downregulation of IRF3 in the 22L-N2a58 cells, we performed knockdown experiments using small interfering RNAs (siRNAs). IRF3 expression was significantly decreased by two types of siRNAs against IRF3, whereas β-actin expression, as the internal standard, was not changed (Fig. 5B)… These data suggest that IRF3 has an inhibitory effect on the production of PrPSc in the 22L-N2a58 cells.

To further evaluate the protective effect of IRF3… After incubation with 22L-infected BH (22L-BH), the cell clones were subcultured for five passages and analyzed by Western blotting with anti-PrP antibodies. The values of the PrPSc/PrPC ratio were inversely correlated with the values of the IRF3/beta-actin ratio (Fig. 5C), indicating that enhanced expression of IRF3 effectively blocks new prion infection.

DISCUSSION

In the present study, we found that a genetic deficiency of IRF3 accelerates the progression of TSE (transmissable prion disease) following i.p. transmission in mice and that the accumulation rate of PrPSc in the spleen is increased in the IRF3−/− mice. Furthermore, we demonstrated that IRF3 has an inhibitory effect on PrPSc accumulation and that the levels of IRF3 are inversely correlated with resistance to prion infection in cell culture.

IRF3 is known to be constitutively expressed in many tissues and cells (6, 22, 45). Indeed, we confirmed the expression of IRF3 in brains (data not shown) and N2a58 cells (Fig. 5). Furthermore, not only glial cells but also neurons express most innate immunity-related genes and produce type I IFN in response to virus infection (11). Although the role of IRF3 in prion propagation into the CNS is still unclear, we speculate that an absence of IRF3 signaling leads to increased prion replication not only in peripheral tissues but also in the CNS. It would be of great value to examine this further using neuron-specific IRF3-disrupted mice or neuron-specific IRF3-expressing mice.

It was reported in prion infection that genetic disturbance of TLR4 (36) or interleukin-10 (IL-10) (41) leads to shorter incubation periods of prion infection. Since these, respectively, are an upstream and a downstream factor of the IRF3-mediated pathway, the findings may be due in part to functional changes in IRF3-mediated signaling.

Based on these results, two hypothetical models are proposed to explain the inhibitory effect of IRF3 on the prion infection. The first is that MyD88-independent pattern recognition receptors (PRRs), such as TLR3, TLR4, or RIG-I/MDA5, might recognize prion, and the resulting activation of IRF3 could induce various IRF3-responsive genes that may participate in the protective effect. The fact that the in vivo administration of IFNs (interferons), a representative of the IRF3-responsive genes, previously failed to show inhibitory effects on TSE (13, 16) suggests that IRF3-responsive genes other than IFNs may be important for the inhibitory effect of IRF3 on prion infection. Of note, the protective effect of IRF3 against several viruses has been suggested to be largely independent of the production of type I IFN and is probably responsible for the antiviral actions of specific IRF3-responsive genes (10, 18, 21). Peritoneal macrophages from wild-type mice moderately induced tumor necrosis factor alpha (TNF-α) or IL-6 following exposure to PrPSc-mimicking PrP peptides (PrP residues 106 to 126 or PrP residues 118 to 135), whereas TLR4 signaling-mutant mice were impaired in their ability to produce these cytokines (36), supporting in part the hypothesis that some PRRs may sense PrPSc as a sort of PAMP. On the other hand, it should be noted that the MyD88-independent pathway activates both NF-κB and IRF3. Although the induction of proinflammatory cytokines essentially depends upon NF-κB, it was unclear whether the activation of IRF3 was induced by these PrP peptides. In fact, the hallmarks of IRF3 activation, such as phosphorylation, dimerization, and cytoplasm-to-nucleus translocation of IRF3 in 22L-N2a58 cells, were not detected (data not shown). Moreover, it was previously reported that IFNs were not detected in the serum, spleens, or brains of mice infected with scrapie (44). In addition, IFN-β mRNA does not increase in the brains of CJD (human prion disease) patients (7) or mice infected with ME7 prion strain (14). Hence, these results argue against the notion that the IRF3-mediated signaling is activated by prion infection, but it remains to be determined whether transient and weak responses are evoked at an early phase in the infection. The question as to whether IRF3-mediated signaling directly suppresses the production of PrPSc or increases its degradation also remains open.

Another explanation is that prion infection itself may have little effect on the pathway but that the basal activity of IRF3 may have some degree of inhibitory effect on prion propagation. It has been reported that IRF3 can be activated not only by viruses but also by multiple activators such as cellular stress and DNA damage (24, 34). Accordingly, it is possible that constitutive activation of IRF3, albeit at a low level, occurs in the brain even in the absence of a pathogen. This notion is further supported by the fact that constitutive, weak IFN signaling in the absence of viral infection plays a role in modifying cellular responsiveness in the immune and other biological systems (38, 40). Accumulating evidence indicates that many viruses have evolved to evade the innate immune system, including IRF3-mediated signaling (15, 23). For instance, an active mutant of IRF3 has been reported to exert a markedly suppressive effect on cellular HIV-1 infection, and administration of poly(I·C) potently inhibits HIV-1 replication in microglia through a pathway requiring IRF3. Nonetheless, HIV-1 itself does not activate IRF3 but, rather, decreases IRF3 protein in HIV-1-infected cells (12, 37). Likewise, prion infection might disturb the activation of IRF3 even though prion is considered to be largely composed of PrPSc. We are currently investigating this possibility. Furthermore, an analogy can be made between the role of IRF3 in prion infection and that of IL-10. The levels of IL-10 are not increased in the brains of scrapie-infected mice (14, 42), whereas IL-10 knockout mice are highly susceptible to the development of scrapie (41).

In conclusion, we have shown that IRF3, a key transcription factor of the MyD88-independent pathways, operates in the host defense machinery against prion infection. The findings provide new insight into understanding of the innate immunity to prion infection.

Source: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347345/

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Interleukin-10 (IL-10), also known as human cytokine synthesis inhibitory factor (CSIF), is an anti-inflammatory cytokine. In humans, IL-10 is encoded by the IL10 gene.[1]

Gene and protein structure

The IL-10 protein is a homodimer; each of its subunits is 178-amino-acid long.[2]

IL-10 is classified as a class-2 cytokine, a set of cytokines including IL-19, IL-20, IL-22, IL-24 (Mda-7), and IL-26, interferons (IFN-alpha, -beta, -epsilon, -kappa, -omega, -delta, -tau, and -gamma) and interferon-like molecules (limitin, IL-28A, IL-28B, and IL-29).[3]

Expression and synthesis

In humans, IL-10 is encoded by the IL10 gene, which is located on chromosome 1 and comprises 5 exons,[1] and is primarily produced by monocytes and, to a lesser extent, lymphocytes, namely type 2 T helper cells (TH2), mastocytes, CD4+CD25+Foxp3+ regulatory T cells, and in a certain subset of activated T cells and B cells.

In biochemistry, a dimer is a macromolecular complex formed by two, usually non-covalently bound, macromolocules like proteins or nucleic acids. It is a quaternary structure of a protein.

A homo-dimer would be formed by two identical molocules (a process called homodimerization). A hetero-dimer would be formed by two different macromolecules (called heterodimerization).

Most dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer would be the enzyme reverse transcriptase, which is composed of two different amino acid chains.[1] An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO.[2]

Some proteins contain specialized domains to ensure dimerization (dimerization domains).

Examples of Homodimer include anti-bodies and Factor VII.

Microglia are a type of glial cell that are the resident macrophages of the brain and spinal chord, and thus act as the first and main form of active immune defense in the central nervous system (CNS).

Microglia constitute 10-15% of the total glial cell population within the brain.[1] Microglia (and astrocytes) are distributed in large non-overlapping regions throughout the brain and spinal cord.[2][3] Microglia are constantly scavenging the CNS for plaques, damaged neurons and infectious agents.[4] The brain and spinal cord are considered “immune privileged” organs in that they are separated from the rest of the body by a series of endothelial cells known as the blood-brain barrier, which prevents most infections from reaching the vulnerable nervous tissue. In the case where infectious agents are directly introduced to the brain or cross the blood–brain barrier, microglial cells must react quickly to decrease inflammation and destroy the infectious agents before they damage the sensitive neural tissue. Due to the unavailability of antibodies from the rest of the body (few antibodies are small enough to cross the blood brain barrier), microglia must be able to recognize foreign bodies, swallow them, and act as antigen-presenting cells activating T-cells. Since this process must be done quickly to prevent potentially fatal damage, microglia are extremely sensitive to even small pathological changes in the CNS.[5] They achieve this sensitivity in part by having unique potassium channels that respond to even small changes in extracellular potassium.

Microglial cells differentiate in the bone marrow from hematopoietic stem cells, the progenitors of all blood cells. During hematopoiesis, some of these stem cells differentiate into monocytes and travel from the bone marrow to the brain, where they settle and further differentiate into microglia.[6]

Monocytes can also differentiate into myeloid dendritic cells and macrophages in the peripheral systems. Like macrophages in the rest of the body, microglia use phagocytic and cytotoxic mechanisms to destroy foreign materials. Microglia and macrophagesboth contribute to the immune response by acting as antigen presenting cells, as well as promoting inflammation and homeostatic mechanisms within the body by secreting cytokines and other signaling molecules.

In their downregulated form, microglia lack the MHC class I/MHC class II proteins, IFN-γ cytokines, CD45 antigens, and many other surface receptors required to act in the antigen-presenting, phagocytic, and cytotoxic roles that hallmark normal macrophages. Microglia also differ from macrophages in that they are much more tightly regulated spatially and temporally in order to maintain a precise immune response.[7]

Another difference between microglia and other cells that differentiate from myeloid progenitor cells is the turnover rate. Macrophages and dendritic cells are constantly being used up and replaced by myeloid progenitor cells which differentiate into the needed type. Due to the blood brain barrier, it would be fairly difficult for the body to constantly replace microglia. Therefore, instead of constantly being replaced with myeloid progenitor cells, the microglia maintain their status quo while in their quiescent state, and then, when they are activated, they rapidly proliferate in order to keep their numbers up. Bone chimera studies have shown, however, that in cases of extreme infection the blood-brain barrier will weaken, and microglia will be replaced with haematogenous, cart-marrow derived cells, namely myeloid progenitor cells and macrophages. Once the infection has decreased the disconnect between peripheral and central systems is reestablished and only microglia are present for the recovery and regrowth period.

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Transport of prion protein across the blood–brain barrier

Abstract

The cellular form of the prion protein (PrPc) is necessary for the development of prion diseases and is a highly conserved protein that may play a role in neuroprotection. PrPc is found in both blood and cerebrospinal fluid and is likely produced by both peripheral tissues and the central nervous system (CNS). Exchange of PrPc between the brain and peripheral tissues could have important pathophysiologic and therapeutic implications, but it is unknown whether PrPc can cross the blood–brain barrier (BBB). Here, we found that radioactively labeled PrPc crossed the BBB in both the brain-to-blood and blood-to-brain directions. PrPc was enzymatically stable in blood and in brain, was cleared by liver and kidney, and was sequestered by spleen and the cervical lymph nodes. Circulating PrPc entered all regions of the CNS, but uptake by the lumbar and cervical spinal cord, hypothalamus, thalamus, and striatum was particularly high. These results show that PrPc has bidirectional, saturable transport across the BBB and selectively targets some CNS regions. Such transport may play a role in PrPc function and prion replication.

Introduction

Cellular prion protein (PrPc) is perhaps best known as a source for the misfolded protein PrPsc (Prusiner, 1997) and as a prerequisite for the development of prion diseases (Mallucci et al., 2000). However, PrPc itself likely has important biological functions. It is found circulating in blood (Volkel et al., 2001) and is found in even higher levels in the cerebrospinal fluid (CSF) (Picard-Hagen et al., 2006). After ischemic events, PrPc levels increase in blood (Mitsios et al., 2007) and in neurons and brain endothelial cells in the peri-infarct region (Mitsios et al., 2007; Weise et al., 2004). These increases may reflect cytoprotective and neuroprotective roles for PrPc as recently reviewed (Roucou & LeBlanc, 2005). PrPc null mice have larger infarct volumes after ischemic events (Weise et al., 2006; Nasu-Nishimura et al., 2008) and more neuronal apoptosis after viral infections (Nasu-Nishimura et al., 2008) than wild type mice. In comparison, mice that overexpress PrPc have smaller infarcts and better neurological outcomes than wild type mice after ischemic events (Shyu et al., 2005). These protective events are likely mediated by PrPc through activation of anti-apoptotic (Spudich et al., 2005) and anti-oxidant pathways (White et al., 1999).

Sources of circulating PrPc likely include platelets (Robertson et al., 2006), endothelial cells (Simak et al., 2002), and lymphocytes (Politopoulou et al., 2000). Among lymphocytes, CD3 and CD8 lymphocytes have especially high levels which increase with aging (Politopoulou et al., 2000). All these cells have membrane bound PrPc that apparently can be released into the circulation. Platelet activation (Robertson et al., 2006) or endothelial apoptosis (Simak et al., 2002), for example, results in release of PrPc from those cells.

Thus, PrPc occurs in both blood and in CSF with levels that are likely responsive to disease states. This raises the question of whether PrPc can cross the blood–brain barrier (BBB). Such passage could link the two pools of PrPc and the events that control their levels. Here, we examined the ability of PrPc to cross the BBB in both the blood-to-brain and the brain-to-blood directions.

Capillary depletion

Capillary depletion as modified for use in the mouse (Triguero et al., 1990; Gutierrez et al., 1993) was used to determine the degree to which PrPc was sequestered and retained by the vascular bed of the brain.

I-PrPc was also taken up by the peripheral tissues of spleen, liver, kidney and cervical lymph nodes (Table 2)… there was a statistically significant decrease in the Ki for brain: F(1,8) = 7.97, p <0.05. This demonstrates that transport of PrPc across the BBB involves a saturable transport system.

Fig. 4 shows values for brain and spinal cord regions. Statistical comparison of the whole brain value to brain regions and olfactory bulb (spinal cord regions excluded) showed a statistically significant variation: F(22,62) = 18.3, p <0.001. The hypothalamus, thalamus, and striatum showed statistically (p <0.01) greater uptake in comparison to whole brain. The highest uptake, however, was into the lumbar region of the spinal cord. Inhibition of uptake by unlabeled PrPc (Table 3; p <0.05) was found for whole brain, olfactory bulb, 4 of the 10 brain regions (occipital cortex, thalamus, striatum, and midbrain) and two of the spinal cord regions (cervical and lumbar)…

Fig. 5 Brain-to-blood efflux of PrPc after icv injection. Half-time clearance from brain was 15.7 min. Inset shows that inclusion of unlabeled PrPc in the icv injection increased retention of radioactively labeled PrPc by brain, demonstrating a saturable component
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Does aluminum in vaccines have a more sinister plot that is stated?

Differential effect of aluminum on the blood-brain barrier transport of peptides, technetium and albumin.

Abstract

Aluminum is a neurotoxin capable of altering membrane structure and function. We investigated whether aluminum also can affect saturable transport across membranes using the blood-brain barrier as our model. Mice were given i.p. or i.v. aluminum (up to 100 mg/kg) as the chloride salt and the disappearance from the brain of several centrally administered substances was measured. We found that aluminum rapidly and profoundly inhibited the saturable system that transports the small, N-tyrosinated peptides Tyr-MIF-1 and the enkephalins from the brain to the blood by acting as a noncompetitive inhibitor. In contrast, the disappearance from the brain of technetium pertechnetate (a substance also transported out of the brain by a different saturable system), albumin or D-Tyr-MIF-1 (a stereoisomer of Tyr-MIF-1 that was confirmed not to be transported by the carrier system) was not affected by aluminum. Aluminum also did not alter either the saturable or nonsaturable component of the uptake of Tyr-MIF-1 by erythrocytes. These findings suggest that one mechanism by which aluminum may induce neurotoxicity is by selective alteration of the transport systems of the blood-brain barrier.

Source: http://www.ncbi.nlm.nih.gov/pubmed/2894456

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An enkephalin is a pentapeptide involved in regulating nociception in the body. The enkephalins are termed endogenous ligands, as they are internally derived and bind to the body’s opioid receptors. Discovered in 1975, two forms of enkephalin were revealed, one containing leucine (“leu”), and the other containing mathione (“met”). Both are products of the proenkephalin gene.

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Endogenous opioid peptides

There are three well-characterized families of opioid peptides produced by the body: enkephalins, endorphines, and dynorphins. The met-enkephalin peptide sequence is coded for by the enkephalin gene; the leu-enkephalin peptide sequence is coded for by both the enkephalin gene and the dynorphin gene.[3] The proopiomelanocortin gene (POMC) also contains the met-enkephalin sequence on the N-terminus of beta-endorphin, but the endorphin peptide is not processed into enkephalin.

Enkephalin receptor

Main article: Opioid recepter
The receptors for enkephalin are the delta opioid receptors. Opioid receptors are a group of G-protein-coupled receptors, with other opioids as ligands as well. The other endogenous opioids are dynorphins (that bind to kappa receptors), endorphines (mu receptors), endomorphins, and nociceptin/orphanin FQ. The opioid receptors are ~40% identical to somatostatin receptors (SSTRs).

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Endomorphins, Met-Enkephalin, Tyr-MIF-1, and the P-glycoprotein Efflux System

Abstract

The P-glycoprotein (P-gp) transport system, responsible for the efflux of many therapeutic drugs out of the brain, recently has been shown to transport the endogenous brain opiate endorphin. We used P-gp knockout mice (Mdr1a) and their controls to determine where P-gp is involved in the saturable efflux systems of four other endogenous opiate-modulating peptides across the blood-brain barrier (BBB). After injection of endomorphin-1 (Tyr-Pro-Trp-Phe-NH2), endomorphin-2 (Tyr-Pro-Phe-Phe-NH2), Met-enkephalin (Tyr-Gly-Gly-Phe-Met-OH), and Tyr-MIF-1 (Tyr-Pro-Leu-Gly-NH2) into the lateral ventricle of the mouse brain, residual radioactivity was measured at 0, 2, 5, 10, and 20 min later. The results showed no difference in the disappearance of any of these peptides from the brains of knockout mice compared with their controls. This demonstrates that unlike endorphin and morphine, P-gp does not seem to be required for the brain-to-blood transport of the endomorphins, Met-enkephalin, or Tyr-MIF-1 across the BBB.

Footnotes

  • This work was supported by the United States Army Medical Research Acquisition Activity (DAMD17-00-0113) and the Department of Veterans Affairs.

Source: http://dmd.aspetjournals.org/content/30/3/231.abstract

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Endorphins (“endogenous morphine”) are endogenous opioid inhibitory neuropeptides. They are produced by the central nervous system and pituitary gland. The term implies a pharmacological activity (analogous to the activity of the corticosteroid category of biochemicals) as opposed to a specific chemical formulation. It consists of two parts: endo- and -orphin; these are short forms of the words endogenous and morphine, intended to mean “a morphine-like substance originating from within the body.”[1]

History

Opioid neuropeptides were first discovered in 1974 by two independent groups of investigators:

  • John Hughes and Hans Kosterlitz of Scotland isolated — from the brain of a pig — what some called enkephalins (from the Greek εγκέφαλος, cerebrum).[2][3]
  • Around the same time, in a calf brain, Rabi Simantov and Solomon H. Snyder of the United States found[4] what Eric Simon (who independently discovered opioid receptors in vertebral brains) later termed “endorphin” by an abreviation of of “endogenous morphine”, meaning “morphine produced naturally in the body”.[1] Importantly, recent studies have demonstrated that human and diverse animal tissues are in fact capable of producing morphine itself, which is not a peptide.[5][6]

Mechanism of action

Beta-endorphin (β-endorphin) is released into blood from the pituitary gland and into the spinal cord and brain from hypothalamic neurons. The β-endorphin that is released into the blood cannot enter the brain in large quantities because of the blood-brain barrier, so the physiological importance of the β-endorphin that can be measured in the blood is far from clear. β-endorphin is a cleavage product of pro-opiomelanocortin (POMC), which is also the precursor hormone for adrenocorticotrophic hormone (ACTH). The behavioural effects of β-endorphin is exerted by its actions in the brain and spinal cord, and it is presumed that the hypothalamic neurons are the major source of β-endorphin at those sites. In situations where the level of ACTH is increased (e.g., Cushing’s disease), the level of β-endorphin also increases slightly.

β-endorphin has the highest affinity for the μ1 opioid receptor, slightly lower affinity for the μ2 and δ opioid receptors, and low affinity for the κ1 opioid receptors. μ-Opioid receptors are the main receptor through which morphine acts. In the classical sense, μ opioid receptors are presynaptic, and inhibit neurotransmitter release. Through that mechanism, they inhibit the release of the inhibitory neurotransmitter GABA, and disinhibit the dopamine pathways, causing more dopamine to be released. By hijacking this process, exogenous opioids cause inappropriate dopamine release, and can lead to aberrant synaptic plasticity, which can cause dependency. Opioid receptors have many other and more important roles in the brain and periphery; however, modulating pain, cardiac, gastric and vascular function as well as possibly panic and satiation. Also, receptors are often found at postsynaptic locations as well as at presynaptic locations…

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Morphine preconditioning reduces lipopolysaccharide and interferon-γ-induced mouse microglial cell injury via δ1 opioid receptor activation

Abstract

Microglial cells play an important role in the inflammatory response of a broad range of brain diseases including stroke, brain infection and neurodegenerative diseases. However, there is very little information regarding how to protect microglial cells. Here, we showed that incubation of the C8-B4 mouse microglial cells with lipopolysaccharide (LPS) plus interferon-γ (IFNγ) induced cytotoxicity as assessed by the amount of lactate dehydrogenase (LDH) released from the cells. Preconditioning the cells with morphine for 30 min concentration-dependently reduced LPS plus IFNγ-induced cell injury. This morphine preconditioning effect was abolished by naloxone, a general opioid receptor antagonist, by naltrindole, a selective δ opioid receptor antagonist and by 7-benzylidenenaltrexone maleate, a selective δ1 opioid receptor antagonist. However, this protective effect was not affected by β-funaltrexamine, a selective μ opioid receptor antagonist, nor-binaltorphimine, a selective κ opioid receptor antagonist or naltriben, a selective δ2 opioid receptor antagonist. LPS plus IFNγ induced the expression of inducible nitric oxide synthase (iNOS), which was not affected by morphine preconditioning. Our results suggest that morphine induced a preconditioning effect in microglial cells. This effect may be mediated by δ1 opioid receptors and may not be through inhibiting the expression of iNOS, a potentially harmful protein.

Source–> http://www.sciencedirect.com/science/article/pii/S0306452210002137

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Prion peptide PrP106-126 induces inducible nitric oxide synthase (iNOS) and proinflammatory cytokine gene expression through the activation of NF-kB in macrophage cells

The inflammatory response in prion diseases is dominated by microglia activation. The molecular mechanisms that lie behind this inflammatory process are not very well understood. In the present study, we examined the activation of nuclear factor-kappa B (NF-κB) upon exposure to PrP106-126 and its role in PrP106-126-induced upregulation of inducible nitric oxide synthase (iNOS) and proinflammatory cytokines (interleukin [IL]-1β, tumor necrosis factor [TNF]-α, IL-6) in Ana-1 macrophages. The results showed that iNOS and proinflammatory cytokine release was significantly elevated in Ana-1 macrophages upon exposure to PrP106-126; that PrP106-126 treatment led to a significant NF-κB activation; that proinflammatory cytokines gene expression was elevated in macrophages upon exposure to PrP106-126; and that NF-κB inhibition significantly abrogated PrP106-126-induced upregulation of iNOS and inflammatory cytokine mRNA expression. These results suggest that treatment with neurotoxic prion peptides leads to the activation of transcription factor NF-κB, which in turn stimulates gene expression of iNOS and proinflammatory cytokines in Ana-1 macrophages.

Source–> http://www.pubfacts.com/detail/22149924/Prion-peptide-PrP106-126-induces-inducible-nitric-oxide-synthase-and-proinflammatory-cytokine-gene-e

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The Transcription Factor Nuclear Factor-kappa B and Cancer

Abstract

Since the discovery of nuclear factor-kappa B (NF-κB) in 1986, many studies have been conducted showing the link between the NF-κB signalling pathway and control of the inflammatory response. Today it is well known that control of the inflammatory response and apoptosis is closely related to the activation of NF-κB. Three NF-κB activation pathways exist. The first (the classical pathway) is normally triggered in response to microbial and viral infections or exposure to pro-inflammatory cytokines that activate the tripartite IKK complex, leading to phosphorylation-induced IκB degradation and depends mainly on IKKβ activity. The second (the alternative pathway), leads to selective activation of p52:RelB dimers by inducing the processing of the NF-κB2/p100 precursor protein, which mostly occurs as a heterodimer with RelB in the cytoplasm. This pathway is triggered by certain members of the tumour necrosis factor cytokine family, through selective activation of IKKα homodimers by the upstream kinase NIK. The third pathway is named CK2 and is IKK independent. NF-κB acts through the transcription of anti-apoptotic proteins, leading to increased proliferation of cells and tumour growth. It is also known that some drugs act directly in the inhibition of NF-κB, thus producing regulation of apoptosis; some examples are aspirin and corticosteroids. Here we review the role of NF-κB in the control of apoptosis, its link to oncogenesis, the evidence of several studies that show that NF-κB activation is closely related to different cancers, and finally the potential target of NF-κB as cancer therapy.

Source–> http://www.sciencedirect.com/science/article/pii/S0936655506004274

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Nuclear factor kappa B (NF-κB) in multiple sclerosis pathology

Highlights

• NF-κB signaling in MS patients and animal models of MS.
NF-κB signaling controls peripheral immune activation at multiple levels.
NF-κB controls inflammatory responses locally in the CNS.
• NF-κB as a therapeutic target for the treatment of MS.

The nuclear factor kappa B (NF-κB) signaling cascade plays a critical role in the regulation of immune and inflammatory responses and has been implicated in the pathogenesis of autoimmune demyelinating diseases such as multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE), the main animal model of MS. NF-κB is essential for peripheral immune cell activation and the induction of pathology, but also plays crucial roles in resident cells of the central nervous system (CNS) during disease development. Here we review recent evidence clarifying the role of NF-κB in the different cell compartments contributing to MS pathology and its implications for the development of therapeutic strategies for the treatment of MS and other demyelinating pathologies of the CNS.

Source–> http://www.sciencedirect.com/science/article/pii/S1471491413001330

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NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA. NF-κB is found in almost all animal cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, ultraviolet radiation, oxidized LDL, and bacterial or viral antigens.[1][2][3][4][5] NF-κB plays a key role in regulating the immune response to infection (k light chains are critical components of immunoglobulins). Incorrect regulation of NF-κB has been linked to cancer, inflammatory, and autoimmune diseases, septic shock, viral infection, and improper immune development. NF-κB has also been implicated in processes of synaptic plasticity and memory.[6][7][8][9][10]

In brief, NF-κB can be understood to be a protein responsible for cytokine production and cell survival.

Structure

All proteins of the NF-κB family share a Rel homology domain in their N-terminus. A subfamily of NF-κB proteins, including RelA, RelB, and c-Rel, have a transactivation domain in their C-termini. In contrast, the NF-κB1 and NF-κB2 proteins are synthesized as large precursors, p105, and p100, which undergo processing to generate the mature NF-κB subunits, p50 and p52, respectively. The processing of p105 and p100 is mediated by the ubiquitin/proteasome pathway and involves selective degradation of their C-terminal region containing ankyrin repeats. Whereas the generation of p52 from p100 is a tightly regulated process, p50 is produced from constitutive processing of p105.[12][13] The p50 and p52 proteins have no intrinsic ability to activate transcription and thus have been proposed to act as transcriptional repressors when binding κB elements as homodimers.[14][15] Indeed, this confounds the interpretation of p105-knockout studies, where the genetic manipulation is removing an IκB (full-length p105) and a likely repressor (p50 homodimers) in addition to a transcriptional activator (the RelA-p50 heterodimer).

Members

NF-κB family members share structural homology with the retroviral oncoprotein v-Rel, resulting in their classification as NF-κB/Rel proteins.[1]

There are five proteins in the mammalian NF-κB family:[16]

Species distribution and evolution

In addition to mammals, NF-κB is found in a number of simple animals as well.[17] These include cnidarians (such as sea anemones, coral and hydra), porifera (sponges), the single-celled eukaryote Capsaspora owczarzaki and insects (such as moths, mosquitoes, and fruit flies). The sequencing of the genomes of the mosquitoes A. aegypti and A. gambiae, and the fruitfly D. melangaster has allowed comparative genetic and evolutionary studies on NF-κB. In those insect species, activation of NF-κB is triggered by the Toll pathway (which evolved independently in insects and mammals) and by the Imd (immune deficiency) pathway.[18]

Toll-like receptors (TLRs) are a class of proteins that play a key role in the innate immune system. They are single, membrane-spanning, non-catalytic receptors usually expressed in sentinel cells such as macrophages and dendritic cells, that recognize structurally conserved molecules derived from microbes. Once these microbes have breached physical barriers such as the skin or intestinal tract mucosa, they are recognized by TLRs, which activate immune cell responses

Signaling

Activation

NF-κB (green) heterodimerizes with RelB (cyan) to form a ternary complex with DNA (orange) that promotes gene transcription.[19]

NF-κB is important in regulating cellular responses because it belongs to the category of “rapid-acting” primary transcription factors, i.e., transcription factors that are present in cells in an inactive state and do not require new protein synthesis in order to become activated (other members of this family include transcription factors such as c-Jun, STATs, and nuclear hormone receptors). This allows NF-κB to be a first responder to harmful cellular stimuli. Known inducers of NF-κB activity are highly variable and include reactive oxygen species (ROS), tumor necrosis factor alpha (TNFa), interleukin 1-beta (IL1β), bacterial lipopolysaccharides (LPS), isoproterenol, cocaine, and ionizing radiation.[20]

Receptor activator of NF-κB (RANK), which is a type of TNFR, is a central activator of NF-κB. Osteoprotegerin (OPG), which is a decoy receptor homolog for RANK ligand, inhibits RANK by binding to RANKL, and, thus, osteoprotegerin is tightly involved in regulating NF-κB activation.[21]

Many bacterial products and stimulation of a wide variety of cell-surface receptors lead to NF-κB activation and fairly rapid changes in gene expression.[1] The identification of Toll-like receptors(TLRs) as specific pattern recognition molecules and the finding that stimulation of TLRs leads to activation of NF-κB improved our understanding of how different pathogens activate NF-κB. For example, studies have identified TLR4 as the receptor for the LPS component of Gram-negative bacteria.[22] TLRs are key regulators of both innate and adaptive immune responses.[23]

Unlike RelA, RelB, and c-Rel, the p50 and p52 NF-κB subunits do not contain transactivation domains in their C terminal halves. Nevertheless, the p50 and p52 NF-κB members play critical roles in modulating the specificity of NF-κB function. Although homodimers of p50 and p52 are, in general, repressors of κB site transcription, both p50 and p52 participate in target gene transactivation by forming heterodimers with RelA, RelB, or c-Rel.[24] In addition, p50 and p52 homodimers also bind to the nuclear protein Bcl-3, and such complexes can function as transcriptional activators.[25][26][27]

Inhibition

In unstimulated cells, the NF-κB dimers are sequestered in the cytoplasm by a family of inhibitors, called IκBs (Inhibitor of κB), which are proteins that contain multiple copies of a sequence called ankyrin repeats. By virtue of their ankyrin repeat domains, the IκB proteins mask the nuclear localization signals (NLS) of NF-κB proteins and keep them sequestered in an inactive state in the cytoplasm.[28]

IκBs are a family of related proteins that have an N-terminal regulatory domain, followed by six or more ankyrin repeats and a PEST domain near their C terminus. Although the IκB family consists of IκBα, IκBβ, IκBε, and Bcl-3, the best-studied and major IκB protein is IκBα. Due to the presence of ankyrin repeats in their C-terminal halves, p105 and p100 also function as IκB proteins. The c-terminal half of p100, that is often referred to as IκBδ, also functions as an inhibitor.[29][30] IκBδ degradation in response to developmental stimuli, such as those transduced through LTβR, potentiate NF-κB dimer activation in a NIK dependent non-canonical pathway.[29][31]

Activation of the NF-κB is initiated by the signal-induced degradation of IκB proteins. This occurs primarily via activation of a kinase called the IκB kinase (IKK). IKK is composed of a heterodimer of the catalytic IKKα and IKKβ subunits and a “master” regulatory protein termed NEMO (NF-κB essential modulator) or IKK gamma. When activated by signals, usually coming from the outside of the cell, the IκB kinase phosphorylates two serine residues located in an IκB regulatory domain. When phosphorylated on these serines (e.g., serines 32 and 36 in human IκBα), the IκB inhibitor molecules are modified by a process called ubiquitination, which then leads them to be degraded by a cell structure called the proteasome.

With the degradation of IκB, the NF-κB complex is then freed to enter the nucleus where it can ‘turn on’ the expression of specific genes that have DNA-binding sites for NF-κB nearby. The activation of these genes by NF-κB then leads to the given physiological response, for example, an inflammatory or immune response, a cell survival response, or cellular proliferation. NF-κB turns on expression of its own repressor, IκBα. The newly synthesized IκBα then re-inhibits NF-κB and, thus, forms an auto feedback loop, which results in oscillating levels of NF-κB activity.[32] In addition, several viruses, including the AIDS virus HIV, have binding sites for NF-κB that controls the expression of viral genes, which in turn contribute to viral replication or viral pathogenicity. In the case of HIV-1, activation of NF-κB may, at least in part, be involved in activation of the virus from a latent, inactive state.[33] YopP is a factor secreted by Yersinia pestis, the causative agent of plague, that prevents the ubiquitination of IκB. This causes this pathogen to effectively inhibit the NF-κB pathway and thus block the immune response of a human infected with Yersinia.[34]

Inhibitors of NF-κB activity

Concerning known protein inhibitors of NF-κB activity, one of them is IFRD1, which represses the activity of NF-κB p65 by enhancing the HDAC-mediated deacetylation of the p65 subunit at lysine 310, by favoring the recruitment of HDAC3 to p65. In fact IFRD1 forms trimolecular complexes with p65 and HDAC3.[35][36]

Non-canonical

A select set of cell-differentiating or developmental stimuli, such as lymphotoxin-α, BAFF or RANKL, activate the non-canonical NF-κB pathway to induce NF-κB/RelB:p52 dimer in the nucleus. In this pathway, activation of the NF-κB inducing kinase (NIK) upon receptor ligation led to the phosphorylation and subsequent proteasomal processing of the NF-κB2 precursor protein p100 into mature p52 subunit in an IKK1/IKKa dependent manner. Then p52 dimerizes with RelB to appear as a nuclear RelB:p52 DNA binding activity and regulate a distinct class of genes.[37] In contrast to the canonical signaling that relies upon NEMO-IKK2 mediated degradation of IκBα, -β, -ε, the non-canonical signaling critically depends on NIK mediated processing of p100 into p52. Given their distinct regulations, these two pathways were thought to be independent of each other. However, recent analyses revealed that synthesis of the constituents of the non-canonical pathway, viz RelB and p52, is controlled by the canonical IKK2-IκB-RelA:p50 signaling.[38] Moreover, generation of the canonical and non-canonical dimers, viz RelA:p50 and RelB:p52, within the cellular milieu are also mechanistically interlinked.[38] These analyses suggest that an integrated NF-κB system network underlies activation of both RelA and RelB containing dimer and that a malfunctioning canonical pathway will lead to an aberrant cellular response also through the non-canonical pathway.

In immunity

NF-κB is a major transcription factor that regulates genes responsible for both the innate and adaptive immune response. Upon activation of either the T- or B-cell receptor, NF-κB becomes activated through distinct signaling components. Upon ligation of the T-cell receptor, protein kinase Lck is recruited and phosphorylates the ITAMs of the CD3 cytoplasmic tail. ZAP70 is then recruited to the phosphorylated ITAMs and helps recruit LAT and PLC-γ, which causes activation of PKC. Through a cascade of phosphorylation events, the kinase complex is activated and NF-κB is able to enter the nucleus to upregulate genes involved in T-cell development, maturation, and proliferation.[39]

In the nervous system

In addition to roles in mediating cell survival, studies by Mark Mattson and others have shown that NF-κB has diverse functions in the nervous system including roles in plasticity, learning, and memory. In addition to stimuli that activate NF-κB in other tissues, NF-κB in the nervous system can be activated by Growth Factors (BDNF, NGF) and synaptic transmission such as glutamate.[7] These activators of NF-κB in the nervous system all converge upon the IKK complex and the canonical pathway.

Recently there has been a great deal of interest in the role of NF-κB in the nervous system. Current studies suggest that NF-κB is important for learning and memory in multiple organisms including crabs,[9][10] fruit flies,[40] and mice.[7][8] NF-κB may regulate learning and memory in part by modulating synaptic plasticity,[6][41] synapse function,[40][42][43] as well as by regulating the growth of dendrites[44] and dendritic spines.[43]

Genes that have NF-κB binding sites are shown to have increased expression following learning,[8] suggesting that the transcriptional targets of NF-κB in the nervous system are important for plasticity. Many NF-κB target genes that may be important for plasticity and learning include growth factors (BDNF, NGF)[45] cytokines (TNF-alpha, TNFR)[46] and kinases (PKAc).[41]

Despite the functional evidence for a role for Rel-family transcription factors in the nervous system, it is still not clear that the neurological effects of NF-κB reflect transcriptional activation in neurons. Most manipulations and assays are performed in the mixed-cell environments found in vivo, in “neuronal” cell cultures that contain significant numbers of glia, or in tumor-derived “neuronal” cell lines. When transfections or other manipulations have been targeted specifically at neurons, the endpoints measured are typically electrophysiology or other parameters far removed from gene transcription. Careful tests of NF-κB-dependent transcription in highly purified cultures of neurons generally show little to no NF-κB activity.[47][48] Some of the reports of NF-κB in neurons appear to have been an artifact of antibody nonspecificity.[49] Of course, artifacts of cell culture—e.g., removal of neurons from the influence of glia—could create spurious results as well. But this has been addressed in at least two coculture approaches. Moerman et al.[50] used a coculture format whereby neurons and glia could be separated after treatment for EMSA analysis, and they found that the NF-κB induced by glutamatergic stimuli was restricted to glia (and, intriguingly, only glia that had been in the presence of neurons for 48 hours). The same investigators explored the issue in another approach, utilizing neurons from an NF-κB reporter transgenic mouse cultured with wild-type glia; glutamatergic stimuli again failed to activate in neurons.[51] Some of the DNA-binding activity noted under certain conditions (particularly that reported as constitutive) appears to result from Sp3 and Sp4 binding to a subset of κB enhancer sequences in neurons.[52] This activity is actually inhibited by glutamate and other conditions that elevate intraneuronal calcium. In the final analysis, the role of NF-κB in neurons remains opaque due to the difficulty of measuring transcription in cells that are simultaneously identified for type. Certainly, learning and memory could be influenced by transcriptional changes in astrocytes and other glial elements. And it should be considered that there could be mechanistic effects of NF-κB aside from direct transactivation of genes.

Clinical significance

Overview of signal transduction pathways involved in apoptosis.

Cancers

NF-κB is widely used by eukaryotic cells as a regulator of genes that control cell proliferation and cell survival. As such, many different types of human tumors have misregulated NF-κB: that is, NF-κB is constitutively active. Active NF-κB turns on the expression of genes that keep the cell proliferating and protect the cell from conditions that would otherwise cause it to die via apoptosis.

Defects in NF-κB results in increased susceptibility to apoptosis leading to increased cell death. This is because NF-κB regulates anti-apoptotic genes especially the TRAF1 and TRAF2 and, therefore, checks the activities of the caspase family of enzymes, which are central to most apoptotic processes.[53]

In tumor cells, NF-κB is active either due to mutations in genes encoding the NF-κB transcription factors themselves or in genes that control NF-κB activity (such as IκB genes); in addition, some tumor cells secrete factors that cause NF-κB to become active. Blocking NF-κB can cause tumor cells to stop proliferating, to die, or to become more sensitive to the action of anti-tumor agents. Thus, NF-κB is the subject of much active research among pharmaceutical companies as a target for anti-cancer therapy.[54]

However, caution should be exercised when considering anti-NF-κB activity as a broad therapeutic strategy in cancer therapy, even though convincing experimental data have identified NF-κB as a critical promoter of cancer development, creating a solid rationale for the development of antitumor therapy that suppresses NF-κB activity. Data have also shown that NF-κB activity enhances tumor cell sensitivity to apoptosis and senescence. In addition, it has been shown that canonical NF-κB is a Fas transcription activator and the alternative NF-κB is a Fas transcription repressor.[55] Therefore, NF-κB promotes Fas-mediated apoptosis in cancer cells, and thus inhibition of NF-κB may suppress Fas-mediated apoptosis to impair host immune cell-mediated tumor suppression.

Inflammation

Because NF-κB controls many genes involved in inflammation, it is not surprising that NF-κB is found to be chronically active in many inflammatory diseases, such as inflammatory bowel disease, arthritis, sepsis, gastritis, asthma, atherosclerosis[56] and others. It is important to note though, that elevation of some NF-κB inhibitors, such as osteoprotegerin (OPG), are associated with elevated mortality, especially from cardiovascular diseases.[57][58] Elevated NF-κB has also been associated with schizophrenia.[59] Recently, NF-κB activation has been suggested as a possible molecular mechanism for the catabolic effects of cigarette smoke in skeletal muscle and sarcopenia.[60]

Non-drug inhibitors

Many natural products (including anti-oxidants) that have been promoted to have anti-cancer and anti-inflammatory activity have also been shown to inhibit NF-κB.[61][62] There is a controversial US patent (US patent 6,410,516)[63] that applies to the discovery and use of agents that can block NF-κB for therapeutic purposes. This patent is involved in several lawsuits, including Ariad v. Lilly. Recent work by Karin,[64] Ben-Neriah[65] and others has highlighted the importance of the connection between NF-κB, inflammation, and cancer, and underscored the value of therapies that regulate the activity of NF-κB.[66]

Extracts from a number of herbs and dietary plants are efficient inhibitors of NF-κB activation in vitro.[67][68][69]

The circumsporozoite protein of Plasmodium falciparum has been shown to be an inhibitor of NF-κB.[70]

As a drug target

Aberrant activation of NF-κB is frequently observed in many cancers. Moreover, suppression of NF-κB limits the proliferation of cancer cells. In addition, NF-κB is a key player in the inflammatory response. Hence methods of inhibiting NF-κB signaling has potential therapeutic application in cancer and inflammatory diseases.[71][72]

The discovery that activation of NF-κB nuclear translocation can be separated from the elevation of oxidant stress[73] gives an important hint to the development of strategies for NF-κB inhibition.

A new drug called denosumab acts to raise bone mineral density and reduce fracture rates in many patient sub-groups by inhibiting RANKL. RANKL acts through its receptor RANK, which in turn promotes NF-κB,[74] RANKL normally works by enabling the differentiation of osteoclasts from monocytes.

Disulfiram, olmesartan and dithiocarbamates can inhibit the nuclear factor-κB (NF-κB) signaling cascade.[75]

Anatabine’s antiinflammatory effects are claimed to result from modulation of NF-κB activity.[76] However the studies purporting its benefit use abnormally high doses in the millimolar range (similar to the extracellular potassium concentration), which are unlikely to be achieved in humans.

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NF-kB

Nuclear factor NF-kappa-B p105 subunit is a protein that in humans is encoded by the NFKB1 gene.[1]

This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S  proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappaB (NF-kB) protein complex. NF-κB is a transcription factor that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NF-κB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions; over 200 known genes are targets of NF-κB in various cell types, under specific conditions. Inappropriate activation of NF-κB has been associated with a number of inflammatory diseases while persistent inhibition of NF-κB leads to inappropriate immune cell development or delayed cell growth.[2]

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Signal Transduction Through Prion Protein

The cellular prion protein PrPc is a glycosylphosphatidylinositol-anchored cell-surface protein whose biological function is unclear. We used the murine 1C11 neuronal differentiation model to search for PrPc-dependent signal transduction through antibody-mediated cross-linking. A caveolin-1–dependent coupling of PrPc to the tyrosine kinase Fyn was observed. Clathrin might also contribute to this coupling. The ability of the 1C11 cell line to trigger PrPc-dependent Fyn activation was restricted to its fully differentiated serotonergic or noradrenergic progenies. Moreover, the signaling activity of PrPc occurred mainly at neurites. Thus, PrPc may be a signal transduction protein.

Science 15 September 2000:
Vol. 289
no. 5486 pp. 1925-1928
DOI:10.1126/science.289.5486.1925
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A cellular gene encodes scrapie PrP 27-30 protein.

Abstract

A clone encoding PrP 27-30, the major protein in purified preparations of scrapie agent, was selected from a scrapie-infected hamster brain cDNA library by oligonucleotide probes corresponding to the N terminus of the protein. Southern blotting with PrP cDNA revealed a single gene with the same restriction patterns in normal and scrapie-infected brain DNA. A single PrP-related gene was also detected in murine and human DNA. PrP-related mRNA was found at similar levels in normal and scrapie-infected hamster brain, as well as in many other normal tissues. Using antisera against PrP 27-30, a PrP-related protein was detected in crude extracts of infected brain and to a lesser extent in extracts of normal brain. Proteinase K digestion yielded PrP 27-30 in infected brain extract, but completely degraded the PrP-related protein in normal brain extract. No PrP-related nucleic acids were found in purified preparations of scrapie prions, indicating that PrP 27-30 is not encoded by a nucleic acid carried within the infectious particles.

Source–> http://www.ncbi.nlm.nih.gov/pubmed/2859120

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Identification of Chemoattractive Factors Involved in the Migration of Bone Marrow-Derived Mesenchymal Stem Cells to Brain Lesions Caused by Prions

ABSTRACT

Bone marrow-derived mesenchymal stem cells (MSCs) have been reported to migrate to brain lesions of neurodegenerative diseases; however, the precise mechanisms by which MSCs migrate remain to be elucidated. In this study, we carried out an in vitro migration assay to investigate the chemoattractive factors for MSCs in the brains of prion-infected mice. The migration of immortalized human MSCs (hMSCs) was reduced by their pretreatment with antibodies against the chemokine receptors, CCR3, CCR5, CXCR3, and CXCR4 and by pretreatment of brain extracts of prion-infected mice with antibodies against the corresponding ligands, suggesting the involvement of these receptors, and their ligands in the migration of hMSCs. In agreement with the results of an in vitro migration assay, hMSCs in the corpus callosum, which are considered to be migrating from the transplanted area toward brain lesions of prion-infected mice, expressed CCR3, CCR5, CXCR3, and CXCR4. The combined in vitro and in vivo analyses suggest that CCR3, CCR5, CXCR3, and CXCR4, and their corresponding ligands are involved in the migration of hMSCs to the brain lesions caused by prion propagation. In addition, hMSCs that had migrated to the right hippocampus of prion-infected mice expressed CCR1, CX3CR1, and CXCR4, implying the involvement of these chemokine receptors in hMSC functions after chemotactic migration. Further elucidation of the mechanisms that underlie the migration of MSCs may provide useful information regarding application of MSCs to the treatment of prion diseases.

INTRODUCTION

Prion diseases are fatal neurodegenerative disorders in humans and animals that are characterized by the accumulation of a disease-specific isoform of the prion protein (PrPSc), astrocytosis, microglial activation, spongiosis, and neuronal cell death in the central nervous system (CNS). Although the etiology of the diseases is not clear, conversion of the normal prion protein to PrPSc plays a key role in the neuropathological changes (44). Therefore, compounds that inhibit PrPSc formation are considered as therapeutic candidates of the diseases, and many compounds have been reported to inhibit PrPSc formation in cell cultures and cell-free systems (reviewed in reference 56). However, only a few of these inhibitors, such as amphotericin B and its derivative (13), pentosan polysulfate (14), porphyrin derivatives (27), certain amyloidophilic compounds (25), and FK506 (37) have been reported to prolong the survival of prion-infected mice even when administered in the middle-late stage of infection but still before clinical onset. We recently reported that intraventricular infusion of anti-PrP antibodies (50) slowed down the progression of the disease even when initiated just after clinical onset. However, in addition to inhibition of PrPSc formation, the protection of neurons or restoration of degenerated neurons is thought to be important for functional recovery.

Bone marrow-derived mesenchymal stem cells (MSCs) differentiate into cells of mesodermal origin such as adipocytes, osteoblasts, and endothelial and muscle cells (41, 43). In addition, MSCs are known to transdifferentiate into neuronal and glial cells. MSCs have been shown to migrate to damaged neuronal tissues and to alleviate the deficits in experimental animal models of cerebral ischemia (10), spinal cord injury (20), Parkinson’s disease (19, 33), and amyotrophic lateral sclerosis (59). MSCs also secrete various neurotrophic factors that may protect neuronal tissues from degradations, as well as stimulate the activity of endogenous neural stem cells (38). Therefore, despite their mesodermal origin, MSCs are considered to be a candidate for cell-mediated therapy for neurodegenerative diseases. One of the characteristics of MSCs is their migration to brain lesions caused by neurodegenerative diseases, including prion diseases (10, 19, 39, 51). This feature may be of further use for cell-mediated therapy of neurodegenerative diseases, particularly for prion diseases, Multiple sclerosis and Alzheimer’s disease, which have diffuse pathological lesions.

Since many cytokines, chemokines, and adhesion molecules are involved in the homing of immune cells (9, 36, 53), evidence that a variety of chemokines and growth factors, as well as their cognate receptors, have a pivotal role in the migration of MSCs has been accumulated. These factors include CXCL12 and its receptor CXCR4 (30, 40; reviewed in reference 52), CCL2 (15, 62, 66), CCL3 (62), interleukin-8 (48, 62), hepatocyte growth factor (16), platelet-derived growth factor AB (PDGF-AB), insulin-like growth factor 1 (IGF-1), CCL5 and CCL22 (42), and integrin β1 (23). Regarding the migration of MSCs to injury in the CNS, the involvement of CCL2 (61), CXCL12/CXCR4, and CX3CL1/CX3CR1 (24) has been reported. However, knowledge of the mechanism by which MSCs migrate to pathological lesions of neurodegenerative diseases is insufficient, and further efforts are required to elucidate this mechanism.

We recently reported that human MSCs (hMSCs) migrate to CNS lesions and prolong the survival of mice infected with prions (51). In the present study, we investigated factors that are involved in the migration of hMSCs to brain lesions of prion diseases.

Source–> http://jvi.asm.org/content/85/21/11069.full

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Conclusion
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To say that the body is one giant communication system is an understatement. The expression of genes and the ability for host cells to operate normally and to chemically call for help when faced with an antigen is esential to health. As discussed above, these prion interferors with the interferon and other defensive signaling processes must be injected to bypass the mucosus and the skin. This can only be accomplished through innoculation and vaccination.

The introduction of foreign proteins and DNA/RNA into the otherwise healthy body is certainly described here as the cause of most disease states in modern times. And from the time that this interferon was discovered, these psychopathic scientists have been working overtime to prevent our bodies from being able to fight what they inject.

What you have just read is the cause and cure for AIDS, cancers, dementias, and a host of other modern medically-induced disease states that revolve around prion infection and misfolding of the signal processing of the body. It is not so much a cure as an acknowledgement of the cause, for when disease is purposefully caused, the word cure seems trivial in practice, and allows the culprits to literally get away with murder.

It was caused by them…

Will we sit by helplessly and hope for a cure to these purposefully caused diseases by the very perpetrators of them?

Isn’t that the American way though?

For as we wait, they merely perfect their science of biological aggression and warfare…

(Note: all unlinked data as descriptions above from Wikipedia, which are well-sourced within that site.)

.

–Clint Richardson (realitybloger.wordpress.com)
–Thursday, December 4rth, 2014

The Prion Chronicles: Prions And ALS


A few months ago, I documented a speculative and fact-based op-ed that espoused my theory that most modern degenerative diseases referred to as “dementia” are at the very least partially caused by what are called prions – malformed or “folded” proteins that infectiously cause other proteins to fold and be rendered useless to the human body – causing disease states ranging from 50% of all cancers to AIDS as a protein “blood cancer” to mental disorders such as Alzheimer’s and ALS.

That research can be found here: http://realitybloger.wordpress.com/2012/11/11/xenotransplantation-creating-the-zombie-appocalypse/

It is my sincere belief that these infectious prions are being spread either inadvertently or purposefully throughout the human and animal population through the use of animal and human DNA and proteins found after the growing and manufacture process for vaccines – the use of human diploid (aborted fetal) cells and animal organs, blood, and parts as cell substrate growth mechanisms for the culturing of vaccines. Prions are the cause of Mad-Cow Disease, as well as equivalent disease states in humans showing protein (prion) misfolding.

While a guy like me will never be considered for a Nobel Prize for such speculation and endless compiling of other people’s research, I will be chronicling any information that comes my way regarding this dyer theory.

Case in point…

On September 20, 2011, the Vancouver Coastal Health Research Institute posted the following article:

Dr. Neil Cashman PrioNet Canada researchers in Vancouver confirm prion-like properties in Amyotrophic Lateral Sclerosis (ALS)

September 20, 2011 – Vancouver, BC: A team of researchers from the University of British Columbia and the Vancouver Coastal Health Research Institute have found a key link between prions and the neurodegenerative disease ALS ( Amyotrophic Lateral Sclerosis), also known as Lou Gehrig’s disease. The discovery is significant as it opens the door to novel approaches to the treatment of ALS.

SOD-1 Dimer A pivotal paper published by the team this week in the Proceedings of the National Academy of Sciences (PNAS), demonstrates that the SOD1 protein (superoxide dismutase 1), which has been shown to be implicated in the ALS disease process, exhibits prion-like properties. The researchers found that SOD1 participates in a process called template-directed misfolding. This term refers to the coercion of one protein by another protein to change shape and accumulate in large complexes in a fashion similar to the process underlying prion diseases.

These findings provide a molecular explanation for the progressive spread of ALS through the nervous system, and highlight the central role of the propagation of misfolded proteins in the pathogenesis of neurodegenerative diseases, including ALS, Alzheimer’s and Parkinson’s.

“Our work has identified a specific molecular target, which when manipulated halts the conversion of the SOD1 protein to a misfolded, disease-causing form,” says Dr. Neil Cashman, Scientific Director of PrioNet Canada, Canada Research Chair in Neurodegeneration and Protein Misfolding at UBC, and academic director of the Vancouver Coastal Health ALS Centre. “This discovery is a first-step toward the development of targeted treatments that may stop progression of ALS.”

ALS is a progressive neuromuscular disease in which nerve cells die, resulting in paralysis and death. Approximately 2,500 to 3,000 Canadians currently live with this fatal disease, for which there is no effective treatment yet.

“For many years, ALS has remained a complex puzzle and we have found a key piece to help guide the research community to solutions,” says Dr. Leslie Grad, a co-first author of the project and current Manager of Scientific Programs at PrioNet Canada. “PrioNet is further exploring this discovery through newly-funded research projects.”

The work was completed by Dr. Neil Cashman’s lab at the Brain Research Centre based at the University of British Columbia and the Vancouver Coastal Health Research Institute, in collaboration with researchers at the University of Alberta. The research was supported by PrioNet Canada and in part by Amorfix Life Sciences and the Canadian Institutes of Health Research.

PrioNet Canada, based in Vancouver, has achieved international attention for scientific discoveries and risk management strategies directed at controlling prion diseases, and is now directing capacity into therapeutic solutions for prion-like diseases of aging, such as Alzheimer’s, Parkinson’s and ALS.

ABOUT:
One of Canada’s Networks of Centres of Excellence, PrioNet Canada (www.prionetcanada.ca) is developing strategies to help solve the food, health safety, and socioeconomic problems associated with prion diseases. The network brings together scientists, industry, and public sector partners through its multidisciplinary research projects, training programs, events, and commercialization activities. PrioNet is hosted by the University of British Columbia and the Vancouver Coastal Health Research Institute in Vancouver.

The University of British Columbia (UBC) is one of North America’s largest public research and teaching institutions, and one of only two Canadian institutions consistently ranked among the world’s 40 best universities. UBC is a place that inspires bold, new ways of thinking that have helped make it a national leader in areas as diverse as community service learning, sustainability and research commercialization. UBC offers more than 50,000 students a range of innovative programs and attracts $550 million per year in research funding from government, non-profit organizations and industry through 7,000 grants.

Vancouver Coastal Health Research Institute (VCHRI) (www.vchri.ca) is the research body of Vancouver Coastal Health Authority, which includes BC’s largest academic and teaching health sciences centres: VGH, UBC Hospital, and GF Strong Rehabilitation Centre. In academic partnership with the University of British Columbia, VCHRI brings innovation and discovery to patient care, advancing healthier lives in healthy communities across British Columbia, Canada, and beyond.

The Brain Research Centre (BRC) (www.brain.ubc.ca) comprises more than 200 investigators with multidisciplinary expertise in neuroscience research ranging from the test tube, to the bedside, to industrial spin-offs. The centre is a partnership of UBC and Vancouver Coastal Health Research Institute.

Media information or to set up interviews:

Gail Bergman, Gail Bergman PR
Tel: (905) 886-1340 or (905) 886-3345
E-mail: info@gailbergmanpr.com

BACKGROUNDER – ALS as a “prion-like” disease

Amyotrophic lateral sclerosis (ALS):

Amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig ‘s disease in the United States and motor neurone disease (MND) in Europe, is a fatal neurodegenerative disease caused by deterioration of motor neurons in the brain and spinal cord. Individuals living with the disease experience progressive paralysis, as well as difficulty breathing or swallowing. At this time, no cure or effective treatment exists.

According to the ALS Society of Canada: ALS is the most common cause of neurological death Every day two or three Canadians die of ALS Eighty per cent of people with ALS die within two to five years of diagnosis; ten per cent of those affected may live for 10 years or longer Approximately 2,500 – 3,000 Canadians currently live with this fatal disease The World Health Organization predicts that neurodegenerative diseases will surpass cancer as the second leading cause of death in Canada by 2040

BACKGROUND:

Recent research highlights links between the biological mechanisms of common neurological disorders, such as ALS, Alzheimer’s and Parkinson’s disease with prion disease. While each of these diseases manifests itself in a different way, the hallmark of each is a progressive accumulation of misfolded protein aggregates in the central nervous system.

Correctly-folded proteins adopt one particular structure in order to carry out their intended function. A protein’s failure to adopt this correct structure is what threatens the health of cells. Prions are “misfolded” proteins – the infectious, aggregating agents in diseases such as Creutzfeldt-Jakob disease (CJD) in humans, chronic wasting disease (CWD) in deer and elk and bovine spongiform encephalopathy (BSE), also known as “mad cow” disease in cattle. In ALS, Alzheimer’s and Parkinson’s, the misfolded proteins are SOD1, amyloid-B and a-synuclein, respectively.

Key Finding:

“Intermolecular transmission of SOD-1 misfolding in living cells” – Published in the Proceedings of the National Academy of Sciences (PNAS), September 2011. The paper shows that superoxide dismutase 1 (SOD1) participates in template-directed misfolding, in other words, the coercion of one protein by another protein to change shape and aggregate such as prion diseases do. The results will be significant to the ALS field because it connects prion mechanisms behind the biological progression of ALS, and provides a molecular explanation for the linear and temporal spread of ALS through the nervous system. Furthermore, the research has identified a specific molecular target, which when manipulated, halts the conversion of SOD1 to a misfolded, disease-causing form. This is a first-step towards the development of targeted treatments that may stop ALS, which PrioNet is further exploiting through newly-funded research. This research was supported by PrioNet Canada and in part by Amorfix Life Sciences and the Canadian Institutes of Health Research.

Other Research:

Studies showing how “seed” misfolded protein induce aggregation of other protein, which provide evidence for prion-like spread: Lary Walker’s group at Emory University in Atlanta, in collaboration with Matthias Jucker and others at the Universities of Tübingen in Germany and Basel in Switzerland, discovered that aggregates of amyloid-β protein from the brain of people with Alzheimer’s disease could be transmitted to the brain of healthy mice. Another study by Patrik Brundin’s group in Sweden demonstrated that healthy tissue surgically implanted into the brain of people with Parkinson’s disease acquired the aggregates of α-synuclein protein characteristic of the disease. Eliezer Masliah of the University of California San Diego and others discovered that aggregates of a-synuclein can travel from cell to cell, forming the aggregates in human neurons that are characteristic of Parkinson’s disease and certain types of dementia. Anne Bertolotti from the University of Cambridge discovered that neuronal cells spontaneously and efficiently take up misfolded mutant SOD1 from their environment. The internalized mutant SOD1 triggers a change in shape of the normally soluble mutant SOD1 protein, which causes its aggregation, and is then transferred to neighbouring cells in a prion-like fashion.

(Article Source: http://www.vchri.ca/feature-stories/articles/2011/09/20/researchers-discovery-may-revolutionize-treatment-als)

–=–

Folks, you will not hear of this on the nightly news, and the doctors and nurses I’ve talked to have never even heard of a “prion”. But you can bet that they have heard of Merck, Astrazeneca, Sanofi Aventis, and Glaxo-Smithkline, because they get paid to sell their pharmaceutical drugs and vaccines!

The most logical and easiest to explain transmissible quality of prions is by far the vaccinations received by humans and animals, which again have been admitted by the vaccine manufacturers to contain DNA and proteins too small and numerous to filter out of the final vaccine product. Thus, we have over 100 million Americans and billions worldwide receiving a direct bodily injection of human and foreign animal proteins through vaccination. This is not a conspiracy theory, but fact – and this consideration of possible prion infection and transmission through vaccination is very likely just one of many dangers already known to the vaccine industry, but ignored due to the profit potential of vaccines. And since the direct blood-to-blood and blood-to-intramuscular transmission of prions in general is only possible under surgery conditions, the only logical transmission agents that would cause such wide-spread prion-based disease states and neuro-degenerative issues in both aging and prematurely young populations (early onset dementia) are the either the food supply and/or the vaccination process – which bypasses the stomach and digestive system’s natural defenses and disposal process.

Like the banking, automobile, and other corporate structures in America, the pharmaceutical industry that manufactures these vaccines may very well be considered “too big to fail” by government – and is certainly one of the most profitable. And these facts alone place a tremendous conflict of interest in seeing justice done by way of recognizing, prosecuting, and suing this industry as being the cause of this wide-spread dementia outbreak among humans – the end result being this industry’s and its shareholders inevitable financial ruin.

I alone cannot force an investigation to take place, and in its stead will be the same medical and pharmaceutical corporations creating drug “symptom-relievers” and “treatments” for the very prion-based diseases that they are now spreading, meaning profitable returns for these corporations and for government institutional investment funds – the main investor in these vaccine manufacture corporations.

I may not be recognized by future generations as the guy who yelled foul, but let this writing stand as a testament to the squashing of information that would literally cure the most profitable of diseases if only the people would participate in their collective quandary.

We stand upon a threshold of immense possibilities in the realm of curing most modern disease, including cancers and degenerative disease states. But without an outcry and outpouring from the people who have suffered by this debacle, nothing will ever be done to halt what I consider to be the greatest man-made plagues of our history. And the rates of suffering and profits will continue to rise, as this information will stay within the medical associations and corporations without publicity.

We are victims of our own ignorance and willful consent and compliance to the tyranny and oppression of deadly pseudo-science.

Be sure to check out the “PrioNet” website for valuable info on prions: http://www.prionetcanada.ca/

.

–Clint Richardson (Realitybloger.wordpress.com)
–Wednesday, February 20, 2013

Xenotransplantation – Creating The Zombie Apocalypse


The following information is based solely on fact and sourced within.

This essay is an addendum to my documentary film, “Lethal Injection: The Story Of Vaccination“. It is of utmost importance that you read this entire article and spread it indefatigably.

What you are about to read may very well be the largest combined cover-up of the confederated government, ranching, meat-packing, medical, and pharmaceutical industry’s history – a collaborative effort to hide the true nature of what can only be called the human race’s modern plague of neurological and other degenerative diseases, from Alzheimer’s to AIDS.

This is not about the dead coming back to life. On the contrary, death is the only sweet release from this disease… a final cure that is always certain, and which never comes soon enough.

This is the real story of an apocalyptic peril that, as it turns out, very likely already lies dormant in us all.

This is not a zombie genre fiction, but is instead the real-life story of what are called “prions“.

The following essay affects anyone and everyone who may be reading this, without exception. This research is not an attempt to scare you or to promote science fiction. It is instead my personal attempt to save the world; to warn the entire planet of what “zombie” fans and fanatics could only before both dream about and dread, and in the end offer what I believe with all of my soul to potentially be the proverbial cure and end of prion-related diseases for ever.

But I digress… for most people – including many nurses and doctors – have never even heard of a prion, let alone considered them as the cause of such conditions that I now believe to be purposefully and falsely diagnosed as Alzheimer’s, Lou Gehrig’s Disease (Amyotrophic lateral sclerosis – ALS), Parkinson’s Disease, and many other debilitating conditions that most medical “professionals” will to this day admit – they do not know the cause of!

Dismiss this information at your own peril…

Or embrace it and fight for your life and your right to live it well!

–≈–
What Is A Zombie?
–≈–

Sorry folks, but you’ll have to come down to Earth for this presentation! Please place all pre-conceived notions securely in the overhead bins and place all tray-tables in their upright and locked positions. It’s time to get real…

For the purposes of this essay, the term “zombie” is defined by the World English Dictionary as:

1. a person who is or appears to be lifeless, apathetic, or totally lacking in independent judgment; automation

And by Dictionary.com as:

2. Informal. a. a person whose behavior or responses are wooden, listless, or seemingly rote; automaton. b. an eccentric or peculiar person.

And Wikipedia gives this alternative description:

The term (zombie) is often figuratively applied to describe a hypnotized person bereft of consciousness and self-awareness, yet ambulant and able to respond to surrounding stimuli.

With the following descriptions in mind, and the Hollywood death worship, gore, and fanfare safely tucked away, we can now safely proceed with what I feel may be some of the most important information you may read in your lifetime.

And anyone who knows of me, certainly knows that I don’t say something like this lightly…

–≈–
Cannibalism As Medicine
–≈–

The virtually unknown and under-discussed scientific and medical topic of what is called “xenotransplantation“, as well as human protein ingestion – including injection (vaccination) of other animals and human cells into the human body – is now a practice as prevalent as the consumption of aspirin. From flavor enhancers labeled as “natural ingredients” or “natural flavors” to oral and inject-able pharmaceutical drugs ranging from insulin to human growth hormone to anti-blood clotting drugs to seasonal vaccines, the human race has unsuspectingly been transformed into a species that consumes itself “for medicinal purposes“.

Be it consumed orally, injected (vaccinated) through the skin to bypass the body’s natural defenses, or purposefully “xeno”-transplanted via surgical procedure, the deadly zombie-creating prion we are about to expose is officially undetectable, ineradicable, untreatable, irreversibly fatal, and unless good people take immediate action and demand public exposure and immediate research, unstoppable!!!

There is a distinct difference between animal and human consumption, both in application and in function. But the dangers in both cases are equally deadly – as in always deadly, without exception, meaning 100% fatal! The reasons for this fact will become inescapably apparent and self-evident as we read on…

–≈–
What is Xenotransplantation?
–≈–

The FDA explains Xenotransplantation as:

Xenotransplantation is any procedure that involves the transplantation, implantation or infusion into a human recipient of either (a) live cells, tissues, or organs from a nonhuman animal source, or (b) human body fluids, cells, tissues or organs that have had ex vivo contact with live nonhuman animal cells, tissues or organs. The development of xenotransplantation is, in part, driven by the fact that the demand for human organs for clinical transplantation far exceeds the supply.

Currently ten patients die each day in the United States while on the waiting list to receive lifesaving vital organ transplants. Moreover, recent evidence has suggested that transplantation of cells and tissues may be therapeutic for certain diseases such as neurodegenerative disorders and diabetes, where, again human materials are not usually available.

Although the potential benefits are considerable, the use of xenotransplantation raises concerns regarding the potential infection of recipients with both recognized and unrecognized infectious agents and the possible subsequent transmission to their close contacts and into the general human population. Of public health concern is the potential for cross-species infection by retroviruses, which may be latent and lead to disease years after infection. Moreover, new infectious agents may not be readily identifiable with current techniques.

(Source: http://www.fda.gov/BiologicsBloodVaccines/Xenotransplantation/default.htm)

–≈–

The FDA also has this information page regarding xenotransplantation:

Information and recommendations for Physicians Involved in the Co-Culture of Human Embryos with Non-Human Animal Cells

The U.S. Food and Drug Administration (FDA) wants you to know that the co-culture of human embryos with nonhuman animal cells raises health concerns for the recipients of such embryos, the offspring resulting from such embryos, and the general public. The use of nonhuman animal cells, tissues or organs in the treatment of human medical conditions is called xenotransplantation…

Co-culture of human embryos with nonhuman animal cells fits the second part of this definition (xenotransplantation, defined above). During co-culturing, human embryos and nonhuman animal cells are maintained together outside the body, in ex vivo contact. Thus, the woman into whom the co-cultured embryos are transferred is a recipient of a xenotransplantation product.

A serious concern regarding the clinical use of xenotransplantation is the potential for the transmission of infectious disease from nonhuman animals to humans. Scientists believe that the potential for transmission of an infectious disease from the animal source to a human is of concern either when live nonhuman animal cells, tissues or organs are implanted directly into a human, or when human cells are exposed to live nonhuman animal cells by ex vivo contact. Experience with organ allotransplantation has shown that diseases such as human immunodeficiency virus (HIV) infection, Creutzfeldt-Jakob disease, hepatitis B virus infection and hepatitis C virus infection can be transmitted from the human donor to the recipient. Similarly, xenotransplantation poses concerns for infection with recognized, or as yet unrecognized, infectious agents from nonhuman animals. These concerns may extend beyond the recipient to the general public because of the potential for subsequent transmission of an infectious agent to the recipient’s contacts and to the general population. Infections originating from animals that have been known to infect and be transmitted from human to human include, for example, HIV and swine influenza. Many viruses exhibit latency, so that the lack of symptoms at the time of the embryo transfer, or in the short term, does not alleviate all concern.

The U.S. Public Health Service has published guidelines on infectious disease issues in xenotransplantation.  These guidelines, as well as FDA guidance documents, can be found at the website http://www.fda.gov/cber/xap/xap.htm, or obtained from FDA. They recommend, for example, that:

  • You should inform recipients of xenotransplantation products that they and their intimate contacts should defer from donation of blood and other tissues.
  • You should inform patients that they have been treated with a xenotransplantation product and of the risks involved.
  • You should archive patient samples, such as blood, to allow future monitoring for potential infections.
  • You should follow patients for their lifetimes and counsel them to be alert to any unusual symptoms.
  • You should archive samples of the xenotransplantation product. In this case, the nonhuman animal cells used for the co-culture process should be archived.

We would be happy to discuss any questions you might have about these recommendations. The nature and level of our concerns may vary depending on the species of nonhuman animal used in the co-culture technique and the source of the culture cells. We plan to have further public discussion of this topic with an appropriate federal advisory committee. At this time, FDA plans to enforce investigation new drug application (IND) requirements for investigations involving further production of embryos co-cultured with live nonhuman animal cells. However, currently it is not our intent to take enforcement action based on the transfer of already existing embryos created by co-culture with live nonhuman animal cells.

(Source: http://www.fda.gov/BiologicsBloodVaccines/Xenotransplantation/ucm136532.htm)

–≈–

Has anybody considered that the growing of human body parts on animals is a gateway for new and more dangerous mutation of prion development and transmission? After all, the animal circulatory system will be directly fused during growth, and transferred during xenotransplantation into or onto the human host.

–≈–

In my film, “Lethal Injection: The Story Of Vaccination”, I covered in great detail the disturbing fact that cloned DNA from human aborted fetuses and other animal proteins are used in the production of vaccines and in the growth of cell substrates for vaccine cell growth (free to view on YouTube, –> here). Some viewers mistook this information as an attempt to promote a “pro-life” political standpoint, indeed missing the very real point that we are literally being forced into eating, injecting, and applying as cosmetics ourselves (other humans) with our unborn aborted children in the name of “medical science” and “beauty”. Thus, to say that “Soylent Green is people” is truly an understatement in modern medicine, food, and cosmetics. Indeed, everything is a choice.

Before we proceed, we must understand exactly what it is that gets directly injected into the human body via the vaccination process. Here is an incomplete list of human and non-human animal proteins and ingredients that are used in the vaccine and other inject-able drug markets. Note that these are listed as “ingredients” of different vaccines:

-residual MRC5 proteins – human diploid cells from aborted fetal tissueincluding DNA and proteins
-human albumin, albumin from human blood
-sucrose human albumin
-chicken embryo
-chick embryonic fluid
-chicken protein
-monkey kidney cells
-phenol red rhesus monkey fetal lung cells
-rhesus monkey fetal diploid cells
-rhesus monkey rotavirus
-3 rhesus-human reassortant live viruses
-guinea pig embryo cells
-mouse serum proteins
-gelatin (collogen – animal proteins, especially flesh and connective tissues. Aborted human fetal material also used in cosmetics)
-lactose (animal milk derived – also added to pills as a cheap “filler”)
-vesicle fluid from calf skins
-calf serum
-bovine fetal serum
-bovine extract, US sourced
-bovine gelatin and serum “from source countries known to be free of bovine spongioform encephalopathy” (Note: this is an impossible claim to prove.)
-Mycobacterium bovis
-polysaccharide from Salmonella typhi Ty2 strain
-recombinant protein (OspA) from the outer surface of the spirochete Borrelia burgdorferi kanamycin – a tick-borne pathogen that causes Lyme disease

(Older) List of vaccines with aborted fetal tissue (cloned):

(Link: http://www.silentvoices.org/vaccinechart.html)

These human and other animal proteins are all but impossible to filter out of the final inject-able product (vaccines), and are being introduced at an alarming rate into the human and animal population of the world with the advent of the popularity and profit-potential of vaccination on a world (United Nations) scale. While the moral implications of this barbarous and unethical practice are more than obvious and should seemingly be enough to defeat the ego when choosing whether or not to vaccinate ones self or ones children, there is a much more sinister and unknown danger in this practice that needs a bit of light shown upon it…

Introducing, the prion

–≈–
The Indefatigable Prion
–≈–

pri·on

noun \ˈprē-ˌän\ (Medical Dictionary)

Any of various infectious proteins that are abnormal forms of normal cellular proteins, that proliferate by inducing the normal protein to convert to the abnormal form, and that in mammals include pathogenic forms which arise sporadically, as a result of genetic mutation, or by transmission (as by ingestion of infected tissue) and which upon accumulation in the brain cause a prion disease.

prion

noun (Concise Encyclopedia)

Disease-causing agent, discovered by Stanley Prusiner, responsible for various fatal neurodegenerative diseases called transmissible spongiform encephalopathies. An abnormal form of a normally harmless protein found in mammals and birds, the disease-causing prion can enter the brain through infection, or it can arise from a mutation in the gene that encodes the protein. Once present in the brain it causes normal proteins to refold into the abnormal shape. As prion proteins multiply, they accumulate within nerve cells, destroying them and eventually causing brain tissue to become riddled with holes. Diseases caused by prions include Creutzfeldt-Jakob disease, mad cow disease, and scrapie. Prions are unlike all other known disease-causing organisms in that they appear to lack nucleic acid (DNA or RNA).

–≈–
Deadly Feasts
–≈–

I am seldom one to promote a book or movie, and yet I feel compelled to share this one with you – a 15 year old warning that has gone unheeded by the corporate and government profit machine, ignored by the media and medical community and as a result the conditioned and ignorant people, and brushed aside out of public view in an effort led by the WHO and the U.S. FDA and CDC.

Deadly Feasts: Tracking The Secrets Of A Terrifying New Plague” was written and researched by Pulitzer prize winning author and researcher Richard Rhodes, published in 1997. I recomend that this book be on your “to read” list, if only to understand what is potentially the worst continuing outbreak of avoidable, man-induced disease in the history of the world.

If you’ve ever been vaccinated or eaten any type of meat or dairy products, you should really pay attention here…

The Introduction to the book, entitled “To The Reader”, states:

“The threat of Ebola virus has haunted our nightmares since Richard Preston published his “terrifying true story” The Hot Zone in 1994. Ebola hides in the African rain forest, but a deadlier disease than Ebola has begun killing young people in Britain and France. Ebola is a terrorist: it sickens people quickly and spares at least one out of ten. The new disease is a stealth agent: it incubates silently for years and kills every last victim it infects. Ebola is a sickness of fever and bleeding, no worse than cholera, a quick if not a merciful death. The new disease is an atrocity of destruction – a headache, a stumble, and then hallucination, palsy, seizure and coma drawn out horribly for months. Victims’ brains go spongy; their minds dim; they lose the ability to walk, to talk, to see, to swallow; they die slowly, drowning in pneumonia, or they starve to death.

Ebola can survive outside of the body for a few days at best. Sunlight kills it. Ultraviolet light kills it. The new disease agent refuses to die. Assault with pressurized, superheated steam in the autoclaves that hospitals use to sterilize instruments for surgery barely slows it. It remains deadly after hours of intense bombardment with hard radiation, months of soaking in formaldehyde, years of burial, decades of freezing. It survives even the fiery furnace of a seven-hundred-degree oven.

How Ebola spreads is still uncertain, but scientists know it’s a virus. In time, a vaccine will protect us from its threat (author’s note: I disagree with this vaccine statement, as is self evident in my film and research). The new disease turns up no virus in victims’ brains. It creeps past the barriers of species and immunity. Evidence accumulates that it’s a bad seed, a mistake of protein, a misshapen crystal that forces the brain to poison itself. If so, it’s a new kind of disease agent that can never be eradicated.

How the new disease spreads is known: it spreads in the cannibalism of animals by animals, it spreads in the industrial cannibalism of animal remains fed to animals, it spreads by the eating of beef…”

Deadly Feasts then discusses the cannibalistic rituals of the Fore tribal people who lived in New Guinea. More specifically, the “revenge” of the female members of the tribes who consumed (ate) the parts of their husbands and menfolk together with vigor and ritualistic joy – the result of the less than loving matrimonial customs of the Fore people. Each internal organ was extracted with care and precision, and then served with various plant sides, sweet potatoes, and other forest condiments.

A tradition that was started by the women of the tribes in the 1930’s, this cannibalism resulted in mass outbreaks of disease locally called “Kuru”. Kuru was thought by the women of the Fore tribes to be nothing short of witchcraft by the menfolk, whom were thought of as “sorcerers” in many Fore tribes. The native word “Kuru” literally meant shivering- in cold or from fear. And once the sorcery of Kuru took hold, the “bewitchment” would, without exception, lead to death.

Kuru’s symptoms are described as if taken straight of Night Of The Living Dead:

The symptoms of Kuru are broken down into three specific stages. The first, ambulant stage, exhibits unsteady stance and gait, decreased muscle control, tremors, deterioration of speech and dysarthria (slurred speech). In the second stage, sedentary stage, the patient is incapable of walking without support, suffers ataxia (loss of muscle coordination) and severe tremors. Furthermore, the victim is emotionally unstable, depressed, yet having uncontrolled sporadic laughter. Interestingly, the tendon reflexes are still normal at this point. In the final, terminal stage, the patient is incapable of sitting without support, suffers severe ataxia (no muscle coordination), is unable to speak, is incontinent (unable to restrain natural discharges/evacuations of urine or feces), has dysphagia (difficulty swallowing), is unresponsive to their surroundings, and acquires ulcerations (sores with pus and necrosis). An infected person usually dies within 3 months to 2 years after the first symptoms, often because of pneumonia or pressure sores infection.

(Source: http://anthropology.ua.edu/bindon/ant570/Papers/McGrath/McGrath.htm)

Please note that the symptom called “necrosis” is defined as:

Necrosis: The death of living cells or tissues. Necrosis can be due, for example, to ischemia (lack of blood flow). From the Greek “nekros” meaning dead body.

Now, despite the fact that the hairs on your back of your neck may be standing up in fibrous nervousness about now, we haven’t yet begun to uncover the zombification of the world yet.

Deadly Feasts” begins its story in Papa New Guinea with the true story of cannibalism and its cost:

“Men lived separately from the women and children, following their wives into their gardens to copulate, sharing the big men’s lodge with the older boys. Men believed contact with women weakened them. They resented the fecundity of women. Men seldom ate the dead and then only the red meat, surreptitiously…”

“The women at their mortuary feast butchered and cooked down in the garden, but they ate in private, carrying the steaming bamboo tubes back to their separate woman’s houses, sharing the feast with their children…”

“They ate every part of the body, even the bones, which they charred at the open fires to soften them before crumbling them into the (bamboo shoot) tubes. The dead woman’s brother’s wife received the vulva as her special portion. If the dead had been a man, his penis, a delicacy, would have gone to his wife…”

“Eating the dead was not a primordial Fore custom. it had started within the lifetime of the oldest grandmothers among them, at the turn of the century (1900) or not long before…”

“Women bewitched with Kuru staggered to walk, walked with a stick and then could no longer walk at all. Before losing the ability to swallow they got fat and the flesh of those who died early of pneumonia was rich meat…”

“Nevertheless, the damage Kuru caused to the brain was similar to the damage caused by the rare condition known as Creutzfeldt-Jakob disease (CJD).

Towards the end of the book, Mr. Rhodes discusses the phenomenon and likely scientific folly of xenotransplantation in an interview with Dr. David White, the cofounder and medical director of a company called Imutran:

“Pioneer xenotransplantation has already begun: in 1984 in the U.S., a baboon heart kept Baby Fae alive for twenty days: a baboon liver was transplanted in 1994; San Francisco AIDS patient Jeff Getty received a baboon-marrow graft in 1995 to shore up his immune system. Advanced biotechnology that may make xenotransplantation routine is under development in the United States and in Britain. Lines of transgenic pigs are being bred for use initially for hearty transplants. Pig blood types are more like human types than those of other animals, but a strong immune response known as hyperacute rejection normally destroys pig tissue grafted into primates in a matter of hours.

I investigated Imutran, a company based in Cambridge, England, that leads the world in xenotransplantation technology, and learned that it has cloned human genes that defeat hyperacute rejection and inserted them into pig embryos.  Imultran has bred hundreds of pigs carrying these human genes. Rejection of transgenic pig hearts still has to be controlled with drugs, just as rejection of transplanted human hearts has to be controlled with drugs. In 1995, Imutran demonstrated that even without such immunosuppressive drugs, monkeys implanted with its transgenic pig hearts survived for five days – well past the time when hyperacute rejection would have destroyed an ordinary pig-heart implant. Implanted monkeys treated with immunosuppressive drugs survived up to sixty days. That achievement led Dr. David White, Imutran’s cofounder and medical director, to predict routine pig-heart transplants in humans before the turn of the century. “The big debate now,” White told the media, “is, do we currently have the skills to keep the hearts functioning in people for a long time; and the only way to answer that question is to put them into people and find out.”

I interviewed White at Imutran’s headquarters in Cambridge in April 1996. He was enthusiastic about his work. “Right from the beginning,” he explained, “our approach was to ask how can we genetically engineer the pig, not how can we treat the patient. From there, we realized that a possible approach would be to put these human regulators into a pig. And the smartest thing I ever did was to take out a patent on the process. Because that’s what pays all the bills.” Although I didn’t know it at the time, White had just sold Imutran to Sandoz Pharma, Ltd., a major drug company.

I will put my career on the line,” he told me, “and say that hyperacute rejection as we know it is dead, gone, finished. You take an organ from one of our pigs and transplant it into a primate and it will go for days without any treatment at all, routinely. We’ve done kidneys, islets [i.e. pancreatic tissue which secretes insulin, to correct diabetes], hearts – I don’t even know the number now, sixty or seventy. Now all we have to do is immunosuppress the monkey in order to achieve long-term survival. We did our first baboon transplant a couple of weeks ago, and on the same day that we successfully transplanted a baboon with a pig heart, one of our patients died waiting for a human heart.”

I came to the point of my visit: “Are you concerned with BSE?”

***Note that BSE stands for bovine spongiform encephalopathy (i.e. Mad Cow Disease).

“Fortunately,” White countered, “pigs don’t get BSE.”

I think there’s evidence they do.”

If you take contaminated brain from a mad cow and inject (vaccinate) the neural tissue directly into the brain of the pig it will get spongiform encephalopathy. But they’ve been feeding infected brain to pigs for five years no and none of the pigs has the disease.”

That was true.

“You have to appreciate that BSE is not an infection. It’s a very curious toxicity really.”

I told Dr. White I’d looked into it.

“Well,” he responded, “then perhaps you can tell me how the hell the bloody thing works. I don’t understand it.”

I tried to explain abnormal protein crystallization (caused by prions).

He listened. “Yes, that could work,” he said finally.

“Your pigs are isolated and presumably not fed meat-and-bone meal,” I prompted him.

“Oh no,” he confirmed. “Disease transmission is an area of considerable concern.” He left his desk and returned with a proprietary study as thick as a telephone book. “We put together a group of the world’s leading experts on pig disease and on the diseases that transplant patients get.” He opened the book. “I’ll just read you some of the headings. ‘Microorganisms Known To Be Pathogenic.’ ‘Microorganisms Pathogenic In Humans.’ ‘Microorganisms Known To Be Pathogenic In Pigs Bt Not Pathogenic In Humans.’ Microorganisms Not Known To Be Pathogenic But Similar To Microorganisms Pathogenic.” And so on. Porcine RNA viruses, porcine DNA viruses, exotic porcine RNA viruses, exotic porcine DNA viruses, a special section on the human measles viruses. Porcine bacteria – the gram negatives, the gram positives – and it goes on and on. A basic risk assessment of them all. A list of pathogens of most concern.” He closed the book. “So when you’ve done all that, you’re left with one problem, which is the retroviruses. We’re currently doing research on our primates to answer the question, will these pig retroviruses jump across the species barrier and recombine with human retroviruses? We haven’t finished, but we think the probability is extremely remote.”

***Author’s note: In my film Lethal Injection: The Story of Vaccination, we see various patents for using Porcine Zona Pellucida (pig ovaries) as inject-able vaccination birth control methods, for use in both animals and humans. The foreign ovary proteins cause an “immune response” in the vaccinated patient and the body’s natural defenses develop “antibodies” inadvertently for the body’s own (human) reproductive functions, while attempting to fight the foreign reproductive ovary or other proteins. This is but one example of xenotransplantation designed to control population growth in animals and humans…

“The pigs wont go to the hospital, White continued, The patient will come somewhere near the pigs. “That is,” he explained, “you will have a few dedicated specialist centers which do xenotransplantation. Those centers will have a sterile pig-production unit nearby. The patients will come there. It is ludicrous that you have to wait for fit, healthy people to die so that you can treat sick people. With a pig, you can come in and the physician will say, ‘I think you’re going to need a heart transplant. ‘You wouldn’t be at the end of the road. Maybe three months, maybe six months away. And we would modify your immune system so that you won’t reject pigs.

It occurred to me that we might be talking about more than hearts. “Are you planning to transplant other organs and tissues from the pig?”

“The heart, the lungs – all those former smokers, the market is huge – the kidney. Possibly the intestine. The substantia nigra is an area of great interest.”

I said: “What?”

“Bit of the brain,” White said. “For the treatment of Parkinson’s disease.”

I knew what substantia nigra was, I just couldn’t believe that a brilliant and innovative physician-businessman who had admitted he didn’t understand what causes spongiform encephalopathy (who does?) was planning to implant pig brain directly into the brains of humans.

In July of 1996, the Committee on Xenograft Transplantation of the U.S. Institute of Medicine, part of the National Academy of Sciences, endorsed xenografting on the grounds that the potential benefits outweigh the risks. “When the science base for specific types of xenotransplants is judged sufficient,” the committee concluded, “and the appropriate safeguards are in place, well-chosen human xenotransplantation trials using animal cells, tissues and organs would be justified and should proceed.” The committee cited “ample evidence,” however, that infectious agents could be transmitted from animals to humans, which indicated a danger “unequivocally greater than zero” that xenotransplantation could transfer new and deadly viruses across the species barrier. And it specifically mentioned transmissible spongiform encephalopathy (Mad Cow Disease).

Most importantly, in analyzing the age-specific incidence of both bovine BSE and sporadic human CJD, Dr. Richard Kimberlin states:

“The shape of the age-specific incidence curve… implies that infection with a common strain [of CJD] occurs in childhood or adolescence, and that the median incubation period is 40 to 50 years.” German researcher Dr. Heino Diringer similarly defends and infectious cause: “It seems more than likely that… the sporadic cases of CJD always originate from direct or indirect transmission from animals to man.” In 1996, Deringer reported finding small virus-like particles in scrapie hamster brain…”

“Carleton Gajduserown freeze-dried a sample of scrapie brain, sealed the sample into a glass ampule and baked it in an oven for one hour at 360 degrees Celsius (nearly 700 degrees Fahrenheit). Reconstituted, the sample still transmitted scrapie to a hamster.”

At the end of his book, Richard Rhodes leaves us with these words (note: there are no spoilers here, just facts):

“I remember something he (Nobel-laureate virologist D. Carleton Gajdusek) asked me at our first meeting, late in 1995, before the British reported out the beginnings of what may be their new Black Death.

“You know the bone meal that people use on their roses?” Gajdusek asked me then. “It’s made from downer cattle. Ground extremely fine. The instructions on the bag warn you not to open it in a closed room. Gets up your nose.” The Nobel-laureate virologist who knows more than anyone else in the world about transmissible spongiform encephalopathy looked at me meaningfully. “Do you use bone meal in your roses?”

I told him I did.

He nodded. “I wouldn’t if I were you.”

The final blurb of Deadly Feasts is an article from the London Daily Telegraph, dated April 4, 1996:

“Gardeners have been reminded by the Royal Horticultural Society to wear gloves and a dust-excluding mask to avoid any risk of BSE when applying a spring dressing of blood and bonemeal to roses and shrubs.

Demand for beef is recovering steadily. At London’s Smithfield wholesale market, the trade in better quality cuts of British beef has recovered from zero a week ago to just over half the normal .

–≈–
Creutzfeldt-Jakob Disease (CJD)
–≈–

Before we read the following report from the Mayo Clinic on CJD, and as we will see once again this clinic reiterating the fact that very few cases of CJD have been reported throughout the world (as has the FDA, CDC, WHO, etc…), we must begin to consider that on an international scale, “prion diseases” are being covered up – quite simply by means of diagnosing them as other diseases such as “Alzheimer’s Disease” – of which these same “organizations” claim not to know the origins or causes of.

In fact, on page 133 of “Deadly Feasts”, Dr. Carlton Gajdusek and Joe Gibbs are quoted as such:

“Gajdusek and Gibbs prepared a technical note for the Journal of Neurosurgery. They reviewed CJD transmissibility. They advised that it was reasonable to assume that the CJD agent was at least as resistant as the scrapie agent to heat, formaldehyde and ultra-violate light. “In particular,” the wrote, “one must assume the agent is not killed by boiling.” They pointed out that physicians often misdiagnosed CJD as Alzheimer’s disease, as the form of cerebral atrophy known as Pick’s disease, or as many other conditions including brain tumors and strokes. They recommended sterilizing instruments used on such patients in an autoclave – a machine used in hospitals that kills even hardy microorganisms with hot steam under pressure – for at least thirty minutes, twice the standard autoclaving time. They recommended treating all organs as infectious, even those fixed in formaldehyde. They had found only one chemical, chlorine bleach, that reliably killed the scrapie agent and they recommended using it to decontaminate floors and other surfaces where tissue might have fallen.

But before this technical note was published… from Deadly Feasts:

“Diseases doctors unintentionally cause are called iatrogenic, Greek for “physician-born”. The first known human-to-human transmission of spongiform encephalopathy outside the Fore was iatrogenic (by Dr. Arthor DeVoe, eye surgeon and chairman of the department of ophthalmology at the College of Physicians and Surgeons of Columbia University in New York)…

A donor became available, a middle aged man with a two-month history of memory loss and involuntary tremors who died of pneumonia. Down in the hospital morgue, an ophthalmologist harvested one of the man’s eyeballs, immersed it in sterile saline in a small jar and delivered it to surgery…

Holding the donor cornea like a contact lens, DeVoe lowered it over the hole in his patient’s eye. It fit perfectly. Meticulously, across the next hour, DeVoe joined the edges of the cornea and the woman’s eyeball together with stitches of fine nylon thread, burying the knots in the wound…

The eye healed. The woman could see again clearly through the dead man’s cornea and the operation seemed a success. But the optic nerve connects the eye directly to the brain, providing a channel for infection, and the brain of the man who died of pneumonia, who had not been autopsied until after his cornea was harvested, showed the characteristic damage of Creutzfeldt-Jakob Disease. A year and a half after her operation, the woman began feeling nauseated, had difficulty swallowing, came to drool and stumble and jerk, went spastic, went mute, gradually introverted into vegetable oblivion. Two years beyond her surgery, emaciated and bedsore, she mercifully died. On autopsy her brain looked like the brain of the man who had donated his cornea – like a sponge. If Arthor DeVoe had only known before the transplant operation. A sickness had oozed from the cornea he’d implanted and eaten holes in his patient’s brain.”

–≈–

Now, when we look at the description for “Alzheimer’s Disease”, which according to the preeminent Spongiform Encephalitis expert is actually a prion disease such as CJV, we see virtually the same symptoms listed.

Alzheimer’s Disease is the most common form of a whole class of diseases generically called “dementia”. There is no stated or listed cure for Alzheimer’s Disease, which worsens as it progresses, and it eventually leads to death without exception from one of the direct or indirect “symptoms”.

Like AIDS, Alzheimer’s is not a disease in and of itself within the medical books, but rather a description for the symptoms of a particular disease state that is not understood – and this is the case with thousands of disease states and their symptoms.

The NINCDS-ADRDA Alzheimer’s Criteria specify eight cognitive domains that may be impaired in AD: memory, language, perceptual skills, attention, constructive abilities, orientation, problem solving and functional abilities.)

Sound familiar?

Now let us consider the number of cases of Alzheimer’s worldwide, and the predictions for humanity’s future.

In 2006 the worldwide prevalence of Alzheimer’s disease was 26.6 million. By 2050, prevalence will quadruple by which time 1 in 85 persons worldwide will be living with the disease. We estimate about 43% of prevalent cases need a high level of care equivalent to that of a nursing home. If interventions could delay both disease onset and progression by a modest 1 year, there would be nearly 9.2 million fewer cases of disease in 2050 with nearly all the decline attributable to decreases in persons needing high level of care.

Interpretation: We face a looming global epidemic of Alzheimer’s disease as the world’s population ages. Modest advances in therapeutic and preventive strategies that lead to even small delays in Alzheimer’s onset and progression can significantly reduce the global burden of the disease.

(Source: “FORECASTING THE GLOBAL BURDEN OF ALZHEIMER’S DISEASE” – Johns Hopkins University, Dept. of Biostatistics Working Papers, Year 2007, Paper 130)

Suddenly, by taking into consideration only the Alheimer’s diagnosis’ worldwide as being an actual “prion disease”, the 1 in one million figure listed as supposedly confirmed worldwide cases of CJV becomes instead a true epidemic – the true black plague of humanity – of prion disease.

And Alzheimer’s is just one of the listed dementia diseases.

Dementia includes many disease descriptions, including the symptoms of this partial list:

Huntington’s disease
Frontotemporal lobar degeneration
Alzheimer’s disease

SCA17 (dominant inheritance)
adrenoleukodystrophy (X-linked)
Gaucher’s disease
metachromatic leukodystrophy
Niemann-Pick disease type C
pantothenate kinase-associated neurodegeneration
Tay-Sachs disease
Wilson’s disease
cryptococcal meningitis

HIV
Lyme disease
progressive multifocal leukoencephalopathy
subacute sclerosing panencephalitis
syphilis
Whipple’s disease
dementia with Lewy bodies
corticobasal degeneration
progressive supranuclear palsy
encephalopathy
viral encephalitis
limbic encephalitis
Hashimoto’s encephalopathy
cerebral vasculitis
lymphoma
glioma
vascular dementia

antiphospholipid syndrome
CADASIL
MELAS
homocystinuria
moyamoya
Binswanger’s disease
Behçet’s disease

multiple sclerosis
sarcoidosis
Sjögren’s syndrome
systemic lupus erythematosus
Alexander disease

Canavan disease

Cerebrotendinous xanthomatosis

Dentatorubral-pallidoluysian atrophy

Fatal familial insomnia

Fragile X-associated tremor/ataxia syndrome

Glutaric aciduria type 1

Krabbe’s disease

Maple syrup urine disease

Niemann Pick disease
type C
Neuronal ceroid lipofuscinosis

Neuroacanthocytosis

Organic acidemias

Pelizaeus-Merzbacher disease

Urea cycle disorder
Sanfilippo syndrome type B
Spinocerebellar ataxia
type 2

Now what happens to all of these classifications/descriptions of disease states and their symptoms when we place them all into the same category of disease – prion disease? What indeed…? What if one thing is responsible for all of the above descriptions of the same disease?

The Mayo Clinic published this report on October 23, 2012:

–Begin report–

.

Creutzfeldt-Jakob Disease

By Mayo Clinic staff

Definition

Creutzfeldt-Jakob (KROITS-felt YAH-kobe) disease is a degenerative brain disorder that leads to dementia and, ultimately, death. Symptoms of Creutzfeldt-Jakob disease (CJD) sometimes resemble those of other dementia-like brain disorders, such as Alzheimer’s, but Creutzfeldt-Jakob disease usually progresses much more rapidly.

Creutzfeldt-Jakob disease captured public attention in the 1990s when some people in the United Kingdom developed a form of the disease — variant CJD (vCJD) — after eating meat from diseased cattle. However, “classic” Creutzfeldt-Jakob disease has not been linked to contaminated beef.

Although serious, CJD is rare, and vCJD is the least common form. Worldwide, there is an estimated one case of Creutzfeldt-Jakob disease diagnosed per million people each year, most commonly in older adults.

Symptoms

Creutzfeldt-Jakob disease is marked by rapid mental deterioration, usually within a few months. Initial signs and symptoms of CJD typically include:

  • Personality changes
  • Anxiety
  • Depression
  • Memory loss
  • Impaired thinking
  • Blurred vision
  • Insomnia
  • Difficulty speaking
  • Difficulty swallowing
  • Sudden, jerky movements

As the disease progresses, mental symptoms worsen. Most people eventually lapse into a coma. Heart failure, respiratory failure, pneumonia or other infections are generally the cause of death. The disease usually runs its course in about seven months, although a few people may live up to one or two years after diagnosis.

In people with the rarer vCJD, psychiatric symptoms may be more prominent in the beginning, with dementia — the loss of the ability to think, reason and remember — developing later in the course of the illness. In addition, this variant affects people at a younger age than classic CJD does, and appears to have a slightly longer duration — 12 to 14 months.

***Author’s note: Does this list of “symptoms” sound like a zombie to you? Sudden, Jerky movements with lack of reason or ability to think; an anxious monster unrecognizable as your mother, father, sibling, or friend due to “personality changes”, who when questioned can only utter guttural sounds due to “difficulty speaking and swallowing”?

Causes

Creutzfeldt-Jakob disease and its variants belong to a broad group of human and animal diseases known as transmissible spongiform encephalopathies (TSEs). The name derives from the spongy holes, visible under a microscope, that develop in affected brain tissue.

The cause of Creutzfeldt-Jakob disease and other TSEs appears to be abnormal versions of a kind of protein called a prion. Normally, these proteins are harmless, but when they’re misshapen they become infectious and can wreak havoc on normal biological processes.

How CJD is transmitted

The risk of CJD is low. The disease can’t be transmitted through coughing or sneezing, touching, or sexual contact. The three ways it develops are:

  • Sporadically. Most people with classic CJD develop the disease for no apparent reason. CJD that occurs without explanation is termed spontaneous CJD or sporadic CJD and accounts for the majority of cases.
  • By inheritance. In the United States, about 5 to 10 percent of people with CJD have a family history of the disease or test positive for a genetic mutation associated with CJD. This type is referred to as familial CJD.
  • By contamination. A small number of people have developed CJD after being exposed to infected human tissue during a medical procedure, such as a cornea or skin transplant. Also, because standard sterilization methods do not destroy abnormal prions, a few people have developed CJD after undergoing brain surgery with contaminated instruments. Cases of CJD related to medical procedures are referred to as iatrogenic CJD. Variant CJD is linked primarily to eating beef infected with bovine spongiform encephalopathy (BSE), the medical term for mad cow disease.

Risk factors

Most cases of Creutzfeldt-Jakob disease occur for unknown reasons, and no risk factors can be identified. However, a few factors seem to be associated with different kinds of CJD.

  • Age. Sporadic CJD tends to develop later in life, usually around the age of 60. Onset of familial CJD occurs only slightly earlier. On the other hand, vCJD has affected people at a much younger age, usually in their late 20s.
  • Genetics. People with familial CJD have a genetic mutation that causes the disease. The disease is inherited in an autosomal dominant fashion, which means you need to inherit only one copy of the mutated gene, from either parent, to develop the disease. If you have the mutation, the chance of passing it on to your children is 50 percent. Genetic analysis in people with iatrogenic and variant CJD suggest that inheriting identical copies of certain variants of the prion gene may predispose a person to developing CJD if exposed to contaminated tissue.
  • Exposure to contaminated tissue. People who’ve received human growth hormone derived from human pituitary glands or who’ve had dura mater grafts may be at risk of iatrogenic CJD. The risk of contracting vCJD from eating contaminated beef is difficult to determine. In general, if countries are effectively implementing public health measures, the risk is virtually nonexistent.

***Author’s note: For anyone that is familiar with FDA standards and the meat packing and dairy industries, as well as the use of beef bone meal and other beef products to feed cattle (cow cannibalism) along with the use of inject-able bovine growth hormone (cow to cow vaccination) as a standard of practice by factory farms, and of course we mustn’t ignore the abhorrent health conditions of these beasts while kept in piles of their own excrement and infectious dung, this last sentence is no reassurance with regards to “public health measures” and the risk being “virtually nonexistent” from the FDA, especially with food now imported from China and other developing countries.

Complications

As with other causes of dementia, Creutzfeldt-Jakob disease profoundly affects the brain as well as the body, although CJD and its variants usually progress much more rapidly. People with CJD usually withdraw from friends and family and eventually lose the ability to recognize or relate to them in any meaningful way. They also lose the ability to care for themselves, and many eventually slip into a coma. The disease ultimately is fatal.

Physical complications, all of which may become life-threatening, include:

  • Infection
  • Heart failure
  • Respiratory failure

Tests and diagnosis

Only a brain biopsy or an examination of brain tissue after death (autopsy) can confirm the presence of Creutzfeldt-Jakob disease. But doctors often can make an accurate diagnosis based on your medical and personal history, a neurological exam, and certain diagnostic tests.

The exam is likely to reveal such characteristic symptoms as muscle twitching and spasms, abnormal reflexes, and coordination problems. People with CJD also may have areas of blindness and changes in visual-spatial perception.

In addition, doctors commonly use these tests to help detect CJD:

  • Electroencephalogram (EEG). Using electrodes placed on your scalp, this test measures your brain’s electrical activity. People with CJD and vCJD show a characteristically abnormal (brain) pattern.
  • Magnetic resonance imaging (MRI). This technique uses radio waves and a magnetic field to create cross-sectional images of your head and body. It’s especially useful in diagnosing brain disorders because of its high-resolution images of the brain’s white matter and gray matter.
  • Spinal fluid tests. Cerebral spinal fluid surrounds and cushions your brain and spinal cord. In a test called a lumbar puncture — popularly known as a spinal tap — doctors use a needle to withdraw a small amount of this fluid for testing. The presence of a particular protein in spinal fluid is often an indication of CJD or vCJD.

Treatments and drugs

No effective treatment exists for Creutzfeldt-Jakob disease or any of its variants. A number of drugs have been tested — including steroids, antibiotics and antiviral agents — and have not shown benefits. For that reason, doctors focus on alleviating pain and other symptoms and on making people with these diseases as comfortable as possible.

Prevention

There is no known way to prevent sporadic CJD. If you have a family history of neurological disease, you may benefit from talking with a genetics counselor, who can help you sort through the risks associated with your particular situation.

Preventing iatrogenic CJD

Hospitals and other medical institutions follow explicit policies to prevent iatrogenic CJD. These measures have included:

  • Exclusive use of synthetic human growth hormone, rather than the kind derived from human pituitary glands
  • Destruction of surgical instruments used on the brain or nervous tissue of someone with known or suspected CJD
  • Single-use kits for spinal taps (lumbar punctures)

To help ensure the safety of the blood supply, people with a risk of exposure to CJD or vCJD aren’t eligible to donate blood. This includes people who:

  • Have a biological relative who has been diagnosed with CJD
  • Have received a dura mater brain graft
  • Have received human growth hormone
  • Spent a total of at least three months in the United Kingdom from 1980 to 1996
  • Spent five years or more in France from 1980 to the present
  • Received a blood transfusion in the U.K. between 1980 and the present
  • Have injected bovine insulin at any time since 1980

***Author’s note: The American Diabetes Association lists the total number of official diabetics in the United States, as of January 2011, at 25.8 million people, or 8.3% of the population, with approximately 7 million of those listed as “undiagnosed”, and with 1.9 million new cases diagnosed in people aged 20 or older in 2010. It also lists an estimated 79 million more cases of “prediabetes”, the precursor symptoms to diabetes. This represents a whole lot of inject-able insulin shots.

Preventing vCJD

The risk of contracting vCJD in the United States remains extremely low. So far, only three cases have been reported in the U.S. According to the Centers for Disease Control and Prevention, strong evidence suggests that these cases were acquired abroad — two in the United Kingdom and one in Saudi Arabia.

In the United Kingdom, where the majority of vCJD cases have occurred, fewer than 200 cases have been reported. After its first appearance in 1995, CJD incidence peaked between 1999 and 2000, and has been declining since.

Regulating potential sources of vCJD

Most countries have taken steps to prevent BSE-infected tissue from entering the food supply, including tight restrictions on importation of cattle from countries where BSE is common; restrictions on animal feed; strict procedures for dealing with sick animals; surveillance and testing methods for tracking cattle health; and restrictions on which parts of cattle can be processed for food.

The risk of vCJD from the following sources is estimated to be extremely low:

  • Vaccines. Some parts of cows, including blood, enzymes and amino acids, are used to grow the bacteria and viruses needed to make certain vaccines. Not all vaccines are grown in cattle parts, however, and the Food and Drug Administration (FDA) recommends that companies producing such vaccines use cattle parts only from low-risk countries. These recommendations apply to cosmetics as well. The FDA keeps a listing on its website of companies that use cattle from countries that aren’t classified as low-risk.
  • Insulin. Insulin sold in the United States isn’t derived from cattle, but you’re allowed to import beef insulin from other countries if you follow specific guidelines. Because there’s no way to guarantee the safety of imported insulin, talk to your doctor about the best way to obtain insulin from sources outside the United States.

–End Mayo Clinic report–

–=–
“Woman with Mad Cow Disease donated her eyes”
–=–

The Associated Press reported in December of 1997 that:

LONDON – Scottish health authorities are investigating how tissue from the eyes of a woman who had suffered from the human form of `mad cow disease” was transplanted into three other people.

“We are aware there is a potential infection risk from tissue retrieved from a patient in Scotland,” a spokesman for the government Scottish Office said Saturday on customary condition of anonymity. “We do not know the full facts, but we are making urgent inquiries into how this could have occurred,” he said.

The 53-year-old woman suffered from lung cancer, but after she died a post-mortem examination showed she also had Creutzfeldt Jakob Disease. The brain-destroying disease is the human form of bovine spongiform encephalopathy, which afflicts cattle and is known as ‘mad cow disease’.”

No further details were given on the grounds of patient confidentiality. But the tabloid Sunday Mail said the post-mortem findings were not passed on to officials handling organ donor arrangements, and parts of her eyes, including the corneas, were transplanted into two men and a woman in her eighties.

Remember what the FDA stated from above?

“Currently ten patients die each day in the United States while on the waiting list to receive lifesaving vital organ transplants…”

Is it at all reasonable to assume that the FDA, Red Cross, AMA, ADA, or any other “association” out there can screen body parts for prions, including these CJD and other variants of “Transmissible spongiform encephalopathies (TSEs)”, also known as prion diseases, considering that they are undetectable without the victim being dead first?

The Red Cross blood donation guidelines website states:

Creutzfeldt-Jakob Disease (CJD)
If you ever received a corneal (eye) transplant, a dura mater (brain covering) transplant or human pituitary growth hormone, you are not eligible to donate. Those who have a close blood relative who had Creutzfeld-Jacob disease or who is in a family that has been told they have a genetic risk for Creutzfeld-Jacob disease are also not eligible to donate. Learn more about CJD.

Creutzfeldt-Jakob Disease, Variant (vCJD); “Mad Cow Disease”
See under Travel Outside of U.S. Learn more about vCJD and blood donation.

Interestingly, the supplied links to learn more information about CJD and vCJD do not link to anything, and a search on this Red Cross website for CJD turns up no search results.

(Source: http://chapters.redcross.org/ky/rivervalley/eligibility.htm)

–≈–
Prions And Cancer
–≈–

Prion related disease is not limited to brain functions, and is a virtually unknown field of research when it comes to the rest of the human body.

Science Daily reported in August of 2009:

Prion Protein Identified As Novel Early Pancreatic Cancer Biomarker

ScienceDaily (Aug. 18, 2009) — Mad cow disease is caused by the accumulation of an abnormal protein, the prion, in the brain of an affected patient. Outside of the brain, very little is known about prions. Case Western Reserve University School of Medicine, researchers have, for the first time, identified the prion as a biomarker for pancreatic cancer. Pancreatic cancer is one of the most deadly cancers in humans; the five year survival rate is less than 10 percent.

Chaoyang Li, Ph.D., Wei Xin, M.D., and professor of pathology, Man-Sun Sy, Ph.D., discovered the mechanism by which prions causes tumors to grow more aggressively. They published these findings in the September issue of the Journal of Clinical Investigation.

Unlike normal cells, in human pancreatic cancer cells the prion is incompletely processed and binds to a molecule inside the cell known as filamin A. Filamin A is an important regulator of the cell’s skeleton and its signaling machineries. The binding of the incompletely processed prion to filamin A disrupts the cell’s organization and signaling. As a result, the tumor cells grow more aggressively. On the other hand, when the prion level is reduced, the tumor cell loses its ability to grow in tissue culture and in animals. Most importantly, Dr. Li, et al. found that a subpopulation of patients had incompletely processed prion protein in their pancreatic cancer. This subgroup of patients had significantly shorter survival compared to patients whose tumors do not have prion.

According to Dr. Sy, “Currently there is no early diagnostic marker for pancreatic cancer. Detection of the incompletely processed prion may provide such a marker. Preventing the binding of prion to filamin A may open new avenues for therapeutic intervention of this deadly disease.”

Next, Drs. Li and Sy will look to determine if this type of prion protein expression is seen in other types of cancer.

There are other examples of truth seeping its way into the public’s eye…

Prions and cancer: A story unfolding

Prions, the causal agents of Mad Cow and other diseases, are very unique infectious particles. They are proteins in which the complex molecular three-dimensional folding process just went astray. For reasons not yet understood, the misfolding nature of prions is associated to their ability to sequester their normal counterparts and induce them to also adopt a misfolding conformation. The ever-growing crowd of misfolded proteins form the aggregates seen in diseases such as Parkinson’s and Alzheimer’s. Once misfolded, a protein can no longer exert its normal functions in the cell.

Now, a group led by Dr Jerson Lima Silva at the Federal University of Rio de Janeiro, Brazil, presents some new evidence that p53, a protein with the daunting task of suppressing tumor formation in the body, may show a typical prion-like behavior when mutated.

It has been known for some time that the buildup of p53 in the cell impairs the protein in preventing tumor growth. This has been observed in neuroblastoma, retinoblastoma, breast, and colon cancers. In a paper entitled “Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: Implications for cancer” and published in the Journal of Biological Chemistry, the group shows that in breast cancer cell lines carrying the most common p53 mutation, the formation of amyloid-like aggregates of p53 proteins may explain the protein’s lack of function.

Whether this prionoid behavior in fact represents a relevant cancer-related mechanism remains to be shown. Development of novel and ingenious strategies to prevent p53 misfolding and aggregation may be just one way to find out.

“We are planning pre-clinical tests with synthesized nucleic acids in an attempt to prevent the changing in conformation of normal p53, and avoid aggregates of misfolded protein,” says Dr. Silva.

If successful, the strategy may help unveil unforeseen molecular mechanisms leading to tumor development. Considering that more than half of the cancers lose p53 function, this prionoid behavior may serve as a potential novel target for cancer therapy, dramatically transforming our way of thinking of cancer and treating cancer patients.

(Source: “Prions and cancer: A story unfolding”)

The good news about prions

By Nancy Shute
Posted 1/11/04

Last month’s discovery of mad cow disease in the U.S. food supply has elevated prions from an obscure biological curiosity to topic A on the talk shows. But just as these villainous, twisted proteins are becoming notorious, researchers are saying: Hold up; they might not be so bad after all. Indeed, prions and their cousin proteins may prove to be benign–even helpful–in normal mental functions like memory.

The same biological tenacity that can devastate the brain, it turns out, may also guard the memory of that first day in kindergarten or that first kiss. And although mad cow and its human version are rare, an understanding of why prions go bad could lead to treatments for diseases as common as cancer and diabetes.

No one really knows why prions exist. And no one knows how memories persist through time. So Nobel laureate Eric Kandel and Susan Lindquist, a prion expert at the Whitehead Institute in Cambridge, Mass., combined a protein involved in learning and memory with yeast prions. The experiment, published last month in Cell, revealed that the memory protein worked while in a stable, prionlike form, suggesting that it could be the mechanism needed for storing memories in brain synapses for decades on end. “We’ve shown for the first time that a prion in its self-perpetuating mode could have a normal physiological function,” Kandel says. His lab is now testing this startling hypothesis in flies and mice. If it proves true, it could illuminate a key mystery of the brain.

Origami. Prions may also hold clues to combating common diseases, because they are simply normal proteins that are misfolded. Misfolded proteins, it turns out, cause a host of major ailments, from cancer and diabetes to Alzheimer’s and Parkinson’s. Proteins are the workhorses of living things; the human body makes at least 50,000 different ones for tasks from building bones and muscle to digesting food and thinking.

As proteins form within cells, their long chains of amino acids fold up like fiendishly intricate origami. Since the 1930s, scientists have known that a protein’s folded shape is key to its function, making it possible for hemoglobin to carry oxygen or for collagen to bind together skin. But figuring out how and why proteins fold the way they do has become one of the great, enduring challenges in biochemistry.

It’s easy for proteins to get corrupted while folding in the crowded confines of a cell, and misfolded proteins can cause all sorts of trouble. One example is the P53 protein, the body’s frontline warrior against cancer. Misfolded P53s lose their tumor-suppressing power, an error that causes about half of all cancers. Cystic fibrosis, too, is caused by misfolded proteins, as is diabetes. Prions are more malevolent, forcing nearby proteins to misfold, too, unleashing a destructive chain reaction. Although Alzheimer’s and Parkinson’s are not known to be caused by prions, the disease process, in which brain proteins glom together into plaques, looks remarkably like that of mad cow and other prion diseases. “We’re starting to think there may be similarities between many diseases of misfolding,” says Jonathan Weissman, a prion researcher at the University of California-San Francisco, “including infectious prion diseases like mad cow and noninfectious diseases like Alzheimer’s.”

Cellular prion protein promotes invasion and metastasis of gastric cancer

Abstract

Cellular prion protein (PrPc) is a glycosylphosphatidylinositol (GPI) -anchored membrane protein that is highly conserved in mammalian species. PrPc has the characteristics of adhesive molecules and is thought to play a role in cell adhesion and membrane signaling. Here we investigated the possible role of PrPc in the process of invasiveness and metastasis in gastric cancers. PrPc was found to be highly expressed in metastatic gastric cancers compared to nonmetastatic ones by immunohistochemical staining. PrPc significantly promoted the adhesive, invasive, and in vivo metastatic abilities of gastric cancer cell lines SGC7901 and MKN45. PrPc also increased promoter activity and the expression of MMP11 by activating phosphorylated ErK1/2 in gastric cancer cells. MEK inhibitor PD98059 and MMP11 antibody (Ab) significantly inhibited in vitro invasive and in vivo metastatic abilities induced by PrPc. N-terminal fragment (amino acid 24–90) was suggested to be an indispensable region for signal transduction and invasion-promoting function of PrPc. Taken together, the present work revealed a novel function of PrPc that the existence of N-terminal region of PrPc could promote the invasive and metastatic abilities of gastric cancer cells at least partially through activation of MEK/ERK pathway and consequent transactivation of MMP11.—Pan, Y., Zhao, L., Liang, J., Liu, J., Shi, Y., Liu, N., Zhang, G., Jin, H., Gao, J., Xie, H., Wang, J., Liu, Z., Fan, D. Cellular prion protein promotes invasion and metastasis of gastric cancer.

  1. State Key Laboratory of Cancer Biology and Institute of Digestive Diseases, Xijing Hospital, the Fourth Military Medical University, Xi’an, Shaanxi Province, P. R. China

Correspondence: State Key Laboratory of Cancer Biology and Institute of Digestive Diseases, Xijing Hospital, the Fourth Military Medical University, 17 Changle Western Rd., Xi’an, Shaanxi Province, 710032, P. R. China. E-mail: fandaim@fmmu.edu.cn

–≈–
A Conclusion,
Rife With Controversy
–≈–

So what about the zombie apocalypse, you ask?

Well my friends, you are currently living through it!

Chances are you were born with the gift of transferred dormant prions from your parents – the gift that keeps on giving.

And the chance that you were, at some time in your life, vaccinated with prion cells is more than likely.

And even if you’ve been a vegetarian your whole life, you have certainly ingested or inhaled animal proteins, such as by taking vitamins in “gelatin” capsules.

You are the walking dead…. you just don’t know it yet; cursed with dormant, brain-eating, mutant prions that will eventually be stimulated and awakened by some “environmental” cause only to subsume and convert other innocent prions into folded crystal zombies – better to devour your brain, my pretty. In short, your brain and body is a prion zombie apocalypse just waiting to happen.

I have no doubt that one of the many prion diseases will take your life; but not before your friends and family watch as you zombify before them, your children visiting you in the west wing of George Bush Memorial Hospital wondering where the old mom or dad went to, and who is this zombie laying there with “Alzheimer’s Disease”? After all, nurses have descriptively nicknamed Alzheimer’s and other dementia patients as “hitters”, “kickers”, “wanderers”, and of course, we can’t forget “biters“.

But let’s steer clear of these horrible zombie-like thoughts, and let’s try not to think about the government’s weapons labs around the country experimenting on different prions, causing them to predictably and unpredictably mutate, and of course, just for fun, seeing if they can be transferred through a bite without dormancy, and attaching them to such things as nano-technologies.
No reason to revolt against the establishment… Nothing to see here…
–=–

It is my belief that the suppressed work and technology of Royal Raymond Rife and of those before and after him even today are the key to ending this prion induced zombification of the people of Earth, and to ending the profitable suffering of generations to come.

While radiation, heat, time, and chemicals will not destroy the infections nature of mutated prions, I believe that this most suppressed of technologies is the one thing not available or known about to those doing the testing.

Here’s the thing…

“The newspaper article provided here was included in a newspaper called The Planet and published February 1986 in Washington, D.C. It was delivered to every member of the U.S. House of Representatives and every member of the United States Senate. Not one representative, senator or staff assistant was motiviated sufficiently to investigate further.

The newspaper was also provided free to the George Washington University Medical School students and professors. Again, not one was motivated to investigate further. All while 7,000 to 10,000 Americans died weekly from cancer!

Good examples of public irresponsibility from people in positions of public trust or professions with public trust implied! Shame!

–Barry Lynes, September 25, 1999

The Cancer Cure That Worked: The Rife Report was published in April 1987, 14 months after the U.S. Congress turned its back on Rife and ignored an incredible opportunity to “jump start” the Rife revival.”

Barry Lynes wrote in 1999 what I am writing here, now in the end of 2012… a pleading for the people of the United States and the world to stand up and demand action, to demand research, and to demand an end to the zombie black death machine that is prion disease in its many hundreds of forms, all separately diagnosed and treated with purposeful ignorance and massive profits.

Barry Lynes article as posted in “The Planet” breifly explained the life and work of Royal Rife:

A mobilization is required, for not only cancer, but AIDS and many other diseases threatening us are potentially capable of being eradicated if we, the people of the United States, get off our collective asses.

In the 1920s a scientist-inventor named Royal Raymond Rife invented a new kind of microscope. In an article in New Age Journal March produced little from New readers), the story of Rife’s cancer cure was detailed. Since then, Rife has been nominated for the “Alternative Nobel Prize” which is annually awarded in Europe as a protest to the more established, less risk taking Swedish honor. Yet, little notice of Rife and his miraculous discovery has infiltrated the establishment consciousness.

Rife’s microscope was a stunning advance. Unlike the electron microscope, Rife’s microscope made it possible to study “living” bacteria, viruses, and so forth. An electron microscope kills its specimens. Rife’s remarkable breakthrough used a new approach to bend light. As a result, Rife was able to prove that bacteria could change their form. In effect, they could become cancer causing viruses.

Rife then implanted his cancer-causing bacteria into rats. Tumors subsequently developed. From here, Rife made the startling discovery that the bacteria could change into a completely different form if the “medium on which they were living” was slightly altered. In other words, Rife’s cancer causing substance was, in some forms and in association with some environments within the body, deadly. But in other forms and in other environments, benign. His cancer causing substance could be changed back and forth from one to the other. The implications of this discovery are obvious. Cancer cells might be transformed to healthy cells again!

Rife then began beaming different frequencies of light on these microorganisms. Up until the early 1950s, Rife perfected this method. As Christopher Bird reported in the New Age article, “tuberculosis, typhoid, leprosy. . . appeared to disintegrate or ‘bIow up’ in the field of his microscope.” This “death ray” was applied to cancers in rats. It worked!

The next step was humans. The result? Here is Rife’s report: “The first clinical work on cancer was completed under the supervision of Milbank Johnson, M.D., which was setup under a special medical research committee of the University of Southern California. Sixteen cases were treated at the clinic for many types of malignancy. After three months, fourteen of these so-called hopeless cases were signed off as clinically cured by a staff of medical doctors and Alvin G. Foord, M. D., pathologist for the group.

Throughout the 1930’s, Rife and associates continued their work. In 1940, Arthur W. Yale, M.D. reported that Rife’s discoveries were an entirely new theory of the origin and cause of cancer, and the treatment and results have been so unique and unbelievable” that we’ may be able to “eliminate the second largest cause of deaths in the United States.

But it was not to be!

There were powerful doctors whose careers were based on the theory that bacteria could not change its form. Rife’s discovery threatened their status and their own research. (It was like the invention of the automobile for a horse-drawn carriage driver.)

One of these “authorities” was Dr. Thomas Rivers of the Rockefeller Institute. Another was Harvard microbiologist Dr. Hans Zinsser. The cancer cure was killed by the powerful.

One of Rife’s supporters, Dr. Edward C. Rosenow, a pioneer bacteriologist, sadly commented at the end of his life, “They simply won’t listen.

Others have followed Rife and have confirmed different aspects of his theory, but since they are few in number and are promoting a cause contrary to the medical establishment’s approved philosophy, they are not supported. Even publishing their findings is difficult if not impossible because of the dominant medical orthodoxy which has reigned since the 1930s!

Christopher Bird’s 1976′ New Age Journal article contained a summation of the political coverup as perceived by the Lee Foundation of Nutritional Research in Milwaukee. According to Bird, the Lee Foundation “maintains that Rife, his microscope and his life work were tabooed by leaders in the U.S. medical profession and that any medical doctor who made use of his practical discoveries was stripped of his privileges as a member of the local medical society.

The Food and Drug Administration (FDA) still bans treatments similar to those of Rife.

–=–

Now, we must realize that Royal Raymond Rife’s frequency research and suppressed technologies took place before the discovery of prions as mutated proteins in the 1960’s. It is my belief that Rife’s research would have eventually located and destroyed the mutated form of prions which cause disease today.

Like Royal Raymond Rife, someone like myself – who is shunned by the mainstream medical (for-profit) profession – can only rely on you the reader of this information to spread, disseminate, and demand that this information be made public and that this prion disease plague that is now killing our elderly, our young adults, and our youngest of children be stopped and prevented.

Currently, the pharmaceutical drug industry is not interested in developing curative or preventative medicines, as that would be anti-corporation in that it would lower profits and take away from shareholder dividends and returns on investments.

Case in point:

The New York Times reported this article in 2008. Note that this was posted not in the health and wellness section… but in the “business” section:

Pfizer to focus on more profitable diseases

Published: Tuesday, September 30, 2008

NEW YORK — Pfizer, the world’s largest drug maker, is ending early-stage development of treatments for a range of illnesses from obesity to heart disease to focus on more profitable diseases.

Pfizer expects to spend $7.2 billion to $7.5 billion on research and development this year, a huge budget for the industry. “Even though it is very large, it is finite,” a Pfizer spokeswoman, Liz Power, said Tuesday.

The changes will not affect drugs in the last of three stages of testing needed for U.S. approval, including the anti-clotting drug apixaban being developed with Bristol-Myers Squibb, Pfizer said in a Sept. 25 memo to employees and confirmed Tuesday. Development will end on at least 11 drugs, including 6 studied for obesity and heart disease and three for digestive disorders.

In a recent interview, Jeffrey Kindler, chief executive of Pfizer, said the company would focus its research budget on medicines for cancer, pain, Alzheimer’s disease and diabetes. Pfizer’s cholesterol pill, Lipitor, the world’s best-selling drug, with $12.7 billion in 2007 revenue, is set to lose patent protection in 2011. Products for cancer and pain are typically more profitable because the makers can charge a higher price, and there is less competition.

Pfizer has identified six high-priority areas for research: cancer, pain, inflammation, diabetes, Alzheimer’s disease and schizophrenia.

These large markets, with rapidly advancing science, are the areas where Pfizer can take a leading position,” the memo said.

Kindler said Pfizer would look to make more acquisitions to fill its pipeline of experimental medicines. Analysts say the company may consider buying ImClone Systems, which makes the cancer drug Erbitux. ImClone has said it received a $70 a share bid by a large drug maker it would not identify. Ray Kerins, a spokesman for Pfizer, said it would not comment on market rumors or speculation.

The memo said Pfizer would also stop early-stage research in anemia, bone health, liver disease, muscle, obesity and some osteoarthritis compounds. Pfizer had 102 drugs in development, including 47 in the first stage of testing and 37 in the second phase, according to the company’s most recent pipeline list, which was updated on Feb. 28. About 20 percent of Pfizer’s research financing now goes toward cancer.

The restructuring will not result in facility closings, and many employees will be shifted to other areas of research, the company said.

Pfizer began reorganizing its research operations in 2007 after halting development on its most promising experimental drug, the cholesterol pill torcetrapib, which was projected to have more than $13 billion in annual sales.

(Source: http://www.nytimes.com/2008/09/30/business/worldbusiness/30iht-pfizer.4.16590893.html?_r=0)

$100 bucks says “Viagra” isn’t on the list of research or patented products to be cut…

Now, besides the blatantly inhuman undertones of this report, stating or at the very least alluding to the fact that profits are of paramount precedent over cures and “promising” drugs, did you notice that the most profitable areas of research and drug development are for the very ailments caused by prion related diseases? Cancer, Alzheimer’s, diabetes, and dementia-related diseases such as schizophrenia… Phizer is not creating preventatives or cures here, but is instead creating symptom relief drugs in order to profit from the ongoing disease. Healing the symptoms is not healing the disease, but is instead profiting from the disease by temporarily treating and relieving only the symptoms caused by the profitable disease.

And this is how our medical and pharmaceutical industry operates as business as usual – symptom relief in lieu of disease prevention and cure.

This unavoidable fact should be quite clear to anyone reading this, straight from the Pfizer horses mouth.

And with this fact in mind, isn’t it time to break the stranglehold and monopoly that this government protected trust of drug and medical associations and corporations has upon the treatment of disease?

The problem is, as Mr. Jeffrey Kindler, chief executive of Pfizer confirmed above, is that in order for this to happen, the American people must “get off of their collective asses” and overthrow this profit-driven medical monopoly that all but promotes prion disease related illnesses for the simple reason and greed of shareholder returns.

It would mean that the people (currently and collectively on their posteriors) would actually have to support someone like me or the many proponents of Rife, Tesla, and so many others who have perfected this technology, which is illegal to utilize publicly as “practicing medicine without a license”, according to the FDA.

But someone like me or someone like Rife will not be embraced by the medical, scientific, or educational “establishment”, and so my research and their discoveries will never reach the people… unless the people say no to the establishment or demand with threat of violence that prion diseases are immediately treated as such.

Will this happen? Will a revolution in the governance of medicine and science take place within my lifetime? As I contemplate my current financial situation, the lack of support, the seemingly hopeless uphill battle to simply inform people without help from a for-profit media… I suppose I can only think about that now famous ad campaign which states that, “A mind is a terrible thing to waste.”

Please, don’t let my efforts here and those of the few suppressed people out there who can actually heal and prevent these profitable diseases (and who would gladly do so without a profit margin) go to waste. Share this information with all you know; with your parents who are reaching the 50 year incubation mark of prion dormancy, with your children who are falling pray to early-onset Alzheimer’s and other prion caused diseases and 1 in 3 with prion related cancers, and with doctors, nurses, and scientists who believe they know what disease is, but really only know what the pharmaceutical and corporate sponsored and written textbooks tell them they know.

The suffering and death on this planet can be halted, prevented, and so much pain can be avoided. But only if the people finally revolt and stop supporting the “establishment”.

To those who blindly invest in the stock of these corporations, I can only ask why? Profit at your own expense? Support of your own enslavement to the medical and pharmaceutical industries?

Are the people so clueless that they would invest in something irregardless of that investments consequences simply because there are dollar signs and investment returns on the other side? This is certainly what government and its pension and other investment fund schemes do. Profit and expansion of profit-making disease is what keeps these companies profitable.

Why do we consent to the federal government “granting” 100’s of billions of dollars to these corporations for “research and development”, placing the bill for that grant on the taxpayers, when we know that those pharmaceutical companies are not out to cure disease, and in fact cause more profitable diseases and symptoms that they help, insuring more profit and more diseases?

And to those who have made fortunes off of this medical and pharma industrial toxic waste production, how can you live knowing that your fortunes were made off causing disease in other people and suppressing the cure for that disease?

How can you live with your fortune when it relies on the suffering of others, and likely yourself in the future?

–≈–

If this writing and research has opened up your eyes or has given you a fragment of hope in an otherwise dark and hopeless world, and you would like to see this information turned into a documentary film, please consider making a donation to myself at the following link:

DONATE HERE

Without the support of the people, I am dead in the water – just like so many who would change and heal the world if only they were given the chance without such organized supression.

If you would like to start an organization or non-governmental research trial for the use of frequency in the treatment of and curing of infectious prions, please contact me and let’s do it! It is doubtful that I will ever receive a research grant in a for-profit world. Perhaps you know somebody who can? Whatever the case, this should be priority number 1!!!

You can Email me here: Introspector48@yahoo.com

Yours and your family’s future health is now in your hands…

Thank you for your time and for sharing this work.

.

Introducing, The Mad Cowboy, Howard Lyman:

–Clint Richardson (Realitybloger.wordpress.com)
–Thursday, November 15, 2011

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