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PHYSIO  February 2001

PHYSIO February 2001

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Subject:

Brain Eroding Diseases

From:

[log in to unmask]

Reply-To:

PHYSIO - for physiotherapists in education and practice <[log in to unmask]>

Date:

Fri, 2 Feb 2001 13:02:29 EST

Content-Type:

text/plain

Parts/Attachments:

Parts/Attachments

text/plain (296 lines)

Most of us will now have been made aware by the media of an horrific brain 
eroding disease called Mad Cow or Creutzfeld-Jakob Disease.  The following 
selections of readings provide some interesting insights into the nature of 
this unique disease.

< http://www.sightings.com/health/madcowinfridge.htm>

Mad Cow Disease causes no antibody response. The damage to the brain is done 
by infectious prions or rogue proteins which become part of the cell walls in 
the infected host. When infection enters any animal, the victim's immune 
system shows no sign of fighting the infection as it does with bacteria, 
germs, and viruses.  This means the immune system can neither detect nor 
fight it, nor can scientists use the antibody-search method to see if someone 
is sick, as we do with AIDS.   CJD (Creutzfeld-Jakob Disease) disease takes 
10 months to 50 years to eat away human brain.

Mad Cow, or BSE, (Bovine Spongiform Encephalopathy) causes transmissable 
genetic mutation which means that if you have it,  all your children will be 
born with it. Sheep and cows pass it to offspring, too, and chickens to their 
eggs. If it weren't transmissable, why for decades has the FDA demanded that 
all donors to the blood supply answer the question 'has anyone in your family 
died of CJD?  That disease is entirely inherited and one drop of blood of a 
descendant of a CJD victims can infect the rest of your line.  PRION diseases 
are well known to be genetic in that they bond with with DNA and are passed 
on.

No scientist can tell if a cow or human is in an incubating phase. Except for 
brain biopsies, there are no tests, no genetic markers. Prions are not 
reliably found in urine. You can see prions in brain tissue but you cannot 
open the skull of a live mammal to scoop them out. If a cow whose milk you 
are drinking has it, her calf, sent to be a veal chop last Winter, also had 
it when you ate it.  A long incubation period means that the farmer cannot 
see that the animal is ill.

Consider the link which scientists are now following.  Alzheimer's is rampant 
in America and yet few people talk about how these scientists think that it 
could also be a prion or protein-borne disease associated with the 
consumption of tainted meat and dairy products.   This research began in 
earnest when Pittsburgh Veterans hospital autopsied 53 SEQUENTIAL Alzheimer's 
victims.  Sample A showed 5.5% had died of Mad-Cow; Sample B showed that 6.3 
Percent died of Mad-Cow. Alzheimer's death tolls are doubling and tripling,  
which is not characteristic of a normal genetic disease.  It appears as if 
some statistics for Mad Cow and CJD are being obscured by Alzheimer’s 
statistics. 

Pasteurization or even radiation cannot destroy prions which can tolerate 
these adverse conditions because they are not living infectious agents. Mad 
Cow prions can't be killed the way we fought the plague or fight cholera 
epidemics, or Ebola, by burning bodies. Prions are, for all practical 
purposes, indestructible. These rogue proteins will only begin to degrade at 
800 degrees fahrenheit, way above the temperature that would reduce them to 
ash! In fact, burning is a bad idea, as prion molecules will rise up in the 
smoke, become airborne and fall back on the land.

No laboratory will accept a Mad Cow autopsy as the laboratory cannot be 
sterilized afterwards. You canot kill prions with fire or disinfecting 
agents. Those are the facts. Remember, beef and sheep farmers have been 
sending livestock to factories to be made into 'protein powder' for livestock 
for the last 26 years.   Mad Cow prions could be in every ounce of meat, 
milk, pork, chicken, egg, cheese, or butter you eat today and in gelatin 
caps, animal glandular supplements, and in the glue on every postage stamp.  
Until all slaughterhouses have brain autopsy labs, until no animal we eat is 
fed another animal's dead body, under penalty of law, and not just leaving it 
to farmers' discretion, nobody can feel safe eating meat, butter, eggs or 
drinking milk any longer. 

Chickens and turkeys are also high risk because cattle blood is sprayed onto 
their feed! The FDA recommended a ban on feeding dead cows to live ones, but 
has said nothing about the practice of using the blood of cattle as food for 
cattle or any other livestock or poultry. Any good doctor will tell you that 
the blood is a carrier of virtually all diseases present in a sick animal.   
So, remember the next time you are in line at the fast food restaurant, or 
heading out to your favourite steak house, you might be about to eat your way 
to a prion eroded brain in a few years' time, especially if the prions are 
found to be the missing link in the Alezheimer’s riddle.

------------------------------------------------------

Here are some sites with plenty of information on Creutzfeld-Jakob (CJD) and 
Mad Cow Disease:

<http://www.cjdfoundation.org/CJDInfo.html>
<http://www.mad-cow.org/>

----------------------

One of the theories explaining these types of disease maintains that special 
infectious proteins called "prions" (proteinaceous infectious particle) cause 
"Mad Cow" disease.  The following websites discuss this topic:

<http://www.sciam.com/askexpert/medicine/medicine14.html>

"The term 'prion' was coined by Stanley B. Prusiner of the University of 
California School of Medicine at San
Francisco in 1982 to distinguish the infectious agent that causes scrapie in 
sheep, Creutzfeldt-Jakob disease
(CJD) in humans and bovine spongiform encephalopathy (BSE) in cattle from 
other, more typical infectious
agents. The prion hypothesis postulates that these diseases are caused not by 
a conventional virus or bacterium
but by a protein that has adopted an abnormal form. 

Here is an article by Dr Prusiner himself reporting  in "The Scientific 
American" on the nature of prions:

<http://www.sciam.com/0896issue/prion.html>

"Fifteen years ago I evoked a good deal of skepticism when I proposed that 
the infectious agents causing certain degenerative disorders of the central 
nervous system in animals and, more rarely, in humans might consist of 
protein and nothing else. At the time, the notion was heretical. Dogma held 
that the conveyers of transmissible diseases required genetic material, 
composed of nucleic acid (DNA or RNA), in order to establish an infection in 
a host. Even viruses, among the simplest microbes, rely on such material to 
direct synthesis of the proteins needed for survival and replication. 

Later, many scientists were similarly dubious when my colleagues and I 
suggested that these "proteinaceous infectious particles"-or "prions," as I 
called the disease-causing agents-could underlie inherited, as well as 
communicable, diseases. Such dual behavior was then unknown to medical 
science. And we met resistance again when we concluded that prions 
(pronounced "pree-ons") multiply in an incredible way; they convert normal 
protein molecules into dangerous ones simply by inducing the benign molecules 
to change their shape. 

Today, however, a wealth of experimental and clinical data has made a 
convincing case that we are correct on all three counts. Prions are indeed 
responsible for transmissible and inherited disorders of protein 
conformation. They can also cause sporadic disease, in which neither 
transmission between individuals nor inheritance is evident. Moreover, there 
are hints that the prions causing the diseases explored thus far may not be 
the only ones. Prions made of rather different proteins may contribute to 
other neurodegenerative diseases that are quite prevalent in humans. They 
might even participate in illnesses that attack muscles."

-------------------------------------------

This article discusses potential risks from vaccines and cultures made from 
cattle:

<http://www.mad-cow.org/00/01jan_news.html>

-------------------------------------------

This article discusses similarities between Mad Cow and Alzheimer's Proteins 

<http://www.cnn.com/2000/HEALTH/08/24/bc.health.madcow.reut/>

WASHINGTON (Reuters) August 24, 2000 -- Proteins linked with Alzheimer's and 
the human version of mad cow disease have some striking similarities -- and 
thus might be susceptible to similar treatments, a researcher said.  Both 
diseases are marked by a gradual deterioration of the brain and both are 
associated with rogue proteins. Both are always fatal. 

Chi Ming Yang, a professor of chemistry at Nankai University in Tianjin, 
China, said he used a computer model to map the prion protein associated with 
Creutzfeldt-Jakob disease (CJD), the human equivalent of mad cow disease, and 
the amyloid precursor protein associated with Alzheimer's. 

Proteins are made up of amino acids, and Yang told a meeting of the American 
Chemical Society in Washington that he found a similar pattern of amino acids 
in the two proteins -- a reductive amino acid followed by three non-reductive 
amino acids.   "This suggests a common molecular mechanism underlying the 
initiation stages of sporadic Alzheimer's disease and both sporadic and 
genetic prion diseases," he said in a statement.

------------------------------------------

The Mystery of Mad Cow Disease:

<http://www.msnbc.com/news/439861.asp?cp1=1&cp1=1#BODY>

"THE CULPRIT behind the so-called transmissible spongiform encephalopathies 
(TSEs), such as mad cow disease or the human version, Creutzfeldt-Jakob 
disease, is thought by many to be a misfolded protein called a prion. These 
misshapen molecules also have been linked to more common, non-infectious 
brain diseases such as Alzheimer’s, Parkinson’s, Huntington’s and Lou 
Gehrig’s.   If prions truly are the culprits behind these diseases, their 
existence flies in the face of the conventional wisdom that only organisms 
with a genome (such as viruses or bacteria) can spread disease or perpetuate 
themselves in living cells."

--------------------------------------

What USA Authorities may not be admitting about CJD:

A cover-up style of article citing instances of where CJD was first spread 
among cattle in the USA, and only later to the UK.  You will have to check 
through various references to extract what is fact and what is not:

<http://home.earthlink.net/~astrology/udder.htm>

"....From the Pittsburgh sampling we realize that there are hundreds if not 
thousands of CJD deaths in America but they are passed off as Alzheimer's.  
BSE (Bovine Spongiform Encephalopathy)  is entrenched in American beef 
regardless of what the US Government wants you to believe, and boy, there 
seems to be an  effort to control what you believe.

Ted Koppel interviewed BSE and CJD expert, Dr. Richard Marsh, on the 
Nightline TV program in 1996.   The interview went like this:

Koppel:   But we (USA) don't feed sheep brains to cows, do we?" 
Dr Marsh blinked. "I don't know where your information comes from, but we 
do." 
He was instantly cut off by a commercial and did not reappear  that night. 
(Capitol Cities which owns ABC was founded by William Casey of the CIA. It is 
as close to being an official mouthpiece of the oligarchy as exists....

The truth is, Virologist Veteran Marsh knows of what he speaks. All those BSE 
cow bodies he saw in Wisconsin 1981-1989 had been fed dead  sheep, yet the 
cows became 'feeder cattle' to feed thousands of other cows who have bred 
thousands of animals. Papuan prions have  been spread to herds from Maine to 
Hawaii. Knowing the genetic mode of transmission of the disease is to all 
offspring, it is reasonable to  suspect that there is sponge brain infection 
slowly crawling up the brain stem of every cow in America as well as all the 
humans who have eaten  them as well as all the offspring of both species. And 
to pigs, chickens who were also fattened with the deadly Soylent Green. As a 
poultry  farmer told a prion researcher, "rendering salesmen brought us bags 
of this powder saying it was wonderful stuff and had ever so many uses:  we 
could use it for fertilizer or to feed our chickens."

As so many CJD deaths are misclassified as Alzheimer and private labs won't 
let CJD tissue in the door to be examined, it is certain the American public 
will not be informed of the disease that is in our food, our kitchens and our 
bodies. We are scheduled to be 'downers' and Ted Koppel doesn't want us to 
know it. 

Dr. Richard Deandrea, a Los Angeles physician who has studied CJD and BSE 
extensively, tells of his first CJD patient. After her death, which  featured 
frills atypical of Alzheimer's (fingers numb, blindness, slurred speech, weak 
knees), Deandrea dogged the Center for Disease Control  for a pathologist 
who'd give him an autopsy to see if it might be CJD.  CDC evaded 3 weeks of 
his calls. Finally, a female CDC staffer told him  that off the record - 
she'd deny it later -"CJD is an issue no pathologist will deal with, a 
virtual death sentence to a lab. A well trained  pathologist knows the 
quarantine would never be lifted. You couldn't sterilize the lab to OSHA 
protocols. It would have to be gutted,  incinerated. Forget it. Your patient 
died of Alzheimer's." So, there may be CJD deaths but there sure aren't going 
to be CJD death certificates. ......>

----------------------------------

Scientific articles on a possible prion role in CJD and Alzheimer's:

<http://www.alzforum.org/members/research/news/index.html#molecularClue>

The process by which a normal prion protein (provoked by an abnormal prion) 
undergoes a conformational change to the abnormal form, and the hypothesized 
resulting neuropathology, is of particular interest to researchers of other 
neurodegenerative diseases that also feature abnormal buildup of toxic 
proteins. Because the presence of abnormal prion alone does not lead to 
neurodegeneration, it is assumed that the protein must work via other 
molecules.  Aguzzi and colleagues in Switzerland and Austria determined that 
plasminogen - a plasma component that serves as the proenzyme for the 
protease plasmin - binds selectively to the prion protein in its abnormal 
form, probably via lysine residues on the prion. They found this to be true 
with mouse prion protein, as well as with prion protein from the brains of 
human Creutzfeldt-Jakob disease patients.

Normal Prion Protein Signals With Fyn (14 September 2000). 

The intracellular protein Fyn, a suspect in the formation of neurofibrillary 
tangles because of its associations with tau protein--has now popped up in 
conjunction with prion diseases. Researchers in France report in tomorrow's 
Science that Fyn couples with the normal form of prion protein, an 
interaction that also involves the protein caveolin-1. 

There is still no demonstrated function for the normal form of prion protein 
(as opposed to the abnormal form thought to cause transmissible spongiform 
encephalopathies such as mad-cow disease and scrapie). The fact that it is 
localized in particularly high concentrations in the cell membranes of 
neurons has led to speculation that it is involved in signal transduction 
across the membrane. The current Science report adds fuel to that idea, 
finding that the normal prion protein is involved in an interactions with the 
intracellular tyrosine kinase Fyn. Because the two proteins are localized in 
different compartments, the researchers searched for an intermediate that 
might be able to link the two and found caveolin-1 involved in this cascade. 
(The protein clathrin, included as a control, also had some effect on the 
interaction, suggesting that it too may be involved.) 

The researchers also noted that Fyn was not activated until the cultured 
cells had differentiated into neurons and that the signaling cascade seemed 
to only involve prion molecules located on neurites, and not on the cell 
body. Implicit in these results is the idea that an extracellular messenger 
must somehow be involved. (See William Klein's comment below on whether there 
might be some common factor in signal cascades in prion disease and in 
Alzheimer's.) 

( Mouillet-Richard S, et al. Science. 15 Sept 2000; 289: 1925-8. 

Comment by William Klein: 

Coupling of cellular prion proteins to Fyn is a real surprise, but maybe it 
shouldn't be. Fyn keeps popping up. Shirazi and Wood showed that 
tangle-bearing neurons in AD have a hefty overload of Fyn. Gloria

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