Mad Cow: A Different Perspective


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jimpeel
January 3, 2004, 02:37 AM
Still No Beef to Mad Cow Mania

Thursday, January 01, 2004
By Steven Milloy

Mad cow hysteria is once again frightening beef consumers and hammering the beef industry. It would be easy to blame ignorant media, opportunistic anti-meat activists and cut-throat business rivals for the current mania. But I won’t.

The blame for the groundless alarm rests squarely on the shoulders of scientists who have given way too much aid and comfort to the still unproven notion that mad cow disease poses a risk to human health.

It is widely taken for granted among scientists that mad cow disease is caused by abnormal proteins called prions that somehow build up in the brain and damage it. These same scientists also believe that disease can be spread by consumption of tissue infected with prions.

Humans, so the story goes, allegedly can contract a supposed human-form of mad cow disease, called “new variant Creutzfeldt-Jakob disease” or nvCJD, if they consume prion-containing tissue from an infected cow.

The alleged confirmation of this theory is the 150 or so human deaths attributed to nvCJD in Europe, mostly in the U.K., that have occurred since the mid-1990s following an outbreak of mad cow among British cattle.

Most of the scientists who buy into this theory are also quick to acknowledge that they believe the risk to human health is small but not zero, citing the relatively low number of deaths despite that hundreds of millions of Europeans who consumed millions of pounds of potentially infected British beef since the 1980s.

The prion theory has also been significantly propelled along by the fact that its developer, Dr. Stanley Pruisner of the University of California at San Francisco, won a Nobel Prize for it in 1997.

Despite Pruisner’s Nobel Prize, however, it has not been scientifically established that prions cause any sort of disease ¯ a fact only reluctantly acknowledged by organizations such as the National Academy of Science’s National Research Council and the National Institutes of Health.

Despite almost 10 years of intense research into the causes and potential ramifications of mad cow disease, the prion theory still does not satisfy the basic scientific test known as Koch’s Postulates for whether a particular microorganism, such as a prion, causes a specific disease, such as mad cow.

Developed by German physician and bacteriologist Robert Koch in 1890, the basic criteria of Koch’s Postulates as applied to the prion theory would be: (1) prions are present in every case of the mad cow disease; (2) prions must be isolated from a diseased cow and grown in pure culture; (3) mad cow disease should be reproduced when the cultured prions are inoculated into a healthy cow; and (4) the prion must be recoverable from the experimentally infected cow.

“The best-kept secret in this field is that [prions] in any form have never shown infectivity,” said the head of Yale University’s surgery department to the United Press International’s Steve Mitchell.

There certainly have been a few exceptions to Koch’ Postulates, but no one has made a case for why prions might be another such exception.

Aside from the propulsion received by virtue of the Nobel Prize, Pruisner’s prion theory seems to have been accepted as the explanation for mad cow simply by default ¯ that is, no other explanations for mad cow and nvCJD have been developed.

It’s the same sort of shallow thinking that explains why the 150 nvCJD deaths are usually attributed to consumption of infected beef. There is, in fact, no evidence that the 150 victims of nvCJD even ate infected beef, but it is assumed they did because no other explanation has been developed for how they could have contracted nvCJD.

It’s not likely that more affirmative-natured explanations will be forthcoming anytime soon.

As the UPI’s Mitchell pointed out this week, virtually all of the $27 million the National Institutes of Health gave to researchers for work on mad cow-type diseases was directed toward prion theory research.

An NIH spokesmen told Mitchell that the reason for not allocating resources to non-prion research is that few researchers seem to be proposing that type of research.

Other researchers, including an anonymous NIH scientist, told Mitchell that the research community isn’t applying for grants because the agency is biased against non-prion theories and will reject applications for such research.

It could very well be that some virus or bacterium is responsible for the mad cow-type diseases ¯ but we might not ever know if NIH persists with its tunnel-vision.

The merit of the prion theory seems to rest almost exclusively in the fact that its developer impressed a Nobel Prize committee. It would be much more impressive, however, if the prion theory satisfied Koch’s Postulates.

Steven Milloy is the publisher of JunkScience.com (http://www.junkscience.com/), an adjunct scholar at the Cato Institute and the author of Junk Science Judo: Self-Defense Against Health Scares and Scams (http://www.amazon.com/exec/obidos/ASIN/1930865120/junksciencecom) (Cato Institute, 2001).

Respond to the Writer (stevenmilloy@yahoo.com)

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Pendragon
January 3, 2004, 02:59 AM
Developed by German physician and bacteriologist Robert Koch in 1890, the basic criteria of Koch’s Postulates as applied to the prion theory would be: (1) prions are present in every case of the mad cow disease; (2) prions must be isolated from a diseased cow and grown in pure culture; (3) mad cow disease should be reproduced when the cultured prions are inoculated into a healthy cow; and (4) the prion must be recoverable from the experimentally infected cow.

So - because some guy in 1890 - when they were JUST begining to understand the microbial world - comes up with a postulate to identify an infectious agent, now that is the infelxible standard?

I'm sorry, but I think that postulate will only work for bacterium. Virii leech RNA off a host cell - a "culture" would have to consist of cellular matter with RNA accessible by the virii. If I remember my 10th grade biology that is.

As for prions, the theory behind them is that they are not an infectious agent, but a defective building block. Bacterium "infect" by multiplying within a host - it is usually the metabolic waste and the immunological response of the host that causes the damage.

Prions are believed to be defective proteins that the body tried to use to manufacture new cells - they do not "fold" properly and problems ensue.

If some people want to think that prions do not exist or that nvCJD is not caused by them, that is their perogative, If the prion vectors are still considered "theoretical", then its a pretty compelling theory.

There are other prion diseases - sheep get "scrapies" but the prion in sheep is not believed to be transferable to humans. The prion diseases have very specific vectors they can take from one species to another.

There is also a primitive tribe - oh crap I think in Australia, but I don't remember for sure - they have a practice of eating the brains of their dead relatives. Anyway - they have a similar disease that appears to be prion based and is passed on through this practice.

There always seems to be people who want to turn what is the conventional wisdom on its ear - that is fine if you can prove it, but usually they just offer deflection and innuendo and speculation - on this and on vaccines and on other issues as well.

If they think it is so safe, why don't they demonstrate their confidence in their beliefs and eat some brain tissue from a cow with the disease?

Of course, it is believed to take about 10 years to "incubate" - not rally the proper term of course, but people understand what is meant by it.

I am not really worried about the beef supply, but I think the disease deserves to be taken notice of and precautions need to be taken.

glocksman
January 3, 2004, 03:17 AM
This is the problem (http://www.usatoday.com/news/health/2003-06-09-beef-cover_x.htm)

If you don't finish your steak at a restaurant, did you know the leftovers might be dinner for a cow? Or that calves, instead of drinking their mothers' milk, are fed formula made from cows' blood?
These practices, all perfectly legal, have come to light with the discovery last month of North America's first homegrown case of "mad cow" disease.

Rocked by the specter of spreading infection on the continent, the U.S. Food and Drug Administration and Department of Agriculture have turned their attention to ways of keeping deadly agents that spread the disease out of cattle and cattle feed.

But opening this delicate topic could have unappetizing consequences for consumers who rarely think about what those sizzling steaks and burgers went through on the way from feedlot to backyard grill. When they do, they might not want to pay higher prices to change the system.

Americans have a bucolic image of cows happily chomping grass in fields. Many don't know that modern animal husbandry practices have provided cheap, plentiful meat through such standard practices as feeding cattle not only pieces of their herd mates (before the practice was banned in 1997) but also chicken litter, leftover restaurant food and out-of-date pet food.


We should simply go back to feeding cows grain and other plant matter. After all, they're herbivores by nature, not omnivores or carnivores.

Cool Hand Luke 22:36
January 3, 2004, 05:41 AM
I would gladly pay higher prices for milk and beef if it meant I could get those products without the low levels of synthetic growth hormone and antibiotic residue that are the current byproducts of modern beef and dairy production.

If the USDA would act to clean up beef and dairy production by outlawing some current practices like the use of synthetic hormones or the use of antibiotics in feed there'd be more jobs in the beef and dairy industries as well as a healthier product.

For example, it makes no sense for the USDA to approve the use of possibly unsafe synthetic hormones to boost milk production at the same time they are spending tax money to buy up dairy herds and encourage dairy farmers to get out of the business due to oversupply.

TallPine
January 3, 2004, 06:33 AM
Venison tastes better all the time. :D

Actually, when we do buy beef, it usually comes from a local shop that does their own butchering of local beef.

You can also buy a steer on the hoof and have it custom processed by a local butcher.

Sergeant Bob
January 3, 2004, 09:23 AM
There is also a primitive tribe - oh crap I think in Australia, but I don't remember for sure - they have a practice of eating the brains of their dead relatives.
I've heard about that. Saw something on the Discovery Channel (I think) about it. The disease was what they referred to as "Kuru" IIRC, but I believe it was in South America.
Venison tastes better all the time.

Actually, when we do buy beef, it usually comes from a local shop that does their own butchering of local beef.

You can also buy a steer on the hoof and have it custom processed by a local butcher.
I don't know if venison is such a good alternative anymore. Some deer are contracting "Chronic Wasting Disease", which is similar to Mad Cow, I believe, and not too much is known about it yet.

Buying local beef could be hazardous also, if it has been fed commercial feeds or nutritional supplements (which is how some think it might the disease might be transmitted), much of which contain products rendered from dead cows (guts, hooves, bones, brains), road kills (including deer), and old meat (out of date sausage, hamburger, resturaunt scraps).

On the other hand, most pet food is made with products from rendering plants. Has anyone heard of houshold pets contracting the disease?Of course, it is believed to take about 10 years to "incubate" - not rally the proper term of course, but people understand what is meant by it.
I've read that too. If true, it must not apply to cows though. Very few cows make it to ten years of age (aged beef does not refer to how many candles were on a steers birthday cake :D ) and even dairy cows are seldom kept for over 4 or 5 years. If so, how could they exhibit the symptoms? Don't know if it is still practiced or not, but Micky D's used to buy slaughtered dairy cows for their "McLean" burgers. The meat from dairy cows is very lean, as most of the fat goes into milk production.
Americans have a bucolic image of cows happily chomping grass in fields. Many don't know that modern animal husbandry practices have provided cheap, plentiful meat through such standard practices as feeding cattle not only pieces of their herd mates (before the practice was banned in 1997) but also chicken litter, leftover restaurant food and out-of-date pet food.
Not sure, but doesn't the ban only address the use of the byproducts of "infected" cows?

Art Eatman
January 3, 2004, 10:01 AM
CSpan showed a discussion of this; bunch of scientists and reporters. The gist is that since prions aren't found in muscle tissue, eating the meat won't give you Mad Cow Disease. (Unless you eat the brain, etc.)

The incubation period is three to six years. Most feedlot steers are slaughtered at around age one+ year or so. They buy feeder calves at around 400 pounds, mas o menos, and feed them out toward 1,000 pounds.

The hazards--including e. coli, etc.--mostly seem to come from the introduction into our food supply of aged cattle that have much of their meat turned into hamburger. Hard to tell, really, but my impression from various news articles is that these animals don't get the same sort of handling care as "Prime Beef" animals. (Don't take this as gospel.)

Art

Harry Tuttle
January 3, 2004, 10:25 AM
mechanically separated meat products are high risk items

maybe the beef jerky market will take a dive,
making more table space available at gunshows

if this thread is still alive on Monday, i will post some Prion research surf, i ran last year
There were a few threads on TFL:
http://www.thefiringline.com/forums/showthread.php?threadid=54971
http://www.thefiringline.com/forums/showthread.php?threadid=138112

The deer herd CWD is thought to come from farm raised deer.
Anyone wonder what they fed Bambi?
Soylent Green?

sm
January 3, 2004, 10:29 AM
Kuru:
http://www.as.ua.edu/ant/bindon/ant570/Papers/McGrath/McGrath.htm

http://www.ninds.nih.gov/health_and_medical/disorders/kuru.htm#What_is_Kuru

TallPine
January 3, 2004, 10:53 AM
Buying local beef could be hazardous also
Not if I buy it from my neighbor and it comes right in off the grass ...

:D

tyme
January 3, 2004, 01:09 PM
Mr. Steven Milloy (aka journalist extraordinaire) doesn't appear to know what he's talking about. The first link SM posted has pretty much a complete explanation of what prion researchers believe is going on. This site's also pretty good:
http://www.tulane.edu/~dmsander/WWW/335/Prions.html

telomerase
January 3, 2004, 02:45 PM
On the other hand, most pet food is made with products from rendering plants. Has anyone heard of houshold pets contracting the disease?

Most pets are carnivores, and their enzymes probably quickly cut the prions into amino acids.

Of course if you have a pet cow that you feed dog food, you should worry.

telomerase
January 3, 2004, 02:55 PM
>As for prions, the theory behind them is that they are not an infectious agent, but a defective building block.

No, "prion" means "Proteinaceous infectious particles". They are infectious just as viruses are; injection of foreign prions into an organism causes misfolding of the native proteins in the host.

Koch's postulates are still relevant today... not that there's always time to use them.

jimpeel
January 3, 2004, 03:12 PM
with the discovery last month of North America's first homegrown case of "mad cow" disease.The cow came from Alberta, Canada.

manwithoutahome
January 3, 2004, 03:14 PM
I'm one of the people in one of the states that got this "beef" and I bought it at Winco.

The "scientist" said that everything should be good for maybe expect ground beef....

I loved the Chili I made with it, and the hamburgers where pretty good also.

I guess in 5 or 6 years, I could get CJD....

Oh well, I'll probably be dead from something else before then anyway...

(all said tougne in cheek, I just think this is more hype then anything else. In England, since 1987 (their first case), 149 people died from CJD. Their systems are still not as good as ours and ours will get better.... I like my steak, and dammit, I ain't goin' let the peta folks keep me from a good meal).

That being said, I need to thaw out another steak for tonight... bought this Dec 03.... :D.

M

jimpeel
January 3, 2004, 03:19 PM
If you don't finish your steak at a restaurant, did you know the leftovers might be dinner for a cow? The reality is that pig farmers contract with restaurants for their garbage, not cattle farmers. Pig farmers also contract with grain and bread manufacturers for their unsold "day-olds".

Why has this disease not cropped up in the pork industry? Pigs and pig farmers participate in all of the activities that are attributed to the cause of the disease. Are they in some manner immune and, if so, -- with the similarities of pig tissue to human tissue and the compatibilities that allow pig heart valves to be used in humans without rejection -- is there ongoing research to find the reason for this immunity -- if such immunity exists -- that could benefit humans?

jimpeel
January 3, 2004, 03:34 PM
if this thread is still alive on Monday,Since this thread is of a nature that includes the furtherance of government interference into our daily lives through further control of the food supply and; it is of a highly informative nature as evidenced by the number of links already posted by members and; since this issue will become a hotbed of Congressional political activity and; a moderator has been participating in the discussion and; there is not much chance of the thread going off in a contentious direction: I don't think it will get closed.

jimpeel
January 3, 2004, 09:45 PM
http://www.cbsnews.com/stories/2004/01/01/health/main591089.shtml

There is also a video at the webpage but I don't know how to link to it

Cow ID System May Be Delayed

YAKIMA, Washington, Jan. 3, 2004

USDA Bans Certain Cow Parts

(CBS/AP) An animal identification system that the Agriculture Department has said would be put in place immediately to help safeguard the meat supply against mad cow disease is expected to take a year or two to phase in, The New York Times reports in its Saturday editions.

Weaknesses in tracking cattle have been revealed in the last week as officials have scrambled to try to locate cows connected to the one in Washington State found to have been infected with mad cow disease, the Times points out.

The purpose of a new system would be to find cows that might have been involved in disease outbreaks and trace them to their origins within 48 hours, the Times says.

According to the newspaper, the new identification plan, described on a government Web site, www.usaip.info, calls for farms and other premises that handle animals to have identification numbers by July 2004, and animals themselves to be numbered by July 2005.

The animals' numbers will be on ear tags that will probably emit a radio frequency that will be read by the same kind of devices, like E-ZPass, that have begun replacing tollbooths on some highways. The tag numbers may also be printed so a person can read them, the Times explains.

Development of the plan has been in the works for more than a year and a half, and it may not be possible to hasten it, despite the mad cow case, the Times says.

"These timelines are very aggressive, and it will be a huge task to get the system in place and operational to the extent we'd like it," Scott Stuart, president of the National Livestock Producers Association, a group in Colorado Springs that has been working on the plan with the Agriculture Department, said to the Times.

Currently, he told the Times, although there is no central identification system for cattle, some animals can be traced by their brands or by ear tags registering their vaccinations for certain diseases.

Meanwhile, a third farm has been quarantined after authorities located a cow from the same Canadian herd as a Holstein stricken with mad cow disease, and - with dozens of cattle from the herd still missing - more farms may be isolated in days to come.

At least some cows quarantined since the discovery last month of the Holstein will be destroyed, either because of possible exposure to the infection or to quell public fear, Dr. Ron DeHaven, the Agriculture Department's chief veterinarian, said Friday.

"It would be safe to assume that ... some or all those animals will need to be sacrificed," DeHaven said of the quarantined cattle. A decision on the first cows to be killed will be made soon, he said.

Results of DNA testing that should determine conclusively whether the original sick cow was born in Alberta, Canada, in April 1997 are expected next week, DeHaven said.

The herd put under quarantine in the last day or two is at a dairy farm in Mattawa, near Yakima, where investigators traced one of 80 cows that entered the United States with the diseased Holstein in late 2001.

Another nine cows and a calf born last month to the sick cow are on the Mabton, Wash., dairy farm that was the Holstein's final home. Another calf is on a farm at Sunnyside, Wash., also near Yakima, that raises bull calves.

Mike Louisell, spokesman for the state Department of Agriculture, said the number of farms to be quarantined in Washington could grow as the search for other cattle from the Canadian herd continues.

However, many people in the cattle industry appeared unfazed.

"They're not going to quarantine everybody," said John Top, co-owner of the Toppenish Livestock Commission about 25 miles southeast of Yakima. "They're going to sit tight on a few farms as they trace these cows, but I would expect by the end of next week they'll know where all those cows are."

"We don't know where that investigation is going to end up or how many dairies, whether it's one more or five more or ten," said Patti Brumbach, executive director of the Washington State Beef Commission. "I have confidence that consumers will continue to look at this rationally and that this is a continuation of the investigation."

The search for the rest of the herd's cattle is still in the early stages and it is too soon to say if more quarantines will be warranted, Agriculture Department spokeswoman Julie Quick said.

The quarantined farms officially have been placed on hold by the state, which means animals can't leave or arrive at the farms. The dairy farms can continue to operate, selling milk, which is not considered at risk of transmitting the disease.

Investigators are trying to find cows from the same herd because the most likely source of infection was contaminated feed that the Holstein ate as a calf, DeHaven said. She was born before August 1997, when cow parts were prohibited from cattle feed in the United States and Canada.

DeHaven told CBS News Correspondent Lou Miliano that U.S and Canadian officials will spend the weekend pouring over records dating back six years.

Both countries limited the contents of feed to reduce the chances of infecting cattle through the food chain.

American officials have stressed that the diseased cow's age and the date of the feed ban suggest the infection occurred in Canada. This idea, if proven, would underline the effectiveness of the ban and, what is more important, would allow U.S. authorities to place the root of the problem north of the border, in Canada.

The offspring of the sick cow are under quarantine because mother-to-calf transmission is considered unlikely but cannot be ruled out. DeHaven said investigators also are trying to trace the cow's mother and siblings.

The government typically pays up to market value for animals that it condemns to death to contain a disease. USDA officials have said they have yet to formulate a payment plan.

Mad cow disease, or bovine spongiform encephalopathy, is a threat because humans can develop a brain-wasting illness, variant Creutzfeldt-Jakob disease, from consuming beef products contaminated with BSE. Although 153 people worldwide have contracted that illness, most in Britain, it has never been diagnosed in an American.

Including the stricken Holstein, 81 animals were believed shipped across the border from the same Alberta farm in 2001.

© MMIII, CBS Broadcasting Inc. All Rights Reserved.

TallPine
January 3, 2004, 10:30 PM
So what's going to be the penalty for possessing an unregistered cow ...? :rolleyes:

I bet some outfits don't even know how many animals they own.

Is BATFE going to be BATFEFA (Bureau of Alcohol, Tobacco, Firearms, Explosives, and Farm Animals ????

Are my neighbors going to be subject to no-knock raids to make sure they don't flush a cow down the toliet ?????????????????

Pendragon
January 4, 2004, 02:58 AM
>As for prions, the theory behind them is that they are not an infectious agent, but a defective building block.

No, "prion" means "Proteinaceous infectious particles". They are infectious just as viruses are; injection of foreign prions into an organism causes misfolding of the native proteins in the host.

Koch's postulates are still relevant today... not that there's always time to use them

Ok, thanks for clarifying.

My understanding of prion disease is based on extensive reading during the problems in the UK about 7 years ago.

After reading some of the links posted, I see that it is considered to be "infectious".

Details aside, I am amazed that the author just discounts the whole situation as he does.

Adam
January 4, 2004, 03:21 AM
Sorry I don't have a lot of time to read all this article, but all I know is that mad cow hysteria is totaly stupid thing. We had here the same problem few months ago, and everything is ok now. No one start panic here like in Western Europe and after some time mad cow problem disappear. Probably in few years someone will find mad chicken disease...so what?

tyme
January 4, 2004, 07:37 AM
Telomerase,Most pets are carnivores, and their enzymes probably quickly cut the prions into amino acids.Is that true? I had assumed that non-affected animals simply didn't have proteins susceptible to misfolding, or at least not by any known common prions. We're carnivores too, and we can't break certain prions down. I assumed things like sheep prions didn't affect us not because we can break them down, but because they can't misfold any of our proteins. Even a large amount of prion in consumed meat can only plaque-to-death a limited number of cells.

But I'm not a bioresearcher, so I don't pretend to be right. :)

Jeff Thomas
January 4, 2004, 12:03 PM
What I find interesting in all of this is our high dependance upon government to save us here.

So far in life, I have never been let down by assuming government is incompetent. There are some notable, general exceptions such as the U.S military and local LEO's around here. But otherwise ... I assume incompetence, and then I am pleasantly surprised when it works.

Having the Agriculture Department tell me that everything is just peachy doesn't make me feel all warm and fuzzy. There appears to be plenty of debate out there.

Remember back to the beginning of Aids? We were told by the CDC and the medical community that the only folks who could get Aids were in the "4H Club" ... Haitians, heroin users, hemophiliacs and homosexuals.

Yep, government, and the medical community ... always quick to tell us everything is just peachy. We'll see.

Regards from TX

cracked butt
January 4, 2004, 12:23 PM
Its my understanding that:
1. Prions are found in the nervous tissues of afflicted animals.
2. mice injected with prions from an afflicted mouse do not contract spongiform encephalopathy.
3. certain parasites or microorganisms might be able to change normal proteins to prions.


Its my belief that:
1. Prions are a symptom not a cause of wasting type diseases.
2. The idea that spongiform encephalopathies are transmitted by prions is based on junk science, or at best incomplete research and lack of data on the diseases.
3. very few people in the media could explain the difference between a prion and a retrovirus, and even fewer if any could explain what either of them does. Every time mad cow disease or chronic wasting disease comes up in wild game, the media as in newspapers and television put up nifty little graphics on how prions can transmit disease.
4. I live in Wisconsin where there is a serious epidemic of chronic wasting disease in whitetail deer. Once agian, everytime its described by the media, prions come up as the cause, on the other hand the DNR describes the cause of the disease and transmission of it unknown.

cracked butt
January 4, 2004, 12:32 PM
My questions to everyone:

How many cases of CJD have been positively linked to eating meat from infected livestock or game? How many deaths have been caused by E. coli or Salmonella infections from eating tainted meat?


I for one have a friend who damn near died last year after eating E. coli contaminated meat.

alan
January 4, 2004, 01:36 PM
Readers might find the following of interest. The article appears in 4 January Pittsburgh Post-Gazette, Forum section, page B-1. Entitled The cow jumped over the USDA, it deals with the present situation, including the fact that the USDA is "conflicted", to use a polite term, to describe a regulatory agency that has fallen under the thrall of the inductry it supposedly regulates.

The picture painted, is not particularly pretty, but it is interesting, as well as disturbing.

jimpeel
January 4, 2004, 03:51 PM
Link, please?

Sergeant Bob
January 4, 2004, 04:12 PM
The Cow Jumped Over the U.S.D.A. NY Times (http://www.nytimes.com/2004/01/02/opinion/02SCHL.html?ex=1073624400&en=8206b7fc2ab15626&ei=5062&partner=GOOGLE)

tyme
January 4, 2004, 11:15 PM
cracked,
Its my understanding that:
1. Prions are found in the nervous tissues of afflicted animals.
2. mice injected with prions from an afflicted mouse do not contract spongiform encephalopathy.
3. certain parasites or microorganisms might be able to change normal proteins to prions.

Its my belief that:
1. Prions are a symptom not a cause of wasting type diseases.
2. The idea that spongiform encephalopathies are transmitted by prions is based on junk science, or at best incomplete research and lack of data on the diseases.
3. very few people in the media could explain the difference between a prion and a retrovirus, and even fewer if any could explain what either of them does. Every time mad cow disease or chronic wasting disease comes up in wild game, the media as in newspapers and television put up nifty little graphics on how prions can transmit disease.
4. I live in Wisconsin where there is a serious epidemic of chronic wasting disease in whitetail deer. Once agian, everytime its described by the media, prions come up as the cause, on the other hand the DNR describes the cause of the disease and transmission of it unknown.
1. I think we can all more or less agree on this. They allegedly show up in the liver and lymphatic system too, but that's incidental.
2. With the genetic susceptibility hypothesis, not all mice/cows/deer need become "infected" to prove that prions are the cause. Only some need to become infected.
3. How would they do this after they've been irradiated/cooked? There must be some non-transcriptional process by which prions are created, and there isn't much in a cell, whether it's a bacterium or a virus-infected animal host cell, that can build/modify proteins after irradiation except other proteins.

1. Your evidence is what?
2. Please explain why the research is "junk science." There's usually enough review of the work of Nobel Prize-winning scientists to prevent junk scientists from winning.
3. Media stupidity has nothing to do with the validity of stories they report.
4. I suspect this is because it would take a very long-winded explanation to explain to people that deer CWD is not suspected to be transmissible to humans, while "mad-cow disease" is. I would guess that they don't want to alarm people unnecessarily.

Harry Tuttle
January 5, 2004, 11:54 AM
http://www.findarticles.com/m0833/9213_355/61794670/p1/article.jhtml
Alzheimer's and prion disease; do they share a pathogenic mechanism?(Brief Article)(Statistical
Data Included)

Author/s: Kathryn Senior
Issue: April 22, 2000

In prion disease, when the normal form of the prion protein (PrP-C) comes into direct contact with the
abnormal form (PrP-Sc), it undergoes a conformational change and is converted to PrP-Sc. This
amyloid form is resistant to breakdown and forms damaging plaques. Now it seems that one of the
mechanisms underlying neurodegeneration in Alzheimer's disease, a far more common disorder,
may also involve a direct molecular interaction-- between the amyloid beta protein (Ab) and the
larger amyloid precursor protein (APP).

A significant feature of Alzheimer's is the formation of plaques composed of fibrils of Ab. "Ten years
ago, we demonstrated that Ab is neurotoxic, and subsequent studies showed that toxicity was due to
Ab aggregation", says Bruce Yankner (Department of Neurology, Harvard Medical School, Boston,
MA, US).

Yankner's group has just published data showing that the neurotoxic fibrillar form of Ab shows
increased binding to neuronal membrane proteins, including APP; when Alfredo Lorenzo, Yankner
and colleagues incubated primary cultures of rat cortical neurons with fibrillar Ab, they saw a
dramatic co-precipitation of APP with Ab. Most of the binding occurred with membrane-bound APP
rather than secreted APP. Ab was neurotoxic when cultured with cortical cells from wild-type mice,
but when the protein was incubated with cortical cells from mice that lacked the gene to make APP
a reduction in toxicity of 20-30% was observed. "This suggests that APP may be one of the major cell
surface mediators of Ab toxicity", says Yankner, "but because the toxicity was only partially reduced,
a large part of the toxic effect must be due to other mechanisms." (Nat Neurosci 2000; 3: 460-4)

"This is an important piece of work", says John Viles (Queen Mary and Westfield College, University
of London, UK), who is investigating how copper ions affect amyloid formation in both Alzheimer's
and prion diseases. "Alzheimer's disease is the fourth biggest killer in the Western world and
identifying the interaction between Ab and APP as a contributory factor in the neurodegeneration
seen in Alzheimer's disease is a major step forward", he adds. The mechanisms by which APP and
Ab interact to cause cell death are not yet clear but "the design of inhibitors to the interaction of Ab
with membrane proteins such as APP may be a useful avenue of research", predicts Viles.

COPYRIGHT 2000 The Lancet Ltd.

'Strikingly Similar' protein may be in Alzheimer's and Mad Cow Disease
http://www.eurekalert.org/releases/acs-ssp080800.html

Washington D.C., August 23 -- A "striking similarity" between proteins involved in the early stages of Alzheimer's disease and mad cow disease was
described here today at the 220th national meeting of the American Chemical Society, the world's largest scientific society. The theory, if verified by
other researchers, could help focus efforts to develop preventive drugs, according to the study's lead researcher, Chi Ming Yang, Ph.D., a professor of
chemistry at Nankai University in Tianjin, China.

Prion diseases — which include, among others, neurodegenerative diseases such as mad cow disease and its human counterpart, Creutzfeldt-Jakob
disease — are caused by a malfunctioning prion protein. In Alzheimer's disease, another neurodegenerative disease, the amyloid precursor protein has
been implicated.

Using computer modeling, Yang discovered a similar pattern of amino acids in the prion protein and the amyloid precursor protein: 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," says Yang.

Reductive amino acids are more prone to damage by oxygen-containing free radicals (molecules with a highly reactive unpaired electron) than other
amino acids, explained Yang. Normally, the body can clear itself of free radicals. But with age, this system may fail. When enough free radicals
accumulate to damage a protein molecule, it can malfunction, he says.

Proteins typically fold into specific three-dimensional structures that determine their functions. A malfunctioning protein may remain partially unfolded,
which can place different amino acids in close proximity, Yang explained. In the case of Alzheimer's and prion diseases, the reductive amino acids in
close proximity can lead to the formation of protein plaques, according to Yang.

Although Alzheimer's and prion diseases seem to start in similar ways, they progress differently. This may explain why Alzheimer's disease advances at
a much slower pace than Creutzfeldt-Jakob disease, says Yang.

Harry Tuttle
January 5, 2004, 11:57 AM
Pruisner's Nobel prize:
NOBEL PRIZE:
Prusiner Recognized for Once-Heretical Prion Theory

Gretchen Vogel

The Nobel committee often honors scientists who spent years working against strong opposition on controversial ideas, but usually the prize arrives long after the
dust has settled. Not so this year for the prize in physiology or medicine. Stockholm's Karolinska Institute announced Monday that it had chosen to honor Stanley
Prusiner "for his discovery of prions--a new biological principle of infection." The University of California, San Francisco, professor of neurology, virology, and
biochemistry has championed the idea that infectious proteins can cause a range of degenerative brain diseases by misfolding and causing other proteins to do
likewise. The committee also departed from tradition by awarding the prize to a single researcher--the first time it has done so since 1987, and only the 10th time
in the last 50 years.

While many of Prusiner's colleagues have come to accept the once-heretical prion theory, most say it still faces some crucial unanswered questions. Many argue,
for example, that definitive proof that prions can cause disease by themselves is still lacking and that a cofactor such as a virus cannot be ruled out. Nevertheless,
they say, Prusiner's work so far in making his case is worthy of the prize. "The distance he has brought [the field] is unbelievable," says Peter Lansbury, a
biochemist at Brigham and Women's Hospital in Boston who studies the possible role of prion-type processes in Alzheimer's disease. In a statement, Charles
Weissmann of the University of Zurich--who some have argued should have shared the prize--called Prusiner "a true pioneer and iconoclast" who "has waged a
scientific battle for over 2 decades to convince his colleagues and the world that the infectious agent responsible for diseases such as scrapie, "mad cow
disease," and Creutzfeldt-Jakob disease [CJD] is an abnormal form of a protein ... and has accumulated the evidence which has convinced the vast majority of
scientists of the correctness of his view."

This year's prize is the second awarded for work with such degenerative brain diseases. D. Carleton Gajdusek won in 1976 for his work a decade earlier
demonstrating that kuru--a brain disease that affected highlanders in New Guinea who practiced ritualized cannibalism--was infectious. At the time, Gajdusek's
work led many to blame the malady on a slow-acting virus, but it is now widely considered to be a prion disease.

Prusiner coined the term in 1982 to describe the "proteinaceous infectious particles" he blamed for causing scrapie in sheep and hamsters. He suggested that
scrapie and a collection of other wasting brain diseases, some inherited, some infectious, and some sporadic, were all due to a common process: a misfolded
protein that propagates and kills brain cells.

In doing so, he was picking up on an idea proposed in the 1960s, when radiation biologist Tikvah Alper, of Hammersmith Hospital in London, and physicist J. S.
Griffith of Bedford College, London, suggested that an infectious agent that lacked nucleic acid could cause disease. Alper, studying scrapie in sheep, found that
brain tissue remained infectious even after she subjected it to radiation that would destroy any DNA or RNA. Griffith suggested in a separate paper that perhaps a
protein, which would usually prefer one folding pattern, could somehow misfold and then catalyze other proteins to do so. Such an idea seemed to threaten the
very foundations of molecular biology, which held that nucleic acids were the only way to transmit information from one generation to the next.

Inspired by a patient who died of the wasting brain condition CJD in 1972, Prusiner set out to determine the causative agent behind the disease, which resembles
both kuru and scrapie. He and his colleagues reported in Science in 1982 that they had found an unusual protein in the brains of scrapie-infected hamsters that
did not seem to be present in healthy animals. A year later, they identified the protein and called it PrP for prion protein.

In the next decade, a series of experiments, many led by Prusiner, demonstrated that PrP actually is present in healthy animals, but in a different form from the
one found in diseased brains. The studies also showed that mice lacking PrP are resistant to prion diseases. Taken together, the results have convinced many
scientists that the protein is indeed the agent behind CJD, scrapie, mad cow disease, and others.

Key questions remain, however. "The most important bit of information has yet to come forward: What triggers the normal cell protein to transform into the
[disease-causing] isotype of the protein?" says Clarence Gibbs, a virologist at the National Institute of Neurological Disorders and Stroke and a longtime colleague
of Gajdusek. (Prusiner addresses part of that question on page 245, where he suggests that a possible missing element, dubbed protein X, might help chaperone
the PrP protein into its infectious shape.) And no one has been able to inject a prion protein synthesized in the test tube--and therefore free of any possible
contaminating virus or other nucleic acid--into a healthy animal and make it sick. "I think it's speculation that the protein itself is infectious," says Laura Manuelidis,
a neuropathologist at Yale University who has argued that a virus or other particle is involved. Prusiner acknowledges that there are still many uncertainties.
"There are all these other experiments that should be done," he says. "I want to know more about all these details."

Although Prusiner had been mentioned frequently as a Nobel candidate, many expected the award would wait for some of those uncertainties to be resolved.
Byron Caughey, of the National Institutes of Health's Rocky Mountain Laboratories in Hamilton, Montana, said in a statement that the award is "somewhat
surprising in view of the incomplete resolution of these questions."

Ralf Pettersson, deputy chair of the Nobel Committee at the Karolinska Institute, says the panel was not bothered by the unanswered questions. The prize was
awarded, he says, for the discovery of the prion and its role in the disease process. "The committee is well aware of where the field stands," he says. "The details
have to be solved in the future. But no one can object to the essential role of the prion protein" in these brain diseases. Lansbury adds that Prusiner "is really a
trailblazer. ... He's captured the imagination of a huge segment of the scientific population." And those imaginations should in no way be limited by this week's
prize, Gibbs advises: "There's another Nobel Prize somewhere in this field."

http://www.sciencemag.org/feature/data/prusiner/214.shl

The Prion Diseases

Prions, once dismissed as an impossibility, have now gained wide recognition as extraordinary agents that cause a number of infectious, genetic and spontaneous
disorders

by Stanley B. Prusiner
http://www.nmia.com/~mdibble/prion.html

In Search of the Cause

I first became intrigued by the prion diseases in 1972, when as a resident in neurology at the University of California School of Medicine at San Francisco, I lost a
patient to Creutzfeldt-Jakob disease. As I reviewed the scientific literature on that and related conditions, I learned that scrapie, Creutzfeldt-Jakob disease and kuru
had all been shown to be transmissible by injecting extracts of diseased brains into the brains of healthy animals. The infections were thought to be caused by a
slow-acting virus, yet no one had managed to isolate the culprit. In the course of reading, I came across an astonishing report in which Tikvah Alper and her
colleagues at the Hammersmith Hospital in London suggested that the scrapie agent might lack nucleic acid, which usually can be degraded by ultraviolet or ionizing
radiation. When the nucleic acid in extracts of scrapie-infected brains was presumably destroyed by those treatments, the extracts retained their ability to transmit
scrapie. If the organism did lack DNA and RNA, the finding would mean that it was not a virus or any other known type of infectious agent, all of which contain genetic
material. What, then, was it? Investigators had many ideas--including, jokingly, linoleum and kryptonite--but no hard answers. I immediately began trying to solve this
mystery when I set up a laboratory at U.C.S.F. in 1974. The first step had to be a mechanical one--purifying the infectious material in scrapie-infected brains so that
its composition could be analyzed. The task was daunting; many investigators had tried and failed in the past. But with the optimism of youth, I forged ahead [see
"Prions," by Stanley B. Prusiner; SCIENTIFIC AMERICAN, October 1984]. By 1982 my colleagues and I had made good progress, producing extracts of hamster
brains consisting almost exclusively of infectious material. We had, furthermore, subjected the extracts to a range of tests designed to reveal the composition of the
disease-causing component.

Amazing Discovery

All our results pointed toward one startling conclusion: the infectious agent in scrapie (and presumably in the related diseases) did indeed lack nucleic acid and
consisted mainly, if not exclusively, of protein. We deduced that DNA and RNA were absent because, like Alper, we saw that procedures known to damage nucleic
acid did not reduce infectivity. And we knew protein was an essential component because procedures that denature (unfold) or degrade protein reduced infectivity. I
thus introduced the term "prion" to distinguish this class of disease conveyer from viruses, bacteria, fungi and other known pathogens. Not long afterward, we
determined that scrapie prions contained a single protein that we called PrP, for "prion protein." Now the major question became; Where did the instructions
specifying the sequence of amino acids in PrP reside? Were they carried by an undetected piece of DNA that traveled with PrP, or were they, perhaps, contained in
a gene housed in the chromosomes of cells? The key to this riddle was the identification in 1984 of some 15 amino acids at one end of the PrP protein. My group
identified this short amino acid sequence in collaboration with Leroy E. Hood and his co-workers at the California Institute of Technology. Knowledge of the
sequence allowed us and others to construct molecular probes, or detectors, able to indicate whether mammalian cells carried the PrP gene. With probes produced
by Hood's team, Bruno Oesch, working in the laboratory of Charles Weissmann at the University of Zurich, showed that hamster cells do contain a gene for PrP. At
about the same time, Bruce Cheseboro of the NIH Rocky Mountain Laboratories made his own probes and established that mouse cells harbor the gene as well.
That work made it possible to isolate the gene and to establish that it resides not in prions but in the chromosomes of hamsters, mice, humans and all other
mammals that have been examined. What is more, most of the time, these animals make PrP without getting sick. One interpretation of such findings was that we
had made a terrible mistake: PrP had nothing to do with prion diseases. Another possibility was that PrP could be produced in two forms, one that generated disease
and one that did not. We soon showed the latter interpretation to be correct. The critical clue was the fact that the PrP found in infected brains resisted breakdown
by cellular enzymes called proteases. Most proteins in cells are degraded fairly easily. I therefore suspected that if a normal, (3) nonthreatening form of PrP existed,
it too would be susceptible to degradation. Ronald A. Barry in my laboratory then identified this hypothetical protease-sensitive form. It thus became clear that
scrapie-causing PrP is a variant of a normal protein. We therefore called the normal protein "cellular PrP" and the infectious (protease-resistant) form "scrapie PrP."
The latter term is now used to refer to the protein molecules that constitute the prions causing all scrapie-like diseases of animals and humans.

same Prusiner article on scientific american's website:
http://www.sciam.com/0896issue/prion.html

Harry Tuttle
January 5, 2004, 12:01 PM
March 08, 2001
http://www.sciam.com/article.cfm?articleID=000A1A5F-E7FF-1C5A-B882809EC588ED9F&catID=1

How Prions Leap Species

Very little is known about prions, proteins that in certain forms cause bovine spongiform encephalopathy (BSE), or "mad cow disease." But since infectious prions have made the jump from cows to humans—in whom they cause Creutzfeldt-Jakob disease—almost 100 people have died, and a mass slaughter of cattle is under way in Europe. Now two scientists from the University of California at San Francisco have looked into how dangerous prions may have made the leap from cows to people in the first place. Their findings were published in today's issue of Nature.

Unlike bacteria or viruses, prions appear to become infectious merely by assuming an altered shape. They then transmit their characteristics via protein-protein interactions, making otherwise normal prion proteins also adopt an abnormal shape. These abnormal proteins become insoluble, which—in mammals, at least—leads them to clump together and create brain-cell-killing plaques.

In order to understand how prions bridged the biological gap between different species, Jonathan Weissman and graduate student Peter Chien stitched together segments of prions from two different species of yeast. They found that the resulting hybrid could become infectious in both original kinds of yeast—exactly the sort of ability needed to cross over into a different organism. --Harald Franzen

jimpeel
January 5, 2004, 01:00 PM
Good articles. Thank you.

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