Mad Cow Scaremongers

Mad Cow Scaremongers by Terry S. Singeltary Sr. a review of the TSE prion agent 2003-2011


Posted On December 20, 2003


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Mad Cow Scaremongers

Secretary of Agriculture Ann Veneman says that "beef is absolutely safe to eat." Harvard University experts note that the risk of Americans contracting mad cow disease is "as close to zero as you can get." Every reputable expert tells us that the American meat supply is still safe. And yet a cabal of animal-rights activists and radical opponents of modern farming are already hitting the airwaves for one purpose: to spread fear and needless alarm. These people are activists, not knowledgeable scientists. Their expertise is in scare mongering, not livestock agriculture. Their goal is to promote animal rights and organic-only, 1800s-style agriculture. And their track record is full of doom-and-gloom predictions that never came true.

Who are these masters of disaster? A rogues gallery follows:

John Stauber -- director of the anti-corporate Center for Media & Democracy, and co-author of the 1997 book Mad Cow USA, which was supported financially by the eco-religious Foundation for Deep Ecology. Stauber sits on the national advisory board of the Organic Consumers Association, as reliable a scaremonger as any about the American food supply. Stauber has become a near-ubiquitous media presence in mad-cow-related stories. Just minutes after Secretary Veneman finished her press conference announcing the discovery of a single sick cow, Stauber told CNN -- without any evidence whatsoever -- that it was just "the tip of an invisible iceberg" and that "mad cow disease is spread throughout North America."

Ronnie Cummins -- head of the Organic Consumers Association, a group founded by radical anti-technology guru Jeremy Rifkin. Cummins has openly expressed his hope that a U.S. mad-cow epidemic would fuel a "crisis of confidence" in American food, similar to the one that he claims drove British consumers to "organic" and other high-priced options. In 1998 Cummins told the Minneapolis City Pages that "consumers and farmers would both be better off if people paid twice as much for their meat and ate half as much." This June he confidently told a Canadian Press reporter that "no case of mad cow has ever been found in a cow raised on an organic farm." This, actually, is not true. The British Central Veterinary Laboratory reports that in 1995 (at the height of the UK outbreak), there were 215 confirmed cases of mad cow disease from 36 different organic farms. And Germany's very first case of mad cow disease was diagnosed in a slaughterhouse that only processed organically-raised cattle.

Michael Greger -- a vegetarian activist doctor who maintains a brisk animal-rights speaking schedule and edits the mad-cow-scare web page of the Organic Consumers Association. He recently provided PETA with a laughable treatise suggesting that the SARS outbreak came from livestock farming. Greger titled his mad-cow stump speech "Mad Cow Disease: Plague of the 21st Century?." He argues: "although no pigs or chickens have been found with the disease ... any animal with a brain has the potential to become infected." Greger has yet to produce any evidence to support this claim, largely because there isn't any. Neither hogs nor hens (nor fish, for that matter) suffer from mad-cow-like illnesses. Greger is planning to hit the lecture circuit in an effort to "keep hammering" the meat industry and " keep this momentum going."

Michael Hansen -- the Consumers Union of the United States' self-proclaimed "expert" on genetically enhanced food, bovine growth hormone, mad cow disease, and any other food issue he deems ripe for scaremongering. When the Canadian mad-cow story broke earlier this year, Hansen blithely suggested that American consumers should eat only grass-fed, "organic," and other specialty beef. Hansen's statements on mad cow have appeared in hundreds of media outlets, and his boss, Jean Halloran, has weighed in as well.

Howard Lyman -- one part animal-rights scold, one part revival tent preacher [click here for video]. Lyman trades on the fact that he was brought up in a cattle-ranching family to imply that his strict vegetarianism is somehow more informed than everyone else's dietary choices. Lyman famously (and incorrectly) predicted on the "Oprah" show that mad cow disease among Americans would "make AIDS look like the common cold." Just 14 hours after the U.S. mad-cow announcement, animal-rights terroristand Sierra Club board member Paul Watson published an op-ed asserting that "Howard Lyman predicted this outbreak years ago. Perhaps now the public might pay more attention to this Montana rancher turned vegan. He knows that of which he speaks." It's no coincidence that Lyman is on the advisory board of Watson's violent Sea Shepard Conservation Society. The front page of The Washington Post's "Style" section seconded Watson's misleading praise of Lyman with an article titled "Ex-Cattleman's Warning Was No Bum Steer."

Dave Louthan -- a disgruntled former employee of the Washington state meat processing plant where the first U.S. mad-cow case was detected. After losing the job he loved (slaughtering cows), Louthan launched a crusade against beef producers and the U.S. Department of Agriculture, a personal jihad supported by animal rights activists who must otherwise recoil at his admitted passion for bloodying beef cattle. This is a man who clearly enjoyed his work -- using a bolt gun to kill cows, buffalo, ostrich, emu and alpaca for Vern’s Moses Lake Meats. He told the New York Times that killing is “really fun,” and beats deboning, which he calls “girls’ work.” In the Seattle Times, Louthan added: “I liked to kill cows. I don’t care if I’m hauling them, feeding them or killing them.”

Like many in the meat business, Louthan lost his source of income because of the mad cow scare recklessly promoted by activist groups. But he’s mad, and he’s fighting back. Despite copious evidence to the contrary, he continues to claim that the famous cow he killed (the one that later tested positive) and many others like it were ground into hamburger and entered the human food chain. “The hamburger surprise in your kids’ school lunch,” Dave claims, “has come from mad cows … Your kids will get mad cow from it.” A man of many contradictions, Louthan warns that the U.S. government “is trying to kill you.” He’s calling on anti-beef and animal-rights groups to send him money so he can “keep up the fight.” Yet he admits continuing to eat beef on a daily basis. The verdict is still out on whether or not this former trucker from Texas can successfully change careers from killing cows to assassinating the character of cattlemen.


Terry Singletary -- A retired machinist and high school dropout, Terry Singletary suffered the tragic loss of his mother to “sporadic” Creutzfeldt-Jakob disease (CJD) in 1997. Desperate to find an explanation for his mother’s death, he has devoted himself to the sad and fruitless task of connecting her death to her diet. Various reports confirm that Mrs. Singletary’s life was claimed by the most common sub-type of CJD (one that accounts for 70 percent of “sporadic” cases). Sporadic CJD, unlike its newer “variant,” is not linked to meat.

As the self-appointed international coordinator of CJD Watch, an organization he co-founded with social worker Deborah Oney, Singletary is cited in media reports as an apparent expert on tracking mad cow disease. This despite his lack of formal education and the absence for support from any credible academic, medical or scientific authority. His sensationalist allegations about the safety of U.S. beef have found their way into hundreds of newspapers and broadcasts. Singletary moderates a mad-cow discussion forum run by a vegetarian activist group; his contributions account for more than half the traffic on the “BSE-L” mailing list, which is generally read by real scientists. Animal rights activists and other food-scare artists frequently refer to him as “Dr. Terry Singletary,” apparently an honorary degree as he has yet to finish high school.

Like many activists, Singletary ignores overwhelming epidemiological and laboratory evidence that rules out a connection between sporadic CJD and beef. Relying entirely on shallow circumstantial evidence and frequent repetition of claims which have been publicly refuted as false, he also blindly insists upon a mad-cow with Alzheimer’s, Parkinson’s, and Lou Gehrig’s disease. His specific allegations have been clearly refuted by Centers for Disease Countrol and Prevention scientists in the journal Neurology.


RE-Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States

26 March 2003

Terry S. Singeltary, retired (medically) CJD WATCH

I lost my mother to hvCJD (Heidenhain Variant CJD). I would like to comment on the CDC's attempts to monitor the occurrence of emerging forms of CJD. Asante, Collinge et al [1] have reported that BSE transmission to the 129-methionine genotype can lead to an alternate phenotype that is indistinguishable from type 2 PrPSc, the commonest sporadic CJD. However, CJD and all human TSEs are not reportable nationally. CJD and all human TSEs must be made reportable in every state and internationally. I hope that the CDC does not continue to expect us to still believe that the 85%+ of all CJD cases which are sporadic are all spontaneous, without route/source. We have many TSEs in the USA in both animal and man. CWD in deer/elk is spreading rapidly and CWD does transmit to mink, ferret, cattle, and squirrel monkey by intracerebral inoculation. With the known incubation periods in other TSEs, oral transmission studies of CWD may take much longer. Every victim/family of CJD/TSEs should be asked about route and source of this agent. To prolong this will only spread the agent and needlessly expose others. In light of the findings of Asante and Collinge et al, there should be drastic measures to safeguard the medical and surgical arena from sporadic CJDs and all human TSEs. I only ponder how many sporadic CJDs in the USA are type 2 PrPSc?


http://www.neurology.org/cgi/eletters/60/2/176
 

Marion Nestle -- New York University's food scold extraordinaire. Although Nestle concedes that the risk of getting mad cow disease is extremely low, she has nonetheless exploited mad cow fears to promote an anti-corporate, pro-organic creed. She has complained: "Until we have a little consumer protection going on in government, consumers have to take care of themselves." How do consumers do that? By purchasing organic food, of course. Nestle told Fox News: "This is a very good time to buy organic."

Bruce Friedrich -- PETA's director of vegan outreach. Friedrich revealed his true agenda when he argued: "I think it would be a great thing if all of these fast-food outlets, and these slaughterhouses, and these laboratories, and the banks that fund them exploded tomorrow. I think it's perfectly appropriate for people to take bricks and toss them through the windows, and everything else along the line. Hallelujah to the people who are willing to do it" [click here for audio]. There is seemingly nothing Bruce won't do to scare people away from meat, including raising fears about mad cow disease. Under Friedrich's leadership, PETA representatives have been handing out "emergency vegetarian starter kits," and holding anti-meat posters outside restaurants and grocery stores all over the country. PETA has also started an aggressive and misleading (what's new?) advertising campaign to frighten the public into vegetarianism.

Neal Barnard -- the animal-rights movement's not-so-secret weapon against meat. Sure he's a doctor (a non-practicing psychiatrist, actually), but his tirades against dairy foods, beef, chicken, and Atkins-style diets are all informed by his connections to PETA. Barnard sits on the board of The PETA Foundation along with PETA co-founder Ingrid Newkirk. And PETA has funneled nearly $1 million to Barnard's misnamed "Physicians Committee for Responsible Medicine." His virulent opposition to animal-based foods was clear in a recent speech at a Food and Drug Administration hearing, where he referred to cheese as "morphine on a cracker" and "dairy crack." PCRM wasted no time after the mad cow news broke, sending out a press release attacking meat and offering a "vegetarian starter kit" for suddenly fearful carnivores.

Caroline Smith DeWaal -- director of the food safety program at the quintessential food cop, the Center for Science in the Public Interest. Smith DeWaal, who has been advising consumers to grind their own beef, told The Washington Post: "Taco filling, pizza toppings, hot dogs, processed meats, these are all likely products that can expose consumers to mad cow disease."

Wayne Pacelle -- senior vice president of the Humane Society of the United States, a radical animal rights group masquerading as an animal-welfare organization. Pacelle immediately began to lobby the federal government on mad cow, petitioning the U.S. Department of Agriculture the morning after Veneman's announcement. Pacelle's goal is to create "a National Rifle Association of the animal rights movement." His opposition to eating meat is so strong that he has "no problems with the extinction of domestic animals."

Gene Bauston -- co-founder of the animal rights group Farm Sanctuary. This group was recently convicted of 210 counts of election fraud, in connection with the $465,000 it illegally trucked into a Florida ballot initiative that gave constitutional rights to pigs. Farm Sanctuary even paid a $50,000 fine. The group issued an e-mail alert to its approximately 18,000 members, requesting that they write to the USDA about mad cow. It also e-mailed a boilerplate "letter to the editor" to over 1,900 activists, asking them to send it to their local newspapers under their own individual signatures. In a gushing article, The New York Times praised the group for its crusade against the processing of "downer" cows. But the paper of record manages to overlook Farm Sanctuary's early association with the domestic-terrorist Animal Liberation Front, as well as its electioneering mischief.

Mark Ritchie -- scaremonger-in-chief at the anti-corporate, anti-modern-agriculture, anti-free-trade Institute for Agriculture and Trade Policy (IATP). He blames "industrialized beef production and liberalized trade" for mad cow disease. IATP has started distributing sound-bites for radio broadcast via a 1-800 number.

Eric Schlosser -- anti-fast food activist and author of Fast Food Nation, which was essentially a screed against the consumption of hamburgers. It's no surprise that Schlosser is using mad-cow fears to buttress his case. He flatly told CNN: "I don't think anyone should eat ground beef." Schlosser's op-ed in The New York Times was similarly full of doom and gloom.

Andrew Knight -- a Seattle veterinarian who recently took over the day-to-day operations of the radical Northwest Animal Rights Network. Knight is raising mad-cow panic levels without disclosing his animal-rights agenda. His letter in The Washington Times (Excerpt: "I, for one, will be stocking up on veggie burgers") identified him only as "Dr. Andrew Knight, Seattle." The San Diego Union-Tribune printed an expanded version of his Times letter as an op-ed. There he wrote: "it is not improbable that for the one mad cow detected thus far, some 1,700 have passed undetected into the food chain, and that the human form of this lethal disease is silently incubating in numerous unsuspecting beef eaters at present." A subsequent op-ed in the Toronto Star used the exact same line.

Karen Hudson -- a consultant for GRACE Factory Farm Project, which can't stand the idea of efficient, large-scale agriculture. The group even compares animal husbandry to the post-apocalyptic movie, The Matrix. Hudson insists -- without providing any evidence -- that "mad cow disease is the product of an increasingly industrialized food system."

Katherine DiMatteo -- executive director of the Organic Trade Association, which represents the $11 billion organic industry in North America. The group issued a media release arguing: "while the retail price of organic meat is generally greater than conventional, to many consumers, the greater peace of mind is priceless."

Larry Bohlen and Brent Blackwelder -- from the radical green group Friends of the Earth. The organization issued a "fact sheet" on mad cow that includes such topics as "mad cow on the rampage." Blackwelder peddles the familiar and false story that the "best way for people to avoid the risk of mad cow disease is to eat organic, grass fed beef or beef alternatives." Bohlen's mad cow comments have found their way into the Los Angeles Times, The Chicago Tribune, and The Seattle Times.

Peter Lurie and Wenonah Hauter -- food safety "experts" at Ralph Nader's Public Citizen. Their public comments are designed to raise unfounded fears about eating conventionally-raised beef.

Felicia Nestor -- chief food-safety worrier at the "whistleblowers' rights" Government Accountability Project. Nestor worked with Public Citizen to author reports called "The Jungle 2000: Is America's Meat Fit to Eat?" and "Hamburger Hell: The Flip Side of USDA's Salmonella Testing Program." She co-founded the Global Safe Food Alliance, which includes mad cow scaremongers like Public Citizen, the Institute for Agriculture and Trade Policy, and the Organic Consumers Association, along with animal-rights groups like Farm Sanctuary, the Physicians Committee for Responsible Medicine, United Poultry Concerns, and the Humane Society of the United States. Nestor's hysterical complaints about mad cow have turned up in The New York Times.

Andrew Kimbrell and Joseph Mendelson -- executive director and legal director of the Center for Food Safety. The Center for Food Safety (not to be confused with the Food and Drug Administration's Center for Food Safety and Applied Nutrition) gets most of its money from the organic food industry and the lunatic Foundation for Deep Ecology.

Robert Cohen -- an animal-rights radical who is convinced that cow's milk is the root of all evil. Cohen warned cattlemen and dairy farmers that mad cow disease would be "a sign" that Americans should "reject your poisons."

http://www.consumerfreedom.com/article_detail.cfm/a/138-mad-cow-scaremongers


Posted On December 20, 2003

AFTER THE FIRST CASE OF MAD COW DISEASE IN THE USA WAS DOCUMENTED

" Like many activists, Singletary ignores overwhelming epidemiological and laboratory evidence that rules out a connection between sporadic CJD and beef. Relying entirely on shallow circumstantial evidence and frequent repetition of claims which have been publicly refuted as false, he also blindly insists upon a mad-cow with Alzheimer’s, Parkinson’s, and Lou Gehrig’s disease. "


http://www.consumerfreedom.com/article_detail.cfm/a/138-mad-cow-scaremongers


SO, just who are The Center for Consumer Freedom ;


http://www.consumerfreedom.com/index.cfm


let's take a closer look shall we ;

The Center for Consumer Freedom (CCF) (formerly called the "Guest Choice Network (GCN)") is a front group for the restaurant, alcohol and tobacco industries. It runs media campaigns which oppose the efforts of scientists, doctors, health advocates, environmentalists and groups like Mothers Against Drunk Driving, calling them "the Nanny Culture -- the growing fraternity of food cops, health care enforcers, anti-meat activists, and meddling bureaucrats who 'know what's best for you.'"

CCF is registered as a tax-exempt, non-profit organization under the IRS code 501(c)(3). Its advisory board is comprised mainly of representatives from the restaurant, meat and alcoholic beverage industries.

http://www.sourcewatch.org/index.php?title=Center_for_Consumer_Freedom


http://en.wikipedia.org/wiki/Center_for_Consumer_Freedom


snip...SEE FULL TEXT HERE ;

http://betaamyloidcjd.blogspot.com/2010/12/alimentary-prion-infections-touch-down.html


UPDATE UPDATE UPDATE
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*** TSE PRION PRION CONFERENCES UPDATES 2015, 2016, AND 2016 ***
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TSE PRION ZOONOSIS 2018

CDC STRONGLY SUGGEST IN 2017;

Do not shoot, handle or eat meat from deer and elk that look sick or are acting strangely or are found dead (road-kill). When field-dressing a deer: Wear latex or rubber gloves when dressing the animal or handling the meat. Minimize how much you handle the organs of the animal, particularly the brain or spinal cord tissues. Do not use household knives or other kitchen utensils for field dressing. Check state wildlife and public health guidance to see whether testing of animals is recommended or required. Recommendations vary by state, but information about testing is available from many state wildlife agencies. Strongly consider having the deer or elk tested for CWD before you eat the meat. If you have your deer or elk commercially processed, consider asking that your animal be processed individually to avoid mixing meat from multiple animals. If your animal tests positive for CWD, do not eat meat from that animal. 

SEE FULL REPORT BELOW!

SUNDAY, DECEMBER 10, 2017 

Detection of Prions in Blood of Cervids at the Asymptomatic Stage of Chronic Wasting Disease

The results showed a sensitivity of 100% in animals with very poor body condition that were IHC-positive in both brain and lymph nodes, 96% in asymptomatic deer IHC-positive in brain and lymph nodes and 53% in animals at early stages of infection that were IHC-positive only in lymph nodes. The overall mean diagnostic sensitivity was 79.3% with 100% specificity. These findings show that PMCA might be useful as a blood test for routine, live animal diagnosis of CWD.

https://www.nature.com/articles/s41598-017-17090-x

http://chronic-wasting-disease.blogspot.com/2017/12/detection-of-prions-in-blood-of-cervids.html

CHRONIC WASTING DISEASE CWD TSE PRION ZOONOTIC ZOONOSIS

PRICE OF TSE PRION POKER GOES UP!

2017

Subject: ***CDC Now Recommends Strongly consider having the deer or elk tested for CWD before you eat the meat

CDC Now Recommends Strongly consider having the deer or elk tested for CWD before you eat the meat 

Chronic Wasting Disease (CWD) 

Prevention 

If CWD could spread to people, it would most likely be through eating of infected deer and elk. In a 2006-2007 CDC survey of U.S. residents, nearly 20 percent of those surveyed said they had hunted deer or elk and more than two-thirds said they had eaten venison or elk meat. However, to date, no CWD infections have been reported in people. 

Hunters must consider many factors when determining whether to eat meat from deer and elk harvested from areas with CWD, including the level of risk they are willing to accept. Hunters harvesting wild deer and elk from areas with reported CWD should check state wildlife and public health guidance to see whether testing of animals is recommended or required in a given state or region. In areas where CWD is known to be present, CDC recommends that hunters strongly consider having those animals tested before eating the meat. 

Tests for CWD are monitoring tools that some state wildlife officials use to look at the rates of CWD in certain animal populations. Testing may not be available in every state, and states may use these tests in different ways. A negative test result does not guarantee that an individual animal is not infected with CWD, but it does make it considerably less likely and may reduce your risk of exposure to CWD. 

To be as safe as possible and decrease their potential risk of exposure to CWD, hunters should take the following steps when hunting in areas with CWD: 

Do not shoot, handle or eat meat from deer and elk that look sick or are acting strangely or are found dead (road-kill). When field-dressing a deer: Wear latex or rubber gloves when dressing the animal or handling the meat. Minimize how much you handle the organs of the animal, particularly the brain or spinal cord tissues. Do not use household knives or other kitchen utensils for field dressing. Check state wildlife and public health guidance to see whether testing of animals is recommended or required. Recommendations vary by state, but information about testing is available from many state wildlife agencies. Strongly consider having the deer or elk tested for CWD before you eat the meat. If you have your deer or elk commercially processed, consider asking that your animal be processed individually to avoid mixing meat from multiple animals. If your animal tests positive for CWD, do not eat meat from that animal. The U.S. Department of Agriculture’s Animal and Plant Health Inspection Service regulates commercially farmed deer and elk. The agency operates a national CWD herd certification program. As part of the voluntary program, states and individual herd owners agree to meet requirements meant to decrease the risk of CWD in their herds. Privately owned herds that do not participate in the herd certification program may be at increased risk for CWD. 

Page last reviewed: August 17, 2017 Page last updated: August 17, 2017 Content source: Centers for Disease Control and Prevention National Center for Emerging and Zoonotic Infectious Diseases (NCEZID) Division of High-Consequence Pathogens and Pathology (DHCPP) 

https://www.cdc.gov/prions/cwd/prevention.html

 > However, to date, no CWD infections have been reported in people. 

key word here is 'reported'. science has shown that CWD in humans will look like sporadic CJD. SO, how can one assume that CWD has not already transmitted to humans? they can't, and it's as simple as that. from all recorded science to date, CWD has already transmitted to humans, and it's being misdiagnosed as sporadic CJD. ...terry 

LOOKING FOR CWD IN HUMANS AS nvCJD or as an ATYPICAL CJD, LOOKING IN ALL THE WRONG PLACES $$$ 

*** These results would seem to suggest that CWD does indeed have zoonotic potential, at least as judged by the compatibility of CWD prions and their human PrPC target. Furthermore, extrapolation from this simple in vitro assay suggests that if zoonotic CWD occurred, it would most likely effect those of the PRNP codon 129-MM genotype and that the PrPres type would be similar to that found in the most common subtype of sCJD (MM1).*** 

http://www.tandfonline.com/doi/full/10.4161/pri.28124?src=recsys

http://www.tandfonline.com/doi/pdf/10.4161/pri.28124?needAccess=true

http://wwwnc.cdc.gov/eid/article/20/1/13-0858_article.htm

TUESDAY, SEPTEMBER 12, 2017 

CDC Now Recommends Strongly consider having the deer or elk tested for CWD before you eat the meat 

http://chronic-wasting-disease.blogspot.com/2017/09/cdc-now-recommends-strongly-consider.html

Prion 2017 Conference Abstracts CWD

 2017 PRION CONFERENCE 

First evidence of intracranial and peroral transmission of Chronic Wasting Disease (CWD) into Cynomolgus macaques: a work in progress 

Stefanie Czub1, Walter Schulz-Schaeffer2, Christiane Stahl-Hennig3, Michael Beekes4, Hermann Schaetzl5 and Dirk Motzkus6 1 

University of Calgary Faculty of Veterinary Medicine/Canadian Food Inspection Agency; 2Universitatsklinikum des Saarlandes und Medizinische Fakultat der Universitat des Saarlandes; 3 Deutsches Primaten Zentrum/Goettingen; 4 Robert-Koch-Institut Berlin; 5 University of Calgary Faculty of Veterinary Medicine; 6 presently: Boehringer Ingelheim Veterinary Research Center; previously: Deutsches Primaten Zentrum/Goettingen 

This is a progress report of a project which started in 2009. 21 cynomolgus macaques were challenged with characterized CWD material from white-tailed deer (WTD) or elk by intracerebral (ic), oral, and skin exposure routes. Additional blood transfusion experiments are supposed to assess the CWD contamination risk of human blood product. Challenge materials originated from symptomatic cervids for ic, skin scarification and partially per oral routes (WTD brain). Challenge material for feeding of muscle derived from preclinical WTD and from preclinical macaques for blood transfusion experiments. We have confirmed that the CWD challenge material contained at least two different CWD agents (brain material) as well as CWD prions in muscle-associated nerves. 

Here we present first data on a group of animals either challenged ic with steel wires or per orally and sacrificed with incubation times ranging from 4.5 to 6.9 years at postmortem. Three animals displayed signs of mild clinical disease, including anxiety, apathy, ataxia and/or tremor. In four animals wasting was observed, two of those had confirmed diabetes. All animals have variable signs of prion neuropathology in spinal cords and brains and by supersensitive IHC, reaction was detected in spinal cord segments of all animals. Protein misfolding cyclic amplification (PMCA), real-time quaking-induced conversion (RT-QuiC) and PET-blot assays to further substantiate these findings are on the way, as well as bioassays in bank voles and transgenic mice. 

At present, a total of 10 animals are sacrificed and read-outs are ongoing. Preclinical incubation of the remaining macaques covers a range from 6.4 to 7.10 years. Based on the species barrier and an incubation time of > 5 years for BSE in macaques and about 10 years for scrapie in macaques, we expected an onset of clinical disease beyond 6 years post inoculation. 

PRION 2017 DECIPHERING NEURODEGENERATIVE DISORDERS 

Subject: PRION 2017 CONFERENCE DECIPHERING NEURODEGENERATIVE DISORDERS VIDEO 

PRION 2017 CONFERENCE DECIPHERING NEURODEGENERATIVE DISORDERS 

*** PRION 2017 CONFERENCE VIDEO 

https://www.youtube.com/embed/Vtt1kAVDhDQ

http://prion2017.org/programme/

TUESDAY, JULY 04, 2017

*** PRION 2017 CONFERENCE ABSTRACTS ON CHRONIC WASTING DISEASE CWD TSE PRION ***

http://chronic-wasting-disease.blogspot.com/2017/07/prion-2017-conference-abstracts-on.html

O.05: Transmission of prions to primates after extended silent incubation periods: Implications for BSE and scrapie risk assessment in human populations

 

Emmanuel Comoy, Jacqueline Mikol, Valerie Durand, Sophie Luccantoni, Evelyne Correia, Nathalie Lescoutra, Capucine Dehen, and Jean-Philippe Deslys Atomic Energy Commission; Fontenay-aux-Roses, France

 

Prion diseases (PD) are the unique neurodegenerative proteinopathies reputed to be transmissible under field conditions since decades. The transmission of Bovine Spongiform Encephalopathy (BSE) to humans evidenced that an animal PD might be zoonotic under appropriate conditions. Contrarily, in the absence of obvious (epidemiological or experimental) elements supporting a transmission or genetic predispositions, PD, like the other proteinopathies, are reputed to occur spontaneously (atpical animal prion strains, sporadic CJD summing 80% of human prion cases). Non-human primate models provided the first evidences supporting the transmissibiity of human prion strains and the zoonotic potential of BSE. Among them, cynomolgus macaques brought major information for BSE risk assessment for human health (Chen, 2014), according to their phylogenetic proximity to humans and extended lifetime. We used this model to assess the zoonotic potential of other animal PD from bovine, ovine and cervid origins even after very long silent incubation periods.

 

*** We recently observed the direct transmission of a natural classical scrapie isolate to macaque after a 10-year silent incubation period,

 

***with features similar to some reported for human cases of sporadic CJD, albeit requiring fourfold long incubation than BSE. Scrapie, as recently evoked in humanized mice (Cassard, 2014),

 

***is the third potentially zoonotic PD (with BSE and L-type BSE),

 

***thus questioning the origin of human sporadic cases. 

We will present an updated panorama of our different transmission studies and discuss the implications of such extended incubation periods on risk assessment of animal PD for human health.

 

===============

 

***thus questioning the origin of human sporadic cases***

 

===============

 

***our findings suggest that possible transmission risk of H-type BSE to sheep and human. Bioassay will be required to determine whether the PMCA products are infectious to these animals.

 

==============

 

 https://prion2015.files.wordpress.com/2015/05/prion2015abstracts.pdf

 

 Transmission data also revealed that several scrapie prions propagate in HuPrP-Tg mice with efficiency comparable to that of cattle BSE. While the efficiency of transmission at primary passage was low, subsequent passages resulted in a highly virulent prion disease in both Met129 and Val129 mice. Transmission of the different scrapie isolates in these mice leads to the emergence of prion strain phenotypes that showed similar characteristics to those displayed by MM1 or VV2 sCJD prion. These results demonstrate that scrapie prions have a zoonotic potential and raise new questions about the possible link between animal and human prions.

 

http://www.tandfonline.com/doi/abs/10.1080/19336896.2016.1163048?journalCode=kprn20

 

http://www.tandfonline.com/doi/abs/10.1080/19336896.2016.1163048?journalCode=kprn20

PRION 2016 TOKYO

Saturday, April 23, 2016

SCRAPIE WS-01: Prion diseases in animals and zoonotic potential 2016

Prion. 10:S15-S21. 2016 ISSN: 1933-6896 printl 1933-690X online

Taylor & Francis

Prion 2016 Animal Prion Disease Workshop Abstracts

WS-01: Prion diseases in animals and zoonotic potential

Juan Maria Torres a, Olivier Andreoletti b, J uan-Carlos Espinosa a. Vincent Beringue c. Patricia Aguilar a,

Natalia Fernandez-Borges a. and Alba Marin-Moreno a

"Centro de Investigacion en Sanidad Animal ( CISA-INIA ). Valdeolmos, Madrid. Spain; b UMR INRA -ENVT 1225 Interactions Holes Agents Pathogenes. ENVT. Toulouse. France: "UR892. Virologie lmmunologie MolécuIaires, Jouy-en-Josas. France

Dietary exposure to bovine spongiform encephalopathy (BSE) contaminated bovine tissues is considered as the origin of variant Creutzfeldt Jakob (vCJD) disease in human. To date, BSE agent is the only recognized zoonotic prion. Despite the variety of Transmissible Spongiform Encephalopathy (TSE) agents that have been circulating for centuries in farmed ruminants there is no apparent epidemiological link between exposure to ruminant products and the occurrence of other form of TSE in human like sporadic Creutzfeldt Jakob Disease (sCJD). However, the zoonotic potential of the diversity of circulating TSE agents has never been systematically assessed. The major issue in experimental assessment of TSEs zoonotic potential lies in the modeling of the ‘species barrier‘, the biological phenomenon that limits TSE agents’ propagation from a species to another. In the last decade, mice genetically engineered to express normal forms of the human prion protein has proved essential in studying human prions pathogenesis and modeling the capacity of TSEs to cross the human species barrier.

To assess the zoonotic potential of prions circulating in farmed ruminants, we study their transmission ability in transgenic mice expressing human PrPC (HuPrP-Tg). Two lines of mice expressing different forms of the human PrPC (129Met or 129Val) are used to determine the role of the Met129Val dimorphism in susceptibility/resistance to the different agents.

These transmission experiments confirm the ability of BSE prions to propagate in 129M- HuPrP-Tg mice and demonstrate that Met129 homozygotes may be susceptible to BSE in sheep or goat to a greater degree than the BSE agent in cattle and that these agents can convey molecular properties and neuropathological indistinguishable from vCJD. However homozygous 129V mice are resistant to all tested BSE derived prions independently of the originating species suggesting a higher transmission barrier for 129V-PrP variant.

Transmission data also revealed that several scrapie prions propagate in HuPrP-Tg mice with efficiency comparable to that of cattle BSE. While the efficiency of transmission at primary passage was low, subsequent passages resulted in a highly virulent prion disease in both Met129 and Val129 mice. Transmission of the different scrapie isolates in these mice leads to the emergence of prion strain phenotypes that showed similar characteristics to those displayed by MM1 or VV2 sCJD prion. These results demonstrate that scrapie prions have a zoonotic potential and raise new questions about the possible link between animal and human prions. 

http://www.tandfonline.com/doi/abs/10.1080/19336896.2016.1163048?journalCode=kprn20

why do we not want to do TSE transmission studies on chimpanzees $

5. A positive result from a chimpanzee challenged severly would likely create alarm in some circles even if the result could not be interpreted for man. I have a view that all these agents could be transmitted provided a large enough dose by appropriate routes was given and the animals kept long enough. Until the mechanisms of the species barrier are more clearly understood it might be best to retain that hypothesis.

snip...

R. BRADLEY

https://web.archive.org/web/20170126051158/http://collections.europarchive.org/tna/20080102222950/http://www.bseinquiry.gov.uk/files/yb/1990/09/23001001.pdf

Title: Transmission of scrapie prions to primate after an extended silent incubation period) 

*** In complement to the recent demonstration that humanized mice are susceptible to scrapie, we report here the first observation of direct transmission of a natural classical scrapie isolate to a macaque after a 10-year incubation period. Neuropathologic examination revealed all of the features of a prion disease: spongiform change, neuronal loss, and accumulation of PrPres throughout the CNS. 

*** This observation strengthens the questioning of the harmlessness of scrapie to humans, at a time when protective measures for human and animal health are being dismantled and reduced as c-BSE is considered controlled and being eradicated. 

*** Our results underscore the importance of precautionary and protective measures and the necessity for long-term experimental transmission studies to assess the zoonotic potential of other animal prion strains. 

http://www.ars.usda.gov/research/publications/publications.htm?SEQ_NO_115=313160

Research Project: TRANSMISSION, DIFFERENTIATION, AND PATHOBIOLOGY OF TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES

Location: Virus and Prion Research

Title: Disease-associated prion protein detected in lymphoid tissues from pigs challenged with the agent of chronic wasting disease

Author item Moore, Sarah item Kunkle, Robert item Kondru, Naveen item Manne, Sireesha item Smith, Jodi item Kanthasamy, Anumantha item West Greenlee, M item Greenlee, Justin

Submitted to: Prion Publication Type: Abstract Only Publication Acceptance Date: 3/15/2017 Publication Date: N/A Citation: N/A Interpretive Summary:

Technical Abstract: Aims: Chronic wasting disease (CWD) is a naturally-occurring, fatal neurodegenerative disease of cervids. We previously demonstrated that disease-associated prion protein (PrPSc) can be detected in the brain and retina from pigs challenged intracranially or orally with the CWD agent. In that study, neurological signs consistent with prion disease were observed only in one pig: an intracranially challenged pig that was euthanized at 64 months post-challenge. The purpose of this study was to use an antigen-capture immunoassay (EIA) and real-time quaking-induced conversion (QuIC) to determine whether PrPSc is present in lymphoid tissues from pigs challenged with the CWD agent.

Methods: At two months of age, crossbred pigs were challenged by the intracranial route (n=20), oral route (n=19), or were left unchallenged (n=9). At approximately 6 months of age, the time at which commercial pigs reach market weight, half of the pigs in each group were culled (<6 challenge="" groups="" month="" pigs="" remaining="" the="">6 month challenge groups) were allowed to incubate for up to 73 months post challenge (mpc). The retropharyngeal lymph node (RPLN) was screened for the presence of PrPSc by EIA and immunohistochemistry (IHC). The RPLN, palatine tonsil, and mesenteric lymph node (MLN) from 6-7 pigs per challenge group were also tested using EIA and QuIC.

Results: PrPSc was not detected by EIA and IHC in any RPLNs. All tonsils and MLNs were negative by IHC, though the MLN from one pig in the oral <6 5="" 6="" at="" by="" detected="" eia.="" examined="" group="" in="" intracranial="" least="" lymphoid="" month="" months="" of="" one="" pigs="" positive="" prpsc="" quic="" the="" tissues="" was="">6 months group, 5/6 pigs in the oral <6 4="" and="" group="" months="" oral="">6 months group. Overall, the MLN was positive in 14/19 (74%) of samples examined, the RPLN in 8/18 (44%), and the tonsil in 10/25 (40%). Conclusions:

This study demonstrates that PrPSc accumulates in lymphoid tissues from pigs challenged intracranially or orally with the CWD agent, and can be detected as early as 4 months after challenge.

CWD-infected pigs rarely develop clinical disease and if they do, they do so after a long incubation period. This raises the possibility that CWD-infected pigs could shed prions into their environment long before they develop clinical disease.

Furthermore, lymphoid tissues from CWD-infected pigs could present a potential source of CWD infectivity in the animal and human food chains.

https://www.ars.usda.gov/research/publications/publication/?seqNo115=337105

CONFIDENTIAL

EXPERIMENTAL PORCINE SPONGIFORM ENCEPHALOPATHY

While this clearly is a cause for concern we should not jump to the conclusion that this means that pigs will necessarily be infected by bone and meat meal fed by the oral route as is the case with cattle. ...

http://web.archive.org/web/20031026000118/www.bseinquiry.gov.uk/files/yb/1990/08/23004001.pdf

we cannot rule out the possibility that unrecognised subclinical spongiform encephalopathy could be present in British pigs though there is no evidence for this: only with parenteral/implantable pharmaceuticals/devices is the theoretical risk to humans of sufficient concern to consider any action.

http://web.archive.org/web/20030822031154/www.bseinquiry.gov.uk/files/yb/1990/09/10007001.pdf

 Our records show that while some use is made of porcine materials in medicinal products, the only products which would appear to be in a hypothetically ''higher risk'' area are the adrenocorticotrophic hormone for which the source material comes from outside the United Kingdom, namely America China Sweden France and Germany. The products are manufactured by Ferring and Armour. A further product, ''Zenoderm Corium implant'' manufactured by Ethicon, makes use of porcine skin - which is not considered to be a ''high risk'' tissue, but one of its uses is described in the data sheet as ''in dural replacement''. This product is sourced from the United Kingdom.....

http://web.archive.org/web/20030822054419/www.bseinquiry.gov.uk/files/yb/1990/09/21009001.pdf

 snip...see much more here ;

WEDNESDAY, APRIL 05, 2017

Disease-associated prion protein detected in lymphoid tissues from pigs challenged with the agent of chronic wasting disease

http://chronic-wasting-disease.blogspot.com/2017/04/disease-associated-prion-protein.html

TUESDAY, JANUARY 17, 2017 

FDA PART 589 -- SUBSTANCES PROHIBITED FROM USE IN ANIMAL FOOD OR FEEDVIOLATIONS OFFICIAL ACTION INDICATED OAI UPDATE 2016 to 2017 BSE TSE PRION

http://bovineprp.blogspot.com/2017/01/fda-part-589-substances-prohibited-from.html

Thursday, November 16, 2017 

Texas Natural Meats Recalls Beef Products Due To Possible Specified Risk Materials Contamination

http://specifiedriskmaterial.blogspot.com/2017/11/texas-natural-meats-recalls-beef.html

MONDAY, NOVEMBER 06, 2017 

Experimental transfusion of variant CJD-infected blood reveals previously uncharacterised prion disorder in mice and macaque

''On secondary and tertiary transmissions, however, the proportion of PrPres positive animals gradually increased to almost 100%. 

''Recent communications suggest that a similar situation might exist in other models of experimental exposure to prions involving swine32 and cattle33.'' 

''Experimental transfusion of variant CJD-infected blood reveals previously uncharacterised prion disorder in mice and macaque''

http://vcjd.blogspot.com/2017/11/experimental-transfusion-of-variant-cjd.html

i am thinking of that 10,000,000 POUNDS OF BLOOD LACED MEAT AND BONE MEAL IN COMMERCE WARNING LETTER back in 2007, see;

SATURDAY, NOVEMBER 4, 2017 

FDA 589.2000, Section 21 C.F.R. Animal Proteins Prohibited in Ruminant Feed WARNING Letters and FEED MILL VIOLATIONS OBSERVATIONS 2017 to 2006

http://bovineprp.blogspot.com/2017/11/fda-5892000-section-21-cfr-animal.html

FRIDAY, NOVEMBER 3, 2017

BSE MAD COW TSE PRION DISEASE PET FOOD FEED IN COMMERCE INDUSTRY VS TERRY S. SINGELTARY Sr. A REVIEW

''I have a neighbor who is a dairy farmer. He tells me that he knows of several farmers who feed their cattle expired dog food. These farmers are unaware of any dangers posed to their cattle from the pet food contents. For these farmers, the pet food is just another source of protein.''

IN CONFIDENCE

http://madcowfeed.blogspot.com/2017/11/bse-mad-cow-tse-prion-disease-pet-food.html

TUESDAY, JULY 18, 2017 

USDA announces Alabama case of Bovine Spongiform Encephalopathy Alabama

http://bovineprp.blogspot.com/2017/07/usda-announces-alabama-case-of-bovine.html

THURSDAY, JULY 20, 2017 

USDA OIE Alabama Atypical L-type BASE Bovine Spongiform Encephalopathy BSE animal feeds for ruminants rule, 21 CFR 589.200

http://bovineprp.blogspot.com/2017/07/usda-oie-alabama-atypical-l-type-base.html

SUNDAY, JULY 30, 2017 

Do we need to explain the occurrence of atypical scrapie?

http://nor-98.blogspot.com/2017/07/do-we-need-to-explain-occurrence-of.html

Alzheimer’s disease, iatrogenic, and Transmissible Spongiform Encephalopathy TSE Prion disease, that is the question ??? 

>>> The only tenable public line will be that "more research is required’’ <<< 

>>> possibility on a transmissible prion remains open<<< 

O.K., so it’s about 23 years later, so somebody please tell me, when is "more research is required’’ enough time for evaluation ?

[9. Whilst this matter is not at the moment directly concerned with the iatrogenic CJD cases from hgH, there remains a possibility of litigation here, and this presents an added complication. There are also results to be made available shortly (1) concerning a farmer with CJD who had BSE animals, (2) on the possible transmissibility of Alzheimer’s and (3) a CMO letter on prevention of iatrogenic CJD transmission in neurosurgery, all of which will serve to increase media interest.]

https://web.archive.org/web/20170126060344/http://collections.europarchive.org/tna/20080102232842/http://www.bseinquiry.gov.uk/files/yb/1992/11/04001001.pdf

https://web.archive.org/web/20040315075058/http://www.bseinquiry.gov.uk/files/yb/1992/12/16005001.pdf

https://web.archive.org/web/20040315075058/www.bseinquiry.gov.uk/files/yb/1992/12/16005001.pdf

snip...see full Singeltary Nature comment here; 

http://www.nature.com/nature/journal/v525/n7568/full/nature15369.html#/comments

 

see Singeltary comments to Plos ; 

Subject: 1992 IN CONFIDENCE TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES POSSIBILITY ON A TRANSMISSIBLE PRION REMAINS OPEN 

BSE101/1 0136 

IN CONFIDENCE 

CMO 

From: . Dr J S Metiers DCMO 4 

November 1992 

TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES 

1. Thank you for showing me Diana Dunstan's letter. I am glad that MRC have recognised the public sensitivity of these findings and intend to report them in their proper context. 'This hopefully will avoid misunderstanding and possible distortion by the media to portray the results as having more greater significance than the findings so far justify. 

2. Using a highly unusual route of transmission (intra-cerebral injection) the researchers have demonstrated the transmission of a pathological process from two cases one of severe Alzheimer's disease the other of Gerstmann-Straussler disease to marmosets. However they have not demonstrated the transmission of either clinical condition as the "animals were behaving normally when killed". As the report emphasises the unanswered question is whether the disease condition would have revealed itself if the marmosets had lived longer. They are planning further research to see if the conditions, as opposed to the partial pathological process, is transmissible. what are the implications for public health? 

3. The route 'of transmission is very specific and in the natural state of things highly unusual. However it could be argued that the results reveal a potential risk, in that brain tissue from these two patients has been shown to transmit a pathological process. Should therefore brain tissue from such cases be regarded as potentially infective? Pathologists, morticians, neuro surgeons and those assisting at neuro surgical procedures and others coming into contact with "raw" human brain tissue could in theory be at risk. 

However, on a priori grounds given the highly specific route of transmission in these experiments that risk must be negligible if the usual precautions for handling brain tissue are observed. 1 

92/11.4/1.1 

BSE101/1 0137 4. 

The other dimension to consider is the public reaction. To some extent the GSS case demonstrates little more than the transmission of BSE to a pig by intra-cerebral injection. If other prion diseases can be transmitted in this way it is little surprise that some pathological findings observed in GSS were also transmissible to a marmoset. But the transmission of features of Alzheimer's pathology is a different matter, given the much greater frequency of this disease and raises the unanswered question whether some cases are the result of a transmissible prion. 

The only tenable public line will be that "more research is required’’ before that hypothesis could be evaluated. The possibility on a transmissible prion remains open. In the meantime MRC needs carefully to consider the range and sequence of studies needed to follow through from the preliminary observations in these two cases. Not a particularly comfortable message, but until we know more about the causation of Alzheimer's disease the total reassurance is not practical. 

J S METTERS Room 509 Richmond House Pager No: 081-884 3344 Callsign: DOH 832 llllYc!eS 2 92/11.4/1.2 

https://web.archive.org/web/20160320084827/http://collections.europarchive.org/tna/20081106170650/http://www.bseinquiry.gov.uk/files/yb/1992/11/04001001.pdf

>>> The only tenable public line will be that "more research is required’’ <<< 

>>> possibility on a transmissible prion remains open<<< 

O.K., so it’s about 23 years later, so somebody please tell me, when is "more research is required’’ enough time for evaluation ? 

Re-Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy 

Nature 525, 247?250 (10 September 2015) doi:10.1038/nature15369 Received 26 April 2015 Accepted 14 August 2015 Published online 09 September 2015 Updated online 11 September 2015 Erratum (October, 2015) 

snip...see full Singeltary Nature comment here; 

Alzheimer's disease

let's not forget the elephant in the room. curing Alzheimer's would be a great and wonderful thing, but for starters, why not start with the obvious, lets prove the cause or causes, and then start to stop that. think iatrogenic, friendly fire, or the pass it forward mode of transmission. think medical, surgical, dental, tissue, blood, related transmission. think transmissible spongiform encephalopathy aka tse prion disease aka mad cow type disease... 

Commentary: Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy

http://journals.plos.org/plosone/article/comment?id=info:doi/10.1371/annotation/933cc83a-a384-45c3-b3b2-336882c30f9d

https://www.frontiersin.org/articles/10.3389/fnagi.2016.00005/full

Self-Propagative Replication of Ab Oligomers Suggests Potential Transmissibility in Alzheimer Disease 

*** Singeltary comment PLoS *** 

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ? 

Posted by flounder on 05 Nov 2014 at 21:27 GMT 

http://www.plosone.org/annotation/listThread.action?root=82860

Ann N Y Acad Sci. 1982;396:131-43. 

Alzheimer's disease and transmissible virus dementia (Creutzfeldt-Jakob disease). 

Brown P, Salazar AM, Gibbs CJ Jr, Gajdusek DC. 

Abstract 

Ample justification exists on clinical, pathologic, and biologic grounds for considering a similar pathogenesis for AD and the spongiform virus encephalopathies. However, the crux of the comparison rests squarely on results of attempts to transmit AD to experimental animals, and these results have not as yet validated a common etiology. Investigations of the biologic similarities between AD and the spongiform virus encephalopathies proceed in several laboratories, and our own observation of inoculated animals will be continued in the hope that incubation periods for AD may be even longer than those of CJD. 

http://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.1982.tb26849.x/abstract 

Sunday, November 22, 2015 

*** Effect of heating on the stability of amyloid A (AA) fibrils and the intra- and cross-species transmission of AA amyloidosis 

Abstract 

Amyloid A (AA) amyloidosis is a protein misfolding disease characterized by extracellular deposition of AA fibrils. AA fibrils are found in several tissues from food animals with AA amyloidosis. For hygienic purposes, heating is widely used to inactivate microbes in food, but it is uncertain whether heating is sufficient to inactivate AA fibrils and prevent intra- or cross-species transmission. We examined the effect of heating (at 60 °C or 100 °C) and autoclaving (at 121 °C or 135 °C) on murine and bovine AA fibrils using Western blot analysis, transmission electron microscopy (TEM), and mouse model transmission experiments. TEM revealed that a mixture of AA fibrils and amorphous aggregates appeared after heating at 100 °C, whereas autoclaving at 135 °C produced large amorphous aggregates. AA fibrils retained antigen specificity in Western blot analysis when heated at 100 °C or autoclaved at 121 °C, but not when autoclaved at 135 °C. Transmissible pathogenicity of murine and bovine AA fibrils subjected to heating (at 60 °C or 100 °C) was significantly stimulated and resulted in amyloid deposition in mice. Autoclaving of murine AA fibrils at 121 °C or 135 °C significantly decreased amyloid deposition. Moreover, amyloid deposition in mice injected with murine AA fibrils was more severe than that in mice injected with bovine AA fibrils. Bovine AA fibrils autoclaved at 121 °C or 135 °C did not induce amyloid deposition in mice. These results suggest that AA fibrils are relatively heat stable and that similar to prions, autoclaving at 135 °C is required to destroy the pathogenicity of AA fibrils. These findings may contribute to the prevention of AA fibril transmission through food materials to different animals and especially to humans. 

Purchase options Price * Issue Purchase USD 511.00 Article Purchase USD 54.00 

http://www.tandfonline.com/doi/abs/10.3109/13506129.2015.1095735?journalCode=iamy20 

http://betaamyloidcjd.blogspot.com/2015/11/effect-of-heating-on-stability-of.html 

WEDNESDAY, NOVEMBER 1, 2017 

Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies

http://betaamyloidcjd.blogspot.com/2017/11/blood-derived-amyloid-protein-induces.html

*** Transmission of Creutzfeldt-Jakob disease to a chimpanzee by electrodes contaminated during neurosurgery *** 

Gibbs CJ Jr, Asher DM, Kobrine A, Amyx HL, Sulima MP, Gajdusek DC. 

Laboratory of Central Nervous System Studies, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892. Stereotactic multicontact electrodes used to probe the cerebral cortex of a middle aged woman with progressive dementia were previously implicated in the accidental transmission of Creutzfeldt-Jakob disease (CJD) to two younger patients. The diagnoses of CJD have been confirmed for all three cases. More than two years after their last use in humans, after three cleanings and repeated sterilisation in ethanol and formaldehyde vapour, the electrodes were implanted in the cortex of a chimpanzee. Eighteen months later the animal became ill with CJD. This finding serves to re-emphasise the potential danger posed by reuse of instruments contaminated with the agents of spongiform encephalopathies, even after scrupulous attempts to clean them. 

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8006664&dopt=Abstract 

Diagnosis and Reporting of Creutzfeldt-Jakob Disease 

Singeltary, Sr et al. JAMA.2001; 285: 733-734. Vol. 285 No. 6, February 14, 2001 JAMA Diagnosis and Reporting of Creutzfeldt-Jakob Disease 

To the Editor: 

In their Research Letter, Dr Gibbons and colleagues1 reported that the annual US death rate due to Creutzfeldt-Jakob disease (CJD) has been stable since 1985. These estimates, however, are based only on reported cases, and do not include misdiagnosed or preclinical cases. It seems to me that misdiagnosis alone would drastically change these figures. An unknown number of persons with a diagnosis of Alzheimer disease in fact may have CJD, although only a small number of these patients receive the postmortem examination necessary to make this diagnosis. Furthermore, only a few states have made CJD reportable. Human and animal transmissible spongiform encephalopathies should be reportable nationwide and internationally. 

Terry S. Singeltary, Sr Bacliff, Tex 

1. Gibbons RV, Holman RC, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States: 1979-1998. JAMA. 2000;284:2322-2323. 

http://jama.jamanetwork.com/article.aspx?articleid=1031186

END OF UPDATE...TSS

Wednesday, September 21, 2011


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



http://transmissiblespongiformencephalopathy.blogspot.com/2011/09/prionet-canada-researchers-in-vancouver.html



PP1:

Does A “Prion-Like” Mechanism Contribute to the Spreading of Neuropathology in Parkinson’s Disease?

Patrik Brundin Neuronal Survival Unit; Wallenberg Neuroscience Center; Dept of Experimental Medical Science; Lund University; Lund, Sweden

Key words: Parkinson’s disease, prion mechanism, alpha-synuclein

Neuropathological aggregates of alpha-synuclein in neuronal cytoplasm and neurites are typical features of Parkinson’s disease (PD). These Lewy neurites and Lewy bodies are prominent in substantia nigra, where dopaminergic neurons degenerate. With advancing disease they are also found in several other widespread brain areas, and it has been suggested that they appear in anterior olfactory structures and the dorsal motor nucleus of the vagal nerve even before the substantia nigra is affected. Recent studies demonstrated that Lewy bodies and neurites appear in grafted embryonic neurons.1-3 They stain for Thioflavin S, are immunoreactive for alpha-synuclein phosphorylated at serine residue 129 and exhibit a fibrillar structure in the electron microscope.4 From 2 to 5% (frequency increases over time) of the grafted dopaminergic neurons display Lewy bodies, starting around one decade after surgery. Despite these changes, some of the PD grafted patients still exhibit signs of functional recovery beyond a decade after surgery. We, and others, are currently exploring possible mechanisms underlying the transfer of alpha-synuclein between cells and their relevance to how neuropathology normally spreads in the PD brain.5,6 We have observed that alpha-synuclein indeed can transfer between cells in culture. The process is clearly time-dependent and once inside the new cell the imported alpha-synuclein can seed aggregation of endogenous alpha-synuclein. Furthermore, we have observed transfer of host-derived alpha-synuclein into embryonic dopamine neurons grafted into the striatum of transgenic mice expressing human alpha-synuclein. We propose that a “prion-like” disease mechanism might contribute to the pathogenesis of PD and other chronic neurodegenerative disorders.6

References

1. Li, et al. Nat Med 2008; 14:501-3. 2. Kordower, et al. Nat Med 2008; 14:504-6. 3. Kordower, et al. Mov Disord 2008; 23:2303-6. 4. Li, et al. Mov Disord 2010; [Epub ahead of print]. 5. Brundin, et al. Nat Rev Neurosci 2008; 9:741-5. 6. Brundin, et al. Nat Rev Mol Cell Biol 2010; 11:301-7. PP: Plenary Lectures Previously published online: www.landesbioscience.com/journals/prion/article/12765


DOI: 10.4161/pri.4.3.12765

===========================

WP8-4: Prion-like Induction of Alzheimer-type Proteopathy in Transgenic Mice

Lary C. Walker

Yerkes Center; Emory University; Atlanta, GA USA

Key words: abeta, Alzheimer, amyloid, prion, seeding, strains, transgenic, transmission

Alzheimer’s disease and prion disease both involve the accumulation of disease-specific proteins in the brain, suggesting pathogenic commonalities. In Alzheimer’s disease, the aggregation of the protein fragment Aßis a seminal event. Similar to the templated corruption of prion protein, cerebral Aßdeposition can be induced in ß-amyloid precursor protein (APP)-transgenic mice and rats by the intracerebral injection of Aß-rich brain extracts from patients with Alzheimer’s disease or APP-transgenic mice. Our studies indicate that the characteristics of the seeded deposits depend on the source of the seeding extract, the type of host, and the seeded brain region. We are using the amyloid-binding agent Pittsburgh Compound B (PIB) as a marker of a potential AD-specific form of multimeric Aß, and are attempting to induce alternative conformations in the transgenic mouse Aß-seeding model. In addition, we are investigating non-intracerebral routes of administration and the ability of heterologous agents to induce Aßdeposition. Analysis of Aß-seeding in vivo could yield fresh insights into the origins of idiopathic Alzheimer’s disease.

Acknowledgements

Key collaborators on these studies are Mathias Jucker (U. Tübingen), Rebecca Rosen (Emory U.) and Harry LeVine III (U. Kentucky). Supported by NIH RR-00165 and the CART Foundation.

===========================

PPo9-1: Prion-like Propagation of SOD1 Misfolding in Amyotrophic Lateral Sclerosis

Neil R. Cashman

University of British Columbia; Vancouver, British Columbia Canada

Key words: protein misfolding, mechanisms of neurodegeneration, transmission

Prion-like propagation of protein misfolding has been implicated in Alzheimer’s, Parkinson’s and Huntington’s diseases, and the tauopathies. Amyotrophic lateral sclerosis (ALS) is a common and incurable adult motor neuron disease, in which mutation of the free-radical defense enzyme superoxide dismutase 1 (SOD1) is responsible for a subtype of familial ALS (fALS). We demonstrate that transfection of fALS SOD1 mutants G127X and G85R, as well as overexpression of non-mutant wild-type (wt) SOD1, can induce misfolding of natively-structured wild-type SOD1 in human mesenchymal and neural cell lines, as determined by molecular surface immunoreactivity with misfolding-specific monoclonal antibodies (mAbs), acquisition of protease sensitivity (suggesting structural loosening), generation of reactive oxygen species (ROS) and formation of non-native intermolecular disulfide bonds. Serial transmission of SOD1 misfolding was established by incubation in conditioned media from mtSOD1- or wtSOD1-transfected HEK cells, and knockdown of endogenous SOD1 expression in HEK cells by siRNA abrogated the transmission of SOD1 misfolding, consistent with endogenously expressed SOD1 being the substrate for conformational conversion. Pre-incubation of SOD1-transfected conditioned media with poly-specific SOD1 antibodies or misfolding-specific mAbs also blocked intercellular transducing activity, and passive administration of misfolding-specific mAbs extends survival in the G37R transgenic mouse model of ALS. We conclude that misfolded SOD1 participates in a template-directed misfolding cascade which provides a plausable molecular mechanism for progression of familial and sporadic ALS. Antibody-mediated neutralization of SOD1 misfolding propagation could prove beneficial in human ALS.

================

http://www.prion2011.ca/files/PRION_2011_-_Posters_(May_5-11).pdf


Alimentary prion infections: Touch-down in the intestine

Volume 5, Issue 1 January/February/March 2011 Bianca Da Costa Dias, Katarina Jovanovic and Stefan F.T. Weiss View affiliations Hide affiliations Bianca Da Costa DiasSchool of Molecular and Cell Biology; University of the Witwatersrand; Johannesburg, Republic of South Africa Katarina JovanovicSchool of Molecular and Cell Biology; University of the Witwatersrand; Johannesburg, Republic of South Africa Stefan F.T. WeissCorresponding author: stefan.weiss@wits.ac.za School of Molecular and Cell Biology; University of the Witwatersrand; Johannesburg, Republic of South Africa

Neurodegenerative diseases are caused by proteinaceous aggregates, usually consisting of misfolded proteins which are often typified by a high proportion of ß-sheets, which accumulate in the Central Nervous System. These diseases, including Morbus Alzheimer, Parkinson disease and Transmissible Spongiform Encephalopathies (TSEs) also termed prion disorders, afflict a substantial proportion of the human population and as such the etiology and pathogenesis of these diseases has been the focus of mounting research. Although many of these diseases arise from genetic mutations or are sporadic in nature, the possible horizontal transmissibility of neurodegenerative diseases poses a great threat to population health. In this article we discuss recent studies which suggest that the “non-transmissible” status bestowed upon Alzheimer and Parkinson diseases may need to be revised as these diseases have been successfully induced through tissue transplants. Furthermore, we highlight the importance of investigating the “natural” mechanism of prion transmission including peroral and perenteral transmission, proposed routes of gastrointestinal uptake and neuroinvasion of ingested infectious prion proteins. We examine the multitude of factors which may influence oral transmissibility and discuss the zoonotic threats which Chronic Wasting Disease (CWD), Bovine Spongiform Encephalopathy (BSE) and Scrapie may pose resulting in vCJD or related disorders. In addition, we suggest that the 37 kDa/67 kDa laminin receptor on the cell surface of enterocytes, a major cell population in the intestine, may play an important role in the intestinal pathophysiology of alimentary prion infections.

http://www.landesbioscience.com/journals/prion/article/14283


Commentary ß-amyloid oligomers and prion protein: Fatal attraction?

Volume 5, Issue 1 January/February/March 2011 Gianluigi Forloni and Claudia Balducci

Gianluigi Forloni Corresponding author: forloni@marionegri.it

Claudia Balducci Biology of Neurodegenerative Diseases Lab; Department of Neuroscience; “Mario Negri” Institute for Pharmacological Research; Milano, Italy

The relationship between Alzheimer disease (AD) and prion-related encephalopathies (TSE) has been proposed by different points of view. Recently, the scientific attention has been attracted by the results proposing the possibility that PrPc, the protein whose pathologic form is responsible of TSE, can mediated the toxic effect of ß amyloid (Aß) oligomers. The oligomers are considered the culprit of the neurodegenerative process associated to AD, although the pathogenic mechanism activated by these small aggregates remain to be elucidated. In the initial study based on the binding screening PrPc was identified as ligand /receptor of Aß oligomers, while long term potentiation (LTP) analysis in vitro and behavioural studies in vivo, demonstrated that the absence of PrPc abolished the damage induced by Aß oligomers. The high affinity binding Aß oligomers-PrPc has been confirmed, whereas a functional role of this association has been excluded by three different studies. We approached this issue by the direct application of Aß oligomers in the brain followed by the behavioural examination of memory deficits. Our data using PrP knock-out mice suggest that Aß 1-42 oligomers are responsible for cognitive impairment in AD but PrPc is not required for their effect. Similarly, in two other studies the LTP alterations induced by Aß 1-42 oligomers was not influenced by the absence of PrP. Possible explanations of these contradictory results are discussed.

http://www.landesbioscience.com/journals/prion/article/14367/


http://www.landesbioscience.com/journals/prion/toc/volume/5/issue/1/


Wednesday, March 31, 2010

Atypical BSE in Cattle

To date the OIE/WAHO assumes that the human and animal health standards set out in the BSE chapter for classical BSE (C-Type) applies to all forms of BSE which include the H-type and L-type atypical forms. This assumption is scientifically not completely justified and accumulating evidence suggests that this may in fact not be the case. Molecular characterization and the spatial distribution pattern of histopathologic lesions and immunohistochemistry (IHC) signals are used to identify and characterize atypical BSE. Both the L-type and H-type atypical cases display significant differences in the conformation and spatial accumulation of the disease associated prion protein (PrPSc) in brains of afflicted cattle. Transmission studies in bovine transgenic and wild type mouse models support that the atypical BSE types might be unique strains because they have different incubation times and lesion profiles when compared to C-type BSE.

When L-type BSE was inoculated into ovine transgenic mice and Syrian hamster the resulting molecular fingerprint had changed, either in the first or a subsequent passage, from L-type into C-type BSE. In addition, non-human primates are specifically susceptible for atypical BSE as demonstrated by an approximately 50% shortened incubation time for L-type BSE as compared to C-type. Considering the current scientific information available, it cannot be assumed that these different BSE types pose the same human health risks as C-type BSE or that these risks are mitigated by the same protective measures.

This study will contribute to a correct definition of specified risk material (SRM) in atypical BSE. The incumbent of this position will develop new and transfer existing, ultra-sensitive methods for the detection of atypical BSE in tissue of experimentally infected cattle.

http://www.prionetcanada.ca/detail.aspx?menu=5&dt=293380&app=93&cat1=387&tp=20&lk=no&cat2



Wednesday, September 21, 2011

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

http://transmissiblespongiformencephalopathy.blogspot.com/2011/09/prionet-canada-researchers-in-vancouver.html


Thursday, August 12, 2010

Seven main threats for the future linked to prions

First threat

The TSE road map defining the evolution of European policy for protection against prion diseases is based on a certain numbers of hypotheses some of which may turn out to be erroneous. In particular, a form of BSE (called atypical Bovine Spongiform Encephalopathy), recently identified by systematic testing in aged cattle without clinical signs, may be the origin of classical BSE and thus potentially constitute a reservoir, which may be impossible to eradicate if a sporadic origin is confirmed.

***Also, a link is suspected between atypical BSE and some apparently sporadic cases of Creutzfeldt-Jakob disease in humans. These atypical BSE cases constitute an unforeseen first threat that could sharply modify the European approach to prion diseases.

Second threat

snip...

http://www.neuroprion.org/en/np-neuroprion.html


http://prionpathy.blogspot.com/2010/08/seven-main-threats-for-future-linked-to.html


http://prionpathy.blogspot.com/


Rural and Regional Affairs and Transport References Committee

The possible impacts and consequences for public health, trade and agriculture of the Government's decision to relax import restrictions on beef Final report June 2010

2.65 At its hearing on 14 May 2010, the committee heard evidence from Dr Alan Fahey who has recently submitted a thesis on the clinical neuropsychiatric, epidemiological and diagnostic features of Creutzfeldt-Jakob disease.48 Dr Fahey told the committee of his concerns regarding the lengthy incubation period for transmissible spongiform encephalopathies, the inadequacy of current tests and the limited nature of our current understanding of this group of diseases.49

2.66 Dr Fahey also told the committee that in the last two years a link has been established between forms of atypical CJD and atypical BSE. Dr Fahey said that: They now believe that those atypical BSEs overseas are in fact causing sporadic Creutzfeldt-Jakob disease. They were not sure if it was due to mad sheep disease or a different form. If you look in the textbooks it looks like this is just arising by itself. But in my research I have a summary of a document which states that there has never been any proof that sporadic Creutzfeldt-Jakob disease has arisen de novo-has arisen of itself. There is no proof of that. The recent research is that in fact it is due to atypical forms of mad cow disease which have been found across Europe, have been found in America and have been found in Asia. These atypical forms of mad cow disease typically have even longer incubation periods than the classical mad cow disease.50

http://www.aph.gov.au/senate/committee/rrat_ctte/mad_cows/report/report.pdf


14th ICID International Scientific Exchange Brochure -

Final Abstract Number: ISE.114

Session: International Scientific Exchange

Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009

T. Singeltary

Bacliff, TX, USA

Background:

An update on atypical BSE and other TSE in North America. Please remember, the typical U.K. c-BSE, the atypical l-BSE (BASE), and h-BSE have all been documented in North America, along with the typical scrapie's, and atypical Nor-98 Scrapie, and to date, 2 different strains of CWD, and also TME. All these TSE in different species have been rendered and fed to food producing animals for humans and animals in North America (TSE in cats and dogs ?), and that the trading of these TSEs via animals and products via the USA and Canada has been immense over the years, decades.

Methods:

12 years independent research of available data

Results:

I propose that the current diagnostic criteria for human TSEs only enhances and helps the spreading of human TSE from the continued belief of the UKBSEnvCJD only theory in 2009. With all the science to date refuting it, to continue to validate this old myth, will only spread this TSE agent through a multitude of potential routes and sources i.e. consumption, medical i.e., surgical, blood, dental, endoscopy, optical, nutritional supplements, cosmetics etc.

Conclusion:

I would like to submit a review of past CJD surveillance in the USA, and the urgent need to make all human TSE in the USA a reportable disease, in every state, of every age group, and to make this mandatory immediately without further delay. The ramifications of not doing so will only allow this agent to spread further in the medical, dental, surgical arena's. Restricting the reporting of CJD and or any human TSE is NOT scientific. Iatrogenic CJD knows NO age group, TSE knows no boundaries. I propose as with Aguzzi, Asante, Collinge, Caughey, Deslys, Dormont, Gibbs, Gajdusek, Ironside, Manuelidis, Marsh, et al and many more, that the world of TSE Transmissible Spongiform Encephalopathy is far from an exact science, but there is enough proven science to date that this myth should be put to rest once and for all, and that we move forward with a new classification for human and animal TSE that would properly identify the infected species, the source species, and then the route.

http://ww2.isid.org/Downloads/14th_ICID_ISE_Abstracts.pdf


Monday, May 23, 2011

Atypical Prion Diseases in Humans and Animals 2011

Top Curr Chem (2011)

DOI: 10.1007/128_2011_161

# Springer-Verlag Berlin Heidelberg 2011

Michael A. Tranulis, Sylvie L. Benestad, Thierry Baron, and Hans Kretzschmar

Abstract

Although prion diseases, such as Creutzfeldt-Jakob disease (CJD) in humans and scrapie in sheep, have long been recognized, our understanding of their epidemiology and pathogenesis is still in its early stages. Progress is hampered by the lengthy incubation periods and the lack of effective ways of monitoring and characterizing these agents. Protease-resistant conformers of the prion protein (PrP), known as the "scrapie form" (PrPSc), are used as disease markers, and for taxonomic purposes, in correlation with clinical, pathological, and genetic data. In humans, prion diseases can arise sporadically (sCJD) or genetically (gCJD and others), caused by mutations in the PrP-gene (PRNP), or as a foodborne infection, with the agent of bovine spongiform encephalopathy (BSE) causing variant CJD (vCJD). Person-to-person spread of human prion disease has only been known to occur following cannibalism (kuru disease in Papua New Guinea) or through medical or surgical treatment (iatrogenic CJD, iCJD). In contrast, scrapie in small ruminants and chronic wasting disease (CWD) in cervids behave as infectious diseases within these species. Recently, however, so-called atypical forms of prion diseases have been discovered in sheep (atypical/Nor98 scrapie) and in cattle, BSE-H and BSE-L. These maladies resemble sporadic or genetic human prion diseases and might be their animal equivalents. This hypothesis also raises the significant public health question of possible epidemiological links between these diseases and their counterparts in humans.

M.A. Tranulis (*)

Norwegian School of Veterinary Science, Oslo, Norway

e-mail: Michael.Tranulis@nvh.no

S.L. Benestad

Norwegian Veterinary Institute, Oslo, Norway

T. Baron

Agence Nationale de Se´curite´ Sanitaire, ANSES, Lyon, France

H. Kretzschmar

Ludwig-Maximilians University of Munich, Munich, Germany

Keywords Animal Atypical Atypical/Nor98 scrapie BSE-H BSE-L Human Prion disease Prion strain Prion type

http://resources.metapress.com/pdf-preview.axd?code=f433r34h34ugg617&size=largest


snip...SEE MORE HERE ;

http://bse-atypical.blogspot.com/2011/05/atypical-prion-diseases-in-humans-and.html


Friday, October 22, 2010

Peripherally Applied Aß-Containing Inoculates Induce Cerebral ß-Amyloidosis

http://betaamyloidcjd.blogspot.com/2010/10/peripherally-applied-containing.html


Friday, September 3, 2010

Alzheimer's, Autism, Amyotrophic Lateral Sclerosis, Parkinson's, Prionoids, Prionpathy, Prionopathy, TSE

http://betaamyloidcjd.blogspot.com/2010/09/alzheimers-autism-amyotrophic-lateral.html


BSE101/1 0136

IN CONFIDENCE

CMO

From: Dr J S Metters DCMO

4 November 1992

TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES

http://collections.europarchive.org/tna/20081106170650/http://www.bseinquiry.gov.uk/files/yb/1992/11/04001001.pdf



CJD1/9 0185

Ref: 1M51A

IN STRICT CONFIDENCE

From: Dr. A Wight

Date: 5 January 1993

Copies:

Dr Metters

Dr Skinner

Dr Pickles

Dr Morris

Mr Murray

TRANSMISSION OF ALZHEIMER-TYPE PLAQUES TO PRIMATES

http://collections.europarchive.org/tna/20080102191246/http://www.bseinquiry.gov.uk/files/yb/1993/01/05004001.pdf



Wednesday, January 5, 2011

ENLARGING SPECTRUM OF PRION-LIKE DISEASES Prusiner Colby et al 2011 Prions

David W. Colby1,* and Stanley B. Prusiner1,2

http://cshperspectives.cshlp.org/content/3/1/a006833.full.pdf+html



http://betaamyloidcjd.blogspot.com/2011/01/enlarging-spectrum-of-prion-like.html



http://betaamyloidcjd.blogspot.com/



Saturday, June 25, 2011

Transmissibility of BSE-L and Cattle-Adapted TME Prion Strain to Cynomolgus Macaque



"BSE-L in North America may have existed for decades"


http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/transmissibility-of-bse-l-and-cattle.html



Over the next 8-10 weeks, approximately 40% of all the adult mink on the farm died from TME.

snip...

The rancher was a ''dead stock'' feeder using mostly (>95%) downer or dead dairy cattle...



http://web.archive.org/web/20030516051623/http://www.bseinquiry.gov.uk/files/mb/m09/tab05.pdf



Sunday, June 26, 2011

Risk Analysis of Low-Dose Prion Exposures in Cynomolgus Macaque

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/risk-analysis-of-low-dose-prion.html



Thursday, June 23, 2011

Experimental H-type bovine spongiform encephalopathy characterized by plaques and glial- and stellate-type prion protein deposits

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/experimental-h-type-bovine-spongiform.html


Thursday, July 21, 2011

A Second Case of Gerstmann-Sträussler-Scheinker Disease Linked to the G131V Mutation in the Prion Protein Gene in a Dutch Patient Journal of Neuropathology & Experimental Neurology:

August 2011 - Volume 70 - Issue 8 - pp 698-702

http://transmissiblespongiformencephalopathy.blogspot.com/2011/07/second-case-of-gerstmann-straussler.html


Saturday, August 14, 2010

BSE Case Associated with Prion Protein Gene Mutation (g-h-BSEalabama) and VPSPr PRIONPATHY

(see mad cow feed in COMMERCE IN ALABAMA...TSS)

http://prionpathy.blogspot.com/2010/08/bse-case-associated-with-prion-protein.html



Saturday, July 23, 2011

CATTLE HEADS WITH TONSILS, BEEF TONGUES, SPINAL CORD, SPECIFIED RISK MATERIALS (SRM's) AND PRIONS, AKA MAD COW DISEASE

http://transmissiblespongiformencephalopathy.blogspot.com/2011/07/cattle-heads-with-tonsils-beef-tongues.html


Saturday, November 6, 2010

TAFS1 Position Paper on Position Paper on Relaxation of the Feed Ban in the EU Berne, 2010 TAFS

INTERNATIONAL FORUM FOR TRANSMISSIBLE ANIMAL DISEASES AND FOOD SAFETY a non-profit Swiss Foundation

http://madcowfeed.blogspot.com/2010/11/tafs1-position-paper-on-position-paper.html


Archive Number 20101206.4364 Published Date 06-DEC-2010 Subject PRO/AH/EDR> Prion disease update 2010 (11)

PRION DISEASE UPDATE 2010 (11)

http://www.promedmail.org/pls/apex/f?p=2400:1001:5492868805159684::NO::F2400_P1001_BACK_PAGE,F2400_P1001_PUB_MAIL_ID:1000,86129



Wednesday, June 15, 2011

Galveston, Texas - Isle port moves through thousands of heifers headed to Russia, none from Texas, Alabama, or Washington, due to BSE risk factor

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/galveston-texas-isle-port-moves-through.html



MAD COW DISEASE, TEXAS STYLE

http://www.organicconsumers.org/articles/article_23850.cfm



Terry S. Singeltary Sr. has added the following comment:

"According to the World Health Organisation, the future public health threat of vCJD in the UK and Europe and potentially the rest of the world is of concern and currently unquantifiable. However, the possibility of a significant and geographically diverse vCJD epidemic occurring over the next few decades cannot be dismissed.

The key word here is diverse. What does diverse mean? If USA scrapie transmitted to USA bovine does not produce pathology as the UK c-BSE, then why would CJD from there look like UK vCJD?"

http://www.promedmail.org/pls/apex/f?p=2400:1001:568933508083034::NO::F2400_P1001_BACK_PAGE,F2400_P1001_PUB_MAIL_ID:1000,82101



Sunday, April 18, 2010

SCRAPIE AND ATYPICAL SCRAPIE TRANSMISSION STUDIES A REVIEW 2010

http://scrapie-usa.blogspot.com/2010/04/scrapie-and-atypical-scrapie.html


Wednesday, January 19, 2011

EFSA and ECDC review scientific evidence on possible links between TSEs in animals and humans Webnachricht 19 Januar 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-and-ecdc-review-scientific.html



Tuesday, January 18, 2011

Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/agent-strain-variation-in-human-prion.html


EVIDENCE OF SCRAPIE IN SHEEP AS A RESULT OF FOOD BORNE EXPOSURE

This is provided by the statistically significant increase in the incidence of sheep scrape from 1985, as determined from analyses of the submissions made to VI Centres, and from individual case and flock incident studies. ........

http://web.archive.org/web/20010305222246/www.bseinquiry.gov.uk/files/yb/1994/02/07002001.pdf


RISK OF BSE TO SHEEP VIA FEED

http://collections.europarchive.org/tna/20090114022605/http://www.bseinquiry.gov.uk/files/sc/seac31/tab01.pdf



Marion Simmons communicated surprising evidence for oral transmissibility of Nor98/atypical scrapie in neonatal sheep and although bioassay is ongoing, infectivity of the distal ileum of 12 and 24 month infected sheep is positive in Tg338 mice.

http://www.goatbse.eu/site/index.php?option=com_content&view=article&id=94:minutes-workshop-2010&catid=9:popular&Itemid=22



SUMMARY REPORTS OF MAFF BSE TRANSMISSION STUDIES AT THE CVL ;


http://collections.europarchive.org/tna/20090114023010/http://www.bseinquiry.gov.uk/files/sc/seac18/tab02b.pdf



THE RISK TO HUMANS FROM SHEEP;

http://collections.europarchive.org/tna/20090114022915/http://www.bseinquiry.gov.uk/files/sc/seac24/tab03.pdf



EXPERIMENTAL TRANSMISSION OF BSE TO SHEEP

http://collections.europarchive.org/tna/20090114023211/http://www.bseinquiry.gov.uk/files/sc/seac25/tab05.pdf



SHEEP AND BSE

PERSONAL AND CONFIDENTIAL

SHEEP AND BSE

A. The experimental transmission of BSE to sheep.

Studies have shown that the ''negative'' line NPU flock of Cheviots can be experimentally infected with BSE by intracerebral (ic) or oral challenge (the latter being equivalent to 0.5 gram of a pool of four cow brains from animals confirmed to have BSE).

http://collections.europarchive.org/tna/20090506010048/http://www.bseinquiry.gov.uk/files/sc/seac33/tab02.pdf



RB264

BSE - TRANSMISSION STUDIES

http://collections.europarchive.org/tna/20090113230127/http://www.bseinquiry.gov.uk/files/sc/Seac06/tab06.pdf



1: J Infect Dis 1980 Aug;142(2):205-8

Oral transmission of kuru, Creutzfeldt-Jakob disease, and scrapie to nonhuman primates.

Gibbs CJ Jr, Amyx HL, Bacote A, Masters CL, Gajdusek DC.

Kuru and Creutzfeldt-Jakob disease of humans and scrapie disease of sheep and goats were transmitted to squirrel monkeys (Saimiri sciureus) that were exposed to the infectious agents only by their nonforced consumption of known infectious tissues. The asymptomatic incubation period in the one monkey exposed to the virus of kuru was 36 months; that in the two monkeys exposed to the virus of Creutzfeldt-Jakob disease was 23 and 27 months, respectively; and that in the two monkeys exposed to the virus of scrapie was 25 and 32 months, respectively. Careful physical examination of the buccal cavities of all of the monkeys failed to reveal signs or oral lesions. One additional monkey similarly exposed to kuru has remained asymptomatic during the 39 months that it has been under observation.

snip...

The successful transmission of kuru, Creutzfeldt-Jakob disease, and scrapie by natural feeding to squirrel monkeys that we have reported provides further grounds for concern that scrapie-infected meat may occasionally give rise in humans to Creutzfeldt-Jakob disease.

PMID: 6997404

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6997404&dopt=Abstract



12/10/76 AGRICULTURAL RESEARCH COUNCIL REPORT OF THE ADVISORY COMMITTE ON SCRAPIE Office Note CHAIRMAN: PROFESSOR PETER WILDY

snip...

A The Present Position with respect to Scrapie A] The Problem Scrapie is a natural disease of sheep and goats. It is a slow and inexorably progressive degenerative disorder of the nervous system and it ia fatal. It is enzootic in the United Kingdom but not in all countries. The field problem has been reviewed by a MAFF working group (ARC 35/77). It is difficult to assess the incidence in Britain for a variety of reasons but the disease causes serious financial loss; it is estimated that it cost Swaledale breeders alone $l.7 M during the five years 1971-1975. A further inestimable loss arises from the closure of certain export markets, in particular those of the United States, to British sheep. It is clear that scrapie in sheep is important commercially and for that reason alone effective measures to control it should be devised as quickly as possible. Recently the question has again been brought up as to whether scrapie is transmissible to man. This has followed reports that the disease has been transmitted to primates.

One particularly lurid speculation (Gajdusek 1977) conjectures that the agents of scrapie, kuru, Creutzfeldt-Jakob disease and transmissible encephalopathy of mink are varieties of a single "virus". The U.S. Department of Agriculture concluded that it could "no longer justify or permit scrapie-blood line and scrapie-exposed sheep and goats to be processed for human or animal food at slaughter or rendering plants" (ARC 84/77)" The problem is emphasised by the finding that some strains of scrapie produce lesions identical to the once which characterise the human dementias" Whether true or not. the hypothesis that these agents might be transmissible to man raises two considerations. First, the safety of laboratory personnel requires prompt attention. Second, action such as the "scorched meat" policy of USDA makes the solution of the acrapie problem urgent if the sheep industry is not to suffer grievously.

snip...

76/10.12/4.6

http://web.archive.org/web/20010305223125/www.bseinquiry.gov.uk/files/yb/1976/10/12004001.pdf



Nature. 1972 Mar 10;236(5341):73-4.

Transmission of scrapie to the cynomolgus monkey (Macaca fascicularis).

Gibbs CJ Jr, Gajdusek DC. Nature 236, 73 - 74 (10 March 1972); doi:10.1038/236073a0

Transmission of Scrapie to the Cynomolgus Monkey (Macaca fascicularis)

C. J. GIBBS jun. & D. C. GAJDUSEK National Institute of Neurological Diseases and Stroke, National Institutes of Health, Bethesda, Maryland

SCRAPIE has been transmitted to the cynomolgus, or crab-eating, monkey (Macaca fascicularis) with an incubation period of more than 5 yr from the time of intracerebral inoculation of scrapie-infected mouse brain. The animal developed a chronic central nervous system degeneration, with ataxia, tremor and myoclonus with associated severe scrapie-like pathology of intensive astroglial hypertrophy and proliferation, neuronal vacuolation and status spongiosus of grey matter. The strain of scrapie virus used was the eighth passage in Swiss mice (NIH) of a Compton strain of scrapie obtained as ninth intracerebral passage of the agent in goat brain, from Dr R. L. Chandler (ARC, Compton, Berkshire).

http://www.nature.com/nature/journal/v236/n5341/abs/236073a0.html


Epidemiology of Scrapie in the United States 1977

http://web.archive.org/web/20030513212324/http://www.bseinquiry.gov.uk/files/mb/m08b/tab64.pdf


Thursday, July 14, 2011

Histopathological Studies of "CH1641-Like" Scrapie Sources Versus Classical Scrapie and BSE Transmitted to Ovine Transgenic Mice (TgOvPrP4)

http://transmissiblespongiformencephalopathy.blogspot.com/2011/07/histopathological-studies-of-ch1641.html


UPDATE TSE PRION DISEASE NORTH AMERICA...FOR YOU INFORMATION, things you might not be aware of...TSS


Monday, June 27, 2011

Zoonotic Potential of CWD: Experimental Transmissions to Non-Human Primates

http://chronic-wasting-disease.blogspot.com/2011/06/zoonotic-potential-of-cwd-experimental.html


UPDATED DATA ON 2ND CWD STRAIN

Wednesday, September 08, 2010

CWD PRION CONGRESS SEPTEMBER 8-11 2010

http://chronic-wasting-disease.blogspot.com/2010/09/cwd-prion-2010.html


Thursday, April 03, 2008

A prion disease of cervids: Chronic wasting disease

2008 1: Vet Res. 2008 Apr 3;39(4):41

A prion disease of cervids: Chronic wasting disease

Sigurdson CJ.

snip...

*** twenty-seven CJD patients who regularly consumed venison were reported to the Surveillance Center***,

snip...

full text ;

http://chronic-wasting-disease.blogspot.com/2008/04/prion-disease-of-cervids-chronic.html


1989

IN CONFIDENCE

Perceptions of unconventional slow virus diseases of animals in the USA

Spraker suggested an interesting explanation for the occurrence of CWD. The deer pens at the Foot Hills Campus were built some 30-40 years ago by a Dr. Bob Davis. At or about that time, allegedly, some scrapie work was conducted at this site. When deer were introduced to the pens they occupied ground that had previously been occupied by sheep. Whether they were scrapie infected sheep or not is unclear.

http://collections.europarchive.org/tna/20080102193705/http://www.bseinquiry.gov.uk/files/mb/m11b/tab01.pdf



http://wildlife.state.co.us/NR/rdonlyres/C82EB818-90C6-4D85-897E-9CE279546CCB/0/JWDEpiCWD.pdf



CJD9/10022

October 1994

Mr R.N. Elmhirst Chairman British Deer Farmers Association Holly Lodge Spencers Lane BerksWell Coventry CV7 7BZ

Dear Mr Elmhirst,

CREUTZFELDT-JAKOB DISEASE (CJD) SURVEILLANCE UNIT REPORT

Thank you for your recent letter concerning the publication of the third annual report from the CJD Surveillance Unit. I am sorry that you are dissatisfied with the way in which this report was published.

The Surveillance Unit is a completely independant outside body and the Department of Health is committed to publishing their reports as soon as they become available. In the circumstances it is not the practice to circulate the report for comment since the findings of the report would not be amended. In future we can ensure that the British Deer Farmers Association receives a copy of the report in advance of publication.

The Chief Medical Officer has undertaken to keep the public fully informed of the results of any research in respect of CJD. This report was entirely the work of the unit and was produced completely independantly of the the Department.

The statistical results reqarding the consumption of venison was put into perspective in the body of the report and was not mentioned at all in the press release. Media attention regarding this report was low key but gave a realistic presentation of the statistical findings of the Unit. This approach to publication was successful in that consumption of venison was highlighted only once by the media ie. in the News at one television proqramme.

I believe that a further statement about the report, or indeed statistical links between CJD and consumption of venison, would increase, and quite possibly give damaging credence, to the whole issue. From the low key media reports of which I am aware it seems unlikely that venison consumption will suffer adversely, if at all.

http://web.archive.org/web/20030511010117/http://www.bseinquiry.gov.uk/files/yb/1994/10/00003001.pdf




PLUS, THE CDC DID NOT PUT THIS WARNING OUT FOR THE WELL BEING OF THE DEER AND ELK ;



Thursday, May 26, 2011

Travel History, Hunting, and Venison Consumption Related to Prion Disease Exposure, 2006-2007 FoodNet Population Survey

Journal of the American Dietetic Association Volume 111, Issue 6 , Pages 858-863, June 2011.

http://transmissiblespongiformencephalopathy.blogspot.com/2011/05/travel-history-hunting-and-venison.html



NOR IS THE FDA recalling this CWD positive elk meat for the well being of the dead elk ;



Wednesday, March 18, 2009

Noah's Ark Holding, LLC, Dawson, MN RECALL Elk products contain meat derived from an elk confirmed to have CWD NV, CA, TX, CO, NY, UT, FL, OK RECALLS AND FIELD CORRECTIONS: FOODS CLASS II

http://chronic-wasting-disease.blogspot.com/2009/03/noahs-ark-holding-llc-dawson-mn-recall.html


CENTAUR GLOBAL NETWORK INFORMATION

[ProMED-mail thanks Terry S Singeltary Sr for drawing attention to this comprehensive document which provides a current evaluation of experimental work designed to explore the zoonotic potential of the various recently recognised TSEs of domestic and other animals. It is concluded that at present the only TSE agent demonstrated to be zoonotic is the classical BSE agent. Nor can it be entirely excluded at the present time that a small proportion of cases of sporadic CJD may be environmentally acquired. - Mod.CP]

http://centaur.vri.cz.web.atin.cz/docs/cnfi/2011-06-16-110.pdf


CANADA CJD UPDATE 2011

CJD Deaths Reported by CJDSS1, 1994-20112 As of January 31, 2011

3. Final classification of 49 cases from 2009, 2010, 2011 is pending.

snip...

http://www.phac-aspc.gc.ca/hcai-iamss/cjd-mcj/cjdss-ssmcj/pdf/stats_0111-eng.pdf


USA 2011

USA

National Prion Disease Pathology Surveillance Center

Cases Examined1

(November 1, 2010)

Year Total Referrals2 Prion Disease Sporadic Familial Iatrogenic vCJD

1996 ; earlier 51 33 28 5 0 0

1997 114 68 59 9 0 0

1998 87 51 43 7 1 0

1999 121 73 65 8 0 0

2000 146 103 89 14 0 0

2001 209 119 109 10 0 0

2002 248 149 125 22 2 0

2003 274 176 137 39 0 0

2004 325 186 164 21 0 13

2005 344 194 157 36 1 0

2006 383 197 166 29 0 24

2007 377 214 187 27 0 0

2008 394 231 205 25 0 0

2009 425 258 215 43 0 0

2010 333 213 158 33 0 0

TOTAL 38315 22656 1907 328 4 3

1 Listed based on the year of death or, if not available, on year of referral;

2 Cases with suspected prion disease for which brain tissue and/or blood (in familial cases) were submitted;

3 Disease acquired in the United Kingdom;

4 Disease was acquired in the United Kingdom in one case and in Saudi Arabia in the other case;

5 Includes 18 cases in which the diagnosis is pending, and 18 inconclusive cases;

6 Includes 23 (22 from 2010) cases with type determination pending in which the diagnosis of vCJD has been excluded.

http://www.cjdsurveillance.com/pdf/case-table.pdf


Please notice where sporadic CJD cases in 1996 went from 28 cases, to 215 cases in 2009, the highest recorded year to date. sporadic CJD is on a steady rise, and has been since 1996.

I also urge you to again notice these disturbing factors in lines 5 and 6 ;

5 Includes 18 cases in which the diagnosis is pending, and 18 inconclusive cases;

6 Includes 23 (22 from 2010) cases with type determination pending in which the diagnosis of vCJD has been excluded.


========end=====tss=====2011


UPDATE JULY 2011 MORE OF THE "PENDING CLASSIFICATION CREUTZFELDT JAKOB DISEASE'' STEADY INCREASING...TSS

case; 5 Includes 13 cases in which the diagnosis is pending, and 18 inconclusive cases; 6 Includes 18 (15 from 2011) cases with type determination pending in which the diagnosis of vCJD has been excluded.

http://www.cjdsurveillance.com/pdf/case-table.pdf


Saturday, March 5, 2011

MAD COW ATYPICAL CJD PRION TSE CASES WITH CLASSIFICATIONS PENDING ON THE RISE IN NORTH AMERICA

http://transmissiblespongiformencephalopathy.blogspot.com/2011/03/mad-cow-atypical-cjd-prion-tse-cases.html



Sunday, August 21, 2011

The British disease, or a disease gone global, The TSE Prion Disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/british-disease-or-disease-gone-global.html



Thursday, August 4, 2011

Terry Singeltary Sr. on the Creutzfeldt-Jakob Disease Public Health Crisis, Date aired: 27 Jun 2011

see video here ;

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/terry-singeltary-sr-on-creutzfeldt.html




Saturday, January 2, 2010

Human Prion Diseases in the United States January 1, 2010 ***FINAL***

http://prionunitusaupdate2008.blogspot.com/2010/01/human-prion-diseases-in-united-states.html




Manuscript Draft Manuscript Number: Title: HUMAN and ANIMAL TSE Classifications i.e. mad cow disease and the UKBSEnvCJD only theory Article Type: Personal View Corresponding Author: Mr. Terry S. Singeltary, Corresponding Author's Institution: na First Author: Terry S Singeltary, none Order of Authors: Terry S Singeltary, none; Terry S. Singeltary Abstract: TSEs have been rampant in the USA for decades in many species, and they all have been rendered and fed back to animals for human/animal consumption. I propose that the current diagnostic criteria for human TSEs only enhances and helps the spreading of human TSE from the continued belief of the UKBSEnvCJD only theory in 2007.

http://www.regulations.gov/fdmspublic/ContentViewer?objectId=090000648027c28e&disposition=attachment&contentType=pdf




my comments to PLosone here ;


http://www.plosone.org/annotation/listThread.action?inReplyTo=info%3Adoi%2F10.1371%2Fannotation%2F04ce2b24-613d-46e6-9802-4131e2bfa6fd&root=info%3Adoi%2F10.1371%2Fannotation%2F04ce2b24-613d-46e6-9802-4131e2bfa6fd




Sunday, August 09, 2009

CJD...Straight talk with...James Ironside...and...Terry Singeltary... 2009

http://creutzfeldt-jakob-disease.blogspot.com/2009/08/cjdstraight-talk-withjames.html



Tuesday, August 18, 2009

BSE-The Untold Story - joe gibbs and singeltary 1999 - 2009

http://madcowusda.blogspot.com/2009/08/bse-untold-story-joe-gibbs-and.html



Friday, February 11, 2011

Creutzfeldt-Jakob disease (CJD) biannual update (2010/1) Emerging infections/CJD

http://creutzfeldt-jakob-disease.blogspot.com/2011/02/creutzfeldt-jakob-disease-cjd-biannual.html



Friday, April 15, 2011

PRION TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHY PROJECTS, RESEARCH FUNDING, BSE VOLUNTARY TESTING UPDATE IN NORTH AMERICA 2011

http://prionunitusaupdate2008.blogspot.com/2011/04/prion-transmissible-spongiform.html



PRION TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHY RESEARCH FUNDING U.S.A.

COMPARE TO USA PRION FUNDING 2011

"which includes the ___elimination___ of Prion activities ($5,473,000),"

All Other Emerging and Zoonotic Infectious Diseases CDC‘s FY 2012 request of $52,658,000 for all other emerging and zoonotic infectious disease activities is a decrease of $13,607,000 below the FY 2010 level, which includes the elimination of Prion activities ($5,473,000), a reduction for other cross-cutting infectious disease activities, and administrative savings. These funds support a range of critical emerging and zoonotic infectious disease programs such Lyme Disease, Chronic Fatigue Syndrome, and Special Pathogens, as well as other activities described below.

http://www.cdc.gov/fmo/topic/Budget%20Information/appropriations_budget_form_pdf/FY2012_CDC_CJ_Final.pdf



THE PATHOLOGICAL PROTEIN

BY Philip Yam

Yam Philip Yam News Editor Scientific American www.sciam.com

Answering critics like Terry Singeltary, who feels that the U.S. under- counts CJD, Schonberger conceded that the current surveillance system has errors but stated that most of the errors will be confined to the older population.

CHAPTER 14

Laying Odds

Are prion diseases more prevalent than we thought?

Researchers and government officials badly underestimated the threat that mad cow disease posed when it first appeared in Britain. They didn't think bovine spongiform encephalopathy was a zoonosis-an animal disease that can sicken people. The 1996 news that BSE could infect humans with a new form of Creutzfeldt-Jakob disease stunned the world. It also got some biomedical researchers wondering whether sporadic CJD may really be a manifestation of a zoonotic sickness. Might it be caused by the ingestion of prions, as variant CJD is?

Revisiting Sporadic CJD

It's not hard to get Terry Singeltary going. "I have my conspiracy theories," admitted the 49-year-old Texan.1 Singeltary is probably the nation's most relentless consumer advocate when it comes to issues in prion diseases. He has helped families learn about the sickness and coordinated efforts with support groups such as CJD Voice and the CJD Foundation. He has also connected with others who are critical of the American way of handling the threat of prion diseases. Such critics include Consumers Union's Michael Hansen, journalist John Stauber, and Thomas Pringle, who used to run the voluminous www.madcow. org Web site. These three lend their expertise to newspaper and magazine stories about prion diseases, and they usually argue that prions represent more of a threat than people realize, and that the government has responded poorly to the dangers because it is more concerned about protecting the beef industry than people's health.

Singeltary has similar inclinations. ...

snip...

THE PATHOLOGICAL PROTEIN

Hardcover, 304 pages plus photos and illustrations. ISBN 0-387-95508-9

June 2003

BY Philip Yam

CHAPTER 14 LAYING ODDS

Answering critics like Terry Singeltary, who feels that the U.S. under- counts CJD, Schonberger conceded that the current surveillance system has errors but stated that most of the errors will be confined to the older population.

http://www.thepathologicalprotein.com/


http://books.google.com/books?id=ePbrQNFrHtoC&pg=PA223&lpg=PA223&dq=the+pathological+protein+laying+odds+It%E2%80%99s+not+hard+to+get+Terry+Singeltary+going&source=bl&ots=um0PFAZSZD&sig=JWaGR7M7-1WeAr2qAXq8D6J_jak&hl=en&ei=MhtjS8jMJM2ztgeFoa2iBg&sa=X&oi=book_result&ct=result&resnum=1&ved=0CAcQ6AEwAA#v=onepage&q=&f=false


http://www.springerlink.com/content/r2k2622661473336/fulltext.pdf?page=1


http://www.thepathologicalprotein.com/


http://prionunitusaupdate2008.blogspot.com/2009/04/national-prion-disease-pathology.html


Newsdesk

The Lancet Infectious Diseases, Volume 3, Issue 8, Page 463, August 2003 doi:10.1016/S1473-3099(03)00715-1Cite or Link Using DOI

Tracking spongiform encephalopathies in North America

Xavier Bosch

"My name is Terry S Singeltary Sr, and I live in Bacliff, Texas. I lost my mom to hvCJD (Heidenhain variant CJD) and have been searching for answers ever since. What I have found is that we have not been told the truth. CWD in deer and elk is a small portion of a much bigger problem." 49-year-old Singeltary is one of a number of people who have remained largely unsatisfied after being told that a close relative died from a rapidly progressive dementia compatible with spontaneous Creutzfeldt-Jakob disease (CJD). So he decided to gather hundreds of documents on transmissible spongiform encephalopathies (TSE) and realised that if Britons could get variant CJD from bovine spongiform encephalopathy (BSE), Americans might get a similar disorder from chronic wasting disease (CWD)-the relative of mad cow disease seen among deer and elk in the USA. Although his feverish.

http://linkinghub.elsevier.com/retrieve/pii/S1473309903007151


http://www.thelancet.com/journals/laninf/article/PIIS1473-3099(03)00715-1/fulltext


http://www.mdconsult.com/das/article/body/180784492-2/jorg=journal&source=&sp=13979213&sid=0/N/368742/1.html?issn=14733099



Diagnosis and Reporting of Creutzfeldt-Jakob Disease


Singeltary, Sr et al. JAMA.2001; 285: 733-734. Vol. 285 No. 6, February 14, 2001 JAMA

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

To the Editor: In their Research Letter, Dr Gibbons and colleagues1 reported that the annual US death rate due to Creutzfeldt-Jakob disease (CJD) has been stable since 1985. These estimates, however, are based only on reported cases, and do not include misdiagnosed or preclinical cases. It seems to me that misdiagnosis alone would drastically change these figures. An unknown number of persons with a diagnosis of Alzheimer disease in fact may have CJD, although only a small number of these patients receive the postmortem examination necessary to make this diagnosis. Furthermore, only a few states have made CJD reportable. Human and animal transmissible spongiform encephalopathies should be reportable nationwide and internationally.

Terry S. Singeltary, Sr Bacliff, Tex

1. Gibbons RV, Holman RC, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States: 1979-1998. JAMA. 2000;284:2322-2323. FREE FULL TEXT

http://jama.ama-assn.org/cgi/content/extract/285/6/733?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=singeltary&searchid=1&FIRSTINDEX=0&resourcetype=HWCIT



http://jama.ama-assn.org/cgi/content/full/285/6/733?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=singeltary&searchid=1&FIRSTINDEX=0&resourcetype=HWCIT



RE-Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States




26 March 2003



Terry S. Singeltary, retired (medically) CJD WATCH



I lost my mother to hvCJD (Heidenhain Variant CJD). I would like to comment on the CDC's attempts to monitor the occurrence of emerging forms of CJD. Asante, Collinge et al [1] have reported that BSE transmission to the 129-methionine genotype can lead to an alternate phenotype that is indistinguishable from type 2 PrPSc, the commonest sporadic CJD. However, CJD and all human TSEs are not reportable nationally. CJD and all human TSEs must be made reportable in every state and internationally. I hope that the CDC does not continue to expect us to still believe that the 85%+ of all CJD cases which are sporadic are all spontaneous, without route/source. We have many TSEs in the USA in both animal and man. CWD in deer/elk is spreading rapidly and CWD does transmit to mink, ferret, cattle, and squirrel monkey by intracerebral inoculation. With the known incubation periods in other TSEs, oral transmission studies of CWD may take much longer. Every victim/family of CJD/TSEs should be asked about route and source of this agent. To prolong this will only spread the agent and needlessly expose others. In light of the findings of Asante and Collinge et al, there should be drastic measures to safeguard the medical and surgical arena from sporadic CJDs and all human TSEs. I only ponder how many sporadic CJDs in the USA are type 2 PrPSc?



http://www.neurology.org/cgi/eletters/60/2/176




DER SPIEGEL (9/2001) - 24.02.2001 (9397 Zeichen) USA: Loch in der Mauer Die BSE-Angst erreicht Amerika: Trotz strikter Auflagen gelangte in Texas verbotenes Tiermehl ins Rinderfutter - die Kontrollen der Aufsichtsbehördensind lax.Link auf diesen Artikel im Archiv:

http://service.spiegel.de/digas/find?DID=18578755


"Löcher wie in einem Schweizer Käse" hat auch Terry Singeltary im Regelwerk der FDA ausgemacht. Der Texaner kam auf einem tragischen Umweg zu dem Thema: Nachdem seine Mutter 1997 binnen weniger Wochen an der Creutzfeldt-Jakob-Krankheit gestorben war, versuchte er, die Ursachen der Infektion aufzuspüren. Er klagte auf die Herausgabe von Regierungsdokumenten und arbeitete sich durch Fachliteratur; heute ist er überzeugt, dass seine Mutter durch die stetige Einnahme von angeblich kräftigenden Mitteln erkrankte, in denen - völlig legal - Anteile aus Rinderprodukten enthalten sind.

Von der Fachwelt wurde Singeltary lange als versponnener Außenseiter belächelt. Doch mittlerweile sorgen sich auch Experten, dass ausgerechnet diese verschreibungsfreien Wundercocktails zur Stärkung von Intelligenz, Immunsystem oder Libido von den Importbeschränkungen ausgenommen sind. Dabei enthalten die Pillen und Ampullen, die in Supermärkten verkauft werden, exotische Mixturen aus Rinderaugen; dazu Extrakte von Hypophyse oder Kälberföten, Prostata, Lymphknoten und gefriergetrocknetem Schweinemagen. In die USA hereingelassen werden auch Blut, Fett, Gelatine und Samen. Diese Stoffe tauchen noch immer in US-Produkten auf, inklusive Medizin und Kosmetika. Selbst in Impfstoffen waren möglicherweise gefährliche Rinderprodukte enthalten. Zwar fordert die FDA schon seit acht Jahren die US-Pharmaindustrie auf, keine Stoffe aus Ländern zu benutzen, in denen die Gefahr einer BSE-Infizierung besteht. Aber erst kürzlich verpflichteten sich fünf Unternehmen, darunter Branchenführer wie GlaxoSmithKline, Aventis und American Home Products, ihre Seren nur noch aus unverdächtigem Material herzustellen.


"Its as full of holes as Swiss Cheese" says Terry Singeltary of the FDA regulations. ...


http://www.spiegel.de/spiegel/print/d-18578755.html


http://wissen.spiegel.de/wissen/image/show.html?did=18578755&aref=image024/E0108/SCSP200100901440145.pdf&thumb=false



http://service.spiegel.de/digas/servlet/find/DID=18578755



Suspect symptoms

What if you can catch old-fashioned CJD by eating meat from a sheep infected with scrapie?

28 Mar 01

Like lambs to the slaughter 31 March 2001 by Debora MacKenzie Magazine issue 2284. Subscribe and get 4 free issues. FOUR years ago, Terry Singeltary watched his mother die horribly from a degenerative brain disease. Doctors told him it was Alzheimer's, but Singeltary was suspicious. The diagnosis didn't fit her violent symptoms, and he demanded an autopsy. It showed she had died of sporadic Creutzfeldt-Jakob disease.

Most doctors believe that sCJD is caused by a prion protein deforming by chance into a killer. But Singeltary thinks otherwise. He is one of a number of campaigners who say that some sCJD, like the variant CJD related to BSE, is caused by eating meat from infected animals. Their suspicions have focused on sheep carrying scrapie, a BSE-like disease that is widespread in flocks across Europe and North America.

Now scientists in France have stumbled across new evidence that adds weight to the campaigners' fears. To their complete surprise, the researchers found that one strain of scrapie causes the same brain damage in mice as sCJD.

"This means we cannot rule out that at least some sCJD may be caused by some strains of scrapie," says team member Jean-Philippe Deslys of the French Atomic Energy Commission's medical research laboratory in Fontenay-aux-Roses, south-west of Paris. Hans Kretschmar of the University of Göttingen, who coordinates CJD surveillance in Germany, is so concerned by the findings that he now wants to trawl back through past sCJD cases to see if any might have been caused by eating infected mutton or lamb.

Scrapie has been around for centuries and until now there has been no evidence that it poses a risk to human health. But if the French finding means that scrapie can cause sCJD in people, countries around the world may have overlooked a CJD crisis to rival that caused by BSE.

Deslys and colleagues were originally studying vCJD, not sCJD. They injected the brains of macaque monkeys with brain from BSE cattle, and from French and British vCJD patients. The brain damage and clinical symptoms in the monkeys were the same for all three. Mice injected with the original sets of brain tissue or with infected monkey brain also developed the same symptoms.

As a control experiment, the team also injected mice with brain tissue from people and animals with other prion diseases: a French case of sCJD; a French patient who caught sCJD from human-derived growth hormone; sheep with a French strain of scrapie; and mice carrying a prion derived from an American scrapie strain. As expected, they all affected the brain in a different way from BSE and vCJD. But while the American strain of scrapie caused different damage from sCJD, the French strain produced exactly the same pathology.

"The main evidence that scrapie does not affect humans has been epidemiology," says Moira Bruce of the neuropathogenesis unit of the Institute for Animal Health in Edinburgh, who was a member of the same team as Deslys. "You see about the same incidence of the disease everywhere, whether or not there are many sheep, and in countries such as New Zealand with no scrapie." In the only previous comparisons of sCJD and scrapie in mice, Bruce found they were dissimilar.

But there are more than 20 strains of scrapie, and six of sCJD. "You would not necessarily see a relationship between the two with epidemiology if only some strains affect only some people," says Deslys. Bruce is cautious about the mouse results, but agrees they require further investigation. Other trials of scrapie and sCJD in mice, she says, are in progress.

People can have three different genetic variations of the human prion protein, and each type of protein can fold up two different ways. Kretschmar has found that these six combinations correspond to six clinical types of sCJD: each type of normal prion produces a particular pathology when it spontaneously deforms to produce sCJD.

But if these proteins deform because of infection with a disease-causing prion, the relationship between pathology and prion type should be different, as it is in vCJD. "If we look at brain samples from sporadic CJD cases and find some that do not fit the pattern," says Kretschmar, "that could mean they were caused by infection."

There are 250 deaths per year from sCJD in the US, and a similar incidence elsewhere. Singeltary and other US activists think that some of these people died after eating contaminated meat or "nutritional" pills containing dried animal brain. Governments will have a hard time facing activists like Singeltary if it turns out that some sCJD isn't as spontaneous as doctors have insisted.

Deslys's work on macaques also provides further proof that the human disease vCJD is caused by BSE. And the experiments showed that vCJD is much more virulent to primates than BSE, even when injected into the bloodstream rather than the brain. This, says Deslys, means that there is an even bigger risk than we thought that vCJD can be passed from one patient to another through contaminated blood transfusions and surgical instruments.

http://www.newscientist.com/article/mg16922840.300-like-lambs-to-the-slaughter.html



2 January 2000

British Medical Journal

U.S. Scientist should be concerned with a CJD epidemic in the U.S., as well


http://www.bmj.com/cgi/eletters/320/7226/8/b#6117



15 November 1999

British Medical Journal

vCJD in the USA * BSE in U.S.


http://www.bmj.com/cgi/eletters/319/7220/1312/b#5406



layperson


Terry S. Singeltary Sr.


UPDATE OCTOBER 4, 2011


04/10/2011


New research shows Alzheimer's disease may originate from the infectious prion disease.

Alzheimer's disease may originate in a similar form to the infectious prion disease, according to new research.
The University of Texas Health Science Centre has published a study showing a potentially infectious spreading of Alzheimer's in animal models.

"Our findings open the possibility that some of the sporadic Alzheimer's cases may arise from an infectious process, which occurs with other neurological diseases such as mad cow and its human form, Creutzfeldt-Jakob disease," stated Claudio Soto, Ph.D., professor of neurology at the University of Texas....

http://www.barchester.com/Healthcare-News/Alzheimer's-disease-may-be-transmissible/376/4827


Tuesday, October 4, 2011

De novo induction of amyloid-β deposition in vivo

Molecular Psychiatry advance online publication 4 October 2011; doi: 10.1038/mp.2011.120


Molecular Psychiatry advance online publication 4 October 2011; doi: 10.1038/mp.2011.120


De novo induction of amyloid-ß deposition in vivo

R Morales1,2, C Duran-Aniotz1,3, J Castilla2,4, L D Estrada2,5 and C Soto1,2

1Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, TX, USA 2University of Texas Medical Branch at Galveston, Galveston, TX, USA 3Universidad de Los Andes, Facultad de Medicina. Av. San Carlos de Apoquindo 2200, Las Condes, Santiago, Chile 4CIC bioGUNE, Parque Tecnologico de Biskaia, Ed 800, 48160 Derio and IKERBASQUE, Basque Foundation for Science, 48011 Bilbao, Spain



Correspondence: Dr C Soto, Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, 6431 Fannin St, Houston, TX 77030, USA. E-mail: Claudio.Soto@uth.tmc.edu


5Current address: Laboratorio de Señalización Celular, Centro de Envejecimiento y Regeneración. P. Universidad Catolica de Chile, Santiago, Chile.


Received 8 March 2011; Revised 15 August 2011; Accepted 25 August 2011; Published online 4 October 2011.


Abstract


Alzheimer's disease (AD), the most common type of senile dementia, is associated to the build-up of misfolded amyloid-ß (Aß) in the brain. Although compelling evidences indicate that the misfolding and oligomerization of Aß is the triggering event in AD, the mechanisms responsible for the initiation of Aß accumulation are unknown. In this study, we show that Aß deposition can be induced by injection of AD brain extracts into animals, which, without exposure to this material, will never develop these alterations. The accumulation of Aß deposits increased progressively with the time after inoculation, and the Aß lesions were observed in brain areas far from the injection site. Our results suggest that some of the typical brain abnormalities associated with AD can be induced by a prion-like mechanism of disease transmission through propagation of protein misfolding. These findings may have broad implications for understanding the molecular mechanisms responsible for the initiation of AD, and may contribute to the development of new strategies for disease prevention and intervention.


Keywords:


amyloid; prion; protein misfolding; disease transmission

http://www.nature.com/mp/journal/vaop/ncurrent/abs/mp2011120a.html


see more here ;


http://betaamyloidcjd.blogspot.com/2011/10/de-novo-induction-of-amyloid-deposition.html


http://transmissiblespongiformencephalopathy.blogspot.com/2011/10/alzheimers-disease-is-transmissible.html


TSS

Bovine spongiform encephalopathy associated insertion/deletion polymorphisms of the prion protein gene in the four beef cattle breeds from North China

Bovine spongiform encephalopathy associated insertion/deletion polymorphisms of the prion protein gene in the four beef cattle breeds from North China



Xiang-Yuan Zhu,a Fu-Ying Feng,a Su-Yuan Xue,b Ting Hou,a Hui-Rong Liua

aDepartment of Biochemistry and Molecular Biology, College of Life Sciences, Inner Mongolia Agricultural University, Hohhot, China.

bInner Mongolia Academy of Agricultural Sciences, Hohhot, China.

Corresponding author: Hui-Rong Liu (e-mail: lhz17@yahoo.com.cn).

Paper handled by associate editor J. Bell

Published on the web 19 September 2011.

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

Genome, 10.1139/g11-043

Abstract

Two insertion/deletion (indel) polymorphisms of the prion protein gene (PRNP), a 23-bp indel in the putative promoter region and a 12-bp indel within intron I, are associated with the susceptibility to bovine spongiform encephalopathy (BSE) in cattle. In the present study, the polymorphism frequencies of the two indels in four main beef cattle breeds (Hereford, Simmental, Black Angus, and Mongolian) from North China were studied. The results showed that the frequencies of deletion genotypes and alleles of 23- and 12-bp indels were lower, whereas the frequencies of insertion genotypes and alleles of the two indels were higher in Mongolian cattle than in the other three cattle breeds. In Mongolian cattle, the 23-bp insertion / 12-bp insertion was the major haplotype, whereas in Hereford, Simmental, and Black Angus cattle, the 23-bp deletion / 12-bp deletion was the major haplotype. These results demonstrated that Mongolian cattle could be more resistant to BSE, compared with the other three cattle breeds, because of its relatively low frequencies of deletion genotypes and alleles of 23- and 12-bp indel polymorphisms. Thus, this race could be important for selective breeding to improve resistance against BSE in this area.

Keywords: prion protein gene, insertion/deletion polymorphism, bovine spongiform encephalopathy, cattle, North China



http://www.nrcresearchpress.com/doi/abs/10.1139/g11-043?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%3dpubmed






An autopsied case of V180I Creutzfeldt-Jakob disease presenting with panencephalopathic-type pathology and a characteristic prion protein type


Yasushi Iwasaki1,*, Keiko Mori1, Masumi Ito1, Masamitsu Nagaoka2, Toshiaki Ieda3, Tetsuyuki Kitamoto4, Mari Yoshida5, Yoshio Hashizume5Article first published online: 27 JAN 2011 DOI: 10.1111/j.1440-1789.2010.01192.x © 2011 Japanese Society of Neuropathology

Keywords: akinetic mutism state; Creutzfeldt-Jakob disease; panencephalopathic-type; prion protein type; V180I

A 73-year-old Japanese woman showed slowly progressive aphasia, apraxia and dementia. She had no family history of prion disease or dementia. One year later she showed parkinsonism and corticobasal degeneration was initially suspected. On MRI, the left temporal neocortex seemed swollen on T2-weighted images in the initial stage, and a later high-signal intensity region was observed in the cerebral cortex in diffusion-weighted images. The patient developed myoclonus and an akinetic mutism state 15 months and 22 months after onset, respectively. Consecutive electroencephalography revealed no periodic sharp-wave complexes. Prion protein (PrP) gene analysis revealed a valine to isoleucine point mutation at codon 180, and methionine homozygosity at codon 129. This patient's clinical symptoms and disease course were atypical for Creutzfeldt–Jakob disease (CJD), and a stable state with nasal tube-feeding lasted several years. She died of respiratory failure at the age of 81, 102 months after the onset. Autopsy revealed widespread spongiform degeneration with weak synaptic-type PrP deposition, confirming the diagnosis of genetic CJD. Neurons in the cerebral cortex were relatively preserved in number and hypertrophic astrocytosis was generally moderate for such long-term disease, but cerebral white matter showed diffuse severe myelin pallor with tissue rarefaction suggestive of panencephalopatic-type pathology. The cerebellar cortex was relatively well preserved with observation of mild spongiform change in the molecular layer, moderate neuron loss in the Purkinje neuron layer, and scattered small plaque-like PrP deposition. Western blot analysis of protease-resistant PrP showed a characteristic pattern without a diglycoform band. V180I CJD is an interesting form of genetic CJD with regards to the clinicopathologic, molecular and genetic findings.


http://onlinelibrary.wiley.com/doi/10.1111/j.1440-1789.2010.01192.x/abstract





Oral.34: Variably Protease-Sensitive Prionopathy: Transmissibility and PMCA Studies

Pierluigi Gambetti,1,† Wenquan Zou,1 Juan Maria Torres,2 Claudio Soto,3 Silvio Notari,2 Juan Carlos Espinosa2 and Xiangzhu Xiao1

1 Case Western Reserve University; Cleveland, OH USA; 2 Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria; Madrid, Spain; 3 Mitchell Center for Alzheimer Disease and Related Brain Disorders, University of Texas; Houston, TX USA†Presenting author; Email: pxg13@case.edu

Variably protease-sensitive prionopathy (VPSPr) is an atypical, apparently sporadic prion disease affects all three genotypes—VV, MV and MM—at codon 129 of the prion protein (PrP) gene. A distinctive and common feature of VPSPr three genotypes is the presence of abnormal PrP forming a ladder-like electrophoretic pattern with variable sensitivity to protease digestion according to the 129 genotype. These atypical features have raised the issue of VPSPr transmissibility to animals and its propensity of being replicated in vitro.

We now report the initial results of an extensive study on the capacity of the VPSPr-associated abnormal PrP to propagate by bioassay and by protein misfolding cyclic amplification (PMCA). Inoculation of brain homogenates from cases of VPSPr-129VV to transgenic (Tg) mice expressing human PrP-129V at 6X normal revealed no clinical phenotype during the normal life span of the inoculated mice. Peculiar PrP plaques with a distinctive topography were present in approximately 30% of the mice with minimal or no spongiform degeneration (SD). Abnormal PrP from several of the plaque-bearing mice displayed a ladder-like electrophoretic profile similar to that of VPSPr. In contrast, Tg mice inoculated with brain homogenate from sporadic CJD-129VV associated with scrapie PrP type 2 became symptomatic and died approximately 220 days post inoculation. They showed widespread SD with only occasional, differently distributed plaques and a typical 3-band or PrP27-30 electrophoretic profile of the protease resistant PrP. Sham- or not inoculated mice revealed no pathology and no ladder or PrP27-30 profiles. The ladder-like electrophoretic profile was also obtained from VPSPr-129VV under modified PMCA conditions. Second passage experiments are underway.

These results support the notion that VPSPr is a prion condition different from classical prion diseases and more like other conformational neurodegenerative diseases such as Alzheimer disease and tauopathies.

Note

Supported by NIH NS062787, AG-08012, AG-14359, CDC UR8/CCU515004 and the Britton Fund.


Bio.183: Association Between a Familial and a Newly-Identified Prion Disease

Xiangzhu Xiao,1 Jue Yuan,1 Ignazio Cali,1 Xiaochen Zhou,1 Jeanne Grosclaude,2 Hubert Laude,2 Robert B. Petersen,1 Pierluigi Gambetti1 and Wenquan Zou1,†

1Case Western Reserve University; Cleveland, OH USA; 2Virologie Immunologie Moléculaires; Jouy-en-Josas, France†Presenting author; Email: wenquan.zou@case.edu

Variably protease-sensitive prionopathy (VPSPr) is a newly-identified sporadic prion disease characterized not only by an atypical clinical phenotype and neuropathology, but also by the deposition in the brain of a peculiar prion (PrPSc). The molecular mechanism underlying the formation of the peculiar PrPSc remains unknown. A naturally-occurring pathogenic mutation, valine (V) to isoleucine (I), at PrP residue 180 is linked to familial Creutzfeldt-Jakob disease (fCJDV180I). Here we report that the prions formed in VPSPr and fCJDV180I exhibit striking similarities in glycosylation, enzymatic fragmentation, and immunoreactivity even though they are associated with either wild-type PrP (PrPWt) or mutated PrP, respectively. First, we demonstrate that lack of the proteinase K (PK)-resistant diglycosylated PrP species (PrPDigly) observed in both fCJDV180I and VPSPr results from loss of glycosylation at the first N-linked glycosylation site. Second, although lack of PrPDigly has also been reported in fCJD linked to the PrP Thr183Ala mutation (fCJDT183A, which abolishes the first glycosylation site) and an atypical CJD case, so far fCJDV180I is the only one that is of the peculiar PrPSc with the five-step ladder-like electrophoretic profile (LLEP), a pathognomonic molecular hallmark of VPSPr. Third, PrP with LLEP from the two diseases is preferentially detected by the anti-PrP antibody 1E4, but not by 3F4 although these PrP fragments contain both epitopes. Fourth, unlike fCJDT183A, both VPSPr and fCJDV180I show lack of PrPDigly only in PK-treated but not in untreated PrP. Finally, PrPDigly was detected in PrPWt and PrPV180I, but not in PrPT183A, in cell models. Our study suggests that fCJDV180I shares similar pathogenetic mechanism(s) with VPSPr and that cells and animals expressing human PrPV180I can be used as models for investigating the molecular mechanism underlying the formation of the peculiar PrPSc.

Supported by the National Institutes of Health (NIH) NS062787, NIH AG-08012, AG-14359, the CJD Foundation, Alliance BioSecure, the University Center on Aging and Health with the support of the McGregor Foundation and the President’s Discretionary Fund (CWRU) as well as CDC Contract UR8/CCU515004.


Bio.135: Characterization of the Agent Strain in Sporadic Creutzfeldt-Jakob Disease by Transmission to Wild-Type Mice

Diane L. Ritchie,1,† Aileen Boyle,2 Irene McConnell,2 Mark W. Head,1 James W. Ironside1 and Moira E. Bruce2

1National CJD Surveillance Unit; Edinburgh, UK; 2Neuropathogenesis Division, The Roslin Institute and Royal (Dick) School of Veterinary Studies, The Roslin Institute, Roslin Biocentre; Roslin, UK†Presenting author; Email: diane.ritchie@ed.ac.uk

Transmissible spongiform encephalopathy (TSE) strains are defined by their biological properties on transmission to wild-type (wt) mice, specifically by their characteristic incubation periods and patterns of vacuolar pathology ("lesion profiles") in the brain. While a single TSE strain has been identified in variant Creutzfeldt-Jakob disease (vCJD), the phenotypic heterogeneity observed in sporadic CJD (sCJD) implies the existence of multiple strains of agent. These distinct strains are proposed to be enciphered by the different conformers of abnormal prion protein (PrP), recognized as different protease resistant PrP (PrPres) types by western blotting (type 1 or type 2) and are thought to be substantially influenced by the prion protein gene (PRNP) codon 129 (M/V) polymorphism.

To test the relationship between disease phenotype and agent strain, we investigated the transmission characteristics of the TSE agents present in brain tissue from 27 sCJD cases (comprising all six possible combinations of PRNP codon 129 genotype and PrPres type) in panels of wt mice using the standard strain typing properties of incubation period and lesion profiles, plus a full analysis of PrP present in the mouse brain. The work was extended to include analysis of subsequent mouse-to-mouse passages.

The results demonstrated the existence of at least two strains of agent, one associated with the MM1/MV1 sCJD subgroup and the other associated with the MM2 subgroup. The lack of transmission in mice challenged with tissues from VV1, MV2 and VV2 sCJD subgroups provided evidence of at least one further sCJD strain. Overall, the PrPres type in sCJD was maintained on transmission, which is consistent with the proposition that PrPres type plays a role in enciphering strain-specific information.

This study highlights a complex relationship between disease phenotype, codon 129 PRNP genotype, PrPres type and agent strain in sCJD and confirms that multiple strains of agent are associated with sCJD, some of which successfully propagate in wt mice. The sCJD strains identified here, by their biological properties partially correlates with the current sub-classification system for sCJD, which is based on the clinical and pathological phenotype of the disease.


Bio.144: Analyses of PrPSc Aggregation State and Protease-Resistance in Human Prions

Daniela Saverioni,1,† Silvio Notari,2 Sabina Capellari1 and Piero Parchi1

1Department of Neurological Sciences, University of Bologna; Bologna, Italy; 2Department of Pathology, National Prion Disease Pathology Surveillance Center, Case Western Reserve University; Cleveland, OH USA†Presenting author; Email: daniela.saverioni@studio.unibo.it

Background. Given the complexity and costs of transmission studies, the analyses of PrPSc properties is increasingly used as surrogate marker for strain typing. Early studies showed that PrPSc extracted from distinct disease phenotypes, in both animals and humans, often differ in physicochemical properties, such as fragment size after protease treatment or glycoform ratio. More recently, studies mainly conducted with scrapie strains isolated in mice or hamster have also reported strain-specific PrPSc differences in the degree of protease resistance, aggregation state, or conformational stability.

Objectives. To establish across the phenotypic spectrum of human prion disease: (1) whether and to what extent distinct PrPSc isoforms differ in protease-resistance; (2) whether and to what extent this PrPSc property is related to the aggregation state of the protein and (3) the relative amount of PK-sensitive PrPSc.

Materials and Methods. Frontal cortex PrPSc from the whole spectrum of sCJD subtypes, vCJD and VPsPr (MM and MV codon 129 genotypes) was purified through sample dilution in Sarkosyl and sequential ultracentrifugation in sucrose cushion and pellet resuspensions by sonication. PrPSc aggregates of different size were isolated after ultracentrifugation in sucrose gradient and fraction (12) collection. Whole purified samples and selected fractions of the sucrose gradient preparation were digested using a wide range of PK activities. A curve or "profile" of PrPSc digestion and the corresponding ED50 (PK activity required to decrease PrPSc by 50%) were obtained for each human strain analyzed.

Results. Protease resistance varied significantly among the TSE groups analysed, being highest in vCJD and sCJDVV2 and lowest in sCJDVV1. Fractions 1–4 always contained a fully PK-sensitive form of PrPSc (PrP-sen). However, PrP-sen only accounted for less than 10% of total purified PrPSc in all subtypes analyzed. Overall, the more "sensitive" subtypes contained a larger proportion of "small" PrPSc aggregates 82 Prion Volume 5 Supplement

(fractions 1–6) with respect to the more "resistant" ones. Nevertheless, PK-resistant aggregates of equal size (fractions 6, 9 and 12) extracted from sCJDMM1 and VV2 maintained, at least in part, the different degree of resistance.

Discussion. Our results indicate that: (1) only a limited portion of PrPSc associated to the majority of human prion strains is fully protease sensitive; (2) the analyses of PrP-sen does not differentiate among human prion strains; (3) the PrPSc forms associated to distinct human prion strains show a significant heterogeneity in the degree of protease resistance, which is at least partially explained by their differing aggregation state.

http://www.prion2011.ca/files/PRION_2011_-_Posters_(May_5-11).pdf




something to ponder i read in an old book (thanks cele!) take these words with how ever many grains of salt you wish.


====================================


The familial mutations, Gajdusek proposed, lowered the barrier to such accidental conversion. "Thus," he wrote in 1996, "with these mutations, this ordinarily rare event becomes a ... dominant inherited trait." But Weissmann's qualification still remained to be refuted: the mutations might simply allow easier entry to a lurking virus. ...page 202 Deadly Feast


===================================


something to think about for sure.

but i interpret this as (1st not the gold standard, just my opinion;-), as because of certain gene mutations, one or a family, would be more susceptible to the many different strains of TSE, and the many different proven routes and sources, (which will cause different symptoms, different incubation periods from onset of clinical symptoms to death, different parts of the brain infected, etc.). in other words, it's NOT the gene mutation that CAUSES the disease, but the fact that it makes you more SUSCEPTIBLE, to the TSEs from the surrounding environment, and PLUS accumulation, i think this plays a critical role. maybe there is a one dose scenario, but i think there is more of the 'accumulators' that go clinical, than the 'one dose'. and what is the threshold to sub-clinical to clinical ?

anyway, just pondering out loud here.

also, for anyone interested, there are some studies with links to follow here ;


http://sporadicffi.blogspot.com/




Saturday, June 25, 2011

Transmissibility of BSE-L and Cattle-Adapted TME Prion Strain to Cynomolgus Macaque

"BSE-L in North America may have existed for decades"

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/transmissibility-of-bse-l-and-cattle.html




Over the next 8-10 weeks, approximately 40% of all the adult mink on the farm died from TME.

snip...

The rancher was a ''dead stock'' feeder using mostly (>95%) downer or dead dairy cattle...



http://web.archive.org/web/20030516051623/http://www.bseinquiry.gov.uk/files/mb/m09/tab05.pdf




Sunday, June 26, 2011

Risk Analysis of Low-Dose Prion Exposures in Cynomolgus Macaque

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/risk-analysis-of-low-dose-prion.html




Thursday, June 23, 2011

Experimental H-type bovine spongiform encephalopathy characterized by plaques and glial- and stellate-type prion protein deposits

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/experimental-h-type-bovine-spongiform.html




Thursday, July 21, 2011

A Second Case of Gerstmann-Sträussler-Scheinker Disease Linked to the G131V Mutation in the Prion Protein Gene in a Dutch Patient Journal of Neuropathology & Experimental Neurology:

August 2011 - Volume 70 - Issue 8 - pp 698-702

http://transmissiblespongiformencephalopathy.blogspot.com/2011/07/second-case-of-gerstmann-straussler.html




Saturday, August 14, 2010

BSE Case Associated with Prion Protein Gene Mutation (g-h-BSEalabama) and VPSPr PRIONPATHY

(see mad cow feed in COMMERCE IN ALABAMA...TSS)

http://prionpathy.blogspot.com/2010/08/bse-case-associated-with-prion-protein.html



Wednesday, June 15, 2011

Galveston, Texas - Isle port moves through thousands of heifers headed to Russia, none from Texas, Alabama, or Washington, due to BSE risk factor

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/galveston-texas-isle-port-moves-through.html



Saturday, March 5, 2011

MAD COW ATYPICAL CJD PRION TSE CASES WITH CLASSIFICATIONS PENDING ON THE RISE IN NORTH AMERICA

http://transmissiblespongiformencephalopathy.blogspot.com/2011/03/mad-cow-atypical-cjd-prion-tse-cases.html




Thursday, August 4, 2011

Terry Singeltary Sr. on the Creutzfeldt-Jakob Disease Public Health Crisis, Date aired: 27 Jun 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/terry-singeltary-sr-on-creutzfeldt.html




kind regards,

terry

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

Researchers’ Discovery May Revolutionize Treatment of ALS

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.

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 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. For more information, visit www.brain.ubc.ca.

- 30 -

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-ß, 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-ß 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 a-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.

Last Updated: 9/20/2011 3:19:45 PM

posted: 9/20/2011


http://www.prionetcanada.ca/detail.aspx?menu=12&dt=293797&app=70&cat1=211&tp=12&lk=no



Intermolecular transmission of superoxide dismutase 1 misfolding in living cells

Leslie I. Grada,1, Will C. Guesta,1, Anat Yanaia, Edward Pokrishevskya, Megan A. O'Neilla, Ebrima Gibbsa, Valentyna Semenchenkob, Masoud Yousefia, David S. Wishartc, Steven S. Plotkind, and Neil R. Cashmana,2

+ Author Affiliations

aBrain Research Centre, University of British Columbia, Vancouver, BC, Canada V6T 2B5;

bNational Institute for Nanotechnology, Edmonton, AB, Canada T6G 2M9;

cDepartments of Biological Sciences and Computing Science, University of Alberta, Edmonton, AB, Canada, T6G 2E8; and

dDepartment of Physics and Astronomy, University of British Columbia, Vancouver, BC, Canada V6T 1Z1

Edited* by Don W. Cleveland, University of California at San Diego, La Jolla, CA, and approved July 25, 2011 (received for review February 23, 2011)

Abstract

Human wild-type superoxide dismutase-1 (wtSOD1) is known to coaggregate with mutant SOD1 in familial amyotrophic lateral sclerosis (FALS), in double transgenic models of FALS, and in cell culture systems, but the structural determinants of this process are unclear. Here we molecularly dissect the effects of intracellular and cell-free obligately misfolded SOD1 mutant proteins on natively structured wild-type SOD1. Expression of the enzymatically inactive, natural familial ALS SOD1 mutations G127X and G85R in human mesenchymal and neural cell lines induces misfolding of wild-type natively structured SOD1, as indicated by: acquisition of immunoreactivity with SOD1 misfolding-specific monoclonal antibodies; markedly enhanced protease sensitivity suggestive of structural loosening; and nonnative disulfide-linked oligomer and multimer formation. Expression of G127X and G85R in mouse cell lines did not induce misfolding of murine wtSOD1, and a species restriction element for human wtSOD1 conversion was mapped to a region of sequence divergence in loop II and ß-strand 3 of the SOD1 ß-barrel (residues 24–36), then further refined surprisingly to a single tryptophan residue at codon 32 (W32) in human SOD1. Time course experiments enabled by W32 restriction revealed that G127X and misfolded wtSOD1 can induce misfolding of cell-endogenous wtSOD1. Finally, aggregated recombinant G127X is capable of inducing misfolding and protease sensitivity of recombinant human wtSOD1 in a cell-free system containing reducing and chelating agents; cell-free wtSOD1 conversion was also restricted by W32. These observations demonstrate that misfolded SOD1 can induce misfolding of natively structured wtSOD1 in a physiological intracellular milieu, consistent with a direct protein–protein interaction.

http://www.pnas.org/content/early/2011/09/13/1102645108.abstract?sid=5736bfb2-5e66-48be-9fed-3516c6bec709%20



Supporting Information Grad et al. 10.1073/pnas.1102645108 SI Materials and Methods

http://www.pnas.org/content/suppl/2011/09/14/1102645108.DCSupplemental/pnas.201102645SI.pdf



Saturday, January 22, 2011

Alzheimer's, Prion, and Neurological disease, and the misdiagnosis there of, a review 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/alzheimers-prion-and-neurological.html



Tuesday, June 7, 2011

Protein aggregate spreading in neurodegenerative diseases: Problems and perspectives

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/protein-aggregate-spreading-in.html



CJD1/9 0185

Ref: 1M51A

IN STRICT CONFIDENCE

Dr McGovern From: Dr A Wight

Date: 5 January 1993

Copies: Dr Metters

Dr Skinner

Dr Pickles

Dr Morris

Mr Murray

TRANSMISSION OF ALZHEIMER-TYPE PLAQUES TO PRIMATES

1. CMO will wish to be aware that a meeting was held at DH yesterday, 4 January, to discuss the above findings. It was chaired by Professor Murray (Chairman of the MRC Co-ordinating Committee on Research in the Spongiform Encephalopathies in Man), and attended by relevant experts in the fields of Neurology, Neuropathology, molecular biology, amyloid biochemistry, and the spongiform encephalopathies, and by representatives of the MRC and AFRC.

2. Briefly, the meeting agreed that:

i) Dr Ridley et als findings of experimental induction of p amyloid in primates were valid, interesting and a significant advance in the understanding of neurodegenerative disorders;

ii) there were no immediate implications for the public health, and no further safeguards were thought to be necessary at present; and

iii) additional research was desirable, both epidemiological and at the molecular level. Possible avenues are being followed up by DH and the MRC, but the details will require further discussion.

93/01.05/4.1tss

http://collections.europarchive.org/tna/20080102191246/http://www.bseinquiry.gov.uk/files/yb/1993/01/05004001.pdf



BSE101/1 0136

IN CONFIDENCE

5 NOV 1992

CMO From: Dr J S Metters DCMO 4 November 1992

TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES

1. Thank you for showing me Diana Dunstan's letter. I am glad that MRC have recognized the public sensitivity of these findings and intend to report them in their proper context. This hopefully will avoid misunderstanding and possible distortion by the media to portray the results as having more greater significance than the findings so far justify.

2. Using a highly unusual route of transmission (intra-cerebral injection) the researchers have demonstrated the transmission of a pathological process from two cases one of severe Alzheimer's disease the other of Gerstmann-Straussler disease to marmosets. However they have not demonstrated the transmission of either clinical condition as the "animals were behaving normally when killed'. As the report emphasizes the unanswered question is whether the disease condition would have revealed itself if the marmosets had lived longer. They are planning further research to see if the conditions, as opposed to the partial pathological process, is transmissible.

What are the implications for public health?

3. . The route of transmission is very specific and in the natural state of things highly unusual. However it could be argued that the results reveal a potential risk, in that brain tissue from these two patients has been shown to transmit a pathological process. Should therefore brain tissue from such cases be regarded as potentially infective? Pathologists, morticians, neuro surgeons and those assisting at neuro surgical procedures and others coming into contact with "raw" human brain tissue could in theory be at risk. However, on a priori grounds given the highly specific route of transmission in these experiments that risk must be negligible if the usual precautions for handling brain tissue are observed.

92/11.4/1-1

BSE101/1 0137

4. The other dimension to consider is the public reaction. To some extent the GSS case demonstrates little more than the transmission of BSE to a pig by intra-cerebral injection. If other prion diseases can be transmitted in this way it is little surprise that some pathological findings observed in GSS were also transmissible to a marmoset. But the transmission of features of Alzheimer's pathology is a different matter, given the much greater frequency of this disease and raises the unanswered question whether some cases are the result of a transmissible prion. The only tenable public line will be that "more research is required" before that hypothesis could be evaluated. The possibility on a transmissible prion remains open. In the meantime MRC needs carefully to consider the range and sequence of studies needed to follow through from the preliminary observations in these two cases. Not a particularly comfortable message, but until we know more about the causation of Alzheimer's disease the total reassurance is not practical.

JS METTERS Room 509 Richmond House Pager No: 081-884 3344 Callsign: DOH 832

121/YdeStss

92/11.4/1.2

http://collections.europarchive.org/tna/20080102232842/http://www.bseinquiry.gov.uk/files/yb/1992/11/04001001.pdf



http://betaamyloidcjd.blogspot.com/


Wednesday, April 27, 2011

GENERATION ALZHEIMER'S: THE DEFINING DISEASE OF THE BABY BOOMERS

http://betaamyloidcjd.blogspot.com/2011/04/generation-alzheimers-defining-disease.html



what are they going to do with all us baby boomers by 2050 where an estimated 13.5 million Americans will be stricken with Alzheimer's, up from 5 million plus ? what about the non paid caregivers of these Alzheimer's figures, where by 2050, these figures for caregivers will rise as well, to some 20 million, if we are all still here ? sadly, to add to all this misery, the price of poker is going up too. i apologize for my mood, but i am mad about all these cuts. they have cut funding for prion disease to ZERO DOLLARS!

All Other Emerging and Zoonotic Infectious Diseases CDC's FY 2012 request of $52,658,000 for all other emerging and zoonotic infectious disease activities is a decrease of $13,607,000 below the FY 2010 level, which includes the elimination of Prion activities ($5,473,000), a reduction for other cross-cutting infectious disease activities, and administrative savings. These funds support a range of critical emerging and zoonotic infectious disease programs such Lyme Disease, Chronic Fatigue Syndrome, and Special Pathogens, as well as other activities described below.

http://www.cdc.gov/fmo/topic/Budget%20Information/appropriations_budget_form_pdf/FY2012_CDC_CJ_Final.pdf




Saturday, January 22, 2011

Alzheimer's, Prion, and Neurological disease, and the misdiagnosis there of, a review 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/alzheimers-prion-and-neurological.html



Friday, September 3, 2010

Alzheimer's, Autism, Amyotrophic Lateral Sclerosis, Parkinson's, Prionoids, Prionpathy, Prionopathy, TSE

http://betaamyloidcjd.blogspot.com/2010/09/alzheimers-autism-amyotrophic-lateral.html



Wednesday, January 5, 2011

ENLARGING SPECTRUM OF PRION-LIKE DISEASES Prusiner Colby et al 2011 Prions

David W. Colby1,* and Stanley B. Prusiner1,2


http://cshperspectives.cshlp.org/content/3/1/a006833.full.pdf+html



http://betaamyloidcjd.blogspot.com/2011/01/enlarging-spectrum-of-prion-like.html



Thursday, December 23, 2010

Alimentary prion infections: Touch-down in the intestine, Alzheimer, Parkinson disease and TSE mad cow diseases $ The Center for Consumer Freedom



http://betaamyloidcjd.blogspot.com/2010/12/alimentary-prion-infections-touch-down.html



http://betaamyloidcjd.blogspot.com/


Wednesday, August 24, 2011

There Is No Safe Dose of Prions

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/there-is-no-safe-dose-of-prions.html



Thursday, August 4, 2011

Terry Singeltary Sr. on the Creutzfeldt-Jakob Disease Public Health Crisis, Date aired: 27 Jun 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/terry-singeltary-sr-on-creutzfeldt.html



Sunday, August 21, 2011

The British disease, or a disease gone global, The TSE Prion Disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/british-disease-or-disease-gone-global.html



tss

We need to know the truth about vCJD numbers

We need to know the truth about vCJD numbers


It's estimated that one in 4,000 people are unknowingly infected. The government must authorise trials of a new blood test


Frank Dobson guardian.co.uk, Monday 19 September 2011 06.06 EDT


'The prions that cause vCJD can lie dormant for decades and people who are infected pose a risk to others if they are blood donors.' Photograph: Toby Melville/Reuters

The government's expert advisers assume that as many as 15,000 people in this country are infected with the prion infection agents that cause the lethal brain disease, variant Creutzfeldt-Jakob (vCJD), the human form of BSE or "mad cow disease". The experts don't know if this is the right figure. It could be a lot higher but ministers are refusing to fund trials of a new test to find out.

So far just 200 of our fellow citizens have developed the disease. But the prions that cause the disease can lie dormant for decades and people who are infected pose a risk to others if they are blood or organ donors, or if surgical instruments used on them are then reused on other patients.

The Medical Research Council Prion Unit at the UCL Institute of Neurology, led by Professor John Collinge, was set up at my behest to come up with ways to treat vCJD and, better still, prevent it. They were also asked to devise a test to identify vCJD in the general population. They recently announced a new blood test that does just that. This is a great breakthrough. It should enable our doctors and scientists, for the first time, to assess accurately the incidence of vCJD infection so policy decisions on how best to protect patients can be based on evidence, not guesswork.

As health secretary, the day I became aware in 1998 that it might be possible to transmit vCJD by blood and blood products, I got the experts together. Their advice was that infection through blood and blood products was likely but not certain and that the infection, if any, would probably be carried in the white blood cells. "What should we do?" I asked. The answer for the blood supply was leucodepletion (removing the white cells) at a cost of £100m. When I told Tony Blair that I'd authorised spending this £100m but hoped it would prove to be a waste of money, his response was "fuck me". The blood for a transfusion usually comes from just a few donors but blood products come from many more donors, so the chances of infection were much greater. I had to agree that we should end UK sourcing of blood products – easier said than done.

At the time these decisions had to be taken, there was no way of assessing how many people might be infected. Officials produced "computer projections", ranging from fewer than 200 vCJD fatalities to 3.5 million. These were no more than guesses. I authorised testing of tissue samples from tonsils and appendixes which eventually produced some data which was a little bit more reliable but not much. And so it has continued to this day. In their current risk assessment, the Department of Health assume that 15,000 people (one person in every 4,000) are infected but don't know.

So largely on the basis of the precautionary principle, no less than £540m has been invested since 1998 to try to protect the integrity of blood supplies and blood products. The current annual cost is over £40m plus £200m a year to supply synthetic clotting factor for the treatment of bleeding disorders.

With so many lives possibly at stake and so much money being spent, the new blood test offers the prospect of certainty for the first time. The researchers want the government to authorise trials of the new blood test so we will know how many people are likely to be infected with vCJD. Things may turn out to be better than expected or may be worse. But at least we will know and will be able to tailor the precautionary measures to the scale of the problem. That in turn may raise ethical problems about advising patients believed to be infected with vCJD until there is a treatment. Fortunately the work carried out by the Prion Unit has made such progress that doctors may soon be able to inhibit the development of vCJD, ultimately to cure it and, better still, prevent it – along with other degenerative diseases of the brain, possibly including Alzheimer's. Sadly, so far, the government have refused to authorise and fund the trials. They prefer to continue to remain in ignorance.

The health secretary Andrew Lansley has a lot on his plate at the moment, but he shouldn't let political problems divert him from his basic duty to promote the long-term interests of the nation's health. He should authorise and fund the trials of the new blood test and do it now.

http://www.guardian.co.uk/commentisfree/2011/sep/19/vcjd-blood-test-trials


Wednesday, August 24, 2011

There Is No Safe Dose of Prions

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/there-is-no-safe-dose-of-prions.html


Wednesday, August 24, 2011

All Clinically-Relevant Blood Components Transmit Prion Disease following a Single Blood Transfusion: A Sheep Model of vCJD

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/all-clinically-relevant-blood.html


Friday, August 12, 2011

Creutzfeldt-Jakob disease (CJD) biannual update (2011/2), Incidents Panel, National Anonymous Tonsil Archive

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/creutzfeldt-jakob-disease-cjd-biannual.html


Thursday, August 4, 2011

Terry Singeltary Sr. on the Creutzfeldt-Jakob Disease Public Health Crisis, Date aired: 27 Jun 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/terry-singeltary-sr-on-creutzfeldt.html



Sunday, August 21, 2011

The British disease, or a disease gone global, The TSE Prion Disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/08/british-disease-or-disease-gone-global.html



Monday, September 12, 2011

BSE PRION Agriculture Animal Feed Question House of Lords Thursday, 8 September 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/09/bse-prion-agriculture-animal-feed.html



Saturday, June 25, 2011

Transmissibility of BSE-L and Cattle-Adapted TME Prion Strain to Cynomolgus Macaque

"BSE-L in North America may have existed for decades"

http://transmissiblespongiformencephalopathy.blogspot.com/2011/06/transmissibility-of-bse-l-and-cattle.html



TSS