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By SANDRA BLAKESLEE DENVER, — Wildlife experts from the United States and Canada are meeting here to discuss strategies for containing the spread of chronic wasting disease, the variant of mad cow disease that kills deer and elk. The malady, once found only in the brushy foothills near Fort Collins, Colo., has now been identified in both captive and wild herds of deer and elk in Kansas, Montana, Nebraska, New Mexico, Oklahoma, South Dakota, Wisconsin and Wyoming and the Canadian provinces of Saskatchewan and Alberta. Some states, like New Mexico, have found only one infected animal in the wild. But Saskatchewan, for example, has diagnosed the disease in more than 100 captive animals bred for their meat and antlers. Copyright 2002 The New York Times Company

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Link ID: 2432 - Posted: 06.24.2010

Experts offer some advice on deer illness By BRIAN TUMULTY Press-Gazette Washington bureau WASHINGTON — Scientists and wildlife experts testifying at a congressional hearing Thursday acknowledged there are many unanswered questions about the always fatal chronic wasting disease that has infected deer and elk in eight states ranging from Colorado to Wisconsin. But they did offer some basic advice for the public: Q. How likely is it that people may become infected? A. It’s highly unlikely. “There’s no evidence that chronic wasting disease poses a threat to humans,” said Russell George, director of the division of wildlife at the Colorado Department of Natural Resources. Q. What does the disease do? A. Animals become emaciated or “wasted” by chronic weight loss. Chronic wasting disease, or CWD as it is often called, is always fatal. But it usually takes 16 to 32 months to incubate. Animals often become listless, lower their heads and walk in repetitive patterns. Some infected elk become highly excited and nervous. Q. Is the disease a virus or bacteria? A. Neither. CWD is a form of protein, according to wildlife veterinarian Michael Miller of the Colorado Department of Natural Resources. It is scientifically described as a transmissible spongiform encephalopathy or TSE. Once an animal is infected, the toxicity builds until the animal dies. Copyright © 2002

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Link ID: 2095 - Posted: 06.24.2010

National Institutes of Health (NIH) scientists investigating how prion diseases destroy the brain have observed a new form of the disease in mice that does not cause the sponge-like brain deterioration typically seen in prion diseases. Instead, it resembles a form of human Alzheimer's disease, cerebral amyloid angiopathy, that damages brain arteries. The study results, reported by NIH scientists at the National Institute of Allergy and Infectious Diseases (NIAID), are similar to findings from two newly reported human cases of the prion disease Gerstmann-Straussler-Scheinker syndrome (GSS). This finding represents a new mechanism of prion disease brain damage, according to study author Bruce Chesebro, M.D., chief of the Laboratory of Persistent Viral Diseases at NIAID’s Rocky Mountain Laboratories. Prion diseases, also known as transmissible spongiform encephalopathies, primarily damage the brain. Prion diseases include mad cow disease or bovine spongiform encephalopathy in cattle; scrapie in sheep; sporadic Creutzfeldt-Jakob disease (CJD), variant CJD and GSS in humans; and chronic wasting disease in deer, elk and moose. The role of a specific cell anchor for prion protein is at the crux of the NIAID study. Normal prion protein uses a specific molecule, glycophosphoinositol (GPI), to fasten to host cells in the brain and other organs. In their study, the NIAID scientists genetically removed the GPI anchor from study mice, preventing the prion protein from fastening to cells and thereby enabling it to diffuse freely in the fluid outside the cells.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
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Link ID: 13838 - Posted: 06.24.2010

By SANDRA BLAKESLEE Researchers are reporting that they have solved a longstanding mystery about the rapid spread of a fatal brain infection in deer, elk and moose in the Midwest and West. The infectious agent, which leads to chronic wasting disease, is spread in the feces of infected animals long before they become ill, according to a study published online Wednesday by the journal Nature. The agent is retained in the soil, where it, along with plants, is eaten by other animals, which then become infected. The finding explains the extremely high rates of transmission among deer, said the study’s lead author, Dr. Stanley B. Prusiner, director of the Institute for Neurodegenerative Diseases at the University of California, San Francisco. First identified in deer in Colorado in 1967, the disease is now found throughout 14 states and 2 Canadian provinces. It leads to emaciation, staggering and death. Unlike other animals, Dr. Prusiner said, deer give off the infectious agent, a form of protein called a prion, from lymph tissue in their intestinal linings up to a year before they develop the disease. By contrast, cattle that develop a related disease, mad cow, do not easily shed prions into the environment but accumulate them in their brains and spinal tissues. There is no evidence to date that humans who hunt, kill and eat deer have developed chronic wasting disease. Nor does the prion that causes it pass naturally to other animal species in the wild. Copyright 2009 The New York Times Company

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
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Link ID: 13262 - Posted: 06.24.2010

By Rachel Ehrenberg Researchers look to the good version of the protein implicated in mad cow disease for insight into the protein’s bad side. When the nefarious Mr. Hyde takes his own life, the good Dr. Jekyll is also killed. Scientists are adopting the reverse approach for halting the protein behind prion diseases such as Creutzfeldt-Jakob and mad cow. By targeting the harmless version of the brain protein whose evil alter ego brings on disease, researchers have prevented the bad version of the protein from continuing its rampage in the brains of infected mice. The results are reported online July 14 in Proceedings of the National Academy of Sciences. The approach of killing Jekyll to get Hyde is very promising, comments biochemist Sina Ghaemmaghami of the Institute for Neurodegenerative Diseases at the University of California, San Francisco. The sinister version of the protein comes in several slightly different forms, making it hard to develop a single attack strategy, Ghaemmaghami says. Led by neuroscientist Giovanna Mallucci of University College London, researchers delivered bits of attack RNA to interfere with production of the normal version of the prion protein. In animals who have prion disease, this protein somehow gets converted into a dangerous form, which then travels through the brain, coaxing other good versions of the protein to go bad. © Society for Science & the Public 2000 - 2008

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
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Link ID: 11829 - Posted: 06.24.2010

Roxanne Khamsi Silencing the genes that produce prion proteins can dramatically slow the progression of mad cow disease, suggests a new study in mice. Researchers say that the approach might one day work to treat human prion illnesses, such as variant Creutzfeldt Jakob Disease (vCJD). People can contract vCJD after eating meat contaminated with mad cow disease. Though the illness is extremely rare, it can lead to schizophrenia-like psychosis and typically causes death within a year of diagnosis. While doctors can prescribe drugs to temporarily treat some of the symptoms of prion disease, which include seizures, they still have no way to stop the progression of the illness. Alexander Pfeifer at the University of Bonn in Germany, and colleagues, explored the possibility of fighting prion disease in mice using a method of gene silencing known as RNA interference (RNAi). This method exploits messenger RNA (mRNA) sequences in the cell, which are responsible producing proteins by using the animal’s genetic code as an instruction list. RNAi relies on molecules that bind to mRNA sequences in the cell, thereby preventing the production of specific proteins. © Copyright Reed Business Information Ltd

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 9685 - Posted: 06.24.2010

Scientists for the first time have watched agents of brain-wasting diseases, called transmissible spongiform encephalopathies (TSE), as they invade a nerve cell and then travel along wire-like circuits to points of contact with other cells. These findings will help scientists better understand TSE diseases and may lead to ways to prevent or minimize their effects. TSE, or prion, diseases include scrapie in sheep and goats; chronic wasting disease in deer and elk; mad cow disease in cattle; and Creutzfeldt-Jacob disease in humans. Under the direction of Byron Caughey, Ph.D., at the Rocky Mountain Laboratories (RML) and Marco Prado, Ph.D. at the University of Minas Gerais in Belo Horizonte, Brazil, the team performed the research in laboratory cultures using a rodent-adapted form of scrapie protein and cells taken from the central nervous system of mouse and hamster brains. The proteins were first “branded” with fluorescent dyes so they could be easily tracked. The work also revealed that a similar trafficking process might occur with the key plaque-forming protein in Alzheimer’s disease, which is not a TSE but a different type of degenerative brain disease, according to Gerald Baron, Ph.D., one of the lead RML researchers. RML, located in Hamilton, MT, is part of the National Institute of Allergy and Infectious Diseases (NIAID) of the National Institutes of Health. The new report appears in the May 25 issue of The Journal of Neuroscience. “These findings offer intriguing leads toward developing therapies to stop the spread of TSE and possibly other degenerative brain diseases,” says NIAID Director Dr. Anthony Fauci.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 7406 - Posted: 06.24.2010

The discovery of a cow suffering from bovine spongiform encephalopathy (BSE) in Washington State at the end of last year brought fears of mad cow disease to the U.S. New findings provide further insight into how prions, the misshapen proteins behind the transmissible spongiform encephalophathy (TSE) diseases, behave. Prions are most often associated with organ tissue but recent findings have indicated that they can accumulate in the muscles of rodents and humans who have succumbed to TSEs. According to a report published online today by the journal Nature Biotechnology, prions can be detected in the muscles of sheep infected with the TSE known as scrapie several months before the disease can be clinically diagnosed. Olivier Andreoletti of National Veterinary School in Toulouse, France and his colleagues infected six sheep with scrapie. After the animals died, the researchers analyzed their muscle tissue and found "small but consistent amounts" of the infectious prion in the creatures’ fore and hindlimbs. The scientists also examined a flock of sheep that had naturally succumbed to scrapie and detected prions in the muscles of two animals out of a dozen that were tested. One of these, which was 13.5 months old when it died, tested positive even though animals typically display clinical signs of scrapie only after 22 months of age. Fewer of the naturally-infected animals tested positive for prions in their muscles, suggesting that the infectious proteins spreads to muscles less efficiently in the wild than in the laboratory. In addition, the prions in the muscle tissues were 5,000 times less infective than were those recovered from brain tissue. Although this is the first observation of prions accumulating in the muscles of animals that enter the human food chain, the authors caution that the results cannot be extrapolated to BSE in cattle. In addition they note that "dietary exposure to scrapie is currently considered nonhazardous to humans." --Sarah Graham © 1996-2004 Scientific American, Inc

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 5517 - Posted: 06.24.2010

Detailed structural studies have revealed new insights into why the same prion protein can have different properties and be either weakly or strongly infectious. The researchers said their observations in prions that infect yeast are likely to hold true for the sorts of prions that infect humans and animals. A research team led by Howard Hughes Medical Institute investigator Jonathan S. Weissman analyzed the structures of two unmodified yeast Sup35 prion proteins in two infectious conformations. They identified key structural differences that explain the different behaviors of these prions. The researchers published their findings online September 2, 2007, in the journal Nature. Weissman and his colleagues are at the University of California, San Francisco. The scientists studied yeast prions, which are similar to mammalian prions in that they act as infectious proteins. In recent years, mammalian prions have gained increasing notoriety for their roles in such fatal brain-destroying human diseases as Creutzfeldt-Jakob disease and kuru, and in the animal diseases, bovine spongiform encephalopathy (“mad cow” disease) and scrapie. Yeast and mammalian prions are proteins that transmit their unique characteristics via interactions in which an abnormally shaped prion protein influences a normal protein to assume an abnormal shape. In mammalian prion infections, these abnormal shapes trigger protein clumping that can kill brain cells. In yeast cells, the insoluble prion protein is not deadly; it merely alters a cell's metabolism. Prions propagate themselves by division of the insoluble clumps to create “seeds” that can continue to grow by causing aggregation of more proteins. © 2007 Howard Hughes Medical Institute.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 10671 - Posted: 06.24.2010

Howard Hughes Medical Institute researchers have identified small regions within a yeast protein that control the protein's conversion to an infectious agent known as a prion. Yeast prions are proteins that are conceptually similar to the mammalian prions that have gained notoriety for their roles in such fatal brain-destroying human diseases as Creutzfeldt-Jakob disease and kuru, and in the animal diseases, scrapie and bovine spongiform encephalopathy, or “mad cow disease.” “No one knew that prion conversion was controlled by such a small region, and in such a specific way,” said HHMI investigator Susan Lindquist at the Whitehead Institute for Biomedical Research. Lindquist and postdoctoral fellow Peter Tessier published a research article describing their findings on May 10, 2007, in the journal Nature. The precision of this process offers key insights into the mysterious behavior of prions, Lindquist observed. Different configurations of the recognition region cause the prion to assume different shapes, or variants. “We've been able to understand some fundamental questions about how prions form different strains and how they establish and overcome species barriers,” said Tessier. First isolated and purified in the early 1980s, prions are proteins that can fold into self-templating configurations, so that proteins of the same type adopt the same configuration. © 2007 Howard Hughes Medical Institute.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 10291 - Posted: 06.24.2010

Debora MacKenzie A third person in the UK has caught variant CJD from another human, in a blood transfusion. Many more people may be at risk of this human form of BSE, experts warn. Three of eight people tested so far in the UK are now confirmed to have been infected with vCJD through blood transfusions, autopsies have revealed. A total of 66 people in UK are known to have received transfusions from blood donors who later went on to develop vCJD. Of those, 34 later died from other causes. The remaining 24 people have been informed that they may be at high risk of developing vCJD, but are not reported to have been tested. In each of the three cases, the victims received blood from someone who went on to develop vCJD between 18 and 40 months after donating blood, which shows that apparently healthy blood donors can pose a threat of infection, at least in the late stages of incubation. Many carriers, unaware of their infection, may have transmitted the mutant prion in donated blood, experts say. For that reason, it was “prudent” in 2004, once the first transfusion-related case was discovered, for the UK to ban transfusion recipients from later donating blood, say Kumanan Wilson and Maura Ricketts of Toronto General Hospital and the Public Health Agency of Canada. They penned a commentary on the case in the medical journal The Lancet, which reported the third case this week (see vCJD death linked to blood transfusion. © Copyright Reed Business Information Ltd.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 9720 - Posted: 06.24.2010

Two independent research groups have established conclusively that prions are proteins, and that they do not depend on genes or other factors for transmission of their traits. According to the scientists, the studies answer a nagging question that had raised doubts among some researchers about the validity of the so-called “protein-only” hypothesis of prion infectivity. Scientists have grappled for years with one of the central tenets of the protein-only hypothesis, namely, that a single prion protein, when unaltered by genetic mutation, can give rise to different strains of prions with varying infectivity and other properties. The two research groups established that the strains could be accounted for by different misfolded conformations of the same protein. The researchers say this finding could contribute to better understanding of the functioning of disease-causing prions in animals and humans. Both groups published their findings in the March 18, 2004, issue of the journal Nature. Howard Hughes Medical Institute investigator Jonathan S. Weissman at the University of California at San Francisco led one group. The other effort was led by Chi-Yen King at Florida State University. ©2004 Howard Hughes Medical Institute

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 5148 - Posted: 06.24.2010

Genetic technique may yield BSE-proof calves. MICHAEL HOPKIN Researchers in the United States and Japan claim to have created cow embryos that cannot produce the protein responsible for bovine spongiform encephalopathy (BSE). Without it, the animals should be immune to mad cow disease. A “handful" of the BSE-free cows will be born early next year, the researchers say. The calves will be tested with a small dose of mad cow protein to see whether they are truly resistant to the disease. The BSE-causing protein, called a prion, is present in both healthy and diseased cattle; it is only when it twists out of shape that it causes problems. When normal prion protein comes into contact with the disease-causing version it can flip into the malignant form, causing rogue prions to spread through the brain. This leads to coordination problems, behavioural changes and death. The US and Japanese researchers aimed to bypass this problem by creating genetically engineered cows that do not produce prions at all. This means that they should be safe from small doses of diseased prions, explains James Robl, president of biotechnology firm Hematech in Sioux Falls, South Dakota, and one of the leaders of the team. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 5579 - Posted: 06.24.2010

Scientists have firmed up the evidence that misshapen protein are responsible for brain-wasting diseases by showing how these infectious prions are created. Researchers from the United States and China have artificially created a disease-causing prion using proteins from mice. Prions are proteins that occur naturally in the cells of mammals. Infectious prions are abnormal, misshapen versions of this protein that cause neurodegenerative diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy, also known as mad cow disease. The scientists used a mouse prion protein, called PrP, created through genetic engineering in bacterial cells in their experiments. They found that the protein interacts with lipids, the fatty molecules in the structures of cell membranes, and becomes contorted and improperly folded, changing it into a disease-causing prion. Jiyan Ma of Ohio State University said the experiment, published this week in Science, is the strongest evidence yet that prions are the cause of these brain-wasting diseases. "The major thing we showed in this study is that the infectious agent in these diseases is truly a misfolded protein," Ma said in a statement. © CBC 2010

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 13727 - Posted: 06.24.2010

Jessica Hamzelou, reporter Prion proteins have a bad reputation. The misfolded forms of this brain protein are responsible for a host of neurological diseases including, notoriously, variant Creutzfeldt-Jakob Disease (vCJD), which has been linked to eating contaminated beef. But what about the normal, correctly folded version of prion protein? Surely it must have a function in the brain? Neurologists still haven't figured out exactly what this is, but several pieces of evidence suggest that prions aren't all bad. The latest study, published in Nature Neuroscience, suggests that prions are important in maintaining the myelin sheath that surrounds nerve cells, enabling them to transmit nerve impulses rapidly. Adriano Aguzzi and his team at University Hospital of Zurich, Switzerland, bred mice lacking prion protein. They found that these mice developed a condition where their peripheral nerves, which connect the limbs to the central nervous system, lost much of their myelin coating. Although it's too early to say whether the finding can be applied to human disease, Aguzzi told Asian News International that he thinks "it is going to be interesting to see if prions play any role in demyelinating diseases that stem from the brain". This isn't the first time prions have been caught doing some good. Over the past 15 years, researchers have been noting that although mice without the prion protein don't develop prion disease - and can even be rescued from it - they end up with all sorts of other problems. © Copyright Reed Business Information Ltd.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 13709 - Posted: 06.24.2010

By Jennifer Couzin-Frankel In mad cow disease, misfolded proteins called prions punch holes in the brain, eventually destroying it. Inherited prion diseases, which are rare and passed through families, do the same thing. But it's long been a puzzle why prions attack neurons more than other types of cells, and how they do their damage. In a new study, researchers propose that prions deplete a poorly understood protein that normally keeps nerve cells healthy. The theory still has a ways to go before it's proven, but researchers are intrigued by this potential new twist on a mysterious disease. Prions are a faulty version of a healthy protein called PrP; when it misfolds, the results are disastrous. Yet researchers don't know exactly why. One argument suggests that whereas healthy PrP is normally located on the cell's surface, prions go astray and end up in the cytosol, the liquid found inside cells, somehow destroying them. The new study bolsters this theory. The first clues came in a paper published in 2003. In that work, researchers reported that mice lacking an obscure protein, Mahogunin, suffered a form of neurodegeneration much like prion disease. Cell biologists Ramanujan Hegde and Oishee Chakrabarti of the National Institute of Child Health and Human Development in Bethesda, Maryland, decided to probe deeper into the Mahogunin connection. © 2009 American Association for the Advancement of Science

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 12943 - Posted: 06.24.2010

By Rachel Zelkowitz Talk about Dr. Jekyll and Mr. Hyde. Misfolded proteins known as prions cause mad cow disease and other fatal neurodegenerative illnesses. But in their properly folded form, the proteins may be important to survival, helping mice and other animals keep their sniffing skills sharp, new research shows. Prions get the bad reputation--and the lion's share of research attention--but interest in the normal form of prion proteins is increasing. Brain tissue is particularly high in these proteins, and a growing body of research has shown that they help neurons conduct copper and may even protect them from destruction by rogue chemicals in the body. But no one had pegged prion proteins to a particular neurological function such as sight or smell. That's changed, thanks to an intriguing finding by electrophysiologist Stuart Firestein of Columbia University. Firestein and colleagues were studying the sense of smell in mice when they noticed high levels of normal prion protein (PrPc) in the cells that make up the animals' olfactory systems. Wondering whether the protein might play a role in this sense, the researchers hid bits of peanut butter cookies in the shredded bedding of a cage. They then timed how long it took both normal mice and rodents genetically engineered to not make PrPc to sniff out the snack. Normal mice spent an average of 73 seconds searching for the treat before they found it, three times faster than their PrPc-free counterparts. Six of the 20 PrPc-free mice never found the cookie at all, the team reports this week in Nature Neuroscience. © 2008 American Association for the Advancement of Science.

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Link ID: 12382 - Posted: 06.24.2010

Colin Barras More than a decade after the first reported cases of debilitating brain disease variant Creutzfeldt-Jakob disease (vCJD), the exact mode of infection remains controversial. Weird self-replicating proteins called prions are the prime suspect, but are yet to be found conclusively guilty. In an effort to solve the mystery biochemists have created the first complete synthetic prion and plan to discover if it can be as toxic as the real thing. The prion is the alter-ego of a protein that naturally exists in cells. But that harmless protein can undergo a Jekyll-and-Hyde transformation into a shape that clumps together into disease-causing plaques. Even worse, those prions convert any normal versions of the protein it meets into the malignant form. In 2005, Bruce Chesebro's team at the US National Institute of Allergy and Infectious Diseases, discovered that prions need a string of molecules that acts as an "anchor" to be toxic. Prions that usually cause the disease scrapie in sheep and goats proved unable to perform their usual toxic tricks in mice when stripped of their anchors (Science, DOI: 10.1126/science.1110837). © Copyright Reed Business Information Ltd.

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 12117 - Posted: 06.24.2010

Amber Dance Infectious prion proteins from hamsters can change normal proteins from mice into new, infectious forms of prion - simply by mixing the proteins together in a test tube. Researchers at the University of Texas Medical Branch in Galveston suggest their discovery could be turned into a useful test for whether a given prion strain is transmissible from one species to another. Prion proteins are responsible for Creutzfeld-Jakob disease and "mad cow" disease. But they also found that when a prion jumps species, it produces a new kind of prion. "This is very worrisome," says Claudio Soto, who led the research, published in Cell1. "The universe of possible prions could be much larger than we thought." Normal prion protein, or PrP, is found throughout the body but is concentrated in the brain. Its exact role is not known, although it has been linked to cell signalling2, metal-ion transport3, and blood-cell manufacture4. The protein can adopt malformed shapes that cause disease. Those proteins, which are resistant to degradation, bind and convert normal protein to their troublesome conformation. Over time, the diseased protein builds up and forms fibrils in the brain, causing neurodegeneration and ultimately death. © 2008 Nature Publishing Group

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 12015 - Posted: 06.24.2010

By MATT APUZZO WASHINGTON -- The Bush administration can prohibit meat packers from testing their animals for mad cow disease, a federal appeals court said Friday. The dispute pits the Agriculture Department, which tests about 1 percent of cows for the potentially deadly disease, against a Kansas meat packer that wants to test all its animals. Larger meat packers opposed such testing. If Creekstone Farms Premium Beef began advertising that its cows have all been tested, other companies fear they too will have to conduct the expensive tests. The Bush administration says the low level of testing reflects the rareness of the disease. Mad cow disease has been linked to more than 150 human deaths worldwide, mostly in Great Britain. Only three cases have been reported in the U.S., all involving cows, not humans. ad_icon A federal judge ruled last year that Creekstone must be allowed to conduct the test because the Agriculture Department can only regulate disease "treatment." Since there is no cure for mad cow disease and the test is performed on dead animals, the judge ruled, the test is not a treatment. The U.S. Court of Appeals for the District of Columbia Circuit overturned that ruling, saying diagnosis can be considered part of treatment. © Copyright 1996-2008 The Washington Post Company

Related chapters from BP7e: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: Biological Basis of Behavioral Disorders
Link ID: 11996 - Posted: 06.24.2010