By Jamie Talan Scientists have new evidence that the normal version of a rogue prion protein is key to unleashing its "evil twin," the prion that causes mad cow disease in animals and its human version, Creutzfeldt-Jakob disease. "The prion protein has a Jekyll-and-Hyde personality," said Anthony Williamson, an associate professor at the Scripps Institute in La Jolla, Calif. Williamson and his colleagues discovered that the abnormal form, called PrPsc, can't destroy the brain without another signal. And that signal, according to a study in Science, is delivered by the normal prion protein, or PrPc. Until now, this process has been a mystery. Copyright © Newsday, Inc.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4914 - Posted: 06.24.2010

Where's the beef? Not on everyone's table. Some wary consumers began banishing the meat from their diets after officials confirmed the first U.S. case of mad cow disease last month. But a technology that is already making the food people eat safer may be the key to eliminating mad cow disease, scientists report in the journal Proceedings of the National Academy of Sciences. Richard Meyer, co-author of the May, 2003 study and a food safety researcher, has found a way to destroy the misshapen proteins called PrPSc prions (normal prions are called PrP), believed to cause mad cow disease, or bovine spongiform encephalopathy (BSE). "We take the meat and re-cook it and then we vacuum pack it in plastic and then go ahead and pressurize it at a certain temperature, for a certain time," Meyer explains. The process seems to stop the action of the renegade PrPSc protein that, left unchecked, forms strings, coils, and folds into different shapes, changing normal chemical function. Inside the body, the deadly protein searches for and latches onto healthy PrP, building a pile of misshaped protein that crystallizes in clumps called "plaque." © ScienCentral, 2000-2003.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4812 - Posted: 06.24.2010

Research suggests sick animals may not show symptoms By TODD HARTMAN, SCRIPPS HOWARD NEWS SERVICE Below the drumbeat of reassurances from government and the cattle industry that the meat supply remains safe despite this one case of mad cow disease, a small universe of scientists working on a family of related illnesses is finding disturbing evidence to the contrary. Several studies, including research at a government laboratory in Montana, continue to spark questions about human susceptibility not only to mad cow, but also to sister diseases such as chronic wasting disease, which mainly affects deer and elk, and scrapie, which infects sheep. Mice research and clusters of cases in which humans contracted a disease similar to mad cow also has a few scientists wondering whether consuming infected meat might have killed far more people than medical experts have long assumed, not only in Great Britain, but in the United States as well. ©1996-2004 Seattle Post-Intelligencer

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4800 - Posted: 06.24.2010

Ben Harder The first appearance in the United States of the cattle-killing ailment known as mad cow disease has rocked the beef industry and raised fears of an outbreak of a similar deadly brain disease in people. However, the threat to both people and animals in the United States remains low as long as the government enforces specific feed-processing and slaughter regulations, risk analysts say. The most crucial safeguard, according to the researchers, is a ban put in place in 1997 that prohibits feeding potentially infective animal parts to cattle. That practice, which provided cheap protein for animal feed, is the main route of transmission of the misshapen proteins that cause mad cow disease, which is formally known as bovine spongiform encephalopathy (BSE). The proteins, called prions, may spread when animals consume brain, spinal cord tissue, bone particles, eyes, and small intestines of infected animals. In people, prions occasionally cause the lethal brain condition known as variant Creutzfeldt-Jakob disease, or vCJD. New safety measures that the government has announced in recent weeks might further reduce the odds of a U.S. outbreak of vCJD in people, says George Gray of the Harvard Center for Risk Analysis in Boston. One of these rules would delay the sale of meat from cattle carcasses until they're tested for BSE, and another would ban or restrict the use of processing technologies that may mix bits of nerve tissue with meat. Copyright ©2004 Science Service.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4786 - Posted: 06.24.2010

Study hints at vital job for two-faced proteins. HELEN PEARSON Mystery proteins called prions, which can flip between two different shapes, might help in laying down memories, according to US researchers. The finding hints at an entirely new set of roles for the proteins. Prions are unusual in the protein world: when they adopt one of their guises, they can reproduce, converting other identical proteins into copies of themselves. Often such replicating prions are harmful - they clog up the brains of cattle with mad cow disease and patients with variant Creutzfeldt-Jakob disease (vCJD). Now a team led by Eric Kandel at Columbia University in New York has found that a prion-like protein called CPEB may help nerve cells store memories. A transient electrical signal in the brain might flip CPEB into its prion form, the researchers suggest, helping to create a permanent memory trace. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders; Chapter 17: Learning and Memory
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders; Chapter 13: Memory and Learning
Link ID: 4743 - Posted: 06.24.2010

First UK case of variant CJD from blood. NICOLA JONES A patient who died from the human form of mad cow disease may have caught the illness from a blood transfusion. Policies governing blood donation may require a rethink as a result. It is not possible to tell whether the patient caught the fatal disease - called variant Creutzfeldt-Jakob disease (vCJD) - from the transfusion or contracted it by eating infected meat. But the incident is the first case of "possible transmission" through transfusion - something that scientists have long known to be a possibility. Britain's Department of Health and the National Blood Service have since contacted 15 other patients who also received blood from donors who later died from vCJD. The patients have been offered counselling. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4725 - Posted: 06.24.2010

NewScientist.com news service A British man has died from variant CJD after receiving a blood transfusion seven years earlier from a donor who also later died from the disease. The UK secretary of state for health announced the case in an emergency statement to parliament on Wednesday. The case may be the first in the world where the human form of BSE - mad cow disease - has been transmitted via a blood transfusion. But John Reid told the House of Commons: "This is a possibility not a proven causal connection." Both individuals might have acquired the devastating illness separately by eating BSE-infected meat, he says, but "the possibility of this being transfusion-related cannot be discounted". © Copyright Reed Business Information Ltd.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4716 - Posted: 06.24.2010

Toxic by-product, not rogue proteins, may cause fatal brain wasting. TOM CLARKE Clumps of rogue proteins are not the cause of fatal conditions such as mad cow disease, but merely a symptom, hints new research. The insight could ultimately help to treat the degenerative brain diseases - the hunt is now on for the real culprit. BSE in cows, scrapie in sheep, chronic wasting disease in deer and variant Creutzfeldt-Jakob Disease in humans occur when an animal or person is infected with a misshapen form of proteins called prions. The molecules accumulate in the brain as they twist healthy prions into their own image. Mutant prions accumulate in dying brain cells and spongy gaps open up in the brain, causing loss of coordination, confusion, mental decline and eventually death. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4452 - Posted: 06.24.2010

Protein molecules are the basic components of life. They have so many functions that many nanotechnologists are interested in harnessing them to make tiny machines. Inside the human body, proteins look like ribbons folded in certain ways. "In order for proteins to function, they have to fold into just the right shape," explains Susan Lindquist, biologist and director of the Whitehead Institute for Biomedical Research. "And unfortunately, sometimes they can get that wrong. Misfolded proteins can be very toxic in cells. They can actually set up a chain reaction that gradually converts all the other proteins of that type in the cell to that same altered form, and poisons their functioning." Proteins that are folded the wrong way are called prions, short for proteinaceous infectious particles. Inside mammals' brain cells, some types of prions can alter cell structure and lead to fatal illnesses such mad cow disease in animals or Creutzfeldt-Jakob disease in people. © ScienCentral, 2000-2003.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4364 - Posted: 06.24.2010

A chance discovery could lead to the development of a drug that blocks prion diseases such as variant CJD. However, it would only be useful when combined with mass screening to identify infected people who have not yet developed any symptoms. Adriano Aguzzi's team at the Institute of Neuropathology in Zurich, Switzerland, discovered the effect by accident. The researchers engineered mice to produce a protein that would stick to the scrapie prion, so the team could retrieve the prion protein for testing. The engineered mice turned out to take twice as long as normal to develop the disease. Because the protein is soluble, it is ideal for use as a drug. Aguzzi now hopes to mass-produce the protein so he can test it on macaque monkeys that have been exposed to BSE. © Copyright Reed Business Information Ltd.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4335 - Posted: 06.24.2010

-- Dirt may help scientists answer a question that has baffled them for decades: How does chronic wasting disease (CWD) in deer and elk spread from animal to animal? By turning to the land, University of Wisconsin-Madison researchers show that prions - infectious proteins considered to be at the root of the disease - literally stick to some soil types, suggesting that the landscape may serve as an environmental reservoir for the disease. The findings will be discussed during a poster presentation on Wednesday, Sept. 10, in New York City at the 226th national meeting of the American Chemical Society. Copyright © 1992-2003 Bio Online, Inc

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 4253 - Posted: 06.24.2010

Chronic wasting disease, a cousin of mad cow disease, is spreading among wild deer in parts of the U.S. Left unchecked, the fatal sickness could threaten North American deer populations--and maybe livestock and humans By Philip Yam A place called the eradication zone, lying about 40 miles west of Madison, Wis., covers some 411 square miles. There thousands of white-tailed deer live--or rather, used to live. Last year the Wisconsin Department of Natural Resources instituted special hunting periods to try to wipe out upward of 18,000 deer. During the fall, dead deer were taken to registration areas, where state employees in protective suits and gloves dragged carcasses from pickup trucks and lifted them onto plastic-covered picnic tables. With hacksaws, they severed the heads, double-bagged them and sent them for testing; the bodies themselves were incinerated. © 1996-2003 Scientific American, Inc.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3812 - Posted: 06.24.2010

NewScientist.com news service An experimental drug given to a UK teenager with the human form of mad cow disease appears to have stopped the fatal disease in its tracks. The controversial treatment may even have improved 18-year-old Jonathan Simms' condition, according to his father. Pentosan polysulphate had never been used in humans for treating vCJD before being injected directly into Jonathan's brain. The treatment began in January 2003 after the family won a High Court ruling against the UK's National Health Service. The NHS had refused to allow doctors to carry out the procedure with an untested drug. But the court ruled the treatment acceptable, as without treatment Jonathan was certain to die. © Copyright Reed Business Information Ltd.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3793 - Posted: 06.24.2010

Captured protein couple may help treat brain disease. HELEN PEARSON Researchers in Switzerland claim to have proved a long-standing theory about prions: that the proteins couple up to breed mad cow disease. Their experiments should fuel the search for a cure. In both the animal disorder and its human equivalent, variant Creutzfeldt-Jakob disease (vCJD) warped prions clump in the brain, eventually destroying it. Misshapen prions were thought to latch onto and warp normal ones. But scientists had not captured this liaison taking place in sick animals. Now Adriano Aguzzi of University Hospital Zurich, Switzerland and his colleagues have caught prions in the act1. They genetically engineered mice to carry a new, artificial version of prions with a tag. Unlike the real thing, this makes them easy to isolate from cells. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3655 - Posted: 06.24.2010

Therapy looks best yet to tackle brain disease. HELEN PEARSON The possibility of using antibodies to treat variant Creutzfeldt-Jakob disease (vCJD) receives a boost this week, with the first promising results from an animal trial. The lethal brain condition - which is a human version of mad cow disease - occurs when healthy proteins called prions become twisted and clump together. Probably caught from eating infected beef, there is currently no known cure for the condition. A team of London researchers injected mice with antibodies that latch onto prions. The animals, who had another form of prion disease called scrapie, stayed healthy for at least two years, rather than dying by the time they reached seven months1. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3522 - Posted: 06.24.2010

Misshapen 'mad cow' proteins, or prions, found in nasal passages Ulysses Torassa, Chronicle Health Writer People with the human form of "mad cow" disease apparently harbor the infectious protein in their noses, scientists are reporting, raising questions about transmission of the disease and opening a possible avenue for detecting it. Researchers in Italy were able to find evidence of prions -- misshapen disease-causing proteins -- in the nasal passages of all nine people they examined who died of Creutzfeldt-Jakob disease, or CJD. Test results were negative in the case of 11 other people who died from other diseases. The findings appear in today's edition of the New England Journal of Medicine. "Our findings call attention to the possibility that endoscopic and surgical procedures involving the upper vault of the nasal cavity represent a risk factor for prion spreading," wrote the researchers at the University of Verona, adding, "We know of no cases of disease transmission by this route." ©2003 San Francisco Chronicle

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders; Chapter 9: Hearing, Balance, Taste, and Smell
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders; Chapter 6: Hearing, Balance, Taste, and Smell
Link ID: 3454 - Posted: 06.24.2010

Primitive prion hints at origins of brain disease. HELEN PEARSON Fish, like sheep, elk and humans, could suffer a version of 'mad cow disease', or BSE, preliminary evidence suggests. The results might help to reveal how the disease jumps from species to species. Infectious prions are thought to cause BSE and human variant Creutzfeldt-Jakob disease (vCJD). They probably crossed from sheep to cows, and then to humans in infected meat. Now a team at the University of Konstanz in Germany has identified a cousin of the prion protein in pufferfish1 . The researchers show that the fish protein is different at key sites from the prion protein found in mammals. It's "unlikely" that transmission could occur between such different animals, says study leader Edward Málaga-Trillo. © Nature News Service / Macmillan Magazines Ltd 2003

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3376 - Posted: 06.24.2010

NewScientist.com news service A British teenager dying from vCJD, the human form of mad cow disease, is to become the first person to be treated with an experimental drug that doctors hope could slow the disease's progression. The drug, pentosan polysulphate, is a commonly used oral remedy for cystitis and bladder pain. However, it will not cross the blood-brain barrier and will therefore be injected directly into the 18-year-old's brain. A tube was inserted on Friday and the first dose will be delivered on Monday. However, the location of the hospital and the names of the surgical team cannot be named for legal reasons. © Copyright Reed Business Information Ltd.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3282 - Posted: 06.24.2010

Mouth's muscle could be a route for infection. HELEN PEARSON Tongue meat could carry a risk of infection from mad cow disease, a new report suggests1. Tongue could contain high levels of the prion protein thought to cause bovine spongiform encephalopathy (BSE) in cattle and variant Creutzfeldt-Jakob disease in humans, say Richard Bessen and his colleagues. Prions injected into hamster brains travelled to the tongue and accumulated to relatively high levels, the team found. This doesn't prove that cows with BSE have prion-loaded tongues, or that eating these tongues could cause human disease, says Bessen, who works at Creighton University in Omaha, Nebraska. But guidelines on the meat allowed into the food-chain should be re-evaluated, he says. © Nature News Service / Macmillan Magazines Ltd 2002

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3234 - Posted: 06.24.2010

NewScientist.com news service The British High Court has given the go-ahead for two teenagers dying from vCJD to be the first to receive an experimental treatment. It would involve injections of a drug called pentosan polysulphate directly into their brains. Pentosan polysulphate is currently used as an oral drug in people to treat cystitis and bladder pain. Research in the UK and Japan has shown that the drug can stop the progression of scrapie, a very similar disease, in mice. It worked by binding to a key site on cells and stopping abnormal prion proteins being created. But research in the field is at an early stage. In October 2002, the UK's Committee on the Safety of Medicines reviewed all existing data on the drug and concluded it was too early to consider using it in human vCJD patients. © Copyright Reed Business Information Ltd.

Related chapters from BN: Chapter 16: Psychopathology: Biological Basis of Behavior Disorders
Related chapters from MM:Chapter 12: Psychopathology: The Biology of Behavioral Disorders
Link ID: 3197 - Posted: 06.24.2010