http://www.sciencedaily.com/news/mind_brain/mad_cow_disease/ Learn all about mad cow disease, TSE, and the prions that cause the disease. Current science articles on symptoms, prevention and more. en-us Sat, 11 Oct 2008 00:05:01 EDT Sat, 11 Oct 2008 00:05:01 EDT 60 http://www.sciencedaily.com/images/logosmall.gif http://www.sciencedaily.com/news/mind_brain/mad_cow_disease/ For more science articles, visit ScienceDaily. http://www.sciencedaily.com/releases/2008/10/081008113430.htm Researchers in Germany and Switzerland have developed a new general method for the synthesis of anchored proteins, such as GPI-anchored prions, which cause scrapie and mad cow disease. Fri, 10 Oct 2008 08:00:00 EDT http://www.sciencedaily.com/releases/2008/10/081008113430.htm http://www.sciencedaily.com/releases/2008/09/080915121216.htm Scientists have discovered that an important cellular quality control mechanism may actually be toxic to some brain cells during prion infection. The research proposes a new general mechanism of cellular dysfunction that can contribute to the devastating and widespread neuronal death characteristic of slowly progressing neurodegenerative diseases. Wed, 17 Sep 2008 05:00:00 EDT http://www.sciencedaily.com/releases/2008/09/080915121216.htm http://www.sciencedaily.com/releases/2008/08/080828135905.htm Blood transfusions are a valuable treatment mechanism in modern medicine, but can come with the risk of donor disease transmission. Researchers are continually studying the biology of blood products to understand how certain diseases are transmitted in an effort to reduce this risk during blood transfusions. Fri, 29 Aug 2008 08:00:00 EDT http://www.sciencedaily.com/releases/2008/08/080828135905.htm http://www.sciencedaily.com/releases/2008/05/080516094455.htm Researchers have shown, in unprecedented detail, how a small molecule is able to selectively take apart abnormally folded protein fibers connected to Alzheimer's disease and prion diseases. Finding a way to dismantle misfolded proteins has implications for new treatments for a host of neurodegenerative diseases. Tue, 20 May 2008 23:00:00 EDT http://www.sciencedaily.com/releases/2008/05/080516094455.htm http://www.sciencedaily.com/releases/2008/04/080422152816.htm For the first time, researchers have peered deeply at the atomic level into the protein that causes hereditary cerebral amyloid angiopathy -- a disease thought to cause stroke and dementia. The study pinpointed a tiny portion of the protein molecule that is key to the formation of plaques in blood vessels in the brain. Thu, 24 Apr 2008 08:00:00 EDT http://www.sciencedaily.com/releases/2008/04/080422152816.htm http://www.sciencedaily.com/releases/2008/02/080211195230.htm Prion infection of neurons increases the free cholesterol content in cell membranes. A new study suggests that disturbances in membrane cholesterol may be the mechanism by which prions cause neurodegeneration and could point to a role for cholesterol in other neurodegenerative diseases. Tue, 12 Feb 2008 20:00:00 EST http://www.sciencedaily.com/releases/2008/02/080211195230.htm http://www.sciencedaily.com/releases/2007/12/071203135744.htm Chemists have characterized the molecular structure of the intermediate stage of plaque-forming amyloid fibrils, believed to cause Alzheimer's disease. The finding may lead to new drug targets for this and other amyloid diseases, such as Parkinson's and Creutzfeldt-Jakob. Fri, 07 Dec 2007 02:00:00 EST http://www.sciencedaily.com/releases/2007/12/071203135744.htm http://www.sciencedaily.com/releases/2007/11/071121221704.htm An effective and sensitive new method for detecting and characterizing prions, the infectious compounds behind diseases like mad cow disease, is now being launched. Mad cow disease (BSE), which has caused the death of more than 200,000 cattle and 165 people in the U.K., has now abated. But other prion disorders are on the rise, and there is concern that new strains will infect humans. Thu, 22 Nov 2007 14:00:00 EST http://www.sciencedaily.com/releases/2007/11/071121221704.htm http://www.sciencedaily.com/releases/2007/10/071025091040.htm Diseases that cause neurons to break down, such as Alzheimer's, continue to be elusive to scientists and resistant to treatments. A new finding demonstrates an unpredicted link between a virtually unknown signaling molecule and neuron health. Scientists connect the loss of this molecule to massive neurodegeneration in the brain, which plays a key role in the survival of nervous system cells. Sun, 28 Oct 2007 08:00:00 EDT http://www.sciencedaily.com/releases/2007/10/071025091040.htm http://www.sciencedaily.com/releases/2007/09/070907095625.htm Prion proteins may activate endogenous retroviruses in infected brain cells. Prions – an abbreviation for proteinaceous infectious particles – work as a trigger to a set of diseases of the brain and nervous system, the so-called spongiform encephalopathies. These include BSE in cattle, scrapie in sheep and Creutzfeldt Jakob’s Disease in humans. Prions are structural variants of a normal protein found in healthy tissues – especially in the brain. Sat, 15 Sep 2007 17:00:00 EDT http://www.sciencedaily.com/releases/2007/09/070907095625.htm http://www.sciencedaily.com/releases/2007/09/070905152439.htm Scientists have shown for the first time that small clumps of abnormal prion proteins called oligomers cause the widespread death of neurons. In contrast, much larger prion aggregates known as fibrils proved to be far less toxic. The findings suggest that small protein aggregates play a central role in prion diseases; similar mechanisms have been proposed for the so-called "amyloid" neurodegenerative diseases, including Alzheimer's. The work may provide novel therapeutic approaches for treating people with these conditions. Mon, 10 Sep 2007 23:00:00 EDT http://www.sciencedaily.com/releases/2007/09/070905152439.htm http://www.sciencedaily.com/releases/2007/08/070816121102.htm Scientists have discovered a new protein that may offer fresh insights into brain function in mad cow disease. Fri, 17 Aug 2007 11:00:00 EDT http://www.sciencedaily.com/releases/2007/08/070816121102.htm http://www.sciencedaily.com/releases/2007/07/070703172054.htm A role for prion proteins, the much debated agents of mad cow disease and vCJD, has been identified. It appears that the normal prions produced by the body help to prevent the plaques that build up in the brain to cause Alzheimer's disease. The possible function for the mysterious proteins was discovered by a team of scientists led by Medical Research Council funded scientist Professor Nigel Hooper of the University of Leeds. Fri, 06 Jul 2007 11:00:00 EDT http://www.sciencedaily.com/releases/2007/07/070703172054.htm http://www.sciencedaily.com/releases/2007/07/070702145402.htm Sheep infected with scrapie and cows infected with BSE have elevated levels of manganese in their blood before clinical symptoms appear, according to new research. Wed, 04 Jul 2007 20:00:00 EDT http://www.sciencedaily.com/releases/2007/07/070702145402.htm http://www.sciencedaily.com/releases/2007/05/070503135420.htm An oral vaccine can prevent mice from developing a brain disease similar to mad cow disease, according to new research. Prion diseases, which include scrapie, mad cow disease and chronic wasting disease, are fatal, and there is no treatment or cure. Thu, 03 May 2007 20:00:00 EDT http://www.sciencedaily.com/releases/2007/05/070503135420.htm http://www.sciencedaily.com/releases/2007/03/070319091103.htm Burying prion-infected carcasses of cattle, deer and other animals in lime may actually enhance the spread of those infectious proteins through soil, a new study suggests. Placing quicklime on carcasses once was thought to be the best way to foster quick decay of bodies and to prevent the spread of disease. Mon, 19 Mar 2007 17:00:00 EDT http://www.sciencedaily.com/releases/2007/03/070319091103.htm http://www.sciencedaily.com/releases/2007/02/070224093334.htm For the first time, experimental results indicate that it is possible to use a resin filter to remove harmful prion proteins from the blood of an infected animal, a finding that has major implications for the removal of infectious prion proteins -- the agents associated with variant Creutzfeldt-Jakob disease, mad cow disease, scrapie and other prion diseases in animals -- during blood transfusions. Mon, 26 Feb 2007 02:00:00 EST http://www.sciencedaily.com/releases/2007/02/070224093334.htm http://www.sciencedaily.com/releases/2007/02/070212182836.htm Using a combination of novel technologies, scientists at the Scripps Research Institute and the Whitehead Institute for Biomedical Research have revealed for the first time a dynamic molecular portrait of individual unfolded yeast prions that form the compound amyloid, a fibrous protein aggregate associated with neurodegenerative diseases such as Alzheimer's disease and variant Creutzfeldt-Jacob disease -- the human version of mad cow disease. Thu, 15 Feb 2007 08:00:00 EST http://www.sciencedaily.com/releases/2007/02/070212182836.htm http://www.sciencedaily.com/releases/2007/01/070131135530.htm Studies in mice have indicated that the effects of prion disease could be reversed if caught early enough. The researchers said that their findings support developing early treatments that aim to reduce levels of prion protein in the brains of people with prion disease. Also, they said that their findings suggest testing the efficacy of treatments in a new way: by analyzing their cognitive effects in prion-infected mice. Thu, 01 Feb 2007 17:00:00 EST http://www.sciencedaily.com/releases/2007/01/070131135530.htm http://www.sciencedaily.com/releases/2007/01/070125114327.htm Do genes affect bovine spongiform encephalopathy--also known as BSE, or "mad cow" disease? Are some cattle more susceptible than others? To address these and other questions, Agricultural Research Service (ARS) scientists at the U.S. Meat Animal Research Center in Clay Center, Neb., have sequenced the bovine prion gene (PRNP) in 192 cattle that represent 16 beef and five dairy breeds common in the United States. Fri, 26 Jan 2007 08:00:00 EST http://www.sciencedaily.com/releases/2007/01/070125114327.htm http://www.sciencedaily.com/releases/2007/01/070123143537.htm Brown University biologists have made another major advance toward understanding the deadly work of prions, the culprits behind fatal brain diseases such as mad cow and their human counterparts. In new work published online in PLoS Biology, researchers show that the protein Hsp104 must be present and active for prions to multiply and cause disease. Wed, 24 Jan 2007 05:00:00 EST http://www.sciencedaily.com/releases/2007/01/070123143537.htm http://www.sciencedaily.com/releases/2007/01/070101103354.htm The U.S. Department of Agriculture's Agricultural Research Service have announced initial results of a research project involving prion-free cattle. ARS scientists evaluated cattle that have been genetically modified so they do not produce prions, and determined that there were no observable adverse effects on the animals' health. Mon, 01 Jan 2007 08:00:00 EST http://www.sciencedaily.com/releases/2007/01/070101103354.htm http://www.sciencedaily.com/releases/2006/12/061201180720.htm A new method of treatment can appreciably slow down the progress of the fatal brain disease scrapie in mice. This has been established by German researchers from the Universities of Munich and Bonn together with their colleagues at the Max Planck Institute in Martinsried. They used an effect discovered by the US researchers Craig Mello and Andrew Fire, for which they were awarded this year's Nobel Prize for Medicine. Mon, 04 Dec 2006 14:00:00 EST http://www.sciencedaily.com/releases/2006/12/061201180720.htm http://www.sciencedaily.com/releases/2006/10/061031141414.htm Researchers at the Animal Health Research Centre (CReSA) are developing immunotherapeutical strategies against diseases produced by prion, such as Bovine Spongiform Encephalitis. The most recent results, published in the Journal of Virology, show that important advances have been made in tests using DNA vaccines on animal models, enabling a significant delay in the arrival of symptoms. In the long term, this research could lead to the production of treatment for humans. Wed, 01 Nov 2006 11:00:00 EST http://www.sciencedaily.com/releases/2006/10/061031141414.htm http://www.sciencedaily.com/releases/2006/10/061030120759.htm The urgent search for a medication to treat prion diseases has led scientists in Germany to synthesize a new group of compounds, including one that is 15 times more potent than an approved drug now being tested in clinical trials. Their report is scheduled for the Nov. 2 issue of the biweekly ACS Journal of Medicinal Chemistry. Tue, 31 Oct 2006 14:00:00 EST http://www.sciencedaily.com/releases/2006/10/061030120759.htm http://www.sciencedaily.com/releases/2006/08/060820195413.htm A study published today in the online edition of the Journal of the Royal Society Interface has been exploring the likelihood that vCJD might be spread via the reuse of surgical instruments, and calls for more data in order to allay fears over the possible transmission of vCJD. Mon, 21 Aug 2006 08:00:00 EDT http://www.sciencedaily.com/releases/2006/08/060820195413.htm http://www.sciencedaily.com/releases/2006/07/060707151953.htm A team of researchers at The Scripps Research Institute, the University of California, San Diego (UCSD), and Rocky Mountain Laboratories of the National Institute of Allergy and Infectious Diseases of the National Institutes of Health (NIH), has shown for the first time that laboratory mice infected with the agent of scrapie -- a brain-wasting disease of sheep-demonstrate high levels of the scrapie agent in their heart 300 days after being infected in the brain. Fri, 07 Jul 2006 05:00:00 EDT http://www.sciencedaily.com/releases/2006/07/060707151953.htm http://www.sciencedaily.com/releases/2006/07/060707021040.htm In the July 7, 2006, issue of the journal Science, researchers at the University of Texas Medical Branch at Galveston (UTMB) describe experiments that may soon lead to a test that will enable medical science to estimate how many people are infected with the human form of mad cow disease, which can take as long as 40 years before manifesting itself. Thu, 06 Jul 2006 11:00:00 EDT http://www.sciencedaily.com/releases/2006/07/060707021040.htm http://www.sciencedaily.com/releases/2006/06/060629105141.htm Brittleness is often seen as a sign of fragility. But in the case of infectious proteins called prions, brittleness makes for a tougher, more menacing pathogen. Howard Hughes Medical Institute researcher have discovered that brittle prion particles break more readily into new "seeds," which spread infection much more quickly. Thu, 29 Jun 2006 05:00:00 EDT http://www.sciencedaily.com/releases/2006/06/060629105141.htm http://www.sciencedaily.com/releases/2006/06/060612082042.htm An exciting new tracer allows visualization of abnormal protein deposits -- called amyloid plaques -- in human diseases like Alzheimer's and Creutzfeldt-Jakob and in prion diseases in animals like scrapie (similar to mad cow disease), according to researchers at the University of Pennsylvania and CHRU Tours in France. Mon, 12 Jun 2006 02:00:00 EDT http://www.sciencedaily.com/releases/2006/06/060612082042.htm http://www.sciencedaily.com/releases/2006/05/060519102407.htm A small study in this week's British Medical Journal suggests a new human genotype may be prone to variant Creutzfeldt-Jakob disease (vCJD). Although this new evidence may rekindle fears of a larger epidemic, others warn that it is important to be cautious in interpreting these results. Fri, 19 May 2006 02:00:00 EDT http://www.sciencedaily.com/releases/2006/05/060519102407.htm http://www.sciencedaily.com/releases/2006/04/060428141132.htm Researchers have demonstrated spread of senile amyloidosis from affected mice to their nursing offspring. The paper by Korenaga et al., "Transmission of amyloidosis in offspring of mice with AApoAII amyloidosis," appears in the March issue of the American Journal of Pathology and is highlighted on the cover of the Journal. Fri, 28 Apr 2006 08:00:00 EDT http://www.sciencedaily.com/releases/2006/04/060428141132.htm http://www.sciencedaily.com/releases/2006/03/060331010409.htm While newly published research confirms that under laboratory circumstances prion-protein can be absorbed across the gut, it also shows that this is unlikely to occur in real life. In addition, the results show that the places in the gut that do take up these disease-associated proteins are different from the locations where infectivity is known to be amplified. The findings will be published in the Journal of Pathology. Fri, 31 Mar 2006 02:00:00 EST http://www.sciencedaily.com/releases/2006/03/060331010409.htm http://www.sciencedaily.com/releases/2006/03/060327215844.htm Researchers at the University of Pennsylvania School of Medicine have discovered how a protein called Pmel17 is sorted by pigment cells in the skin and eye to make a fiber matrix that eventually sequesters melanin, the dark pigment found in skin, hair, and eyes. Understanding the molecular steps prior to fiber formation -- and when this process goes awry -- may lead to a better understanding of melanoma and Alzheimer's disease. Tue, 28 Mar 2006 02:00:00 EST http://www.sciencedaily.com/releases/2006/03/060327215844.htm http://www.sciencedaily.com/releases/2006/03/060322134755.htm Researchers at Texas A&M University have successfully "knocked down" the expression of possible disease-causing genes in a cloned goat fetus, perhaps paving the way for breeding disease resistance in other animals, even those genes that might cause bovine spongiform encephalopathy (BSE), commonly known as Mad Cow Disease. Wed, 22 Mar 2006 11:00:00 EST http://www.sciencedaily.com/releases/2006/03/060322134755.htm http://www.sciencedaily.com/releases/2006/02/060210091420.htm Misfolded and damaged proteins are common to all human neurodegenerative diseases, but explanations for the mechanism that kills neurons have varied widely. Northwestern University scientists now offer a clue that may establish a common mechanism in these diseases. Their findings suggest that the disease-associated, aggregation-prone proteins may exert their destabilizing effects by interfering with other proteins that are having difficulty folding, causing them to lose function. Over time, this can cause the organism to die. Fri, 10 Feb 2006 05:00:00 EST http://www.sciencedaily.com/releases/2006/02/060210091420.htm http://www.sciencedaily.com/releases/2006/01/060108221506.htm Internal standards allow meaningful comparison of PrP(Sc) profiles from different origins. Applying the new method to 50 postmortem samples from patients with sporadic CJD reveals substantial differences in molecular pathology, according to a paper published in the open access journal <I>PLoS Medicine</I>. Mon, 09 Jan 2006 08:00:00 EST http://www.sciencedaily.com/releases/2006/01/060108221506.htm http://www.sciencedaily.com/releases/2006/01/060103183333.htm In a new study published by the journal Genome Research, a team of scientists reports that 'mad cow'-like diseases have not been a major force in human history, nor have been cannibalistic rituals that are known to be associated with disease transmission. Their work also has important scientific implications for researchers using a specific class of DNA markers called single nucleotide polymorphisms. Wed, 04 Jan 2006 08:00:00 EST http://www.sciencedaily.com/releases/2006/01/060103183333.htm http://www.sciencedaily.com/releases/2005/12/051209175822.htm Most people with a rare type of dementia called primary progressive aphasia (PPA) have a specific combination of prion gene variants, a new study shows. The study is the first to link the prion protein gene to this disorder. The researchers also looked at the prion gene in people with Alzheimer's disease and amyotrophic lateral sclerosis (ALS or Lou Gehrig's disease) and did not find any association with specific gene variants in those disorders. Fri, 09 Dec 2005 08:00:00 EST http://www.sciencedaily.com/releases/2005/12/051209175822.htm http://www.sciencedaily.com/releases/2005/10/051022111510.htm Research at Yale University School of Medicine shows that infection with a weak strain of Creutzfeldt-Jacob Disease (CJD) prevents infection by more virulent strains and that the protection requires persistent replication by the infectious agent, but not misfolded prions. Protection with a weak animal agent may account for the low incidence of CJD linked to Mad Cow Disease in people. Sat, 22 Oct 2005 05:00:00 EDT http://www.sciencedaily.com/releases/2005/10/051022111510.htm http://www.sciencedaily.com/releases/2005/10/051020091336.htm The scientific magazine <i>Brain Research</i> has recently published the results of research work by scientists from the University of Navarra. The work describes the presence and location of the cellular prion protein (PrPC) in the brain of the rat and characterises the neurones expressed therein, above all within the cerebral cortex of this rodent. Thu, 20 Oct 2005 11:00:00 EDT http://www.sciencedaily.com/releases/2005/10/051020091336.htm http://www.sciencedaily.com/releases/2005/09/050908083333.htm A new study of prions--apparently malformed proteins that initiate deadly brain diseases such as Creutzfeldt-Jakob disease in humans--has yielded surprising information about how the size of prions relates to their infectivity. Scientists have found that small prions are much more efficiently infectious than large ones, yet there also is a lower size limit, below which infectivity is lost. Thu, 08 Sep 2005 11:00:00 EDT http://www.sciencedaily.com/releases/2005/09/050908083333.htm http://www.sciencedaily.com/releases/2005/09/050908083457.htm Brown Medical School researchers have discovered that prions -- the culprits behind fatal brain diseases such as mad cow and its human counterparts -- convert healthy protein into abnormal protein through an ultrafast process similar to DNA replication. The breakthrough finding, published in Nature, helps explain how prions multiply and lead to illness. Thu, 08 Sep 2005 08:00:00 EDT http://www.sciencedaily.com/releases/2005/09/050908083457.htm http://www.sciencedaily.com/releases/2005/08/050829080815.htm Researchers have found a way to detect in blood the malformed proteins that cause "mad cow disease," the first time such "prions" have been detected biochemically in blood. The discovery is expected to lead to a much more effective detection method for the infectious proteins responsible for brain-destroying disorders, such as bovine spongiform encephalopathy (BSE) in cattle and variant Creutzfeldt-Jakob disease (vCJD) in humans. Mon, 29 Aug 2005 08:00:00 EDT http://www.sciencedaily.com/releases/2005/08/050829080815.htm http://www.sciencedaily.com/releases/2005/06/050615001037.htm Abnormal prion proteins are little understood disease agents involved in causing horrific brain-wasting diseases such as Creutzfeldt-Jacob disease in people, mad cow disease in cattle and chronic wasting disease in deer and elk. Now, new research suggests that a variant form of abnormal prion protein--one lacking an 'anchor' into the cell membrane--may be unable to signal cells to start the lethal disease process. Wed, 15 Jun 2005 05:00:00 EDT http://www.sciencedaily.com/releases/2005/06/050615001037.htm http://www.sciencedaily.com/releases/2005/05/050524225513.htm 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. Wed, 25 May 2005 02:00:00 EDT http://www.sciencedaily.com/releases/2005/05/050524225513.htm http://www.sciencedaily.com/releases/2005/05/050514111648.htm NYU School of Medicine scientists have created the first active vaccine that can significantly delay and possibly prevent the onset of a disease in mice that is similar to mad cow disease. Sat, 14 May 2005 08:00:00 EDT http://www.sciencedaily.com/releases/2005/05/050514111648.htm http://www.sciencedaily.com/releases/2005/04/050426215458.htm In a laboratory study, a mutant prion protein was found to assume its normal shape in the cell, but after it was unfolded it failed to return to its normal shape. This may explain why a prion disease called GSS is age-related since the healthy young cell can properly fold and maintain the mutant protein, but deficits in cellular machinery associated with aging might promote accumulation of the aberrant form of the prion protein resulting in disease. Wed, 27 Apr 2005 02:00:00 EDT http://www.sciencedaily.com/releases/2005/04/050426215458.htm