http://www.physorg.com/ en-us Physorg.com internet news portal provides the latest news on science including: Physics, Nanotechnology, Life Sciences, Space Science, Earth Science, Environment, Health and Medicine. (PhysOrg.com) -- A laboratory connection between Alzheimer's disease and brain-wasting diseases such as the human form of mad cow disease has moved into the clinic for what is believed to be the first time, manifesting itself in the brains of patients with a rare inherited disorder. http://www.physorg.com/news179570626.html Medicine & Health Wed, 09 Dec 2009 08:45:01 EST news179570626 A new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease (CJD) could be a step closer based on new results from scientists at the University of Leeds. The team has found that a protein called Glypican-1 plays a key role in the development of BSE. Details are published November 20 in the open-access journal PLoS Pathogens. http://www.physorg.com/news177917282.html Medicine & Health Fri, 20 Nov 2009 05:28:23 EST news177917282 A University of Toronto-led team has uncovered the evolutionary ancestry of the prion gene, which may reveal new understandings of how the prion protein causes diseases such as bovine spongiform encephalopathy (BSE), also known as "mad cow disease." http://www.physorg.com/news173359598.html Medicine & Health Mon, 28 Sep 2009 12:27:22 EST news173359598 (PhysOrg.com) -- An investigation of a rare, inherited form of Creutzfeldt-Jakob disease suggests that disrupted regulation of copper ions in the brain may be a key factor in this and other prion diseases. http://www.physorg.com/news159170135.html Chemistry Fri, 17 Apr 2009 06:55:57 EST news159170135 The discovery in common brewer's yeast of a new, infectious, misfolded protein -- or prion -- by University of Illinois at Chicago molecular biologists raises new questions about the roles played by these curious molecules, often associated with degenerative brain diseases like "mad cow" and its human counterpart, Creutzfeldt-Jakob. http://www.physorg.com/news156180264.html Biology Fri, 13 Mar 2009 16:25:13 EST news156180264 Imbalance of iron homeostasis is a common feature of prion disease-affected human, mouse, and hamster brains, according to a new study by Dr. Neena Singh and colleagues at Case Western Reserve University School of Medicine, alongside collaborators from Creighton University. These findings, published March 13 in the open-access journal PLoS Pathogens, provide new insight into the mechanism of neurotoxicity in prion disorders, and novel avenues for the development of therapeutic strategies. http://www.physorg.com/news156173016.html Medicine & Health Fri, 13 Mar 2009 14:25:12 EST news156173016 For over twenty years, scientists have known that a normal protein in the brain, PrP, or prion protein, can turn harmful and cause deadly illnesses like Creutzfeldt-Jakob disease (CJD) in humans, and bovine spongiform encephalopathy (BSE) in cattle. What they could not explain is why large amounts of this normal protein are produced by our bodies in the first place. In a new study published in this week's PLoS Biology, researchers from the University of Konstanz in Germany reveal that PrP indeed plays a beneficial role for the organism - PrP helps cells communicate with one another during embryonic development. http://www.physorg.com/news155888796.html Biology Tue, 10 Mar 2009 07:27:30 EST news155888796 (PhysOrg.com) -- Antibodies that stick to a brain prion protein called PrP could be the key to treating prion diseases like variant CJD and preventing people accidentally exposed to prions from going on to develop the fatal brain disease. Using a precise visualisation technique, called X-ray crystallography, carried out at the Synchrotron Radiation Source (SRS) at the Science and Technology Facilities Councils (STFC) Daresbury Laboratory in Cheshire, scientists have identified an antibody that has the best ability to bind to PrP in the brain. Experiments using cells in the laboratory and in mice have suggested it could stop prion infection in its tracks. http://www.physorg.com/news153681509.html Biology Thu, 12 Feb 2009 17:18:48 EST news153681509 A worldwide group of scientists has created an infectious prion disease in a mouse model, in a step that may help unravel the mystery of this progressive disease that affects the nervous system in humans and animals. The research team, including Christina J. Sigurdson, D.V.M., Ph.D., assistant professor of pathology at the University of California, San Diego School of Medicine, also discovered that changing the structure of the prion protein by altering just two nucleic acids leads to a fatal neurological disorder in mice. Their findings will be published on line in Proceedings of the National Academy of Sciences (PNAS) the week of December 1. http://www.physorg.com/news147702312.html Biology Fri, 05 Dec 2008 12:25:12 EST news147702312 (PhysOrg.com) -- The cause of diseases such as BSE in cattle and Creutzfeld -Jakob disease in humans is a prion protein. This protein attaches to cell membranes by way of an anchor made of sugar and lipid components (a glycosylphosphatidylinositol, GPI) anchor. The anchoring of the prions seems to have a strong influence on the transformation of the normal form of the protein into its pathogenic form, which causes scrapie and mad cow disease. http://www.physorg.com/news142595542.html Chemistry Tue, 07 Oct 2008 10:52:22 EST news142595542 Prion protein, a form of protein that triggers BSE, is associated with other brain diseases in cattle, raising the possibility of a significant increase in the range of prion disease. Publishing their findings in the open access journal BMC Veterinary Research, scientists have detected changes in the production and accumulation of the prion protein in the brains of cattle with a rare neurodegenerative disorder. http://www.physorg.com/news141989399.html Medicine & Health Tue, 30 Sep 2008 10:29:59 EST news141989399 A team from the French Food Safety Agency, Lyon, France, has identified a prion protein characteristic that is unique to some natural but unusual sheep scrapie cases. This finding, reported August 29th in the open-access journal PLoS Pathogens, may provide a novel method by which to study prion diversity and their possible changes during cross-species transmission. http://www.physorg.com/news139206108.html Biology Fri, 29 Aug 2008 05:21:48 EST news139206108