WHAT: 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.
The Atomic Force Microscope depicts on its screen the few nanometer thick and few micrometer long fibers as white flexible sticks, crisscrossing the surface on which they are deposited. The very peculiar property of these proteins lies in fact that they can self assemble into complex ribbon-like twisted fibers. Researchers at ETH ZĂ rich, EPF Lausanne and University of Fribourg have teamed up to take Atomic Force Microscopy images of the fibers and to analyze them using concepts from polymer physics and theoretical modeling. This combination of expertise has lead them to propose a set of general rules governing the assembly of filaments into thicker and twisted ribbon like fibers. Their results are published in the current issue of the scientific journal Nature Nanotechnology. "The model that we propose is extremely precise in its predictions", says Raffaele Mezzenga, Professor of Food and Soft Materials Sciences at the ETH ZĂ rich.
The Coroner's Society "failed" in its duty to protect public health by refusing to take part in vCJD study. The creation of a post-mortem tissue archive for a study of the human form of mad cow disease failed because of a "misguided" refusal by coroners to participate. The Coroners' Society of England and Wales (CSEW) did not recognise its "moral obligation to protect public health" from potential new risks associated with variant Creutzfeldt-Jakob disease (vCJD) when it decided not to allow the collection of tissue from autopsies. That is the conclusion of a paper co-written by a researcher at the London School of Hygiene & Tropical Medicine, which has been published online and is set to appear in a forthcoming edition of the journal Public Health. The authors say they believe the reasons given by the CSEW were insufficient to justify not taking part in the study and call for a wider review of the role of coroners in future public health measures.
Chronix Biomedical Partners With University Of Calgary To Commercialize Serum DNA-Based Blood Test For Mad Cow Disease
Chronix Biomedical today announced that it is partnering with the University of Calgary to develop a commercial version of its serum DNA-based blood test for the early detection of bovine spongiform encephalopathy (BSE), also known as mad cow disease. Chronix researchers have published data demonstrating that the company's proprietary techniques can accurately detect BSE in cattle before any disease symptoms are evident. Currently BSE can only be definitively diagnosed with a post-mortem brain biopsy. Development of the commercial BSE assay is supported by a grant from the Alberta Livestock and Meat Agency (ALMA) and Genome Canada. Chronix intends to begin offering BSE testing services to the cattle industry once the commercial test is finalized and validated. Chronix's technology identifies disease-specific genetic fingerprints based on circulating DNA that is released into the bloodstream by damaged and dying cells.
Creutzfeldt-Jakob disease (CJD) is a rare neurodegenerative disease that rapidly, progressively and severely affects the brain. Creutzfeldt-Jakob disease is one cause of dementia and results in the destruction of brain cells in the brain. Creutzfeldt-Jakob disease eventually leads to the development of many tiny holes in the brain. The disease was first described by German neurologist Hans Gerhard Creutzfeldt in 1920, and shortly afterwards by Alfons Maria Jakob, giving it the name Creutzfeldt-Jakob. According to Medilexicon's medical dictionary : Creutzfeldt-Jakob disease is a progressive neurologic disorder, one of the subacute spongiform encephalopathies caused by prions. Clinical features of CJD include a progressive cerebellar syndrome, including ataxia, abnormalities of gait and speech, and dementia.