prions
Specific cells within the immune system could help explain why younger people are more susceptible to variant CJD, scientists believe.
Patients diagnosed with variant CJD are, on average, 28 years old but it has been unclear why older people are not as affected by the disease.
A collaboration between scientists at Vanderbilt University and the University of California, San Francisco has led to the first direct information about the molecular structure of prions. In addition, the study has revealed surprisingly large structural differences between natural prions and the closest synthetic analogs that scientists have created in the lab.
Mad cow disease is caused by the accumulation of an abnormal protein, the prion, in the brain of an affected patient. Outside of the brain, very little is known about prions. Case Western Reserve University School of Medicine, researchers have, for the first time, identified the prion as a biomarker for pancreatic cancer.
North Carolina State University researchers have discovered a link between copper and the normal functioning of prion proteins, which are associated with transmissible spongiform encephalopathy diseases such as Cruetzfeldt-Jakob in humans or "mad cow" disease in cattle.
JUPITER, FL, May 28, 2009 ?Current tests to identify specific strains of infectious prions, which cause a range of transmissible diseases (such as mad cow) in animals and humans, can take anywhere from six months to a year to yield results ? a time-lag that may put human populations at risk.
CAMBRIDGE, Mass. (April 2, 2009) - Whitehead Institute researchers have quintupled the number of identifiable prion proteins in yeast and have further clarified the role prions play in the inheritance of both beneficial and detrimental traits.
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.
Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.
Prions, infectious proteins associated with bovine spongiform encephalopathy (BSE) or Mad Cow Disease, were previously thought to accumulate mainly in the brain, but Yale and University of Zurich researchers report in Science that other organs can also become infected. Past research had shown that the brain and spinal cord bear the highest infection risk for BSE, followed by organs such as the spleen, lymph nodes and tonsils. All other organs were thought to be devoid of prions.
A new study shows that the infectious version of prion proteins, the main culprits behind the human form of mad cow disease or variant Creutzfeldt-Jakob Disease (vCJD), are not destroyed by digestive enzymes found in the stomach. Furthermore, the study finds that the infectious prion proteins, also known as prions, cross the normally stringent intestinal barrier by riding piggyback on ferritin, a protein normally absorbed by the intestine and abundantly present in a typical meat dish.
There is increasing evidence that infectious prions that can cause variant Creutzfeldt-Jakob Disease (vCJD), the human form of ''mad cow'' disease, can be transmitted through blood transfusion, according to Roger Eglin, Ph.D., Head of National Transfusion Microbiology Laboratories for the English National Blood Service. He spoke at a symposium on Transmissible Spongiform Encephalopathies (TSEs) where he was joined by prominent government, public health and blood safety experts from around the globe, including the U.S. and Canada, who raised concerns about a second wave of the disease brought about by human-to-human transmission via blood transfusions.
UCSF scientists are reporting what they say is compelling evidence that the infectious agent known as prion is composed solely of protein. Their findings promise to create new tools for early diagnosis of prions causing bovine spongiform encephalopathy, or ''mad cow'' disease, in cattle and Creutzfeldt-Jakob disease in people, they say. The researchers believe that their work may also help advance investigations of more common neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis.
Scientists have produced a prion protein that can trigger the development of a neurological disorder in mice that is similar to ''mad cow'' disease, according to a new study supported by the National Institute on Aging (NIA), a part of the National Institutes of Health. The findings demonstrate that prions, an unusual class of infectious proteins, can make copies of themselves without the presence of viral DNA or RNA, damage brain tissue, and cause neurological diseases.
Kirin Brewery Company, as part of its joint project with Hematech LLC to develop a cow that can produce human antibodies, has succeeded in producing a cow fetus in which neither bovine antibody gene1 nor the gene for the prions2 that are the cause of BSE are present. The process developed utilizes cells derived from bovine embryos that continuously destroy the bovine genes for antibodies and prions. This is the first successful production of a cell that continuously destroys two differing genes, and the first time that a cow fetus with these characteristics has been created through cell nuclear transfer.
Researchers have taken a major step towards understanding how abnormal prion proteins, the suspected cause of mad cow and related diseases, change shape to jump from one animal species to another. In test tube experiments, they were able to make human prion proteins exhibit characteristics of mouse prions or hamster prions through the substitution of either one or two amino acids. Furthermore, they describe how prions may overcome natural transmissibility barriers between two species of mammals. This may happen if prion proteins from one of these two species have been exposed to abnormal prions from a third species.
