 |
|
Is there more to prion protein than mad cow disease?
September 30, 2008Prion 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.
Martin Jeffrey of the Veterinary Laboratories Agency led a research team that tested 15 brains of cattle with idiopathic brainstem neuronal chromatolysis and hippocampal sclerosis (IBNC). They are the first group to show that the brains of animals with this disease accumulate prion protein (PrP), the protein that misfolds to cause BSE and which, when transmitted to humans through the food chain, can cause the deadly Variant Creutzfeldt-Jakob disease
IBNC is a rare neurological disease of adult cattle. It was first characterised in 1988 following laboratory tests from cattle suspected of having BSE. Although IBNC has some clinical similarities to BSE, the brains of affected cattle do not have the neuronal vacuolation (lesions) typical of BSE.
Further laboratory tests suggest that the misfolded form of PrP, which accumulates in the brains of BSE cases, is not present in IBNC cases. Commercial BSE testing kits did not detect the telltale, BSE-inducing form of PrP either. However, the presence of increased levels of PrP was detected.
"We've shown for the first time that prion protein is somehow involved in IBNC," says Jeffrey, "In this disease, there is an association with abnormally high levels of a prion protein in the brain but clearly this PrP is in a different form to that involved in BSE and CJD. This may have implications for diagnosis and recognition of typical forms of BSE as well as the related diseases in sheep, deer and in man.
BioMed Central
Further laboratory tests suggest that the misfolded form of PrP, which accumulates in the brains of BSE cases, is not present in IBNC cases. Commercial BSE testing kits did not detect the telltale, BSE-inducing form of PrP either. However, the presence of increased levels of PrP was detected.
"We've shown for the first time that prion protein is somehow involved in IBNC," says Jeffrey, "In this disease, there is an association with abnormally high levels of a prion protein in the brain but clearly this PrP is in a different form to that involved in BSE and CJD. This may have implications for diagnosis and recognition of typical forms of BSE as well as the related diseases in sheep, deer and in man.
BioMed Central
Prion Protein Current Events and Prion Protein News RSSU of T led research team uncovers evolutionary origins of prion disease gene
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."
A Penny for Your Prions
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.
Scripps Florida scientists devise accelerated method to determine infectious prion strainsScripps Florida scientists devise accelerated method to determine infectious prion strains
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.
Prevalence of variant CJD agent in Britain remains uncertain
First results from a large tissue survey in Britain of the agent that causes variant Creutzfeldt-Jakob disease (vCJD) are unable so far to establish that the prevalence is lower than that given by previous estimates, concludes a study published on bmj.com today.
Iron is involved in prion disease-associated neuronal demise
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.
Antibody key to treating variant CJD, scientists find
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.
Mutant proteins result in infectious prion disease in mice
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.
K-State professor's USDA research shows mad cow disease also caused by genetic mutation
New findings about the causes of mad cow disease show that sometimes it may be genetic.
How small molecule can take apart Alzheimer's disease protein fibers
Researchers from the University of Pennsylvania School of Medicine 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.
Europe develops new technologies to boost health of livestock
A range of new technologies including genetic modification (GM) and RNA Interference are being deployed to improve the health of farm animals in a series of European and global initiatives. The ground was laid for a European platform to develop new treatments that exploit these technologies at a recent workshop organised by the European Science Foundation (ESF).
More Prion Protein Current Events and Prion Protein News Articles
 |
Amyloid, Prions, and Other Protein Aggregates, Volume 309 (Methods in Enzymology) by John N. Abelson (Editor), Melvin I. Simon (Editor), Ronald Wetzel (Editor) This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential... |
 |
Prions: The New Biology of Proteins by Claudio Soto (Author) The current interest in prion diseases has been fueled by the panic that originated from the appearance of a new variant of Creutzfeldt-Jakob disease and the evidence linking it to human exposure to the bovine spongiform encephalopathy (BSE) agent. Peer-reviewed to assure accuracy, this book describes the science, concepts, hypothesis, and mechanisms of prion disease transmission. It covers human and animal prion diseases, their incidence, prevalence, origin, and clinical and neuropathologic characteristics. The author provides scientific facts and a clear explanation of the relevance and implications of the findings for science in general. |
 |
Amyloid, Prions, and Other Protein Aggregates, Part B, Volume 412 (Methods in Enzymology) by Ronald Wetzel (Editor), Indu Kheterpal (Editor) The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies. * Presents detailed protocols * Includes troubleshooting tips * Provides coverage on structural biology, computational... |
 |
Fatal Protein: The Story of CJD, BSE, and Other Prion Diseases by Rosalind M. Ridley (Author), Harry F. Baker (Author) This book presents a clear and authoritative survey of the prion diseases, designed mainly for the non-specialist. It deals with the history of scrapie in sheep, the spread of kuru through cannibalism in Papua New Guinea, and the BSE epidemic in Britain--"mad cow disease"--which claimed over 170,000 cattle and threatened the rest of Europe. The authors present a detailed description of the human prion diseases, and examine the evidence that the new variant of the Creutzfeld-Jakob disease results from eating infected by BSE. At the heart of this book lies a discussion of the still controversial idea that the infectious agent in prion diseases is a normal brain protein which takes on abnormal, mutant shape. This is the so-called "prion theory". The potential of similar processes underlying... |
 |
Prion Protein Protocols (Methods in Molecular Biology) by Andrew F. Hill (Editor) While much information has been gained over the last two decades regarding the molecular nature of prion proteins, only recently have several research groups begun to cast light on turning the normal prion protein into its aberrant, infectious form. In "Prion Protein Protocols", an international team of experts provide an up-to-date collection of current methods in this unique area of neuroscience. The chapters contained in this volume, both protocols and useful review chapters, feature topics such as the cell biology of prions, techniques and approaches to studying prion infection in cultured cells, how these systems can be used as a rapid bioassay, and prion protein mis folding. As a volume in the highly successful "Methods in Molecular Biology" series, the chapters include readily... |
|
Prions: The New Biology of Proteins.(Book review): An article from: Emerging Infectious Diseases by Ermias D. Belay (Author) This digital document is an article from Emerging Infectious Diseases, published by Thomson Gale on June 1, 2007. The length of the article is 537 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser. Citation Details Title: Prions: The New Biology of Proteins.(Book review) Author: Ermias D. Belay Publication: Emerging Infectious Diseases (Magazine/Journal) Date: June 1, 2007 Publisher: Thomson Gale Volume: 13 Issue: 6 Page: 959(1) Article Type: Book review Distributed by Thomson... | |
![Fate of prions in soil: Interaction of a recombinant ovine prion protein with synthetic humic-like mineral complexes [An article from: Soil Biology and Biochemistry]](http://ecx.images-amazon.com/images/I/51FQM3CAMYL._SL160_.jpg) |
Fate of prions in soil: Interaction of a recombinant ovine prion protein with synthetic humic-like mineral complexes [An article from: Soil Biology and Biochemistry] by M.A. Rao (Author), F. Russo (Author), V. Granata (Author), R. Berisio (Author), Zagari (Author) This digital document is a journal article from Soil Biology and Biochemistry, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: Prion proteins are regarded as the main agents of transmissible spongiform encephalopathies. Understanding their fate in soil may be crucial to elucidate the dissemination of the prion in the environment, associated with a possible transmission of infectivity. Studies were performed with simplified model systems, derived by the birnessite-mediated oxidative polymerization of catechol, which simulate processes naturally occurring in soil. A benign full-length recombinant purified ovine protein (PrP)... |
|
Similar biochemical signatures and prion protein genotypes in atypical scrapie and Nor98 cases, France and Norway.: An article from: Emerging Infectious Diseases by Jean-Noel Arsac (Author), Olivier Andreoletti (Author), Jean-Marc Bilheude (Author), Caroline Lacroux (Author), Sylvie L. Benestad (Author), Thierry Baron (Author) This digital document is an article from Emerging Infectious Diseases, published by Thomson Gale on January 1, 2007. The length of the article is 5490 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser. Citation Details Title: Similar biochemical signatures and prion protein genotypes in atypical scrapie and Nor98 cases, France and Norway. Author: Jean-Noel Arsac Publication: Emerging Infectious Diseases (Magazine/Journal) Date: January 1, 2007 Publisher: Thomson Gale Volume: 13 Issue: 1 Page: 58(8) Distributed by Thomson... | |
|
Physiological function of the cellular prion protein (PrPc): protein profiling study in two cell culture systems by Sanja Ramljak (Author) The physiological role of the cellular prion protein (PrPc) is still not fully understood. This study gives a further insight into the possible physiological function(s) of PrPc via recognizing proteome changes influenced by different levels of PrPc expression in human embryonic kidney (HEK) 293 and PrPc-deficient (Prnp0/0) ell line. The two cell lines gave largely non-intersecting results. A high proportion of proteins deregulated following PrPc overexpression in HEK 293 cells is involved in energy metabolism and cellular homeostasis. Hence, the previously reported increased sensitivity of PrPc overexpressing cells to apoptotic stimuli might be caused by perturbed expression of proteins essential for energy production and maintenance of cellular homeostasis. A particularly significant... | |
 |
The Prion Protein by Jorg Tatzelt (Editor) A conformational transition of the cellular prion protein (PrPC) into an aberrantly folded isoform designated scrapie prion protein (PrPSc) is the hallmark of a variety of neurodegenerative disorders collectively called prion diseases. They include Creutzfeldt-Jakob disease and Gerstmann-Stäussler-Scheinker syndrome in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease (CWD) in free-ranging deer. In contrast to the deadly properties of misfolded PrP, PrPC seems to possess a neuroprotective activity. More-over, animal models indicated that the stress-protective activity of PrPC and the neurotoxic effects of PrPSc are somehow interconnected. In this timely book, leading scientists in the field have come together to highlight the... |
| © 2009 BrightSurf.com |