 |
|
New insights into the diversity of Creutzfeldt-Jakob disease agents
March 18, 2008Researchers from the United Kingdom and France have identified four separate biochemical subgroups in a selection of cases of Creutzfeldt-Jakob disease. The study, published March 14th in the open-access journal PLoS Pathogens, suggests that these subgroups could represent distinct prion strains in what is the most common human prion disease.
Prion diseases are transmissible neurodegenerative disorders characterized by accumulation of an abnormal isoform (PrPSc) of a host-encoded protein (PrPC) in affected tissues. Although considered a spontaneous disorder, the clinicopathological characteristics of sporadic Creutzfeldt-Jakob disease (sCJD) are variable and substantially influenced by a particular variation in the DNA of the prion protein gene (PRNP). Due to the strong influence of host factors on the characteristics of the disease, diversity of prion agents responsible for CJD remains extremely difficult to investigate.
In this study, using two new biochemical assays, the authors identified four distinct biochemical PrPSc subgroups in 41 sCJD cases. These subgroups correlate with the current sCJD subclassification. The subgroups were also found in 12 iatrogenic CJD (iCJD) cases from different countries. Iatrogenic CJD occurs following human-to-human sCJD transmission. In contrast to the sCJD cases, however, there was no particular correlation with the PRNP codon in the iCJD cases, indicating that observed biochemical properties could be specific to the prion agent.
Further studies are required to confirm that the four biochemical subgroups identified correlate with distinct biological infectious agents.
Public Library of Science
Further studies are required to confirm that the four biochemical subgroups identified correlate with distinct biological infectious agents.
Public Library of Science
Creutzfeldt-Jakob News and Current Creutzfeldt-Jakob Events RSS'Intrabody' can mop up mutant protein in Huntington's disease model
Scientists have created a tool for mopping up the clumps of mutant protein that drive neurodegeneration in Huntington's disease. Emory University researchers engineered a virus to make an intracellular antibody or "intrabody" against huntingtin, the protein whose mutant forms poison the brain cells of people with Huntington's.
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.
Seeing Alzheimer's amyloids
In an important step toward demystifying the role protein clumps play in the development of neurodegenerative disease, researchers have created a stunning three-dimensional picture of an Alzheimer's peptide aggregate using electron microscopy.
US stands to lose a generation of young researchers
Five consecutive years of flat funding the budget of the National Institutes of Health (NIH) is deterring promising young researchers and threatening the future of Americans' health, a group of seven preeminent academic research institutions warned today.
UIC chemists characterize Alzheimer's neurotoxin structure
Amyloid plaques, the hallmark of Alzheimer's disease, are clumps of fiber-like misfolded proteins which many experts think cause this devastating neurodegenerative disease.
Blood transfusion-transmitted infections: A global perspective
Thanks to the many blood-safety interventions introduced since 1984, the overall risk for most transfusion-transmitted infections has become exceedingly small.
Call for data on reuse of surgical instruments to allay fears over vCJD transmission
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.
Prion disease agent causes heart damage in mouse study
These findings raise the possibility that heart infection could be a new aspect of prion diseases, including those that affect humans and livestock, and that these diseases could travel through the blood.
Prion find points way to test for human 'mad cow' disease
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.
Brittle prions are more infectious
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.
More Creutzfeldt-Jakob News Articles
 | The Official Patient's Sourcebook on Creutzfeldt-Jakob Disease: A Revised and Updated Directory for the Internet Age by Icon Health Publications This sourcebook has been created for patients who have decided to make education and Internet-based research an integral part of the treatment process. Although it gives information useful to doctors, caregivers and other health professionals, it also tells patients where and how to look for information covering virtually all topics related to creutzfeldt-jakob disease, from the essentials to the... |
| Rare brain disorder suspected in death.(Health)(Fatal illness: Doctors say Creutzfeldt-Jakob Disease may have killed Jerry Ray Collins.): An article from: The Register-Guard (Eugene, OR) This digital document is an article from The Register-Guard (Eugene, OR), published by The Register Guard on July 31, 2002. The length of the article is 1039 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... | |
 | Neurochemical Aspects of Excitotoxicity by Akhlaq A. Farooqui, Wei-Yi Ong, Lloyd Horrocks About 40% of central nervous system synapses use glutamate as the neurotransmitter. Over-stimulation of glutamate receptors produces neuronal injury or death by excitotoxicity, which is closely associated with neurochemical and neuropathological changes involved in acute neural trauma (stroke, spinal cord trauma, and head injury) and neurodegenerative diseases such as Alzheimer disease, Parkinson... |
 | Prion Protein Protocols (Methods in Molecular Biology) 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.... |
 | Mad Cow USA: Could the Nightmare Happen Here? by Sheldon Rampton, John Stauber Mad Cow U.S.A. is not the book to read before you go out for a steak. In fact, it's not really a book to read before eating anything; this chronicle of government cave-in to pressure from the food industry just might scare away your appetite. Authors Sheldon Rampton and John Stauber argue that both the American and British governments colluded with beef producers to suppress important facts... |
| Prions: Novel Infectious Pathogens Causing Scrapie and Creutzfeldt-Jakob Disease by Stanley B. Prusiner | |
 | Creutzfeldt-Jakob Disease: Managing the Risk of Transmission by Blood, Plasma, and Tissues |
| Enfermedad de Creutzfeldt-Jakob y Otras Enfermedad by Pierre Beauvais | |
| PALL PRION PROTECTS BLOOD SUPPLY FROM VARIANT CJD.: An article from: Biotech Business This digital document is an article from Biotech Business, published by Thomson Gale on December 1, 2005. The length of the article is 804 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 DetailsTitle: PALL... | |
| Creutzfeldt-Jakob Disease by Creutzfeldt-Jakob Disease Network |
| © 2008 BrightSurf.com |