News tagged with prion
Unravelling the mystery of misfolding prions
(Phys.org) -- Researchers at the University of Alberta's physics department and the National Institute for Nanotechnology (NINT) are the first to map out the folding pathways of prions, malformed ...
May 30, 2012 |
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Prions in the brain eliminated by homing molecules
Toxic prions in the brain can be detected with self-illuminating polymers. The originators, at Linköping University in Sweden, has now shown that the same molecules can also render the prions harmless, and potentially ...
Apr 24, 2012 |
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Researchers develop novel technique for early detection of misfolded protein
(Phys.org) -- University of Delaware assistant professor David W. Colby is co-author of a paper in the March 23 issue of the Journal of Biological Chemistry that suggests protein misfolding may occur early in th ...
Apr 06, 2012 |
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Ozone treated water v. lethal microbial material
A University of Alberta research team has discovered that technology commonly used to decontaminate food industry equipment can also rid meat processing plants of lethal microbial material responsible for the human version ...
Mar 02, 2012 |
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Prion proteins play powerful role in survival, evolution of wild yeast strains
Prions, the much-maligned proteins most commonly known for causing "mad cow" disease, are commonly used in yeast to produce beneficial traits in the wild. Moreover, such traits can be passed on to subsequent generations and ...
Feb 15, 2012 |
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Killing prions with ozone
When it comes to infectious agents, it doesn’t get much worse than prions. These misfolded proteins are highly resistant to a wide variety of extreme disinfectant procedures. They have been identified ...
Feb 15, 2012 |
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New study shows prions able to jump between species more easily than thought
(PhysOrg.com) -- A group of French researchers has found that prions are more easily able to jump between species than has been previously thought. In their paper published in Science, they show that prions ...
Jan 27, 2012 |
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Cellular stress can induce yeast to promote prion formation
It's a chicken and egg question. Where do the infectious protein particles called prions come from? Essentially clumps of misfolded proteins, prions cause neurodegenerative disorders, such as mad cow/Creutzfeld-Jakob disease, ...
Jul 23, 2011 |
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Simulating amyloid formation
Many neurodegenerative diseases are characterized by proteins that assume an abnormal configuration, which leads to their aggregation and deposition in and around rve cells, causing cell death. This process, ...
May 04, 2011 |
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Multitarget drugs against prion diseases
The central nervous systems of humans and cattle alike are attacked by prions (abnormal insoluble amyloidogenic proteins) when they suffer from Creutzfeldt–Jakob disease (CJD) or bovine spongiform encephalopathy ...
Mar 21, 2011 |
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Mutant prions help cells foil harmful protein misfolding
Romping clumps of misfolded proteins are prime suspects in many neurological disorders including Alzheimer's, Parkinson's, and Creutzfeld-Jakob Disease. Those diseases are devastating and incurable, but a team of biologists ...
Mar 20, 2011 |
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New research focuses on prion diseases
New research by Chongsuk Ryou, researcher at the UK Sanders-Brown Center on Aging and professor of microbiology, immunology and molecular genetics in the UK College of Medicine, may shed light on possible treatments for prion ...
Mar 14, 2011 |
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Needle-in-a-haystack search identifies potential brain disease drug
Scientists who examined more than 10,000 chemical compounds during the last year in search of potential new drugs for a group of untreatable brain diseases, are reporting that one substance shows unusual promise. The early ...
Medicine & Health / Medical research
Feb 23, 2011 |
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Unraveling how prion proteins move along axons in the brain
Researchers at the University of California, San Diego School of Medicine have identified the motors that move non-infectious prion proteins (PrPC) – found within many mammalian cells – up and down long, neuronal ...
Medicine & Health / Medical research
Feb 17, 2011 |
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BSE pathogens can be transmitted by air
Airborne prions are also infectious and can induce mad cow disease or Creutzfeldt-Jakob disorder. This is the surprising conclusion of researchers at the University of Zurich, the University Hospital Zurich and the University ...
Medicine & Health / Diseases, Conditions, Syndromes
Jan 13, 2011 |
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Prion
A prion (pronounced /ˈpriː.ɒn/ ( listen)) is an infectious agent that is composed of protein. To date, all such agents that have been discovered propagate by transmitting a mis-folded protein state; the protein does not itself self-replicate and the process is dependent on the presence of the polypeptide in the host organism. The mis-folded form of the prion protein has been implicated in a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and Creutzfeldt-Jakob disease (CJD) in humans. All known prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and are always fatal. In general usage, prion refers to the theoretical unit of infection. In scientific notation, PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSC refers to the misfolded form of PrP, that is responsible for the formation of amyloid plaques that lead to neurodegeneration.
Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing tissue damage and cell death. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.
Proteins showing prion-type behavior are also found in some fungi and this has been important in helping to understand mammalian prions. However, fungal prions do not appear to cause disease in their hosts and may even confer an evolutionary advantage through a form of protein-based inheritance.
The word prion is a compound word derived from the initial letters of the words proteinaceous and infectious, with -on added by analogy to the word virion.
For more information about Prion, read the full article at
Wikipedia.
This text uses material from Wikipedia and is available under the GNU Free Documentation License.
