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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Scientists show 'lifeless' prions capable of evolutionary change and adaptation
Scientists from The Scripps Research Institute have determined for the first time that prions, bits of infectious protein devoid of DNA or RNA that can cause fatal neurodegenerative disease, are capable of Darwinian evolution.
Medicine & Health / Medical research
Dec 31, 2009 |
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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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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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Researchers find new piece in Alzheimer's puzzle
Yale researchers have filled in a missing gap on the molecular road map of Alzheimer's disease. In the Feb. 26 issue of the journal Nature, the Yale team reports that cellular prion proteins trigger the process by which ...
Medicine & Health / Diseases, Conditions, Syndromes
Feb 25, 2009 |
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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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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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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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Research identifies drug target for prion diseases, 'mad cow'
Scientists at the University of Kentucky have discovered that plasminogen, a protein used by the body to break up blood clots, speeds up the progress of prion diseases such as mad cow disease.
Medicine & Health / Medical research
Jan 10, 2011 |
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Size of protein aggregates, not abundance, drives spread of prion-based disease
Mad Cow disease and its human variant Creutzfeldt-Jakob disease, which are incurable and fatal, have been on a welcome hiatus from the news for years, but because mammals remain as vulnerable as ever to infectious diseases ...
Medicine & Health / Medical research
Oct 28, 2010 |
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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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Study shows infectious prions can arise spontaneously in normal brain tissue
In a startling new study that involved research on both sides of the Atlantic, scientists from The Scripps Research Institute in Florida and the University College London (UCL) Institute of Neurology in England have shown ...
Medicine & Health / Medical research
Jul 26, 2010 |
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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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First direct information about the prion's molecular structure reported
(PhysOrg.com) -- 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. ...
Oct 05, 2009 |
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Dual role for immune cells in the brain
We all have at one time or another experienced the typical signs of an infection: the fever, the listlessness, the lack of appetite. They are orchestrated by the brain in response to circulating cytokines, ...
Medicine & Health / Neuroscience
Jan 13, 2010 |
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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.
