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Detecting Prions
Joan Stephenson, PhD
JAMA. 2001;286:159.
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| Since this article does not have an abstract, we have provided the first 150 words of the full text and any section headings. |
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Diagnosis of diseases believed to be caused by the abnormal proteins called prions has been hampered by the fact that current tests are unable to detect the small amounts of prions in tissues outside the brain. Now, a new technique for replicating minute amounts of prions could pave the way for early detection of prion diseases such as scrapie and bovine spongiform encephalopathy in animals and variant Creutzfeldt-Jakob disease in humans, according to a new report in the June 14 Nature.
Claudio Soto, PhD, and colleagues at the Serono Pharmaceutical Research Institute in Geneva, Switzerland, developed the prion-amplifying method, called protein misfolding cyclic amplification (PMCA). The technique speeds up the rate at which a prion protein transforms its normal counterpart into the pathologic form, accomplishing in a few hours in the laboratory a process that takes years to unfold in the brain.
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