Ludwig-Maximilians-Universität, Chair of Metabolic Biochemistry

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The Prion Protein: Friend and Foe

Curr Issues Mol Biol. 2009 Sep 18;12(2):49-50. [Epub ahead of print]

Publication Date: 2009
Type of Publication: Journal Article
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-Staussler-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. 

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