Cellular prion protein (PrPC) is a highly conserved, 33-35 kDa protease-sensitive, sialoglycoprotein of unknown function which is endogenously expressed in brain. Studies have shown this protein to be anchored to the external surface of the cell membrane by glycosyl phosphatidylinositol. A post-translationally altered, protease-resistant PrPC isoform ( PrP-Scrapie or PrPSc) of 27-30 kDa is found in association with several fatal neurodegenerative disorders collectively termed transmissible spongiform encephalopathies (TSEs). Deposition of PrPSc in the central nervous system is a reliable indication of a TSE. Prion diseases include scrapie in sheep and goats, bovine spongiform encephalopathy or ""Mad Cow disease"", and chronic wasting disease (CWD) in deer and elk. PrP is responsible for Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker (GSS) disease, Fatal Familial Insomnia (FFI), and Kuru in humans.
Alternative prion protein; AltPrP; ASCR; CD230; CD230 antigen; CJD; GSS; Major prion protein; MGC26679; prion-related protein; PRNP; PrP; PrP27-30; PrP33-35C; PrPc
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