Human prion protein (PrP), also known as PRNP, is a ubiquitously expressed GPI-anchored cell surface glycoprotein associating with lipid raft components and functioning as a signaling molecule. PrP plays a role in apoptosis in a cell context-dependent manner, is involved in proliferation of epithelial cells and in distribution of junction-associated proteins in human enterocytes. Conversion of this normal cellular prion protein (PrPc) into an abnormal conformer (PrPSc) is the crucial step associated with triggering the pathogenesis of the prion neurodegenerative disorders, such as the Creutzfeld-Jakob disease (CJD). Whereas PrPc is rich in alpha-helices, the PrPSc form has higher content of beta-sheets and is resistant to proteinase K.
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Protein Aliases: Alternative prion protein; AltPrP; ASCR; CD230; CD230 antigen; CJD; GSS; Major prion protein; prion; prion protein; prion protein, PrP; prion protein, structural; prion-related protein; PRNP; PrP; PrP27 30; PrP27-30; PrP33 35C; PrP33-35C; PrPc
AA960666; AI325101; ALTPRP; ASCR; CD230; CJD; GSS; KURU; p27-30; PRIP; Prn; Prn-i; Prn-p; PRNP; PRP; PrP27-30; PrP33-35C; PrP