The PRNP gene encodes the major prion protein (PrP, CD230), a widely-expressed glycoprotein expressed at high levels in the central nervous system. While the typical cellular function of PrP is not well defined, it is a putative antioxidant and a metal-binding protein that may be involved in signal transduction. Prion proteins can adopt different conformations; the cellular PrPc prion protein may be converted following translation into the β-sheet-rich scrapie isoform (PrPsc) responsible for several prion diseases, including bovine spongiform encephalopathy and human Creutzfeldt-Jakob disease. Unlike most neurodegenerative diseases, prion diseases are infectious as prions are capable of propagating by conferring an abnormally folded state onto properly folded cellular proteins. In addition, the cellular PrPc has may be involved in β-amyloid peptide oligomerization and synaptic toxicity.
