Analysis of endogenous PrPC processing in neuronal and non-neuronal cell lines.

Abstract

Numerous transmembrane and glycosylphosphatidylinositol (GPI)-anchored proteins, covering a vast range of structural and functional classes, are recognized to undergo proteolytic cleavage or shedding from the plasma membrane. Although this widespread phenomenon seems fundamental to normal cellular biology, proteolytic processing also seems to play a central role in the pathogenesis of some neurodegenerative disorders such as Alzheimer's disease. An analogous situation may exist in prion disorders. The GPI-anchored cellular prion protein (PrP(C)) may be endoproteolytically cleaved at two different sites: one at the C-terminal end of the octameric repeat region and the other within a potential..