Abstract
Like numerous proteins of various structural and functional classes, the glycosylphosphatidylinositol (GPI)-anchored cellular prion protein (PrPC) has been recognized to undergo endoproteolytic processing for decades, a phenomenon observed in various cultured cell lines, as well as human and several animal tissue extracts. Despite this, the physiological significance of PrPC proteolytic cleavage has not yet been entirely elucidated. Experimental evidence suggests independent normal biological functions of the full-length and truncated PrPC species, as well as probable links of endoproteolysis to prion disease transmission susceptibility, pathogenesis, and toxicity. The accurate characterization of constitutive PrPC processing, through the method outlined in this chapter, is therefore an important tool in order to investigate the biological relevance of the alternative cleavage events.
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