In Vitro Expression and Biosynthesis of Prion Protein

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Abstract
Prion protein (PrP) is an endogenous protein of central nervous system and a variety of other mammalian tissues (Chesebro et al. 1985; Oesch et al. 1985; Hope et al. 1986; Meyer et al. 1986; Rubenstein et al. 1986; Cho 1986; Hope et al. 1988; Caughey et al. 1988a). Although its function is not clear, it has been reported recently that PrP may participate in lymphocyte activation (Cashman et al. 1990). In addition, a partially homologous protein of chickens has been reported to be involved in the regulation of the expression of a neurotransmitter receptor at the neuromuscular junction (Harris et al. 1989). A common feature of scrapie, Creutzfeldt-Jakob disease, kuru, Gerstmann-Sträussler syndrome and related transmissible neurodegenerative diseases is the accumulation of a protease-resistant form of prion protein (PrP-res1) in tissues harboring substantial amounts of the transmissible agent (Bolton et al. 1982; Diringer et al. 1983; McKinley et al. 1983; Brown et al. 1986). Unlike the normal, protease-sensitive PrP (PrP-sen1), PrP-res has the tendency to aggregate into amyloid-like fibrils (Prusiner et al. 1983; Diringer et al. 1983; DeArmond et al. 1985; Cho 1986; Wiley et al. 1987; Merz et al. 1987) and plaques (Bendheim et al. 1984; DeArmond et al. 1985; Roberts et al. 1986; Wiley et al. 1987) and has been identified as a major component of brain fractions enriched for the scrapie agent (Bolton et al. 1982; Diringer et al. 1983).