Cellular biology of prion protein

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1 hinese Bulletin of Life Sciences Vol. 16, o. 2 Apr., (2004) Q2;Q51 A ellular biology of prion protein ZHAG Dong-Wei, A Shan-Ji, ZHAO Jie-Xu* (Department of eurology, the First Hospital, Jilin University, hangchun , hina) Abstract: Prion diseases are fatal neurodegenerative disorders of humans and animals that are important because of their impact on public health and because they exemplify a novel mechanism of infectivity and biological information transfer. These diseases are caused by conformational conversion of a normal host glycoprotein (PrP ) into an infectious isoform (PrP Sc ) that is devoid of nucleic acid. This review focuses on the current understanding of prion diseases at the cellular biological level. Information is then presented about the structure, expression, biosynthesis, and possible function of PrP and PrP Sc, as well as its posttranslational processing, cellular localization, and trafficking. The review concludes with suggestions of several important avenues for future investigation. Key words: prion protein; cellular biology; prion diseases prion protein PrP (PrP ) [1] (Kuru disease) (reutzfeldt- Jakob disease, JD) GSS (Gerstmann- Sträussler syndrome, GSS) (fatal familial insomnia, FFI) [2] (PrP Sc ) (1971 ) (1976 ) 1942 *

2 mra [5] PrP PrP mra mra [3~4] PrP [10] PrP 1.3 [11] [6] [12] [7] 10kD 1.4 [13] [14] [8] (glycosyl-phosphatidylinositol anchor ) 1.5 (phosphatidylinositol-specific phospholipase, [15] PI-PL), [16] [9]

3 98 [17] 1 ~5 [22] PI-PL [14] ~6 24~48 [23] [19] PI-PL (PI-PL resistance) 2a P12 HO PI-PL β [18] 10 1 (detergent insolubility) 30 [24] [19] resistance) 6 (protease HO P12 ; 2.4 [20] 110 [25] 89 [26] 2.2 2a [21] [27~28]

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