Cell biology of the prion protein.
Cell biology of the prion protein.
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朊病毒蛋白的细胞生物学。
DOI：
10.1007/978-3-642-60983-1_7
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发表时间：
1996
影响因子：
--
通讯作者：
Shyng,SL
中科院分区：
文献类型：
--
作者：
Harris,DA;Gorodinsky,A;Lehmann,S;Moulder,K;Shyng,SL
朊病毒是导致一组致命的神经退行性疾病（称为海绵状脑病）的传染性颗粒（PRUSINERand DEARMOND 1994 年综述）。该组包括人类的克雅氏病、库鲁病、格斯特曼-斯特劳斯勒综合征和致命的家族性失眠症，以及动物的痒病和牛海绵状脑病。朊病毒的主要成分是糖蛋白 PrPSc，它是宿主正常细胞表面蛋白 PrPc 的翻译后修饰亚型（OESCHet al. 1985）。 PrPC 和 PrPSc 在二级结构上彼此不同，并表现出明显不同的生化特性（CAUGHEYet al. 1991；Panet al. 1993；SAFARet al. 1993）。假设当感染 PrPScjn 的接种物与宿主 PrPc 特异性相互作用，催化其转化为 PrPc 时，就会发生朊病毒复制（PRUSINERetal. 1990）。据推测，这种转变在携带与家族性朊病毒病相关的突变的 PrPScm 分子中自发发生。
Prions are the infectious particles responsible for a group of fatal neurodegenerative diseases known as spongiform encephalopathies (reviewed in PRUSINERand DEARMOND1994). This group includes Creutzfeldt-Jakob disease, kuru, Gerstmann-Sträussler syndrome, and fatal familial insomnia in human beings, and scrapie and bovine spongiform encephalopathy in animals. The principal component of prions is the glycoprotein PrPSc, which is a posttranslationally modified isoform of a normal cell-surface protein of the host called PrPc(OESCHet al. 1985). PrPCand PrPScdiffer from each other in secondary structure and display markedly different biochemical properties (CAUGHEYet al. 1991; Panet al. 1993; SAFARet al. 1993). Prion replication is hypothesized to occur when PrPScjn infecting inoculum interacts specifically with host PrPc, catalyzing its conversion to PrPc(PRUSINERetal. 1990). It is postulated that this conversion takes place spontaneously in PrPScmolecules carrying mutations that have been linked to familial forms of prion disease.