Proteolytic fragmentation of the murine prion protein: role of Tyr-128 and His-177

被引：10

作者：

Perera, WSS ^{[1
]}

Hooper, NM ^{[1
]}

机构：

[1] Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

FEBS LETTERS | 1999年 / 463卷 / 03期

基金：

英国医学研究理事会;

关键词：

transmissible spongiform encephalopathy; proteolysis; glycosyl-phosphatidylinositol anchor; serine protease; signal peptidase;

D O I：

10.1016/S0014-5793(99)01648-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The prion protein (PrP) has been proposed to display sequence and structural similarities to membrane-anchored signal peptidases [Glockshuber et al. (1998) FEES Lett, 426, 291-296], We hare investigated the role of Tyr-128 and His-177 in the proteolytic fragmentation of murine PrP by mutating these residues to Phe and Leu. respectively, and expressing the resultant mutants in the human neuroblastoma SH-SY5Y. Both PrP-Y128F and PrP-H177L were expressed at the cell surface as glycosyl-phosphatidylinositol-anchor forms and were localised in detergent-insoluble membrane domains similar to wild type PrP, Following deglycosylation, the 19 kDa proteolytic fragment PrP-II was present in cells expressing either mutant, indicating that Tyr-128 and His-177 are not involved in the proteolytic fragmentation of PrP. (C) 1999 Federation of European Biochemical Societies.

引用

页码：273 / 276

页数：4

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