The importance of the disulfide bond in prion protein conversion

被引：81

作者：

Herrmann, LM ^{[1
]}

Caughey, B ^{[1
]}

机构：

[1] NIAID, Rocky Mt Labs, Persistent Viral Dis Lab, NIH, Hamilton, MT 59840 USA

来源：

NEUROREPORT | 1998年 / 9卷 / 11期

关键词：

conversion; disulfide; prion; PrP; reduction; scrapie; TSE;

D O I：

10.1097/00001756-199808030-00006

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

THE conversion of normal, protease sensitive prion protein (PrP-sen) to the abnormal protease-resistant form (PrP-res) is of central importance in the pathogenesis of scrapie and other transmissible spongiform encephalopathies. In the present study, the effects of reduction of the disulfide bond on the PrP-sen to PrP-res conversion in a cell-free system were examined. The addition of the disulfide reducing agent dithiothreitol inhibited the cell-free conversion reaction with an IC,, of 2-2.5 mM. Separate pretreatment of either PrP-sen or PrP-res with dithiothreitol and an alkylating agent also inhibited the conversion reaction. Results of this study show that preservation of the disulfide bond is important in the conversion of PrP-sen to PrP-res. NeuroReport 9: 2457-2461 (C) 1998 Rapid Science Ltd.

引用

页码：2457 / 2461

页数：5

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