Detection of protein S-nitrosylation with the biotin-switch technique

被引：249

作者：

Forrester, Michael T. ^{[1
,2
]}

Foster, Matthew W. ^{[3
]}

Benhar, Moran ^{[3
]}

Stamler, Jonathan S. ^{[1
,3
]}

机构：

[1] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA

[2] Duke Univ, Med Ctr, Med Scientist Training Program, Durham, NC 27710 USA

[3] Duke Univ, Med Ctr, Dept Med, Durham, NC 27710 USA

来源：

FREE RADICAL BIOLOGY AND MEDICINE | 2009年 / 46卷 / 02期

基金：

美国国家卫生研究院;

关键词：

Biotin-switch technique; S-nitrosylation; S-nitrosothiol; Redox; Cysteine; Thiol; Nitric oxide; Nitrosative stress; Free radicals; NITRIC-OXIDE SYNTHASE; DIFFERENCE GEL-ELECTROPHORESIS; NEURONAL CELL-DEATH; ASCORBIC-ACID; NITROSATIVE STRESS; RYANODINE RECEPTOR; DISTINCT MECHANISMS; PARKINSONS-DISEASE; ENDOTHELIAL-CELLS; OXIDATIVE STRESS;

D O I：

10.1016/j.freeradbiomed.2008.09.034

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：

Protein S-nitrosylation, the posttranslational modification of cysteine thiols to form S-nitrosothiols, is a principle mechanism of nitric oxide-based signaling. Studies have demonstrated myriad roles for S-nitrosylation in organisms from bacteria to humans, and recent efforts have greatly advanced Our scientific understanding of how this redox-based modification is dynamically regulated during physiological and pathophysiological conditions, The focus of this review is the biotin-switch technique (BST), which has become a mainstay assay for detecting S-nitrosylated proteins in complex biological systems. Potential pitfalls and modern adaptations of the BST are discussed, as are future directions for this assay in the burgeoning field of protein S-nitrosylation. (C) 2008 Elsevier Inc. All rights reserved.

引用

页码：119 / 126

页数：8

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