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
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
收藏
页码:119 / 126
页数:8
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