Biochemical methods for monitoring protein thiol redox states in biological systems

被引:90
|
作者
Rudyk, Olena [1 ]
Eaton, Philip [1 ]
机构
[1] Kings Coll London, St Thomas Hosp, Rayne Inst, Cardiovasc Div,British Heart Fdn,Ctr Excellence, London SE1 7EH, England
来源
REDOX BIOLOGY | 2014年 / 2卷
基金
英国医学研究理事会; 欧洲研究理事会;
关键词
Redox state; Disulfide; S-nitrosation; Hyperoxidation; Keap1; Methods; CYSTEINE-SULFINIC ACID; ENCODED FLUORESCENT INDICATOR; S-NITROSYLATION; SULFENIC ACID; HYDROGEN-PEROXIDE; OXIDATIVE STRESS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; DISULFIDE; QUANTIFICATION; INACTIVATION;
D O I
10.1016/j.redox.2014.06.005
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
Oxidative post-translational modifications of proteins resulting from events that increase cellular oxidant levels play important roles in physiological and pathophysiological processes. Evaluation of alterations to protein redox states is increasingly common place because of methodological advances that have enabled detection, quantification and identification of such changes in cells and tissues. This mini-review provides a synopsis of biochemical methods that can be utilized to monitor the array of different oxidative and electrophilic modifications that can occur to protein thiols and can be important in the regulatory or maladaptive impact oxidants can have on biological systems. Several of the methods discussed are valuable for monitoring the redox state of established redox sensing proteins such as Keap1. (C) 2014 Published by Elsevier B.V.
引用
收藏
页码:803 / 813
页数:11
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