Redox Regulation of Mitochondrial ATP Synthase

被引：66
|
作者：
Wang, Sheng-Bing [1 ]
Murray, Christopher I. [2 ]
Chung, Heaseung S. [2 ]
Van Eyk, Jennifer E. [1 ,2 ]
机构：
[1] Johns Hopkins Univ, Sch Med, Dept Med, Div Cardiol, Baltimore, MD 21224 USA
[2] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21224 USA
来源：
TRENDS IN CARDIOVASCULAR MEDICINE | 2013年 / 23卷 / 01期
关键词：
S-NITROSYLATION; THIOL CHEMISTRY; REACTIVE OXYGEN; GLUTATHIONYLATION; SITE;
D O I：
10.1016/j.tcm.2012.08.005
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
Reversible cysteine oxidative post-translational modifications (Ox-PTMs) represent an important mechanism to regulate protein structure and function. In mitochondria, redox reactions can modulate components of the electron transport chain (ETC), the F1F0-ATP synthase complex, and other matrix proteins/enzymes. Emerging evidence has linked Ox-FTMs to mitochondrial dysfunction and heart failure, highlighting some potential therapeutic avenues. Ox-PTMs can modify a variety of amino acid residues, including cysteine, and have the potential to modulate the function of a large number of proteins. Among this group, there is a selected subset of amino acid residues that can function as redox switches. These unique sites are proposed to monitor the cell's oxidative balance through their response to the various Ox-PTMs. In this review, the role of Ox-PTMs in the regulation of the F1F0-ATP synthase complex is discussed in the context of heart failure and its possible clinical treatment. (Trends Cardiovasc Med 23:14-18) (C) 2013 Elsevier Inc. All rights reserved.
引用
收藏
页码：14 / 18
页数：5
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