Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease

被引:70
|
作者
Musaogullari, Aysenur [1 ]
Chai, Yuh-Cherng [1 ]
机构
[1] John Carroll Univ, Dept Chem, University Hts, OH 44118 USA
关键词
S-glutathionylation; redox modification; protein post-translational modification; GSH; GSSG; oxidative stress; NF-KAPPA-B; TYROSINE-PHOSPHATASE; 1B; NECROSIS-FACTOR-ALPHA; FATTY LIVER-DISEASE; JUN DNA-BINDING; OXIDATIVE STRESS; HYDROGEN-PEROXIDE; THIYL RADICALS; REVERSIBLE INACTIVATION; CYSTEINE RESIDUES;
D O I
10.3390/ijms21218113
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
S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases.
引用
收藏
页码:1 / 25
页数:25
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