期刊
PROTEIN AND PEPTIDE LETTERS
卷 17, 期 10, 页码 1234-1244出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986610792231573
关键词
Antioxidant; glutathione; glutathionylation; oxidative stress; redox regulation; reactive oxygen species
资金
- Jiangnan University
- National Science Fund for Distinguished Young Scholars [20625619]
- Major State Basic Research Development Program of China [2007CB 714306]
- National Innovation Experiment Program for University Students [081029504]
- Innovative Research Team in University, Jiangsu Province, China
- National High Technology Research and Development Program of China [2006AA10Z313]
- National Natural Science Foundation of Jiangsu Province [BK2008096]
Glutathionylation, covalently attaching glutathione(s) to cysteine residue(s) of a protein, has attracted great attention in recent years. The importance of glutathionylation was initially recognized for its role in protecting proteins from irreversible oxidation; however, more studies indicate that glutathionylation is also involved in redox regulation under both normal physiological conditions and oxidative stresses. Potential mechanisms for the formation of glutathionylated proteins have been proposed. Despite the differences among the details of these mechanisms, glutathionylation is generally induced by intermediates including glutathione disulfide, protein-sulfenic acids, and thiyl radical. Taking advantages of proteomics techniques, authors have established methods to identify glutathionylation utilizing S-35-cysteine- or biotinlabeled glutathione, or anti-GSH antibodies. Glutathionylation serves multiple roles in cellular biochemistry, such as modulation of enzymatic activity, glutathione storage, and dynamic regulation of protein function. Development of more efficient methods for glutathionylation identification, systematic investigation of its roles in the context of cellular biochemistry, the interaction with other types of protein modification, and its relevance to some health-threatening diseases will be the wider focus of studies in protein glutathionylation.
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