Protein S-glutathionylation: a regulatory device from bacteria to humans.

来自 Semantic Scholar

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157

作者：

I Dalle-Donne，R Rossi，G Colombo，D Giustarini，A Milzani

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摘要：

S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the tripeptide glutathione, the most abundant and important low-molecular-mass thiol within most cell types. Protein S-glutathionylation is promoted by oxidative or nitrosative stress but also occurs in unstressed cells. It can serve to regulate a variety of cellular processes by modulating protein function and to prevent irreversible oxidation of protein thiols. Recent findings support an essential role for S-glutathionylation in the control of cell-signalling pathways associated with viral infections and with tumour necrosis factor-(-induced apoptosis. Glyceraldehyde-3-phosphate dehydrogenase has recently been implicated in the regulation of endothelin-1 synthesis by a novel, S-glutathionylation-based mechanism involving messenger RNA stability. Moreover, recent studies have identified S-glutathionylation as a redox signalling mechanism in plants.

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关键词：

Animals Humans Glutathione Bacterial Proteins Signal Transduction Protein Processing, Post-Translational Protein Folding RNA Stability Oxidation-Reduction Oxidative Stress