作者: John J. Mieyal , Melissa D. Shelton
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摘要: S-glutathionylation is a reversible post-translational modification that continues to gain eminence as redox regulatory mechanism of protein activity and associated cellular functions. Many diverse proteins such transcription factors, adhesion molecules, enzymes, cytokines are reported undergo glutathionylation, although the functional impact has been less well characterized. De-glutathionylation catalyzed specifically efficiently by glutaredoxin (GRx, aka thioltransferase), facile reversibility critical in determining physiological relevance glutathionylation means regulation. Thus, studies with cohesive themes addressing both corresponding GRx especially useful advancing understanding. Reactive oxygen species (ROS) regulation accepted playing role inflammatory processes, leukostasis destruction foreign particles macrophages. We discuss this review current implications and/or response diseases chronic inflammation, namely diabetes, atherosclerosis, lung disease, cancer, Alzheimer’s viral infections.