Glutathione and Thiols

作者: Lou Ann S. Brown , Dean P. Jones

DOI: 10.1007/978-3-319-19096-9_7

关键词:

摘要: Oxidation of the antioxidant glutathione (GSH) to a disulfide (GSSG) has long been an indicator oxidative stress. GSH is also critical in detoxification xenobiotics (drugs, pollutants, carcinogens) through broad range reactions with GSH- dependent enzymes containing redox sensitive cysteine (Cys) residue that undergoes reversible oxidation and reduction at active site: reductase (GR), glutaredoxin (Grx), families peroxidases (Gpxs) GSH-S-transferases (GSTs). GSSG are involved many cellular processes termed S-glutathionylation where bonds formed protein Cys residues subsequently alter enzymatic activity or function. The equipoise GSH/GSSG pivotal signal transduction pathways mediated by reaction reactive oxygen species (ROS) crucial residues. ROS-dependent signaling involves reduced/oxidized thiol pairs including thioredoxin (Trx-SH/Trx-SS) its oxidized form cystine (CySS). Although not equilibrium, these thiol/disulfide couples organized into circuits cross-talk. When disrupted, sites become functions perturbed. Understanding roles homeostasis for other responses organelle cell redox-active chemicals central determining effects such on macromolecular structure, regulation, during life cycle. Through better mechanistic understanding, like resilience adaptability diet environmental exposures likely emerge.

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