Glutathione, an antioxidant tripeptide: Dual roles in Carcinogenesis and Chemoprevention.

Glutathione, an antioxidant tripeptide: Dual roles in Carcinogenesis and Chemoprevention. Curr Protein Pept Sci. 2019 Feb 06;: Authors: Narayanankutty A, Jdevagiri JT, Narayanankutty V Abstract Glutathione (GSH or reduced glutathione) is a tripeptide of gamma-Glutamyl-cysteinyl-glycine and the predominant intracellular antioxidant in many organisms including humans. GSH and associated enzymes are controlled by a transcription factor-nuclear factor-2 related erythroid factor-2 (Nrf2). In cellular milieu, GSH protects the cells essentially against a wide variety of free radicals including reactive oxygen species, lipid hydroperoxides, xenobiotic toxicants, and heavy metals. It has two forms, the reduced form or reduced glutathione (GSH) and oxidized form (GSSG), where two GSH moieties combine by sulfhydryl bonds. Glutathione peroxidase (GPx) and glutathione-s-transferase (GST) essentially perform the detoxification reactions using GSH, converting it into GSSG. Glutathione reductase (GR) operates the salvage pathway by converting GSSG to GSH with the expense of NADPH and restores the cellular GSH pool. Hence, GSH and GSH-dependent enzymes are necessary for maintaining the normal redox balance in the body and help in cell survival under stress conditions. In addition, GST removes various carcinogenic compounds offering a chemopreventive property, whereas the GSH system plays a significant role in regulating the cellular survival by offer...
Source: Current Protein and Peptide Science - Category: Biochemistry Authors: Tags: Curr Protein Pept Sci Source Type: research