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drugs [bromobenzenes and acetaminophen], pollutants, carcinogens) to form mercaptures.[27] Beside conjugation of xenobiotics, GST-Pi act as Jun N-terminal kinase (JNK)-inhibitor, thus preventing c-Jun phosphorylation, by forming macromolecular complexes with JNK in vitro .[124] It is capable of forming disulfide bonds with cysteine residues of protein known as S-glutathionylation.[112] S-glutathionylation of proteins (ubiquitin-conjugating enzyme, cytochrome c oxidase and thioredoxin) plays an important role in cell physiology,[27] affecting members of signal transduction chains involved in cell proliferation.[112] Increase in apoptosis and reduction in cellular proliferation by the activation of several signaling pathways like protein kinase B, H-ras, T-cell p59, c-JNK, apoptosis signal-regulated kinase 1, protein phosphatase 1 and 2A, calcineurin, nuclear factor-kB (NF-kB)/p50, and mitogen-activated protein kinase, is evident by the reduction in GSH/GSSG ratio.[27,112] Glutathione is needed for the conversion of Dopa-quinone to glutathione-Dopa synthesis of pheomelanin and trichochromes, as well as a coenzyme for liver enzyme for activation of methionine to form active form “S-adenosyl methionine.”[9] GSSG is harmful to red blood cell (RBC) membranes and lens proteins and is converted to reduced glutathione, which is required for the integrity of RBCs membrane and lens proteins.[9] Recent studies have shown the pro-oxidant properties of glutathione in which glutathione and its catabolites (e.g
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