Glutathione (gamma-glutamyl-cysteinyl-glycine; GSH) is the most abundant low-molecular-weight thiol, and GSH/glutathione disulfide is the major redox couple in animal cells. The synthesis of GSH from glutamate, cysteine, and glycine is catalyzed sequentially by two cytosolic enzymes, gamma-glutamylcysteine synthetase and GSH synthetase. Compelling evidence shows that GSH synthesis is regulated ...

Reduced glutathione (GSH) is a ubiquitous tripeptide found in all eukaryotic cells, including all mammalian tissue. GSH is available to the mammalian organism through cellular synthesis from constituent amino acids, and also through dietary intake. Depletion of GSH in the substantia nigra is one of the earliest reported biochemical events to occur in Parkinson's disease (PD). 1 e GSH content of...

During inflammatory processes, immunocompetent cells are exposed to substantial amounts of free radicals and toxic compounds. Glutathione is a cysteine-containing tripeptide that an important ubiquitous antioxidant molecule produced in human organs. The intracellular content GSH regulates the detoxifying capacity cells, as well immune response. particularly liver, where it serves major non-prot...

Materials and methods: Classical biochemical methods were used to determine plasma malondialdehyde (MDA), nitric oxide (NO), glutathione peroxidase (GSH-Px), catalase (CAT), superoxide dismutase (SOD), and glutathione (GSH) levels. Enzyme-linked immunosorbent assay was used to determine plasma insulin levels and reverse transcriptasepolymerase chain reaction was used to determine the levels of ...

The tripeptide thiol glutathione (GSH) has facile electron-donating capacity, linked to its sulfhydryl (-SH) group. Glutathione is an important water-phase antioxidant and essential cofactor for antioxidant enzymes; it provides protection also for the mitochondria against endogenous oxygen radicals. Its high electron-donating capacity combined with its high intracellular concentration endows GS...

Normal cellular functions essentially depend on a balanced redox environment. Free radicals and nonradical oxidants can shift the redox balance toward a more “oxidized” state, which is counteracted by the intracellular antioxidant defense systems. These include the enzymes superoxide dismutase and catalase, as well as the thiol-reducing systems (glutathione, glutaredoxin, and thioredoxin). Glut...

Glutathione, gamma-glutamyl cysteine synthetase (gamma -GCS) and glutathione reductase (GSH-R) activity were determined biochemically in the lens during various stages after subcutaneous administration of sodium selenite in multiple low dosages and single high dosages. The GSH concentration and gamma-GCS and GSH-R activity declined progressively after the selenite administration. The changes ob...

One member of the OATP family of transporters, rat Oatp1, functions as an anion exchanger that is driven in part by the glutathione (GSH) electrochemical gradient, indicating that other OATP-related transporters may also be energized by this mechanism. The present study examined whether rat Oatp2 is also an anion exchanger, and, if so, whether it is energized by the GSH electrochemical gradient...


 Purpose: To determine the effect of glutathione (GSH) suppressors styrene oxide (SO) and diethyl maleate (DEM) on hepatic expression cytochrome P450 family 1 (Cyp1) isoforms that are related to carcinogenesis including Cyp1a1, Cyp1a2, Cyp1b1.
 Methods: Seven-week-old ICR mice were intraperitoneally injected with SO (150 300 mg/kg/day), DEM (175 350 or N-acetylcysteine (NAC; 600 mg/k...

Glutathione export from uninfected human erythrocytes was compared with that from cells infected with the malaria parasite Plasmodium falciparum using two separate methods that distinguish between oxidized (GSSG) and reduced (GSH) glutathione. One involved enzymatic recycling with or without thiol-masking; the other involved rapid derivatization followed by HPLC. Glutathione efflux from uninfec...