Disease relevance of glutathione

• Glutathione (GSH; gamma-glutamylcysteinylglycine), a crucial molecule in the maintenance of cellular redox status, plays a critical role in development, and it is also protective against methylmercury toxicity [1].
• Glutathione synthetic capacity is increased in liver and other tissues during the acute phase of experimental sepsis [2].

High impact information on glutathione

• Glutathione (L-gamma-glutamyl-L-cysteinylglycine, GSH), is a vital intra- and extracellular protective antioxidant [3].
• Glutathione (L-gamma-glutamyl-L-cysteinylglycine, GSH) is synthesized from its constituent amino acids by the sequential action of gamma-glutamylcysteine synthetase (gamma-GCS) and GSH synthetase [4].
• Specifically, HGF exerted its protective effect by counteracting: (i) the overproduction of either hydrogen peroxide and superoxide anion, (ii) the reduction of intracellular gamma-glutamylcysteinylglycine level, and (iii) the depolarization of mitochondrial membrane, induced by prolonged FFAs exposure [5].
• In the CLP group, ReGSH and CAT were decreased (P = 0.0001, P = 0.07, respectively); and MDA, MPO, and NN were increased (P = 0.02, P = 0.0001, P = 0.043, respectively), compared with the sham group [6].
• The pre-treatment with gamma-glutamylcysteinylglycine or estrogen, both effective antioxidants, significantly attenuated TRAIL-induced apoptosis through the reduction of ROS accumulation and diminished caspases activity [7].

Psychiatry related information on glutathione

• Up-regulation of thioredoxin reductase, peroxiredoxins, catalases, and cytochrome c peroxidase in the glrA-deletion strain revealed interplay between the glutathione system and both the thioredoxin system and hydrogen peroxide defense mechanisms [8].

Biological context of glutathione

• Altered gamma-glutamylcysteinylglycine homeostasis has been implicated in a wide variety of human diseases [9].

Anatomical context of glutathione

• In order to investigate the nature of NAC's protective effect, we measured L-gamma-glutamyl-L-cysteinylglycine (GSH), oxidized glutathione (GSSG), malondialdehyde (MDA) and catalase activity both in the presence and absence of NAC in lead-exposed CHO cells [10].

Associations of glutathione with other chemical compounds

• Inhibition of glutathione synthesis by buthionine sulfoximine enhanced the anti-cancer activity of melphalan in preclinical models of multiple myeloma. [11]
• Assuming sufficient glutathione reductase activity and non-limiting NADPH supply, the observed almost full reduction of roGFP2 in vivo suggests that a 2.5 mm cytosolic glutathione buffer would contain only 25 nm oxidized glutathione disulfide (GSSG) [12].
• SB203580, an inhibitor of p38 MAPK, abolished glutathione elevation and cytoprotection by lactacystin [13].
• Buthionine sulfoximine treatment resulted in a 24% reduction in canine atrial glutathione content, a reduction in atrial contractility, and an attenuation of I(Ca,L) in the canine atrial myocytes [14].
• At the concentration that produced >80% yeast GR inhibition, 2-AAPA showed no inhibition against glutamylcysteine synthetase, glutathione synthetase, catalase, and superoxide dismutase, but minimal inhibition against glutathione S-transferase and glutathione peroxidase [15].

Gene context of glutathione

• Glutathione (gamma-glutamylcysteinylglycine, GSH) is an important cellular antioxidant [16].
• These data indicate that the higher resistance in microglia against HSV infections may be due to the expression of GLT-1, which can maintain the glutathione levels and provide a mechanism for microglial self-defense against HSV [17].

References