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. 2000 . Glutathione metabolism and oxidative stress in neurodegeneration . Eur. J. Biochem. 267 : 4903 . Grace , S.C. , Logan , B.A. 1996 . Acclimation of foliar
Yeast protein sequence-based homology search for glutathione (GSH) metabolic enzymes and GSH transporters demonstrated that Aspergillus nidulans has a robust GSH uptake and metabolic system with several paralogous genes. In wet laboratory experiments, two key genes of GSH metabolism, gcsA, and glrA, encoding γ-l-glutamyl-l-cysteine synthetase and glutathione reductase, respectively, were deleted. The gene gcsA was essential, and the ΔgcsA mutant required GSH supplementation at considerably higher concentration than the Saccharomyces cerevisiae gsh1 mutant (8–10 mmol l−1 vs. 0.5 μmol l−1). In addition to some functions known previously, both genes were important in the germination of conidiospores, and both gene deletion strains required the addition of extra GSH to reach wild-type germination rates in liquid cultures. Nevertheless, the supplementation of cultures with 10 mmol l−1 GSH was toxic for the control and ΔglrA strains especially during vegetative growth, which should be considered in future development of high GSH-producer fungal strains. Importantly, the ΔglrA strain was characterized by increased sensitivity toward a wide spectrum of osmotic, cell wall integrity and antimycotic stress conditions in addition to previously reported temperature and oxidative stress sensitivities. These novel phenotypes underline the distinguished functions of GSH and GSH metabolic enzymes in the stress responses of fungi.
Emri, T., Pócsi, I., Szentirmai, A. (1997) Glutathione metabolism and protection against oxidative stress caused by peroxides in Penicillium chrysogenum . Free Radicals in Biology and Medicine 23 , 809
Glutathione (g-L-glutamyl-L-cysteinyl-glycine; GSH) shares structural similarities with the b-lactam biosynthetic intermediate ACV-tripeptide {d-(L-a-aminoadipyl)-L-cysteinyl-D-valine}. Not surprisingly, GSH has been reported to inhibit the b-lactam biosynthetic machinery quite effectively and, hence, strategies to decrease the intracellular GSH concentrations without influencing negatively the physiological status of idiophasic mycelia would attract industrial interests. Here we present a detailed map of the GSH metabolic network of P. chrysogenum and show a promising way to keep the GSH pool selectively down under penicillin producing conditions. This procedure includes a well-controlled and transient lowering of pH at the beginning of the production phase, and it relies on the GSH-dependent detoxification of the protonophore penicillin side-chain precursors phenoxyacetic acid (POA) and phenylacetic acid (PA). Encouraging preliminary fed-batch fermentation experiments have been performed to test this technological proposal. Interestingly, the mechanism of the activation of POA and PA to the appropriate CoA derivatives has remained yet to be answered but the involvement of GSH seems to be rather unlikely in this case. Our data also challenge the hypothesis that the formation of different kinds of penicillins would be an alternative to GSH-dependent detoxification processes in P. chrysogenum.
metabolism and its role in hepatotoxicity. Pharmacol. Ther. 52 , 287–305. Kaplowitz N. Glutathione metabolism and its role in hepatotoxicity Pharmacol
. 176 973 984 Emri, T., Pócsi, I., Szentirmai, A. (1997) Glutathione metabolism and protection against oxidative stress caused by peroxides in
mays seedlings by the regulation of ascorbate and glutathione metabolism . Biol. Plant. doi:10.1007/s10535-016-0669-4 Dalton , D.A. , Russell , S.A. , Hanus , F.J. , Pascoe
– 7338 . Shan , C. , Liang , Z. 2010 . Jasmonic acid regulates ascorbate and glutathione metabolism in Agropyron cristatum leaves under water stress . Plant Sci. 178
Az ischaemiatolerancia növelésének lehetőségei a májsebészetben
Increased ischemic tolerance in liver surgery
Regulative potential of glutamine – relation to glutathione metabolism Nutr 18 217 21 .