2018
DOI: 10.2478/aiht-2018-69-2966
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Glutathionylation: a regulatory role of glutathione in physiological processes

Abstract: Glutathione (γ-glutamyl-cysteinyl-glycine) is an intracellular thiol molecule and a potent antioxidant that participates in the toxic metabolism phase II biotransformation of xenobiotics. It can bind to a variety of proteins in a process known as glutathionylation. Protein glutathionylation is now recognised as one of important posttranslational regulatory mechanisms in cell and tissue physiology. Direct and indirect regulatory roles in physiological processes include glutathionylation of major transcriptional… Show more

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Cited by 47 publications
(39 citation statements)
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References 221 publications
(375 reference statements)
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“…Except for glutathione, GDAS includes enzymes such as GP, GR, GT etc. [47,48]. In this study, GP activity decreased in MIA-OA group in 1.5 times, compared to control group (Table 3).…”
Section: Resultssupporting
confidence: 49%
“…Except for glutathione, GDAS includes enzymes such as GP, GR, GT etc. [47,48]. In this study, GP activity decreased in MIA-OA group in 1.5 times, compared to control group (Table 3).…”
Section: Resultssupporting
confidence: 49%
“…Glutathionylation of specific cysteine residues in mitogen-activated protein kinases (MAPK) [69][70][71] and PTPs [12,27,72] affect their transduction and regulatory properties and ultimately lead to an altered tight junction functionality. Both GSH depletion and GSSG accumulation seem to be crucial events in this mechanism [13,73]. Here, redox changes in target proteins, initiated by reactive oxygen species or GSH redox imbalance, often precede protein glutathionylation and affects the binding strength of GSH to a protein [74,75].…”
Section: Abrupt Weaning Was Associated With Barrier Disruption and Tmentioning
confidence: 99%
“…Enzymes like leukotriene C4 synthase, prostaglandin‐endoperoxide synthase 1 or 2 and prostaglandin E synthase, require glutathione as a cofactor for their activity. These enzymes are part of the superfamily of large, membrane‐associated proteins in eicosanoid and glutathione metabolism (MAPEG), sharing structural evolutionary relationship with GSTs .…”
Section: Introductionmentioning
confidence: 99%