Glutathione and Sulfur Amino Acids in Human Health and Disease 2008
DOI: 10.1002/9780470475973.ch6
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Glutathione and Sulfur Containing Amino Acids: Antioxidant and Conjugation Activities

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Cited by 12 publications
(13 citation statements)
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“…Its role in replenishing pools of GSH is critical for maintaining a reducing environment within the cell (Huseby et al 2009). The active site of GR is a redox-active disulfide bond which receives electrons from the bound FAD cofactor.…”
Section: Introductionmentioning
confidence: 99%
“…Its role in replenishing pools of GSH is critical for maintaining a reducing environment within the cell (Huseby et al 2009). The active site of GR is a redox-active disulfide bond which receives electrons from the bound FAD cofactor.…”
Section: Introductionmentioning
confidence: 99%
“…GSH reduces intracellular reactive oxygen species (ROS)-it is regulated by the activities of glutathione peroxidase (GPx) and glutathione reductase: the former catalyses the oxidation of GSH to glutathione disulphide (GSSG), while the latter reduces GSSG back to GSH [11]. GSH also plays an important role in the detoxification of xenobiotics, via conjugation with glutathione-S-transferase (GST) [12,13]. Each cell must synthesize all required GSH, as GSH cannot be imported from circulation-membrane-bound γ-glutamyl transferase produces cysteinylglycine (CYS-GLY) [14,15], which is subsequently hydrolysed to cysteine and glycine [16,17].…”
Section: ]mentioning
confidence: 99%
“…Colitis was confirmed after 5 days of DSS administration by the presence of occult blood in faeces using Hemoccult© testing system (Beckman Coulter, Mississauga, ON). On the final day of study, synthesis of GSH was determined in the fed state by a 5-h infusion of the stable isotope tracer [ 15 N, 13 C 2 ]glycine (Cambridge Isotope Laboratories, Andover, MA), Infusion rates were 75 μmol/kg/h, following a priming dose of 150 μmol/kg. Blood was sampled hourly to determine GSH synthesis and metabolite profile in red blood cells.…”
Section: Animals and Study Protocolmentioning
confidence: 99%
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“…For example, a more oxidised cellular environment favors the release of the nuclear factor-erythroid 2-related factor 2act as electron buffers due to their ability to readily cycle between oxidised and reduced forms. The major cellular redox couples are reduced/oxidised glutathione (2GSH/GSSG), cysteine (2Cys/CySS) and thioredoxin (Trx(SH) 2 /TrxSS) [20]. The ratios and levels of 2GSH/GSSG is the most important cellular redox couple, and a common measure used to assess the cellular redox environment [16].…”
Section: Introductionmentioning
confidence: 99%