Glutathione and thioredoxin
WebIt has been reported that oxidative and nitrative stress might be the pathogenesis of endometriosis. This prospective case-control study attempted to check the connection … WebOct 31, 2012 · Increased glutathione (GSH) and thioredoxin (Trx) metabolism are mechanisms that are widely implicated in resistance of cancer cells to chemotherapy. The current study determined if simultaneous inhibition of GSH and Trx metabolism enhanced cell killing of human head and neck squamous cell carcinoma (HNSCC) cells by a …
Glutathione and thioredoxin
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WebJul 8, 2016 · The organo-seleniumdrug ebselen exhibits a wide range of pharmacological effects that are predominantly due to its interference with redox systems catalyzed by seleno enzymes, e.g., glutathione peroxidase and thioredoxin reductase. Moreover, ebselen can covalently interact with thiol groups of several enzymes. According to its pleiotropic mode … WebJun 8, 2016 · The glutathione- and thioredoxin-dependent systems are also involved in antioxidant defense (Carmel-Harel and Storz 2000) (Fig. 1S). In E. coli , both thioredoxins (Trx) and glutaredoxins (Grx) are small proteins containing a Trx fold and catalyzing oxidoreductase reactions using the redox chemistry of cysteine residues.
The primary function of Thioredoxin (Trx) is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds. Multiple in vitro substrates for thioredoxin have been identified, including ribonuclease, choriogonadotropins, coagulation factors, glucocorticoid receptor, and insulin. Reduction of insulin is classically used as an activity test. The thioredoxins are maintained in their reduced state by the flavoenzyme thioredoxin reductase, in a NADPH-dependent reaction… WebJan 8, 2014 · The thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance. The Trx system provides the electrons to thiol-dependent peroxidases …
WebJun 2, 2009 · NADPH-dependent glutathione reductase (GR), a member of the FAD-binding disulfide reductase superfamily, is the major enzyme responsible for reduction of GSSG to GSH in most organisms, with only … WebThree-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme. The results suggest that mammalian TrxR evolved from the GR scaffold rather than from its prokaryotic counterpart, which renders cell growth dependent on selenium.
http://pubs.acs.org/doi/abs/10.1021/bi051321w#:~:text=Thioredoxin%2Fglutathione%20reductase%20%28TGR%29%20is%20a%20recently%20discovered%20member,and%20exhibits%20a%20wide%20spectrum%20of%20enzyme%20activities.
WebGlutathione-protein mixed disulfide bonds are regulated by glutaredoxins (Glrxs), thioltransferase members of the thioredoxin family. Glrxs reduce GSylated proteins and make them available for another redox signaling cycle. Glrxs and GSylation play an important role in cardiovascular diseases, such as myocardial ischemia and reperfusion ... korean of sisterWebJan 24, 2014 · Furthermore, glutathione and thioredoxin gene expression, under axenic growth conditions, was dependent on both the presence of glucose and the M. oryzae … korean of strongWebJul 15, 2002 · Thioredoxin (Trx; ref. 1 ), a ubiquitous redox protein, is an essential cofactor electron donor for ribonucleotide reductase, but also has many other cellular functions, … korean of teacher