| Name | glutathione reductase |
|---|---|
| Synonyms | GLUR; GR; GRD 1; GRD1; GRase; GSR; Glutathione reductase; GRases… |
| Name | diquat |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 10746947 | Gupta S, Husser RC, Geske RS, Welty SE, Smith CV: Sex differences in diquat-induced hepatic necrosis and DNA fragmentation in Fischer 344 rats. Toxicol Sci. 2000 Mar;54(1):203-11. Hepatic activities of superoxide dismutase (SOD) and peroxidase (GPX) were similar in the two genders, and activities of glutathione reductase (GR) and glutathione S-transferase-alpha (GST-alpha) activities were higher in the male rats. |
1(0,0,0,1) | Details |
| 11814326 | Slaughter MR, Thakkar H, O'Brien PJ: Effect of diquat on the antioxidant system and cell growth in human neuroblastoma cells. Toxicol Appl Pharmacol. 2002 Jan 15;178(2):63-70. Viable cells were assayed for (GSH) and activities of catalase (CAT), superoxide dismutase (SOD), glutathione reductase (GR), peroxidase (GPX), and glucose-6-phosphate dehydrogenase (GPDH). |
1(0,0,0,1) | Details |
| 12215683 | Rogers LK, Gupta S, Welty SE, Hansen TN, Smith CV: Nuclear and nucleolar glutathione reductase, peroxidase, and transferase activities in livers of male and female Fischer-344 rats. Toxicol Sci. 2002 Sep;69(1):279-85. The present studies were to test the hypotheses that glutathione reductase (GR), peroxidase (GPX), and glutathione S-transferase (GST) activities are expressed in nuclei and nucleoli of rat liver cells, and that differences in activities of these enzymes would correlate with the greater resistance of female than of male Fischer-344 rats to hepatic necrosis in vivo, mediated by reactive species generated by redox-cycling metabolism of diquat. |
32(0,1,1,2) | Details |
| 2825600 | Sandy MS, Moldeus P, Ross D, Smith MT: Cytotoxicity of the redox cycling compound diquat in isolated hepatocytes: involvement of peroxide and transition metals. Arch Biochem Biophys. 1987 Nov 15;259(1):29-37. Diquat is a hepatotoxin whose toxicity in vivo and in vitro is mediated by redox cycling and greatly enhanced by pretreatment with 1,3-bis (2-chloroethyl)-1-nitrosourea (BCNU), an inhibitor of glutathione reductase. |
81(1,1,1,1) | Details |
| 3505239 | Eklow-Lastbom L, Rossi L, Thor H, Orrenius S: Effects of oxidative stress caused by hyperoxia and diquat. Free Radic Res Commun. 1986;2(1-2):57-68. Diquat toxicity was also greatly enhanced when glutathione reductase was inhibited by pretreatment of the cells with 1,3-bis (2-chloroethyl)-1-nitrosourea. |
32(0,1,1,2) | Details |
| 3579917 | Smith CV: Effect of BCNU pretreatment on diquat-induced oxidant stress and hepatotoxicity. Biochem Biophys Res Commun. 1987 Apr 14;144(1):415-21. Pretreatment of both strains of rats with 80 mg/kg of 1,3-bis (2-chloroethyl)-N-nitrosourea (BCNU) inhibited hepatic glutathione reductase by 75 percent and increased dramatically the biliary efflux of produced by administration of diquat. |
31(0,1,1,1) | Details |
| 3632716 | Cotgreave IA, Sandy MS, Berggren M, Moldeus PW, Smith MT: and -dependent protective effect of PZ51 (Ebselen) against diquat-induced cytotoxicity in isolated hepatocytes. Biochem Pharmacol. 1987 Sep 15;36(18):2899-904. The redox-cycling bipyridylium compound diquat generates active species, depletes intracellular and is cytotoxic in isolated hepatocytes pretreated with the glutathione reductase inhibitor 1,3-bis (Z-chloro-ethyl)-1-nitrosourea (BCNU). |
31(0,1,1,1) | Details |
| 8382845 | Rikans LE, Cai Y: Diquat-induced oxidative damage in BCNU-pretreated hepatocytes of mature and old rats. Toxicol Appl Pharmacol. 1993 Feb;118(2):263-70. The effects of postmaturational aging on the toxicity of diquat, a redox cycling compound, were investigated in hepatocytes that were isolated from mature (6 months) and old (27 months) male Fischer 344 rats and pretreated with 1,3-bis (2-chloroethyl)-1- nitrosourea (BCNU), an inhibitor of glutathione reductase. |
31(0,1,1,1) | Details |
| 3421716 | Tsokos-Kuhn JO: Lethal injury by diquat redox cycling in an isolated hepatocyte model. Arch Biochem Biophys. 1988 Sep;265(2):415-24. Hepatocyte isolated by collagenase perfusion of livers of male Fischer-344 rats, and treated with 1,3-bis (2-chloroethyl)-1-nitrosourea (BCNU) (50 microM for 30 min at 37 degrees C) to inhibit glutathione reductase, were significantly more vulnerable to cytotoxicity of the bipyridyl herbicide diquat than similarly treated cells of Sprague-Dawley rats. |
31(0,1,1,1) | Details |
| 17078987 | Rogers LK, Bates CM, Welty SE, Smith CV: Diquat induces renal proximal tubule injury in glutathione reductase-deficient mice. Toxicol Appl Pharmacol. 2006 Dec 15;217(3):289-98. Epub 2006 Sep 26. |
6(0,0,1,1) | Details |
| 2806354 | Boutin JA, Norbeck K, Moldeus P, Genton A, Paraire M, Bizzari JP, Lavielle G, Cudennec CA: Effects of the new nitrosourea derivative, fotemustine, on the glutathione reductase activity in rat tissues in vivo and in isolated rat hepatocytes. Eur J Cancer Clin Oncol. 1989 Sep;25(9):1311-6. Furthermore, association of fotemustine with a H2O2 production leading drug, diquat, was shown to be inefficient--while BCNU is efficient--in potentiating the diquat toxicity. |
2(0,0,0,2) | Details |
| 15104113 | Jopperi-Davis KS, Park MS, Rogers LK, Backes CH Jr, Lim IK, Smith CV: Compartmental inhibition of hepatic glutathione reductase activities by 1,3-bis (2-chloroethyl)-N-nitrosourea (BCNU) in Sprague-Dawley and Fischer-344 rats. Toxicol Lett. 2004 Mar 7;147(3):219-28. BCNU pretreatment greatly exacerbates the hepatic necrosis caused by diquat in F344 rats, but does not similarly potentiate liver injury in SD rats. |
2(0,0,0,2) | Details |
| 2383572 | Navarro JA, Roncel M, Tollin G: Steady-state and laser flash induced photoreduction of yeast glutathione reductase by 5-deazariboflavin and by a viologen analogue: stabilization of semiquinone species by complexation. Biochemistry. 1990 Jun 26;29(25):6102-7. |
2(0,0,0,2) | Details |
| 3019355 | Sandy MS, Moldeus P, Ross D, Smith MT: Role of redox cycling and lipid peroxidation in bipyridyl herbicide cytotoxicity. Biochem Pharmacol. 1986 Sep 15;35(18):3095-101. The role of active species and lipid peroxidation in the toxic effects of diquat, paraquat and other bipyridyl herbicides remains controversial. This ability of the bipyridyls to generate active was positively correlated with the ability to induce toxicity in hepatocytes pretreated with 1,3-bis-(2-chloroethyl)-1-nitrosourea (BCNU) to inhibit their glutathione reductase activity, i.e. |
1(0,0,0,1) | Details |