| Name | glutathione reductase |
|---|---|
| Synonyms | GLUR; GR; GRD 1; GRD1; GRase; GSR; Glutathione reductase; GRases… |
| Name | acrolein |
|---|---|
| CAS | 2-propenal |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 9175718 | Vander Jagt DL, Hunsaker LA, Vander Jagt TJ, Gomez MS, Gonzales DM, Deck LM, Royer RE: Inactivation of glutathione reductase by and other endogenous aldehydes. Biochem Pharmacol. 1997 Apr 25;53(8):1133-40. Inactivation appears to involve the initial formation of an enzyme-inactivator complex, K (D) = 0.5 microM, followed by the inactivation reaction, k = 1.3 x 10 (-2) min (-1). alpha,beta-Unsaturated aldehydes such as acrolein, crotonaldehyde, and also inactivated glutathione reductase, although rates varied widely. |
88(1,1,1,8) | Details |
| 7728738 | Subramaniam S, Subramaniam S, Shyamala Devi CS: Erythrocyte antioxidant enzyme activity in CMF treated breast cancer patients. Cancer Biochem Biophys. 1994 Oct;14(3):177-82. Acrolein and phosphoramide mustard are the metabolites of cyclophosphamide which are among the causative agents which reduce the activity of dismultase, catalase, peroxidase, glutathione reductase, glutathione-S-transferase and glucose-6-phosphate dehydrogenase in erythrocytes of CMF treated breast cancer patients. |
31(0,1,1,1) | Details |
| 18501200 | Ansari MA, Roberts KN, Scheff SW: Oxidative stress and modification of synaptic proteins in hippocampus after traumatic brain injury. Free Radic Biol Med. 2008 Aug 15;45(4):443-52. Epub 2008 May 3. At various times post-TBI, animals were killed and the hippocampus was analyzed for antioxidants (GSH, peroxidase, glutathione reductase, glutathione-S-transferase, glucose-6-phosphate dehydrogenase, superoxide dismutase, and catalase) and oxidants (acrolein, protein carbonyl, and |
6(0,0,1,1) | Details |
| 18607771 | Zhu H, Jia Z, Strobl JS, Ehrich M, Misra HP, Li Y: Potent induction of total cellular and mitochondrial antioxidants and phase 2 enzymes by cruciferous in rat aortic smooth muscle cells: cytoprotection against oxidative and electrophilic stress. Cardiovasc Toxicol. 2008 Fall;8(3):115-25. Epub 2008 Jul 8. Here we report that incubation of rat aortic smooth muscle A10 cells with (0.25-5 microM) resulted in concentration-dependent induction of a spectrum of important cellular antioxidants and phase 2 enzymes, including superoxide dismutase (SOD), catalase, the reduced form of (GSH), peroxidase, glutathione reductase (GR), glutathione S-transferase (GST), and NAD (P) H:quinone oxidoreductase 1 (NQO1). Pretreatment with (0.5, 1, and 5 microM) protected aortic smooth muscle cells from oxidative and electrophilic cytotoxicity induced by xanthine oxidase (XO)/ H2O2, SIN-1-derived and acrolein. |
1(0,0,0,1) | Details |
| 14673659 | Iuchi Y, Kaneko T, Matsuki S, Ishii T, Ikeda Y, Uchida K, Fujii J: Carbonyl stress and detoxification ability in the male genital tract and testis of rats. Histochem Cell Biol. 2004 Feb;121(2):123-30. Epub 2003 Dec 13. While acrolein inactivated glutathione reductase, an enzyme involved in recycling AKR activity was affected at the high concentration only. |
31(0,1,1,1) | Details |
| 8742318 | Cassee FR, Groten JP, Feron VJ: Changes in the nasal epithelium of rats exposed by inhalation to mixtures of and acrolein. Fundam Appl Toxicol. 1996 Feb;29(2):208-18. Activities of glutathione S-transferase and glutathione reductase after 3 days of exposure to acrolein, alone or in combination with and were depressed whereas the peroxidase activity was elevated. |
6(0,0,1,1) | Details |
| 12747729 | Lauderback CM, Drake J, Zhou D, Hackett JM, Castegna A, Kanski J, Tsoras M, Varadarajan S, Butterfield DA: Derivatives of xanthic acid are novel antioxidants: application to synaptosomes. Free Radic Res. 2003 Apr;37(4):355-65. Xanthates scavenge and peroxide, form disulfide bonds (dixanthogens), and react with electrophilic products of lipid oxidation (acrolein) in a manner similar to GSH. Further, upon disulfide formation, dixanthogens are reduced by glutathione reductase to a redox active xanthate. |
1(0,0,0,1) | Details |
| 10378479 | Monteil C, Le Prieur E, Buisson S, Morin JP, Guerbet M, Jouany JM: Acrolein toxicity: comparative in vitro study with lung slices and pneumocytes type II cell line from rats. Toxicology. 1999 Apr 15;133(2-3):129-38. This increase was concomitant with glutathione-S-transferase (GST) and glutathione reductase (GRED) activities in L2 cells. |
1(0,0,0,1) | Details |
| 16828947 | Bhatia K, Kaur M, Atif F, Ali M, Rehman H, Rahman S, Raisuddin S: Aqueous extract of Trigonella foenum-graecum L. ameliorates additive urotoxicity of buthionine sulfoximine and cyclophosphamide in mice. Food Chem Toxicol. 2006 Oct;44(10):1744-50. Epub 2006 Jun 3. Cyclophosphamide (CP) is a commonly used anti-cancer drug which causes toxicity by its reactive metabolites such as acrolein and phosphoramide mustard. CP-treated animals exhibited a significant decrease in the activities of glutathione S-transferase (GST), glutathione reductase (GR), peroxidase (GP) and catalase (CAT) when compared to the controls. |
1(0,0,0,1) | Details |
| 18367636 | Zhu H, Jia Z, Zhang L, Yamamoto M, Misra HP, Trush MA, Li Y: Antioxidants and phase 2 enzymes in macrophages: regulation by Nrf2 signaling and protection against oxidative and electrophilic stress. Exp Biol Med. 2008 Apr;233(4):463-74. As compared with wild-type cells, Nrf2 (- /-) macrophages were much more susceptible to cell injury induced by reactive / species, as well as two known macrophage toxins, acrolein and cadmium. Incubation of wild-type macrophages with 3H-1,2-dithiole-3-thione (D3T) led to significant induction of various antioxidants and phase 2 enzymes, including catalase, peroxidase (GPx), glutathione reductase, glutathione S-transferase, and NAD (P) H:quinone oxidoreductase 1. |
1(0,0,0,1) | Details |
| 4029094 | Patel JM, Block ER: Cyclophosphamide-induced depression of the antioxidant defense mechanisms of the lung. Exp Lung Res. 1985;8(2-3):153-65. We hypothesized that cyclophosphamide or one of its toxic metabolites, acrolein, may potentiate O2 toxicity by depressing lung antioxidant defense mechanisms. Excised lungs were analyzed for (GSH) content, glucose-6-phosphate dehydrogenase (G6PD), glutathione reductase (GSH-R), peroxidase (GSH-P), and superoxide dismutase (SOD) activities. |
1(0,0,0,1) | Details |
| 16781455 | Shao C, Roberts KN, Markesbery WR, Scheff SW, Lovell MA: Oxidative stress in head trauma in aging. Free Radic Biol Med. 2006 Jul 1;41(1):77-85. Epub 2006 Apr 3. Analysis of (4-HNE) and acrolein, by-products of lipid peroxidation, shows significant (P < 0.05) age-dependent increases in ipsilateral (IP) hippocampus 1 and 7 days post injury. Glutathione reductase activity also showed an age-dependent decrease. |
1(0,0,0,1) | Details |
| 11741210 | Ren S, Slatterly JT: Inhibition of carboxyethylphosphoramide mustard formation from 4-hydroxycyclophosphamide by carmustine. AAPS PharmSci. 1999;1(3):E14. The inhibition of ALDH1 may contribute to the observed lower incidence of toxicity when BCNU was split into 4 doses compared with single dose and coadministered with CY although dose-dependent effects of BCNU on and glutathione reductase are also likely to contribute. The calculated %inhibition of ALDH1 activity by acrolein and BCNU in patients receiving BCNU in 4 split doses with CY was 81%, and it increased to 92% in single dose BCNU regimen. |
1(0,0,0,1) | Details |
| 19408115 | Jia Z, Zhu H, Li Y, Misra HP: Cruciferous nutraceutical 3H-1,2-dithiole-3-thione protects human primary astrocytes against neurocytotoxicity elicited by MPTP, MPP (+), 6-OHDA, HNE and acrolein. Neurochem Res. 2009 Nov;34(11):1924-34. Epub 2009 May 1. In this study, we show that incubation of human primary astrocytes with micromolar concentrations (5-100 microM) of D3T for 24 h resulted in significant increases in the levels of (GSH), glutathione reductase (GR), and the phase 2 enzyme NAD (P) H:quinone oxidoreductase 1 (NQO1). |
1(0,0,0,1) | Details |
| 3421708 | Miccadei S, Nakae D, Kyle ME, Gilfor D, Farber JL: Oxidative cell injury in the killing of cultured hepatocytes by allyl Arch Biochem Biophys. 1988 Sep;265(2):302-10. The killing of cultured hepatocytes by allyl depended on the metabolism of this hepatotoxin by alcohol dehydrogenase to the reactive electrophile, acrolein. |
0(0,0,0,0) | Details |