| Name | aldehyde reductase |
|---|---|
| Synonyms | ADR; ALDR 1; ALDR1; Aldehyde reductase; AKR1B1; AKR1B1 protein; AR; Aldehyde reductase 1… |
| Name | acrolein |
|---|---|
| CAS | 2-propenal |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 8183257 | Kolb NS, Hunsaker LA, Vander Jagt DL: Aldose reductase-catalyzed reduction of acrolein: implications in cyclophosphamide toxicity. Mol Pharmacol. 1994 Apr;45(4):797-801. |
225(2,4,4,5) | Details |
| 19073213 | Jia Z, Misra BR, Zhu H, Li Y, Misra HP: Upregulation of cellular by 3H-1,2-dithiole-3-thione as a possible treatment strategy for protecting against acrolein-induced neurocytotoxicity. Neurotoxicology. 2009 Jan;30(1):1-9. Epub 2008 Nov 27. In this study, we have investigated the induction of glutathione (GSH), GSH S-transferase (GST), and aldose reductase (AR) by the unique nutraceutical compound 3H-1,2-dithiole-3-thione (D3T); and the protective effects of the D3T-mediated cellular defenses on acrolein-mediated toxicity in human neuroblastoma SH-SY5Y cells. |
31(0,1,1,1) | Details |
| 19031314 | Kang ES, Kim GH, Woo IS, Kim HJ, Eun SY, Ham SA, Jin H, Kim MY, Park MH, Kim HJ, Chang KC, Lee JH, Kim JH, Yabe-Nishimura C, Seo HG: Down-regulation of aldose reductase renders J774A.1 cells more susceptible to acrolein- or peroxide-induced cell death. Free Radic Res. 2008 Nov;42(11-12):930-8. |
7(0,0,1,2) | Details |
| 14676331 | Keightley JA, Shang L, Kinter M: Proteomic analysis of oxidative stress-resistant cells: a specific role for aldose reductase overexpression in cytoprotection. Mol Cell Proteomics. 2004 Feb;3(2):167-75. Epub 2003 Dec 15. Based on this observation, the role of AR in the resistant phenotype was investigated by using a combination of AR induction with ethoxyquin and AR inhibition with Alrestatin to test the cytotoxicity of two oxidation-derived aldehydes: acrolein and |
2(0,0,0,2) | Details |
| 9890881 | Srivastava S, Watowich SJ, Petrash JM, Srivastava SK, Bhatnagar A: Structural and kinetic determinants of reduction by aldose reductase. Biochemistry. 1999 Jan 5;38(1):42-54. Short-chain aldehydes such as and acrolein were reduced less efficiently. |
2(0,0,0,2) | Details |
| 11306073 | Ramana KV, Dixit BL, Srivastava S, Bhatnagar A, Balendiran GK, Watowich SJ, Petrash JM, Srivastava SK: Characterization of the binding site of aldose reductase. . Chem Biol Interact. 2001 Jan 30;130-132(1-3):537-48. For instance, the GS conjugate of acrolein is reduced with a catalytic efficiency 1000-fold higher than the parent indicating specific recognition of by the active site residues of AR. |
2(0,0,0,2) | Details |
| 10764810 | Dixit BL, Balendiran GK, Watowich SJ, Srivastava S, Ramana KV, Petrash JM, Bhatnagar A, Srivastava SK: Kinetic and structural characterization of the -binding site of aldose reductase. J Biol Chem. 2000 Jul 14;275(28):21587-95. The catalytic efficiency of AR in the reduction of the conjugates of acrolein, trans-2-hexenal, trans-2-nonenal, and trans,trans-2,4-decadienal was 4-1000-fold higher than for the corresponding free alkanal. |
2(0,0,0,2) | Details |
| 19041636 | Keith RJ, Haberzettl P, Vladykovskaya E, Hill BG, Kaiserova K, Srivastava S, Barski O, Bhatnagar A: Aldose reductase decreases endoplasmic reticulum stress in ischemic hearts. Chem Biol Interact. 2009 Mar 16;178(1-3):242-9. Epub 2008 Nov 11. In cell culture experiments, exposure to model lipid peroxidation aldehydes-4-hydroxy-trans-2-nonenal (HNE), 1-palmitoyl-2-oxovaleroyl (POVPC) or acrolein led to an increase in the phosphorylation of ER stress markers PERK and eIF2-alpha and an increase in ATF3. |
2(0,0,0,2) | Details |
| 18211903 | Perez JM, Arenas FA, Pradenas GA, Sandoval JM, Vasquez CC: Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes. J Biol Chem. 2008 Mar 21;283(12):7346-53. Epub 2008 Jan 22. Increased tolerance was also observed for the lipid peroxidation-derived aldehydes acrolein, and malondialdehyde and the membrane-peroxidizing compound tert-butylhydroperoxide. |
1(0,0,0,1) | Details |
| 18845131 | Endo S, Matsunaga T, Mamiya H, Hara A, Kitade Y, Tajima K, El-Kabbani O: Characterization of a rat -dependent aldo-keto reductase (AKR1B13) induced by oxidative stress. Chem Biol Interact. 2009 Mar 16;178(1-3):151-7. Epub 2008 Sep 19. Recombinant AKR1B13 exhibited -linked reductase activity towards various aldehydes and alpha-dicarbonyl compounds, which include reactive compounds such as glyoxal, acrolein, and 3-deoxyglucosone. The enzyme exhibited low (+)-linked dehydrogenase activity towards aliphatic and aromatic and was inhibited by aldose reductase inhibitors, flavonoids, benzbromarone and hexestrol. |
1(0,0,0,1) | Details |
| 12604212 | Hinshelwood A, McGarvie G, Ellis EM: Substrate specificity of mouse aldo-keto reductase AKR7A5. Chem Biol Interact. 2003 Feb 1;143-144:263-9. We have determined the substrate specificity of a mouse aldo-keto reductase (AKR) AKR7A5, an enzyme that is similar to rat aflatoxin aldehyde reductase (AKR7A1) and to human brain reductase (AKR7A2). It has low specific activity towards ketones, and alpha,beta-unsaturated carbonyls such as acrolein and 4-hydroxynonal. |
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. To elucidate involvement of AKR in detoxification of endogenously produced carbonyls in the male reproductive system, we investigated the differential expression and tissue localization of aldehyde reductase (ALR) and protein adducts produced by reaction with lipid peroxidation products. Virtually the same cells were stained with a monoclonal antibody (mAb) 5F6, raised against an acrolein-modified protein. |
1(0,0,0,1) | Details |