Human aldo-keto reductases 1B1 and 1B10: A comparative study on their enzyme activity toward electrophilic carbonyl compounds

Chemico-Biological Interactions

Volumn 191, Issue 1-3, 2011, Pages 192-198

  Shen, Yi ^a   Zhong, Linlin ^a   Johnson, Stephen ^b   Cao, Deliang ^a  

^a SOUTHERN ILLINOIS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Carbon Dynamics Institute   (United States)

Author keywords

Aldo keto reductase family 1 member B1; Aldo keto reductase family 1 member B10; Electrophilic carbonyl compounds; Enzyme kinetics; Glutathione carbonyls

Indexed keywords

4 HYDROXYNONENAL; ACROLEIN; ALDEHYDE REDUCTASE; ALDO KETO REDUCTASE FAMILY 1 MEMBER B1; ALDO KETO REDUCTASE FAMILY 1 MEMBER B10; CARBONYL DERIVATIVE; CROTONALDEHYDE; ELECTROPHILE; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE; HEXOBARBITAL; PROPIONALDEHYDE; TRANS 2,4 HEXADIENAL; UNCLASSIFIED DRUG;

CATALYSIS; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME SPECIFICITY; ENZYME SYNTHESIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; PROTEIN EXPRESSION; PROTEIN FUNCTION; STEADY STATE;

ALDEHYDE REDUCTASE; ALDEHYDES; DIET; GLUTATHIONE; HEK293 CELLS; HUMANS; KINETICS;

EID: 79957571968     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2011.02.004     Document Type: Conference Paper

References (38)

1. R.D. Mindnich, T.M. Penning, Aldo-keto reductase (AKR) superfamily: genomics and annotation, Hum. Genomics 3 (4) (2009) 362-370.
2. J.M. Jez, T.G. Flynn, T.M. Penning, A new nomenclature for the aldo-keto reductase superfamily, Biochem. Pharmacol. 54 (6) (1997) 639-647.
3. O.A. Barski, S.M. Tipparaju, A. Bhatnagar, The aldo-keto reductase superfamily and its role in drug metabolism and detoxification, Drug Metab. Rev. 40 (4) (2008) 553-624.
4. J.M. Petrash, All in the family: aldose reductase and closely related aldo-keto reductases, Cell. Mol. Life Sci. 61 (7-8) (2004) 737-749. (Pubitemid 38659658)
5. Y. Jin, T.M. Penning, Aldo-keto reductases and bioactivation/ detoxication, Annu. Rev. Pharmacol. Toxicol. 47 (2007) 263-292.
6. N. Yasuda, K. Fujino, T. Shiraji, F. Nambu, K. Kondo, Effects of steroid 5alpha-reductase inhibitor ONO-9302 and anti-androgen allylestrenol on the prostatic growth, and plasma and prostatic hormone levels in rats, Jpn. J. Pharmacol. 74 (3) (1997) 243-252. (Pubitemid 27376038)
7. J. Jin, P.A. Krishack, D. Cao, Role of aldo-keto reductases in development of prostate and breast cancer, Front. Biosci. 11 (2006) 2767-2773.
8. K.W. Lee, B.C. Ko, Z. Jiang, D. Cao, S.S. Chung, Overexpression of aldose reductase in liver cancers may contribute to drug resistance, Anticancer Drugs 12 (2) (2001) 129-132. (Pubitemid 32207361)
9. C. Wang, R. Yan, D. Luo, K. Watabe, D.F. Liao, D. Cao, Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls, J. Biol. Chem. 284 (39) (2009) 26742-26748.
10. J. Ma, R. Yan, X. Zu, J.M. Cheng, K. Rao, D.F. Liao, D. Cao, Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl- CoA carboxylase-alpha in breast cancer cells, J. Biol. Chem. 283 (6) (2008) 3418-3423.
11. R. Tammali, A.B. Reddy, K.V. Ramana, J.M. Petrash, S.K. Srivastava, Aldose reductase deficiency in mice prevents azoxymethane-induced colonic preneoplastic aberrant crypt foci formation, Carcinogenesis 30 (5) (2009) 799-807.
12. D. Cao, S.T. Fan, S.S. Chung, Identification and characterization of a novel human aldose reductase-like gene, J. Biol. Chem. 273 (19) (1998) 11429-11435.
13. S. Chung, J. LaMendola, Cloning and sequence determination of human placental aldose reductase gene, J. Biol. Chem. 264 (25) (1989) 14775-14777.
14. D.J. Hyndman, T.G. Flynn, Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family, Biochim. Biophys. Acta 1399 (2-3) (1998) 198-202.
15. G. Aldini, I. Dalle-Donne, R.M. Facino, A. Milzani, M. Carini, Intervention strategies to inhibit protein carbonylation by lipoxidation-derived reactive carbonyls, Med. Res. Rev. 27 (6) (2007) 817-868. (Pubitemid 350035121)
16. L. Zhong, Z. Liu, R. Yan, S. Johnson, Y. Zhao, X. Fang, D. Cao, Aldo-keto reductase family 1 B10 protein detoxifies dietary and lipid-derived alpha, beta-unsaturated carbonyls at physiological levels, Biochem. Biophys. Res. Commun. 387 (2) (2009) 245-250.
17. M. Spite, S.P. Baba, Y. Ahmed, O.A. Barski, K. Nijhawan, J.M. Petrash, A. Bhatnagar, S. Srivastava, Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes, Biochem. J. 405 (1) (2007) 95-105. (Pubitemid 46999929)
18. H.J. Martin, E. Maser, Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes, Chem. Biol. Interact. 178 (1-3) (2009) 145-150.
19. F.X. Ruiz, O. Gallego, A. Ardevol, A. Moro, M. Dominguez, S. Alvarez, R. Alvarez, A.R. de Lera, C. Rovira, I. Fita, X. Pares, J. Farres, Aldo-keto reductases from the AKR1B subfamily: retinoid specificity and control of cellular retinoic acid levels, Chem. Biol. Interact. 178 (1-3) (2009) 171-177.
20. O. Gallego, F.X. Ruiz, A. Ardevol, M. Dominguez, R. Alvarez, A.R. de Lera, C. Rovira, J. Farres, I. Fita, X. Pares, Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10, Proc. Natl. Acad. Sci. U.S.A. 104 (52) (2007) 20764-20769.
21. A.M. Quinn, R.G. Harvey, T.M. Penning, Oxidation of PAH trans-dihydrodiols by human aldo-keto reductase AKR1B10, Chem. Res. Toxicol. 21 (11) (2008) 2207-2215.
22. H.J. Martin, U. Breyer-Pfaff, V. Wsol, S. Venz, S. Block, E. Maser, Purification and characterization of akr1b10 from human liver: role in carbonyl reduction of xenobiotics, Drug Metab. Dispos. 34 (3) (2006) 464-470.
23. G.K. Balendiran, H.J. Martin, Y. El-Hawari, E. Maser, Cancer biomarker AKR1B10 and carbonyl metabolism, Chem. Biol. Interact. 178 (1-3) (2009) 134-137.
24. G.K. Balendiran, Fibrates in the chemical action of daunorubicin, Curr. Cancer Drug Targets 9 (3) (2009) 366-369.
25. R. De Bont, N. van Larebeke, Endogenous DNA damage in humans: a review of quantitative data, Mutagenesis 19 (3) (2004) 169-185. (Pubitemid 38744825)
26. V.V. Davydov, N.M. Dobaeva, A.I. Bozhkov, Possible role of alteration of aldehyde's scavenger enzymes during aging, Exp. Gerontol. 39 (1) (2004) 11-16.
27. K. Berhane, M. Widersten, A. Engstrom, J.W. Kozarich, B. Mannervik, Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases, Proc. Natl. Acad. Sci. U.S.A. 91 (4) (1994) 1480-1484.
28. H. Esterbauer, P. Eckl, A. Ortner, Possible mutagens derived from lipids and lipid precursors, Mutat. Res. 238 (3) (1990) 223-233.
29. G.W. Wang, Y. Guo, T.M. Vondriska, J. Zhang, S. Zhang, L.L. Tsai, N.C. Zong, R. Bolli, A. Bhatnagar, S.D. Prabhu, Acrolein consumption exacerbates myocardial ischemic injury and blocks nitric oxide-induced PKCepsilon signaling and cardioprotection, J. Mol. Cell. Cardiol. 44 (6) (2008) 1016-1022.
30. B.D. Schuler, E. Eder, Development of a 32P-postlabelling method for the detection of 1,N2-propanodeoxyguanosine adducts of crotonaldehyde in vivo, Arch. Toxicol. 74 (7) (2000) 404-414.
31. M.D. Stout, E. Bodes, R. Schoonhoven, P.B. Upton, G.S. Travlos, J.A. Swenberg, Toxicity, DNA binding, and cell proliferation in male F344 rats following short-term gavage exposures to trans-2-hexenal, Toxicol. Pathol. 36 (2) (2008) 232-246. (Pubitemid 351534481)
32. S. Srivastava, S.J. Watowich, J.M. Petrash, S.K. Srivastava, A. Bhatnagar, Structural and kinetic determinants of aldehyde reduction by aldose reductase, Biochemistry 38 (1) (1999) 42-54. (Pubitemid 29035669)
33. X. Zu, R. Yan, S. Robbins, P.A. Krishack, D.F. Liao, D. Cao, Reduced 293T cell susceptibility to acrolein due to aldose reductase-like-1 protein expression, Toxicol. Sci. 97 (2) (2007) 562-568.
34. J.Z. Cheng, R. Sharma, Y. Yang, S.S. Singhal, A. Sharma, M.K. Saini, S.V. Singh, P. Zimniak, S. Awasthi, Y.C. Awasthi, Accelerated metabolism and exclusion of 4- hydroxynonenal through induction of RLIP76 and hGST5.8 is an early adaptive response of cells to heat and oxidative stress, J. Biol. Chem. 276 (44) (2001) 41213-41223.
35. B.F. Coles, F.F. Kadlubar, Detoxification of electrophilic compounds by glutathione S-transferase catalysis: determinants of individual response to chemical carcinogens and chemotherapeutic drugs? BioFactors (Oxford, England) 17 (1-4) (2003) 115-130.
36. S. Srivastava, A. Chandra, A. Bhatnagar, S.K. Srivastava, N.H. Ansari, Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase, Biochem. Biophys. Res. Commun. 217 (3) (1995) 741-746.
37. R. Yan, X. Zu, J. Ma, Z. Liu, M. Adeyanju, D. Cao, Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention, Int. J. Cancer 121 (10) (2007) 2301-2306. (Pubitemid 47585613)
38. Y. Shen, L. Zhong, S. Markwell, D. Cao, Thiol-disulfide exchanges modulate aldo-keto reductase family 1member B10 activity and sensitivity to inhibitors, Biochimie 92 (5) (2010) 530-537.