Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers

European Journal of Pharmacology

Volumn 584, Issue 2-3, 2008, Pages 213-221

  Verma, Malkhey ^a   Martin, Hans Joerg ^b   Haq, Wahajul ^c   O'Connor, Timothy R ^a   Maser, Edmund ^b   Balendiran, Ganesaratnam K ^a  

^a CITY OF HOPE NATIONAL MEDICAL CENTER   (United States)

^b UNIVERSITY HOSPITAL SCHLESWIG HOLSTEIN   (Germany)

^c CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

AKR1B10; Cancer; Fenofibrate; Liver; Lung

Indexed keywords

AKR1B10 ENZYME; ALDEHYDE REDUCTASE; CIPROFIBRATE; DAUNORUBICIN; ENZYME INHIBITOR; ETHYL 1 BENZYL 3 HYDROXY 2(5H) OXOPYRROLE 4 CARBOXYLIC ACID; FENOFIBRATE; FENOFIBRIC ACID; GEMFIBROZIL; GLYCERALDEHYDE; PIRINIXIC ACID; SORBINIL; UNCLASSIFIED DRUG; ZOPOLRESTAT;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DRUG MECHANISM; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; UPREGULATION;

ALDEHYDE REDUCTASE; ANTIBIOTICS, ANTINEOPLASTIC; ANTINEOPLASTIC AGENTS; BENZOTHIAZOLES; CLOFIBRIC ACID; CYSTEINE; DAUNORUBICIN; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; GLYCERALDEHYDE; HUMANS; IMIDAZOLIDINES; KINETICS; MUTATION; NEOPLASMS; OXIDATION-REDUCTION; PHTHALAZINES; PYRIMIDINES; RECOMBINANT PROTEINS; SERINE;

EID: 41249097311     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2008.01.036     Document Type: Article

References (38)

1. Balendiran G.K., and Rajkumar B. Fibrates inhibit aldose reductase activity in the forward and reverse reactions. Biochem. Pharmacol. 70 (2005) 1653-1663
2. Balendiran G.K., Verma M., and Perry E. Chemistory of fibrates. Curr. Chem. Biol. 1 (2007) 311-316
3. Bohren K.M., Bullock B., Wermuth B., and Gabbay K.H. The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 264 (1989) 9547-9551
4. Bohren K.M., and Gabbay K.H. Cys298 is responsible for reversible thiol-induced variation in aldose reductase activity. Adv. Exp. Med. Biol. 328 (1993) 267-277
5. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
6. Cao D., Fan S.T., and Chung S.S. Identification and characterization of a novel human aldose reductase-like gene. J. Biol. Chem. 273 (1998) 11429-11435
7. Cappiello M., Voltarelli M., Cecconi I., Vilardo P.G., Dal Monte M., Marini I., Del Corso A., Wilson D.K., Quiocho F.A., Petrash J.M., and Mura U. Specifically targeted modification of human aldose reductase by physiological disulfides. J. Biol. Chem. 271 (1996) 33539-33544
8. Crosas B., Hyndman D.J., Gallego O., Martras S., Pares X., Flynn T.G., and Farres J. Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Biochem. J. 373 (2003) 973-979
9. Forcheron F., Cachefo A., Thevenon S., Pinteur C., and Beylot M. Mechanisms of the triglyceride- and cholesterol-lowering effect of fenofibrate in hyperlipidemic type 2 diabetic patients. Diabetes 51 (2002) 3486-3491
10. Fruchart J.C., Brewer Jr. H.B., and Leitersdorf E. Consensus for the use of fibrates in the treatment of dyslipoproteinemia and coronary heart disease. Fibrate Consensus Group. Am. J. Cardiol. 81 (1998) 912-917
11. Fukumoto S., Yamauchi N., Moriguchi H., Hippo Y., Watanabe A., Shibahara J., Taniguchi H., Ishikawa S., Ito H., Yamamoto S., Iwanari H., Hironaka M., Ishikawa Y., Niki T., Sohara Y., Kodama T., Nishimura M., Fukayama M., Dosaka-Akita H., and Aburatani H. Overexpression of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers' non-small cell lung carcinomas. Clin. Cancer Res. 11 (2005) 1776-1785
12. Gariot P., Barrat E., Mejean L., Pointel J.P., Drouin P., and Debry G. Fenofibrate and human liver. Lack of proliferation of peroxisomes. Arch. Toxicol. 53 (1983) 151-163
13. Gonzalez F.J. The peroxisome proliferator-activated receptor alpha (PPARalpha): role in hepatocarcinogenesis. Mol. Cell. Endocrinol. 193 (2002) 71-79
14. Grimshaw C.E. Direct measurement of the rate of ring opening of d-glucose by enzyme-catalyzed reduction. Carbohydr. Res. 148 (1986) 345-348
15. Group S.R.T.R. A randomized trial of sorbinil, an aldose reductase inhibitor, in diabetic retinopathy. Sorbinil Retinopathy Trial Research Group. Arch. Ophthalmol. 108 (1990) 1234-1244
16. Hess R., Staubli W., and Reiss W. Nature of the hepatomegalic effect produced by ethyl-chlorphenoxyisobutyrate in the rat. Nature 208 (1965) 856-858
17. Hyndman D.J., and Flynn T.G. Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim. Biophys. Acta. 1399 (1998) 198-202
18. Inagaki K., Miwa I., and Okuda J. Affinity purification and glucose specificity of aldose reductase from bovine lens. Arch. Biochem. Biophys. 216 (1982) 337-344
19. Jez J.M., Flynn T.G., and Penning T.M. A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 54 (1997) 639-647
20. Jones I.R., Swai A., Taylor R., Miller M., Laker M.F., and Alberti K.G. Lowering of plasma glucose concentrations with bezafibrate in patients with moderately controlled NIDDM. Diabetes Care 13 (1990) 855-863
21. Kim B., Lee H.J., Choi H.Y., Shin Y., Nam S., Seo G., Son D.S., Jo J., Kim J., Lee J., Kim J., Kim K., and Lee S. Clinical validity of the lung cancer biomarkers identified by bioinformatics analysis of public expression data. Cancer Res. 67 (2007) 7431-7438
22. Klemin S., Calvo R.Y., Bond S., Dingess H., Rajkumar B., Perez R., Chow L., and Balendiran G.K. WY 14,643 inhibits human aldose reductase activity. J. Enzyme Inhib. Med. Chem. 21 (2006) 569-573
23. Martin H.J., Breyer-Pfaff U., Wsol V., Venz S., Block S., and Maser E. Purification and characterization of AKR1B10 from human liver: role in carbonyl reduction of xenobiotics. Drug Metab. Dispos. 34 (2006) 464-470
24. Miller D.B., and Spence J.D. Clinical pharmacokinetics of fibric acid derivatives (fibrates). Clin. Pharmacokinet. 34 (1998) 155-162
25. Nishimura C., Yamaoka T., Mizutani M., Yamashita K., Akera T., and Tanimoto T. Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system. Biochim. Biophys. Acta. 1078 (1991) 171-178
26. Peters J.M., Cheung C., and Gonzalez F.J. Peroxisome proliferator-activated receptor-alpha and liver cancer: where do we stand?. J. Mol. Med. 83 (2005) 774-785
27. Petrash J.M., Harter T.M., Devine C.S., Olins P.O., Bhatnagar A., Liu S., and Srivastava S.K. Involvement of cysteine residues in catalysis and inhibition of human aldose reductase. Site-directed mutagenesis of Cys-80, -298, and -303. J. Biol. Chem. 267 (1992) 24833-24840
28. Rath N.P., Haq W., and Balendiran G.K. Fenofibric acid. Acta Crystallogr C. 61 (2005) 81-84
29. Reddy J.K., Azarnoff D.L., and Hignite C.E. Hypolipidaemic hepatic peroxisome proliferators form a novel class of chemical carcinogens. Nature 283 (1980) 397-398
30. Rubins H.B., Robins S.J., Collins D., Fye C.L., Anderson J.W., Elam M.B., Faas F.H., Linares E., Schaefer E.J., Schectman G., Wilt T.J., and Wittes J. Gemfibrozil for the secondary prevention of coronary heart disease in men with low levels of high-density lipoprotein cholesterol. Veterans Affairs High-density Lipoprotein Cholesterol Intervention Trial Study Group. N. Engl. J. Med. 341 (1999) 410-418
31. Sato S., and Kador P.F. Inhibition of aldehyde reductase by aldose reductase inhibitors. Biochem. Pharmacol. 40 (1990) 1033-1042
32. Scuric Z., Stain S.C., Anderson W.F., and Hwang J.J. New member of aldose reductase family proteins overexpressed in human hepatocellular carcinoma. Hepatology 27 (1998) 943-950
33. Steuber H., Zentgraf M., Gerlach C., Sotriffer C.A., Heine A., and Klebe G. Expect the unexpected or caveat for drug designers: multiple structure determinations using aldose reductase crystals treated under varying soaking and co-crystallisation conditions. J. Mol. Biol. 363 (2006) 174-187
34. Urzhumtsev A., Tete-Favier F., Mitschler A., Barbanton J., Barth P., Urzhumtseva L., Biellmann J.F., Podjarny A., and Moras D. A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil. Structure 5 (1997) 601-612
35. Vander Jagt D.L., Torres J.E., Hunsaker L.A., Deck L.M., and Royer R.E. Physiological substrates of human aldose and aldehyde reductases. Adv. Exp. Med. Biol. 414 (1996) 491-497
36. Wilson D.K., Tarle I., Petrash J.M., and Quiocho F.A. Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9847-9851
37. Yan R., Zu X., Ma J., Liu Z., Adeyanju M., and Cao D. Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention. Int. J. Cancer. 121 (2007) 2301-2306
38. Yoshitake H., Takahashi M., Ishikawa H., Nojima M., Iwanari H., Watanabe A., Aburatani H., Yoshida K., Ishi K., Takamori K., Ogawa H., Hamakubo T., Kodama T., and Araki Y. Aldo-keto reductase family 1, member B10 in uterine carcinomas: a potential risk factor of recurrence after surgical therapy in cervical cancer. Int. J. Gynecol. Cancer. 17 (2007) 1300-1306