AKR1B10 induces cell resistance to daunorubicin and idarubicin by reducing C13 ketonic group

Toxicology and Applied Pharmacology

Volumn 255, Issue 1, 2011, Pages 40-47

  Zhong, Linlin ^a   Shen, Honglin ^b   Huang, Chenfei ^a   Jing, Hongwu ^c   Cao, Deliang ^a  

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

^b The 6th Affiliated Hospital of Shenzhen University Health Science Center   (China)

^c NONE   (United States)

Author keywords

Aldo keto reductase family 1 member B10; Anthracyclines; Drug metabolism; Drug resistance; Enzyme kinetics

Indexed keywords

ALCOHOL DERIVATIVE; ALDO KETO REDUCTASE FAMILY 1 B10; DAUNORUBICIN; DAUNORUBICINOL; DOXORUBICIN; EPALRESTAT; EPIRUBICIN; HYDROXYL GROUP; IDARUBICIN; KETONE DERIVATIVE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; BIOTRANSFORMATION; CANCER RESISTANCE; CATALYSIS; CELL METABOLISM; CELL RESPIRATION; CONTROLLED STUDY; DRUG METABOLISM; DRUG POTENTIATION; ENZYME ACTIVITY; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IN VITRO STUDY; LIVER CARCINOMA; LUNG CARCINOMA; PROTEIN EXPRESSION;

ALDEHYDE REDUCTASE; ANTIBIOTICS, ANTINEOPLASTIC; CELLS, CULTURED; DAUNORUBICIN; DRUG RESISTANCE, NEOPLASM; HUMANS; IDARUBICIN; KETONES; OXIDATION-REDUCTION;

EID: 79960841454     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2011.05.014     Document Type: Article

References (51)

1. Asano T., Saito Y., Kawakami M., Yamada N. Fidarestat (SNK-860), a potent aldose reductase inhibitor, normalizes the elevated sorbitol accumulation in erythrocytes of diabetic patients. J. Diabetes Complications 2002, 16:133-138.
2. Asbell M.A., Schwartzbach E., Bullock F.J., Yesair D.W. Daunomycin and adriamycin metabolism via reductive glycosidic cleavage. The Journal of pharmacology and experimental therapeutics 1972, 182:63-69.
3. Balendiran G.K. Fibrates in the chemical action of daunorubicin. Current cancer drug targets 2009, 9:366-369.
4. Barski O.A., Tipparaju S.M., Bhatnagar A. The aldo-keto reductase superfamily and its role in drug metabolism and detoxification. Drug Metab. Rev. 2008, 40:553-624.
5. Beran M., Andersson B., Eksborg S., Ehrsson H. Comparative studies on the in vitro killing of human normal and leukemic clonogenic cells (CFUc) by daunorubicin, daunorubicinol, and daunorubicin-DNA complex. Cancer Chemother. Pharmacol. 1979, 2:19-24.
6. Bril V., Hirose T., Tomioka S., Buchanan R. Ranirestat for the management of diabetic sensorimotor polyneuropathy. Diabetes Care 2009, 32:1256-1260.
7. Cao D., Fan S.T., Chung S.S. Identification and characterization of a novel human aldose reductase-like gene. J. Biol. Chem. 1998, 273:11429-11435.
8. Chung S., LaMendola J. Cloning and sequence determination of human placental aldose reductase gene. J. Biol. Chem. 1989, 264:14775-14777.
9. Den Boer M.L., Pieters R., Veerman A.J. Mechanisms of cellular anthracycline resistance in childhood acute leukemia. Leukemia 1998, 12:1657-1670.
10. Dimarco A., Gaetani M., Orezzi P., Scarpinato B.M., Silvestrini R., Soldati M., Dasdia T., Valentini L. 'Daunomycin', a new antibiotic of the rhodomycin group. Nature 1964, 201:706-707.
11. Felsted R.L., Bachur N.R. Human liver daunorubicin reductases. Progress in clinical and biological research 1982, 114:291-305.
12. 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., Aburatani H. Overexpression of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers' non-small cell lung carcinomas. Clin. Cancer Res. 2005, 11:1776-1785.
13. Galettis P., Boutagy J., Ma D.D. Daunorubicin pharmacokinetics and the correlation with P-glycoprotein and response in patients with acute leukaemia. Br. J. Cancer 1994, 70:324-329.
14. Gallego O., Ruiz F.X., Ardevol A., Dominguez M., Alvarez R., de Lera A.R., Rovira C., Farres J., Fita I., Pares X. Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:20764-20769.
15. Gavelova M., Hladikova J., Vildova L., Novotna R., Vondracek J., Krcmar P., Machala M., Skalova L. Reduction of doxorubicin and oracin and induction of carbonyl reductase in human breast carcinoma MCF-7 cells. Chemico-biological interactions 2008, 176:9-18.
16. Gewirtz D.A. A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin. Biochem. Pharmacol. 1999, 57:727-741.
17. Gianni L. Anthracycline resistance: the problem and its current definition. Semin. Oncol. 1997, 24. S10-11-S10-17.
18. Giannoukakis N. Ranirestat as a therapeutic aldose reductase inhibitor for diabetic complications. Expert Opin. Investig. Drugs 2008, 17:575-581.
19. Gottesman M.M. Mechanisms of cancer drug resistance. Annual review of medicine 2002, 53:615-627.
20. Hembruff S.L., Laberge M.L., Villeneuve D.J., Guo B., Veitch Z., Cecchetto M., Parissenti A.M. Role of drug transporters and drug accumulation in the temporal acquisition of drug resistance. BMC Cancer 2008, 8:318.
21. Hotta N., Sakamoto N., Shigeta Y., Kikkawa R., Goto Y. Clinical investigation of epalrestat, an aldose reductase inhibitor, on diabetic neuropathy in Japan: multicenter study, Diabetic Neuropathy Study Group in Japan. J. Diabetes Complications 1996, 10:168-172.
22. Hussein M.A. Preclinical rationale, mechanisms of action, and clinical activity of anthracyclines in myeloma. Clin. Lymphoma Myeloma 2007, 7(Suppl 4):S145-S149.
23. Hyndman D.J., Flynn T.G. Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim. Biophys. Acta 1998, 1399:198-202.
24. Hyndman D., Bauman D.R., Heredia V.V., Penning T.M. The aldo-keto reductase superfamily homepage. Chem. Biol. Interact. 2003, 143-144:621-631.
25. Jez J.M., Flynn T.G., Penning T.M. A nomenclature system for the aldo-keto reductase superfamily. Adv. Exp. Med. Biol. 1997, 414:579-600.
26. Jin Y., Penning T.M. Aldo-keto reductases and bioactivation/detoxication. Annu. Rev. Pharmacol. Toxicol. 2007, 47:263-292.
27. Krentz A.J., Honigsberger L., Ellis S.H., Hardman M., Nattrass M. A 12-month randomized controlled study of the aldose reductase inhibitor ponalrestat in patients with chronic symptomatic diabetic neuropathy. Diabet. Med. 1992, 9:463-468.
28. Kuffel M.J., Reid J.M., Ames M.M. Anthracyclines and their C-13 alcohol metabolites: growth inhibition and DNA damage following incubation with human tumor cells in culture. Cancer Chemother. Pharmacol. 1992, 30:51-57.
29. Lee K.W., Ko B.C., Jiang Z., Cao D., Chung S.S. Overexpression of aldose reductase in liver cancers may contribute to drug resistance. Anticancer Drugs 2001, 12:129-132.
30. Liu Z., Zhong L., Krishack P.A., Robbins S., Cao J.X., Zhao Y., Chung S., Cao D. Structure and promoter characterization of aldo-keto reductase family 1 B10 gene. Gene 2009, 437:39-44.
31. Martin H.J., Breyer-Pfaff U., Wsol V., Venz S., Block S., Maser E. Purification and characterization of akr1b10 from human liver: role in carbonyl reduction of xenobiotics. Drug Metab. Dispos. 2006, 34:464-470.
32. Menna P., Minotti G., Salvatorelli E. In vitro modeling of the structure-activity determinants of anthracycline cardiotoxicity. Cell Biol. Toxicol. 2007, 23:49-62.
33. Moretti E., Oakman C., Di Leo A. Predicting anthracycline benefit: have we made any progress?. Curr. Opin. Oncol. 2009, 21:507-515.
34. Muggia F.M., Green M.D. New anthracycline antitumor antibiotics. Crit. Rev. Oncol. Hematol. 1991, 11:43-64.
35. Murphy G.P., Lawrence W., Lenhard R.E. American Society Textbook of Clinical Oncology 1995, second edition.
36. Niitsu N., Kasukabe T., Yokoyama A., Okabe-Kado J., Yamamoto-Yamaguchi Y., Umeda M., Honma Y. Anticancer derivative of butyric acid (Pivalyloxymethyl butyrate) specifically potentiates the cytotoxicity of doxorubicin and daunorubicin through the suppression of microsomal glycosidic activity. Molecular pharmacology 2000, 58:27-36.
37. Ohara H., Miyabe Y., Deyashiki Y., Matsuura K., Hara A. Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase and aldehyde reductase of human liver. Biochem. Pharmacol. 1995, 50:221-227.
38. Ohtake, S., Miyawaki, S., Fujita, H., Kiyoi, H., Shinagawa, K., Usui, N., Okumura, H., Miyamura, K., Nakaseko, C., Miyazaki, Y., Fujieda, A., Nagai, T., Yamane, T., Taniwaki, M., Takahashi, M., Yagasaki, F., Kimura, Y., Asou, N., Sakamaki, H., Handa, H., Honda, S., Ohnishi, K., Naoe, T., Ohno, R., 2011. Randomized study of induction therapy comparing standard-dose idarubicin with high-dose daunorubicin in adult patients with previously untreated acute myeloid leukemia: JALSG AML201 Study. Blood 117, 2358-2365.
39. Petrash J.M. All in the family: aldose reductase and closely related aldo-keto reductases. Cell. Mol. Life Sci. 2004, 61:737-749.
40. Plebuch M., Soldan M., Hungerer C., Koch L., Maser E. Increased resistance of tumor cells to daunorubicin after transfection of cDNAs coding for anthracycline inactivating enzymes. Cancer Lett. 2007, 255:49-56.
41. Reid J.M., Pendergrass T.W., Krailo M.D., Hammond G.D., Ames M.M. Plasma pharmacokinetics and cerebrospinal fluid concentrations of idarubicin and idarubicinol in pediatric leukemia patients: a Children's Cancer Study Group report. Cancer Res. 1990, 50:6525-6528.
42. Schroterova L., Kaiserova H., Baliharova V., Velik J., Gersl V., Kvasnickova E. The effect of new lipophilic chelators on the activities of cytosolic reductases and P450 cytochromes involved in the metabolism of anthracycline antibiotics: studies in vitro. Physiological research/Academia Scientiarum Bohemoslovaca 2004, 53:683-691.
43. Shan K., Lincoff A.M., Young J.B. Anthracycline-induced cardiotoxicity. Ann. Intern. Med. 1996, 125:47-58.
44. Shen Y., Zhong L., Markwell S., Cao D. Thiol-disulfide exchanges modulate aldo-keto reductase family 1 member B10 activity and sensitivity to inhibitors. Biochimie 2010, 92:530-537.
45. Soldan M., Ax W., Plebuch M., Koch L., Maser E. Cytostatic drug resistance, role of phase-I daunorubicin metabolism in cancer cells. Adv. Exp. Med. Biol. 1999, 463:529-538.
46. Verma M., Martin H.J., Haq W., O'Connor T.R., Maser E., Balendiran G.K. Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers. Eur. J. Pharmacol. 2008, 584:213-221.
47. Wang C., Yan R., Luo D., Watabe K., Liao D.F., Cao D. Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls. J. Biol. Chem. 2009, 284:26742-26748.
48. Wermuth B., Bohren K.M., Heinemann G., von Wartburg J.P., Gabbay K.H. Human carbonyl reductase, Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. The Journal of biological chemistry 1988, 263:16185-16188.
49. Wiernik P.H., Dutcher J.P. Clinical importance of anthracyclines in the treatment of acute myeloid leukemia. Leukemia 1992, 6(Suppl 1):67-69.
50. Zhong L., Liu Z., Yan R., Johnson S., Zhao Y., Fang X., Cao D. Aldo-keto reductase family 1 B10 protein detoxifies dietary and lipid-derived alpha, beta-unsaturated carbonyls at physiological levels. Biochem. Biophys. Res. Commun. 2009, 387:245-250.
51. Zu X., Yan R., Robbins S., Krishack P.A., Liao D.F., Cao D. Reduced 293T cell susceptibility to acrolein due to aldose reductase-like-1 protein expression. Toxicol. Sci. 2007, 97:562-568.