Downregulation of AKR1B10 expression in colorectal cancer

Molecular Biology

Volumn 44, Issue 2, 2010, Pages 216-222

  Kropotova, E S ^a   Tychko, R A ^a   Zinov'eva, O L ^a   Zyryanova, A F ^a   Khankin, S L ^b   Cherkes, V L ^c   Aliev, V A ^c   Beresten, S F ^a   Oparina, N Yu ^a   Mashkova, T D ^a  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^b Discipline cyclic Department of Special Disciplines and Professional Modules   (Russian Federation)

^c N N BLOKHIN RUSSIAN CANCER RESEARCH CENTER   (Russian Federation)

Author keywords

Aldo keto reductase; B1 and B10 aldose reductases; Colorectal cancer; Gene expression; Real time PCR; RT PCR; Tumor markers

Indexed keywords

EID: 77951763378     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893310020056     Document Type: Article

References (35)

1. Hyndman D., Bauman D. R., Heredia V. V., Penning T. M. 2003. The aldo-keto reductase superfamily homepage. Chem. Biol. Interact. 143/144, 621-631.
2. Jin Y., Penning T. M. 2007. Aldo-keto reductases and bioactivation/detoxication. Annu. Rev. Pharmacol. Toxicol. 47, 263-292.
3. Cao D., Fan S. T., Chung S. S. 1998. Identification and characterization of a novel human aldose reductase-like gene. J. Biol. Chem. 273, 11429-11435.
4. Yabe-Nishimura C. 1998. Aldose reductase in glucose toxicity: A potential target for the prevention of diabetic complications. Pharmacol. Rev. 50, 21-33.
5. Ko B., Ruepp B., Bohren K. M., Gabbay K. H., Chung S. S. 1997. Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J. Biol. Chem. 272, 16431-16437.
6. Liu Z., Zhong L., Krishack P. A., Robbins S., Cao J. X., Zhao Yu., Chung S., Cao D. 2009. Structure and promoter characterization of aldo-keto reductase family 1 B10 gene. Gene. 437, 39-44.
7. Crosas B., Hyndman D. J., Gallego O., Martras S., Parés X., Flynn T. G., Farrés J. 2003. Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: Consequences for retinoid metabolism. Biochem. J. 373, 973-979.
8. Gallego O., Belyaeva O. V., Porté S., Ruiz F. X., Stetsenko A. V., Shabrova E. V., Kostereva N. V., Farrés J., Parés X., Kedishvili N. Y. 2006. Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases, and aldo-keto reductases with retinoids. Biochem. J. 399, 101-109.
9. Grimshaw C. E., Mathur E. J. 1989. Immunoquantitation of aldose reductase in human tissues. Anal. Biochem. 176, 66-71.
10. Hyndman D. J., Flynn T. G. 1998. Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim. Biophys. Acta. 1399, 198-202.
11. Penning T. M., Drury J. E. 2007. Human aldo-keto reductases: Functions, gene regulation, and single nucleotide polymorphisms. Arch. Biochem. Biophys. 464, 241-250.
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. 2005. Overexpression of the aldo-keto reductase family protein AKR1B10 is highly correlated with smokers' nonsmall cell lung carcinomas. Clin. Cancer Res. 11, 1776-1785.
13. Penning T. M. 2005. AKR1B10: A new diagnostic marker of non-small cell lung carcinoma in smokers. Clin. Cancer Res. 11, 1687-1690.
14. Ruiz F. X, Gallego O., Ardevol A., Moro A., Dominguez M., Alvarez S., Alvarez R., de Lera A. R., Rovira C., Fita I., Parés X., Farrés J. 2009. Aldo-keto reductases from the AKR1B subfamily: Retinoid specificity and control of cellular retinoic acid levels. Chem. Biol. Interact. 178, 171-177.
15. Mashkova T. D., Oparina N. I., Zinovyeva O. L., Kropotova E. S., Dubovaya V. I., Poltaraus A. V., Fridman M. V., Kopantsev E. P., Vinogradova T. M., Zinovyeva M. V., Laktionov K. K., Kasymova O. T., Zborovskaya I. V., Sverdlov E. D., Kisselev L. L. 2006. Transcription of TIMP3, DAPK1, and AKR1V10 in squamous-cell lung cancer. Mol. Biol. 40, 945-951.
16. Nagaraj N. S., Beckers S., Mensah J. K., Waigel S., Vigneswaran N., Zacharias W. 2006. Cigarette smoke condensate induces cytochromes P450 and aldo-keto reductases in oral cancer cells. Toxicol. Lett. 165, 182-194.
17. Scuric Z., Stain S. C., Anderson W. F., Hwang J. J. 1998. New member of aldose reductase family proteins over-expressed in human hepatocellular carcinoma. Hepatology. 27, 943-950.
18. Lee K. W., Ko B. C., Jiang Z., Cao D., Chung S. S. 2001. Overexpression of aldose reductase in liver cancers may contribute to drug resistance. Anticancer Drugs. 12, 129-132.
19. 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., Araki Y. 2007. 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, 1300-1306.
20. Hyndman D., Flynn T. G. 1999. The aldo-keto reductases and their role in cancer. Adv. Exp. Med. Biol. 463, 427-434.
21. Jin J., Krishack P. A., Cao D. 2006. Role of aldo-keto reductases in development of prostate and breast cancer. Front Biosci. 11, 2767-2773.
22. Saraswat M., Mrudula T., Kumar P. U., Suneetha A., Rao T. S., Srinivasulu M., Reddy B. 2006. Overexpression of aldose reductase in human cancer tissues. Med. Sci. Monit. 12, CR525-CR529.
23. Jemal A., Siegel R., Ward E., Murray T., Xu J., Smigal C., Thun M. J. 2006. Cancer statistics. CA Cancer J. Clin. 56, 36-30.
24. Manzeniuk O. Y., Malakho S. G., Pekhov V. M., Kosorukova I. S., Poltaraus A. V. 2006. Characterization of Russian universal kits for real-time PCR: Application to molecular oncodiagnosis. Mol. Biol. 40, 305-311.
25. Hackenberg M., Previti C., Luque-Escamilla P. L., Carpena P., Martinez-Aroza J., Oliver J. L. 2006. CpG-cluster: A distance-based algorithm for CpG-island detection. BMC Bioinform. 7, 446.
26. Lefrancois-Martinez A. M., Bertherat J., Val P., Tournaire C., Gallo-Payet N., Hyndman D., Veyssiere G., Bertagna X., Jean C., Martinez A. 2004. Decreased expression of cyclic adenosine monophosphate-regulated aldose reductase (AKR1B1) is associated with malignancy in human sporadic adrenocortical tumors. J. Clin. Endocrinol. Metab. 89, 3010-3019.
27. Camps J., Grade M., Nguyen O. T., Hormann P., Becker S., Hummon A. B., Rodriguez V., Chandrasekharappa S., Chen Y., Difilippantonio M. J., Becker H., Ghadimi B. M., Ried T. 2008. Chromosomal breakpoints in primary colon cancer at sites of structural variants in the genome. Cancer Res. 68, 1284-1295.
28. von Lintig J., Vogt K. 2000. Filling the gap in vitamin A research: Molecular identification of an enzyme cleaving beta-carotene to retinal. J. Biol. Chem. 275, 11915-11920.
29. Martin H. J., Maser E. 2009. Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes. Chem. Biol. Interact. 178, 145-150.
30. Ames B. N. 1983. Dietary carcinogens and anticarcinogens. Oxygen radicals and degenerative diseases. Science. 221, 1256-1264.
31. Homann N., Tillonen J., Salaspuro M. 2000. Microbially produced acetaldehyde from ethanol may increase the risk of colon cancer via folate deficiency. Int. J. Cancer. 86, 169-173.
32. Zu X., Yan R., Robbins S., Krishack P. A., Liao D. F., Cao D. 2007. Reduced 293T cell susceptibility to acrolein due to aldose reductase-like-1 protein expression. Toxicol. Sci. 97, 562-528.
33. Yan R., Zu X., Ma J., Liu Z., Adeyanju M., Cao D. 2007. Aldo-keto reductase family 1B10 gene silencing results in growth inhibition of colorectal cancer cells: Implication for cancer intervention. Int. J. Cancer. 121, 2301-2306.
34. Kurtz A. J., Lloyd R. S. 2003. 1, N2-deoxyguanosine adducts of acrolein, crotonaldehyde, and trans-4-hydroxynonenal cross-link to peptides via Schiff base linkage. J. Biol. Chem. 278, 5970-5976.
35. Hashimoto M., Sibata T., Wasada H., Toyokuni S., Uchida K. 2003. Structural basis of protein-bound endogenous aldehydes: Chemical and immunochemical characterizations of configurational isomers of a 4-hydroxy-2-nonenal-histidine adduct. J. Biol. Chem. 278, 5044-5051.