Potent and selective inhibition of the tumor marker AKR1B10 by bisdemethoxycurcumin: Probing the active site of the enzyme with molecular modeling and site-directed mutagenesis

Biochemical and Biophysical Research Communications

Volumn 389, Issue 1, 2009, Pages 128-132

  Matsunaga, Toshiyuki ^a   Endo, Satoshi ^a   Soda, Midori ^a   Zhao, Hai Tao ^b   El Kabbani, Ossama ^b   Tajima, Kazuo ^c   Hara, Akira ^a  

^a GIFU PHARMACEUTICAL UNIVERSITY   (Japan)

^b MONASH UNIVERSITY   (Australia)

^c HOKURIKU UNIVERSITY   (Japan)

Author keywords

AKR1B10; Aldose reductase; Aldose reductase like 1; Bisdemethoxycurcumin; Curcumin; Polyphenol

Indexed keywords

BISDEMETHOXCURCUMIN; CURCUMIN; DEMETHOXYCURCUMIN; HONOKIOL; MAGNOLOL; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; POLYPHENOL DERIVATIVE; RESVERATROL; TUMOR MARKER; UNCLASSIFIED DRUG;

ARTICLE; CELL LEVEL; COMPETITIVE INHIBITION; DRUG POTENCY; DRUG SELECTIVITY; ENZYME ACTIVE SITE; ENZYME INHIBITION; HUMAN; HUMAN CELL; MOLECULAR DOCKING; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ALDEHYDE REDUCTASE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CURCUMIN; ENZYME INHIBITORS; FLAVONOIDS; GLUTAMINE; HELA CELLS; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENOLS; TUMOR MARKERS, BIOLOGICAL; VALINE;

EID: 70349107198     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.107     Document Type: Article

References (26)

1. 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
2. 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
3. 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
4. Martin H.J., and Maser E. Role of human aldo-keto reductase AKR1B10 in the protection against toxic aldehydes. Chem. Biol. Interact. 178 (2009) 145-150
5. Spite M., Baba S.P., Ahmed Y., Barski O.A., Nijhawan K., Petrash J.M., Bhatnagar A., and Srivastava S. Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes. Biochem. J. 405 (2007) 95-105
6. Crosas B., Hyndman D.J., Gallego O., Martras S., Parès X., Flynn T.G., and Farrès J. Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Biochem. J. 373 (2003) 973-979
7. Endo S., Matsunaga T., Mamiya H., Ohta C., Soda M., Kitade Y., Tajima K., Zhao H.T., El-Kabbani O., and Hara A. Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids. Arch. Biochem. Biophys. 487 (2009) 1-9
8. Zeindl-Eberhart E., Haraida S., Liebmann S., Jungblut P.R., Lamer S., Mayer D., Jäger G., Chung S., and Rabes H.M. Detection and identification of tumor-associated protein variants in human hepatocellular carcinomas. Hepatology 39 (2004) 540-549
9. 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
10. 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
11. Breton J., Gage M.C., Hay A.W., Keen J.N., Wild C.P., Donnellan C., Findlay J.B., and Hardie L.J. Proteomic screening of a cell line model of esophageal carcinogenesis identifies cathepsin D and aldo-keto reductase 1C2 and 1B10 dysregulation in Barrett's esophagus and esophageal adenocarcinoma. J. Proteome Res. 7 (2008) 1953-1962
12. Ruiz F.X., Gallego O., Ardèvol A., Moro A., Domínguez M., Alvarez S., Alvarez R., de Lera A.R., Rovira C., Fita I., Parés X., and Farrés J. Aldo-keto reductases from the AKR1B subfamily: retinoid specificity and control of cellular retinoic acid levels. Chem. Biol. Interact. 178 (2009) 171-177
13. Ma J., Yan R., Zu X., Cheng J.M., Rao K., Liao D.F., and Cao D. Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-α in breast cancer cells. J. Biol. Chem. 283 (2008) 3418-3423
14. Verma M., Martin H.J., Haq W., O'Connor T.R., Maser E., and Balendiran G.K. Inhibiting wild-type and C299S mutant AKR1B10; a homologue of aldose reductase upregulated in cancers. Eur. J. Pharmacol. 584 (2008) 213-221
15. 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
16. Gallego O., Ruiz F.X., Ardèvol A., Domínguez M., Alvarez R., de Lera A.R., Rovira C., Farrés J., Fita I., and Parès X. Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker, AKR1B10. Proc. Natl. Acad. Sci. USA 104 (2007) 20764-20769
17. Sa G., and Das T. Anti cancer effects of curcumin: cycle of life and death. Cell Div. 3 (2008) 14
18. Itokawa H., Shi Q., Akiyama T., Morris-Natschke S.L., and Lee K.H. Recent advances in the investigation of curcuminoids. Chin. Med. 3 (2008) 11
19. Aggarwal B.B., Sethi G., Ahn K.S., Sandur S.K., Pandey M.K., Kunnumakkara A.B., Sung B., and Ichikawa H. Targeting signal-transducer- and-activator-of-transcription-3 for prevention and therapy of cancer: modern target but ancient solution. Ann. NY Acad. Sci. 1091 (2006) 151-169
20. Liu H., Zang C., Emde A., Planas-Silva M.D., Rosche M., Kühnl A., Schulz C.O., Elstner E., Possinger K., and Eucker J. Anti-tumor effect of honokiol alone and in combination with other anti-cancer agents in breast cancer. Eur. J. Pharmacol. 591 (2008) 43-51
21. Iino T., Tabata M., Takikawa S., Sawada H., Shintaku H., Ishikura S., and Hara A. Tetrahydrobiopterin is synthesized from 6-pyruvoyl-tetrahydropterin by the human aldo-keto reductase AKR1 family members. Arch. Biochem. Biophys. 416 (2003) 180-187
22. Friesner R.A., Banks J.L., Murphy R.B., Halgreb T.A., Klicic J.J., Mainz D.T., Repasky M.P., Knoll E.H., Shelley M., Perry J.K., Shaw D.E., Francis P., and Shenkin P.S. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J. Med. Chem. 47 (2004) 1739-1749
23. 2, cyclooxygenases and 5-lipoxygenase. Carcinogenesis 25 (2004) 1671-1679
24. Kang H.M., Son K.H., Yang D.C., Han D.C., Kim J.H., Baek N.I., and Kwon B.M. Inhibitory activity of diarylheptanoids on farnesyl protein transferase. Nat. Prod. Res. 18 (2004) 295-299
25. Santel T., Pflug G., Hemdan N.Y., Schäfer A., Hollenbach M., Buchold M., Hintersdorf A., Lindner I., Otto A., Bigl M., Oerlecke I., Hutschenreuter A., Sack U., Huse K., Groth M., Birkemeyer C., Schellenberger W., Gebhardt R., Platzer M., Weiss T., Vijayalakshmi M.A., Krüger M., and Birkenmeier G. Curcumin inhibits glyoxalase 1: a possible link to its anti-inflammatory and anti-tumor activity. PLoS One 3 (2008) e3508
26. Milacic V., Banerjee S., Landis-Piwowar K.R., Sarkar F.H., Majumdar A.P., and Dou Q.P. Curcumin inhibits the proteasome activity in human colon cancer cells in vitro and in vivo. Cancer Res. 68 (2008) 7283-7292