Browse > Article
http://dx.doi.org/10.5483/BMBRep.2010.43.4.268

Inhibitory effects of polyphenols isolated from Rhus verniciflua on Aldo-keto reductase family 1 B10  

Song, Dae-Geun (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Lee, Joo-Young (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Lee, Eun-Ha (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Jung, Sang-Hoon (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Nho, Chu-Won (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Cha, Kwang-Hyun (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Koo, Song-Yi (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Pan, Cheol-Ho (Natural Products Research Center, Korea Institute of Science and Technology Gangneung Institute)
Publication Information
BMB Reports / v.43, no.4, 2010 , pp. 268-272 More about this Journal
Abstract
Aldo-keto reductase family 1 B10 (AKR1B10) is a member of the NADPH-dependent aldo-keto reductase (AKR) superfamily, and has been considered to be a potential cancer therapeutic target. Total extract from the bark of Rhus verniciflua (Toxicodendron vernicifluum (Stokes)) showed AKR1B10 inhibitory activity. To identify the active compounds from R. verniciflua responsible for AKR1B10 inhibition, nine compounds were isolated via bioactivity-guided isolation and tested for their effects against recombinant human AKR1B10 (rhAKR1B10). Results showed that butein, isolated from the ethyl acetate fraction, was most able to inhibit rhAKR1B10. The inhibitory rate of butein against rhAKR1B10 was 42.86% at $1\;{\mu}M$ with an IC50 value of $1.47\;{\mu}M$, and enzyme kinetic analysis revealed its inhibition mode to be uncompetitive.
Keywords
AKR1B10; Aldo-keto reductase; Aldose reductase-like; Anticancer; Butein; Polyphenol; Rhus verniciflua;
Citations & Related Records
Times Cited By KSCI : 3  (Citation Analysis)
Times Cited By Web Of Science : 4  (Related Records In Web of Science)
Times Cited By SCOPUS : 7
연도 인용수 순위
1 Zhang, L., Chen, W. and Li, X. (2008) A novel anticancer effect of butein: inhibition of invasion through the ERK1/2 and NF-kappa B signaling pathways in bladder cancer cells. FEBS. Lett. 582, 1821-1828   DOI   ScienceOn
2 Penning, T. M. (2005) AKR1B10: a new diagnostic marker of non-small cell lung carcinoma in smokers. Clin. Cancer. Res. 11, 1687-1690   DOI   ScienceOn
3 Lee, E. H., Song, D. G., Lee, J. Y., Pan, C. H., Um, B. H. and Jung, S. H. (2008) Inhibitory effect of the compounds isolated from Rhus verniciflua on aldose reductase and advanced glycation endproducts. Biol. Pharm. Bull. 31, 1626-1630   DOI   ScienceOn
4 Samoszuk, M., Tan, J. and Chorn, G. (2005) The chalcone butein from Rhus verniciflua Stokes inhibits clonogenic growth of human breast cancer cells co-cultured with fibroblasts. BMC. Complement. Altern. Med. 5, 5   DOI   ScienceOn
5 Matsunaga, T., Endo, S., Soda, M., Zhao, H. T., El- abbani, O., Tajima, K. and Hara, A. (2009) 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. Biochem. Biophys. Res. Commun. 389, 128-132   DOI   ScienceOn
6 Lee, J. Y., Song, D. G,. Jung, S. H., Kim, J. H., Ahn, S. Y., Nho, C. W. and Pan, C. H. (2009) Inhibitory effects of Korean local plant extracts on AKR1B10. Korean J. Pharmacognosy. 40, 238-243
7 Wang, C., Yan, R., Luo, D., Watabe, K., Liao, D. F. and Cao, D. (2009) Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls. J. Biol. Chem. 284, 26742-26748
8 Pan, C. H., Lee, J. Y., Song. D. G., Kim, J. H., Ahn, S. Y., Bae, D. S., Kim, Y. H. and Lee, J. K. (2009) Antioxidant and Aldo-keto reductase family 1 B10 inhibition activities of Korean local plant extracts. J. Appl. Biol. Chem. 52, 216-220   DOI   ScienceOn
9 Young, R. J., Ewing, D. J. and Clarke, B. F. (1983) A controlled trial of sorbinil, an aldose reductase inhibitor, in chronic painful diabetic neuropathy. Diabetes. 32, 938-942   DOI   ScienceOn
10 Spite, M., Baba, S. P., Ahmed, Y., Barski, O. A., Nijhawan, K., Petrash, J. M., Bhatnagar, A. and Srivastava, S. (2007) Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes. Biochem. J. 405, 95-105   DOI   PUBMED
11 Ma, J., Yan, R., Zu, X., Cheng, J. M., Rao, K., Liao, D. F. and Cao, D. (2008) 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, 3418-3423   DOI   PUBMED   ScienceOn
12 Cao, D., Fan, S. T. and Chung, S. S. (1998) Identification and characterization of a novel human aldose reductase-like gene. J. Biol. Chem. 273, 11429-11435   DOI   ScienceOn
13 Scuric, Z., Stain, S. C., Anderson, W. F. and Hwang, J. J. (1998) New member of aldose reductase family proteins overexpressed in human hepatocellular carcinoma. Hepatology. 27, 943-950   DOI   ScienceOn
14 Yan, R., Zu, X., Ma, J., Liu, Z., Adeyanju, M. and Cao, D. (2007) Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention. Int. J. Cancer. 121, 2301-2306   DOI   ScienceOn
15 Moon, D. O., Kim, M. O., Choi, Y. H., Hyun, J. W., Chang, W. Y. and Kim, G. Y. (2010) Butein induces G(2)/phase arrest and apoptosis in human hepatoma cancer cells through ROS generation. Cancer Lett. 288, 204-213   DOI   ScienceOn
16 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. (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   DOI   PUBMED
17 Robison, W. G., Jr., Nagata, M., Laver, N., Hohman, T. C. and Kinoshita, J. H. (1989) Diabetic-like retinopathy in rats prevented with an aldose reductase inhibitor. Invest. Ophthalmol. Vis. Sci. 30, 2285-2292   PUBMED
18 Dunlop, M. (2000) Aldose reductase and the role of the polyol pathway in diabetic nephropathy. Kidney Int. Suppl. 77, S3-12   DOI   ScienceOn
19 Frank, R. N., Keirn, R. J., Kennedy, A. and Frank, K. W. (1983) Galactose-induced retinal capillary basement membrane thickening: prevention by Sorbinil. Invest. Ophthalmol. Vis. Sci. 24, 1519-1524   PUBMED
20 Endo, S., Matsunaga, T., Mamiya, H., Ohta, C., Soda, M., Kitade, Y., Tajima, K., Zhao, H. T., El-Kabbani, O. and Hara, A. (2009) Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids. Arch. Biochem. Biophys. 487, 1-9   DOI   ScienceOn
21 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. (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   DOI   ScienceOn
22 Sato, S. and Kador, P. F. (1990) Inhibition of aldehyde reductase by aldose reductase inhibitors. Biochem. Pharmacol. 40, 1033-1042   DOI   ScienceOn
23 Lee, J. Y., Song, D. G., Lee, E. H., Jung, S. H., Nho, C. W., Cha, K. H. and Pan, C. H. (2009) Inhibitory effects of 3,5-O-dicaffeoyl-epi-quinic acid from Gymnaster koraiensis on AKR1B10. J. Korean. Soc. Appl. Biol. Chem. 52, 731-734   DOI   ScienceOn
24 Crosas, B., Hyndman, D. J., Gallego, O., Martras, S., Pares, X., Flynn, T. G. and Farres, J. (2003) Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Biochem J. 373, 973-979   DOI   ScienceOn
25 Gallego, O., Ruiz, F. X., Ardevol, A., Dominguez, M., Alvarez, R., de Lera, A. R., Rovira, C., Farres, J., Fita, I. and Pares, X. (2007) Structural basis for the high alltrans-retinaldehyde reductase activity of the tumor marker AKR1B10. Proc. Natl. Acad. Sci. U.S.A. 104, 20764-20769   DOI   ScienceOn
26 Jung, C. H., Kim, J. H., Hong, M. H., Seog, H. M., Oh, S. H., Lee, P. J., Kim, G. J., Kim, H. M., Um, J. Y. and Ko, S. G. (2007) Phenolic-rich fraction from Rhus verniciflua Stokes (RVS) suppress inflammatory response via NFappaB and JNK pathway in lipopolysaccharide-induced RAW 264.7 macrophages. J. Ethnopharmacol. 110, 490-497   DOI   ScienceOn
27 de la Fuente, J. A. and Manzanaro, S. (2003) Aldose reductase inhibitors from natural sources. Nat. Prod. Rep. 20, 243-251   DOI   ScienceOn