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Volumn 29, Issue 2, 2014, Pages 112-119

Differences in the glucuronidation of resveratrol and pterostilbene: Altered enzyme specificity and potential gender differences

Author keywords

Gender; Glucuronidation; Pterostilbene; Resveratrol; UDP glucuronosyltransferase

Indexed keywords

GLUCURONIC ACID; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A10; GLUCURONOSYLTRANSFERASE 1A3; GLUCURONOSYLTRANSFERASE 1A8; GLUCURONOSYLTRANSFERASE 1A9; HYDROXYL GROUP; POLYPHENOL; PTEROSTILBENE; RESVERATROL; STILBENE DERIVATIVE; SULFOTRANSFERASE; UNCLASSIFIED DRUG; GLUCURONIDE; ISOENZYME; UDP-GLUCURONOSYLTRANSFERASE, UGT1A3; UGT1A1 ENZYME;

EID: 84901230961     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.DMPK-13-RG-012     Document Type: Article
Times cited : (73)

References (37)
  • 1
    • 38749129056 scopus 로고    scopus 로고
    • Protective effects of resveratrol on UVB-irradiated HaCaT cells through attenuation of the caspase pathway
    • Park, K. and Lee, J. H.: Protective effects of resveratrol on UVB-irradiated HaCaT cells through attenuation of the caspase pathway. Oncol. Rep., 19: 413-417 (2008).
    • (2008) Oncol. Rep. , vol.19 , pp. 413-417
    • Park, K.1    Lee, J.H.2
  • 2
    • 84863267798 scopus 로고    scopus 로고
    • Cellular and molecular effects of resveratrol in health and disease
    • Yu, W., Fu, Y. C. and Wang, W.: Cellular and molecular effects of resveratrol in health and disease. J. Cell. Biochem., 113: 752-759 (2012).
    • (2012) J. Cell. Biochem. , vol.113 , pp. 752-759
    • Yu, W.1    Fu, Y.C.2    Wang, W.3
  • 4
    • 79952661832 scopus 로고    scopus 로고
    • The grape antioxidant resveratrol for skin disorders: Promise, prospects, and challenges
    • Ndiaye, M., Philippe, C., Mukhtar, H. and Ahmad, N.: The grape antioxidant resveratrol for skin disorders: Promise, prospects, and challenges. Arch. Biochem. Biophys., 508: 164-170 (2011).
    • (2011) Arch. Biochem. Biophys. , vol.508 , pp. 164-170
    • Ndiaye, M.1    Philippe, C.2    Mukhtar, H.3    Ahmad, N.4
  • 9
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression, and disease
    • Tukey, R. H. and Strassburg, C. P.: Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu. Rev. Pharmacol. Toxicol., 40: 581 -616 (2000).
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 10
    • 33645120407 scopus 로고    scopus 로고
    • Uridine diphosphoglucuronosyltransferase pharmacogenetics and cancer
    • Nagar, S. and Remmel, R. P.: Uridine diphosphoglucuronosyltransferase pharmacogenetics and cancer. Oncogene, 25: 1659-1672 (2006).
    • (2006) Oncogene , vol.25 , pp. 1659-1672
    • Nagar, S.1    Remmel, R.P.2
  • 14
    • 41749096772 scopus 로고    scopus 로고
    • Identification of UDP-glucuronosyltransferase 1A10 in non-malignant and malignant human breast tissues
    • Starlard-Davenport, A., Lyn-Cook, B. and Radominska-Pandya, A.: Identification of UDP-glucuronosyltransferase 1A10 in non-malignant and malignant human breast tissues. Steroids, 73: 611-620 (2008).
    • (2008) Steroids , vol.73 , pp. 611-620
    • Starlard-Davenport, A.1    Lyn-Cook, B.2    Radominska-Pandya, A.3
  • 15
    • 80052594437 scopus 로고    scopus 로고
    • Hepatic glucuronidation of resveratrol: Interspecies comparison of enzyme kinetic profiles in human, mouse, rat, and dog
    • Maier-Salamon, A., Bohmdorfer, M., Thalhammer, T., Szekeres, T. and Jaeger, W.: Hepatic glucuronidation of resveratrol: interspecies comparison of enzyme kinetic profiles in human, mouse, rat, and dog. Drug Metab. Pharmacokinet., 26: 364-373 (2011).
    • (2011) Drug Metab. Pharmacokinet. , vol.26 , pp. 364-373
    • Maier-Salamon, A.1    Bohmdorfer, M.2    Thalhammer, T.3    Szekeres, T.4    Jaeger, W.5
  • 16
    • 79961047423 scopus 로고    scopus 로고
    • Resveratrol and health - A comprehensive review of human clinical trials
    • Smoliga, J. M., Baur, J. A. and Hausenblas, H. A.: Resveratrol and health - a comprehensive review of human clinical trials. Mol. Nutr. Food Res., 55: 1129-1141 (2011).
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1129-1141
    • Smoliga, J.M.1    Baur, J.A.2    Hausenblas, H.A.3
  • 17
    • 84870368353 scopus 로고    scopus 로고
    • Resveratrol-loaded solid lipid nanoparticles versus nanostructured lipid carriers: Evaluation of antioxidant potential for dermal applications
    • Gokce, E. H., Korkmaz, E., Dellera, E., Sandri, G., Bonferoni, M. C. and Ozer, O.: Resveratrol-loaded solid lipid nanoparticles versus nanostructured lipid carriers: evaluation of antioxidant potential for dermal applications. Int. J. Nanomedicine, 7: 1841-1850 (2012).
    • (2012) Int. J. Nanomedicine , vol.7 , pp. 1841-1850
    • Gokce, E.H.1    Korkmaz, E.2    Dellera, E.3    Sandri, G.4    Bonferoni, M.C.5    Ozer, O.6
  • 18
    • 84858291668 scopus 로고    scopus 로고
    • Pterostilbene and cancer: Current review
    • McCormack, D. and McFadden, D.: Pterostilbene and cancer: current review. J. Surg. Res., 173: e53-e61 (2012).
    • (2012) J. Surg. Res. , vol.173
    • McCormack, D.1    McFadden, D.2
  • 19
    • 20544470196 scopus 로고    scopus 로고
    • Selective COX-2 inhibition by a Pterocarpus marsupium extract characterized by pterostilbene, and its activity in healthy human volunteers
    • Hougee, S., Faber, J., Sanders, A., de Jong, R. B., van den Berg, W. B., Garssen, J., Hoijer, M. A. and Smit, H. F.: Selective COX-2 inhibition by a Pterocarpus marsupium extract characterized by pterostilbene, and its activity in healthy human volunteers. Planta Med., 71: 387-392 (2005).
    • (2005) Planta Med. , vol.71 , pp. 387-392
    • Hougee, S.1    Faber, J.2    Sanders, A.3    De Jong, R.B.4    Van Den Berg, W.B.5    Garssen, J.6    Hoijer, M.A.7    Smit, H.F.8
  • 20
    • 84871757601 scopus 로고    scopus 로고
    • Pterostilbene, a natural analogue of resveratrol, potently inhibits 7,12-dimethylbenz[a]anthracene (DMBA)/12-O-tetradecanoylphorbol-13-acetate (TPA)-induced mouse skin carcinogenesis
    • Tsai, M. L., Lai, C. S., Chang, Y. H., Chen, W. J., Ho, C. T. and Pan, M. H.: Pterostilbene, a natural analogue of resveratrol, potently inhibits 7,12-dimethylbenz[a]anthracene (DMBA)/12-O-tetradecanoylphorbol-13-acetate (TPA)-induced mouse skin carcinogenesis. Food Funct, 3: 1185-1194 (2012).
    • (2012) Food Funct , vol.3 , pp. 1185-1194
    • Tsai, M.L.1    Lai, C.S.2    Chang, Y.H.3    Chen, W.J.4    Ho, C.T.5    Pan, M.H.6
  • 21
    • 79952756381 scopus 로고    scopus 로고
    • Pterostilbene is more potent than resveratrol in preventing azoxymethane (AOM)-induced colon tumorigenesis via activation of the NF-E2-related factor 2 (Nrf2)-mediated antioxidant signaling pathway
    • Chiou, Y. S., Tsai, M. L., Nagabhushanam, K., Wang, Y. J., Wu, C. H., Ho, C. T. and Pan, M. H.: Pterostilbene is more potent than resveratrol in preventing azoxymethane (AOM)-induced colon tumorigenesis via activation of the NF-E2-related factor 2 (Nrf2)-mediated antioxidant signaling pathway. J. Agric. Food Chem., 59: 2725-2733 (2011).
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 2725-2733
    • Chiou, Y.S.1    Tsai, M.L.2    Nagabhushanam, K.3    Wang, Y.J.4    Wu, C.H.5    Ho, C.T.6    Pan, M.H.7
  • 22
    • 67650105291 scopus 로고    scopus 로고
    • Pterostilbene inhibited tumor invasion via suppressing multiple signal transduction pathways in human hepatocellular carcinoma cells
    • Pan, M. H., Chiou, Y. S., Chen, W. J., Wang, J. M., Badmaev, V. and Ho, C. T.: Pterostilbene inhibited tumor invasion via suppressing multiple signal transduction pathways in human hepatocellular carcinoma cells. Carcinogenesis, 30: 1234-1242 (2009).
    • (2009) Carcinogenesis , vol.30 , pp. 1234-1242
    • Pan, M.H.1    Chiou, Y.S.2    Chen, W.J.3    Wang, J.M.4    Badmaev, V.5    Ho, C.T.6
  • 23
    • 80054014686 scopus 로고    scopus 로고
    • Pharmacokinetics, oral bioavailability, and metabolic profile of resveratrol and its dimethylether analog, pterostilbene, in rats
    • Kapetanovic, I. M., Muzzio, M., Huang, Z., Thompson, T. N. and McCormick, D. L.: Pharmacokinetics, oral bioavailability, and metabolic profile of resveratrol and its dimethylether analog, pterostilbene, in rats. Cancer Chemother. Pharmacol., 68: 593-601 (2011).
    • (2011) Cancer Chemother. Pharmacol. , vol.68 , pp. 593-601
    • Kapetanovic, I.M.1    Muzzio, M.2    Huang, Z.3    Thompson, T.N.4    McCormick, D.L.5
  • 24
    • 70349294431 scopus 로고    scopus 로고
    • Functional characterization of low-prevalence missense polymorphisms in the UDP-glucuronosyltransferase 1A9 gene
    • Olson, K. C., Dellinger, R. W., Zhong, Q., Sun, D., Amin, S., Spratt, T. E. and Lazarus, P.: Functional characterization of low-prevalence missense polymorphisms in the UDP-glucuronosyltransferase 1A9 gene. Drug Metab. Dispos., 37: 1999-2007 (2009).
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1999-2007
    • Olson, K.C.1    Dellinger, R.W.2    Zhong, Q.3    Sun, D.4    Amin, S.5    Spratt, T.E.6    Lazarus, P.7
  • 25
    • 33646804138 scopus 로고    scopus 로고
    • Importance of UDP-glucuronosyltransferase 1A10 (UGT1A10) in the detoxification of polycyclic aromatic hydrocarbons: Decreased glucuronidative activity of the UGT1A10139Lys isoform
    • Dellinger, R. W., Fang, J. L., Chen, G., Weinberg, R. and Lazarus, P.: Importance of UDP-glucuronosyltransferase 1A10 (UGT1A10) in the detoxification of polycyclic aromatic hydrocarbons: decreased glucuronidative activity of the UGT1A10139Lys isoform. Drug Metab. Dispos., 34: 943-949 (2006).
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 943-949
    • Dellinger, R.W.1    Fang, J.L.2    Chen, G.3    Weinberg, R.4    Lazarus, P.5
  • 27
    • 77953213678 scopus 로고    scopus 로고
    • Structural identification of mouse urinary metabolites of pterostilbene using liquid chromatography/tandem mass spectrometry
    • Shao, X., Chen, X., Badmaev, V., Ho, C. T. and Sang, S.: Structural identification of mouse urinary metabolites of pterostilbene using liquid chromatography/tandem mass spectrometry. Rapid Commun. Mass Spectrom., 24: 1770-1778 (2010).
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 1770-1778
    • Shao, X.1    Chen, X.2    Badmaev, V.3    Ho, C.T.4    Sang, S.5
  • 28
    • 34247618754 scopus 로고    scopus 로고
    • Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7
    • Miley, M. J., Zielinska, A. K., Keenan, J. E., Bratton, S. M., Radominska-Pandya, A. and Redinbo, M. R.: Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7. J. Mol. Biol., 369: 498-511 (2007).
    • (2007) J. Mol. Biol. , vol.369 , pp. 498-511
    • Miley, M.J.1    Zielinska, A.K.2    Keenan, J.E.3    Bratton, S.M.4    Radominska-Pandya, A.5    Redinbo, M.R.6
  • 29
    • 84863678590 scopus 로고    scopus 로고
    • Understanding substrate selectivity of human UDP-glucuronosyltransferases through QSAR modeling and analysis of homologous enzymes
    • Dong, D., Ako, R., Hu, M. and Wu, B.: Understanding substrate selectivity of human UDP-glucuronosyltransferases through QSAR modeling and analysis of homologous enzymes. Xenobiotica, 42: 808-820 (2012).
    • (2012) Xenobiotica , vol.42 , pp. 808-820
    • Dong, D.1    Ako, R.2    Hu, M.3    Wu, B.4
  • 31
    • 58149467072 scopus 로고    scopus 로고
    • Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction
    • Ohno, S. and Nakajin, S.: Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction. Drug Metab. Dispos., 37: 32-40 (2009).
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 32-40
    • Ohno, S.1    Nakajin, S.2
  • 33
    • 77955937122 scopus 로고    scopus 로고
    • Species and gender differences affect the metabolism of emodin via glucuronidation
    • Liu, W., Tang, L., Ye, L., Cai, Z., Xia, B., Zhang, J., Hu, M. and Liu, Z.: Species and gender differences affect the metabolism of emodin via glucuronidation. AAPS J., 12: 424-436 (2010).
    • (2010) AAPS J. , vol.12 , pp. 424-436
    • Liu, W.1    Tang, L.2    Ye, L.3    Cai, Z.4    Xia, B.5    Zhang, J.6    Hu, M.7    Liu, Z.8
  • 34
    • 70349142306 scopus 로고    scopus 로고
    • Up-regulation of UDP-glucuronosyltransferase (UGT) 1A4 by 17beta-estradiol: A potential mechanism of increased lamotrigine elimination in pregnancy
    • Chen, H., Yang, K., Choi, S., Fischer, J. H. and Jeong, H.: Up-regulation of UDP-glucuronosyltransferase (UGT) 1A4 by 17beta-estradiol: a potential mechanism of increased lamotrigine elimination in pregnancy. Drug Metab. Dispos., 37: 1841-1847 (2009).
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1841-1847
    • Chen, H.1    Yang, K.2    Choi, S.3    Fischer, J.H.4    Jeong, H.5
  • 35
    • 37549060373 scopus 로고    scopus 로고
    • Regulation of UDP-glucuronosyltransferase (UGT) 1A1 by progesterone and its impact on labetalol elimination
    • Jeong, H., Choi, S., Song, J. W., Chen, H. and Fischer, J. H.: Regulation of UDP-glucuronosyltransferase (UGT) 1A1 by progesterone and its impact on labetalol elimination. Xenobiotica, 38: 62-75 (2008).
    • (2008) Xenobiotica , vol.38 , pp. 62-75
    • Jeong, H.1    Choi, S.2    Song, J.W.3    Chen, H.4    Fischer, J.H.5
  • 36
    • 37049018023 scopus 로고    scopus 로고
    • Novel identification of UDP-glucuronosyltransferase 1A10 as an estrogen-regulated target gene
    • Starlard-Davenport, A., Lyn-Cook, B. and Radominska-Pandya, A.: Novel identification of UDP-glucuronosyltransferase 1A10 as an estrogen-regulated target gene. Steroids, 73: 139-147 (2008).
    • (2008) Steroids , vol.73 , pp. 139-147
    • Starlard-Davenport, A.1    Lyn-Cook, B.2    Radominska-Pandya, A.3
  • 37
    • 33746043754 scopus 로고    scopus 로고
    • Estrogen regulation of the glucuronidation enzyme UGT2B15 in estrogen receptor-positive breast cancer cells
    • Harrington, W. R., Sengupta, S. and Katzenellenbogen, B. S.: Estrogen regulation of the glucuronidation enzyme UGT2B15 in estrogen receptor-positive breast cancer cells. Endocrinology, 147: 3843-3850 (2006).
    • (2006) Endocrinology , vol.147 , pp. 3843-3850
    • Harrington, W.R.1    Sengupta, S.2    Katzenellenbogen, B.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.