메뉴 건너뛰기




Volumn 26, Issue 1, 2011, Pages 94-101

Effect of tea beverages on aldehyde oxidase activity

Author keywords

Aldehyde oxidase; Catechin; Drug drug interaction; Tea beverage

Indexed keywords

1 METHYL 6 OXONICOTINAMIDE; 1 METHYLNICOTINAMIDE; ALDEHYDE OXIDASE; AMIDE; ASCORBIC ACID; CAFFEINE; CATECHIN; EPICATECHIN; EPICATECHIN GALLATE; EPIGALLOCATECHIN; EPIGALLOCATECHIN GALLATE; GALLOCATECHIN GALLATE; MINERAL WATER; N 1 METHYL 4 PYRIDONE 3 CARBOXAMIDE; UNCLASSIFIED DRUG; XANTHINE OXIDASE;

EID: 79952761589     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.DMPK-10-NT-078     Document Type: Note
Times cited : (23)

References (46)
  • 1
    • 0022343014 scopus 로고
    • Molybdenum hydroxylases as drug metabolizing enzyme
    • Beedham, C.: Molybdenum hydroxylases as drug metabolizing enzyme. Drug Metab. Rev., 16: 119-156 1985
    • (1985) Drug Metab. Rev , vol.16 , pp. 119-156
    • Beedham, C.1
  • 2
    • 0029098663 scopus 로고
    • Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial amyotrophic lateral sclerosis
    • Berger, R., Mezey, E., Clancy, K. P., Harta, G., Wright, R. M., Repine, J. E., Brown, R. H., Brownstein, M. and Patterson, D.: Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial amyotrophic lateral sclerosis. Somat. Cell Mol. Genet., 21: 121-131 1995.
    • (1995) Somat. Cell Mol. Genet , vol.21 , pp. 121-131
    • Berger, R.1    Mezey, E.2    Clancy, K.P.3    Harta, G.4    Wright, R.M.5    Repine, J.E.6    Brown, R.H.7    Brownstein, M.8    Patterson, D.9
  • 3
    • 0030944134 scopus 로고    scopus 로고
    • Distribution and pathophysiologic role of molybdenum-containing enzymes
    • Moriwaki, Y., Yamamoto, T. and Higashino, K.: Distribution and pathophysiologic role of molybdenum-containing enzymes. Histol. Histopathol., 12: 513-524 1997.
    • (1997) Histol. Histopathol , vol.1 , pp. 513-552
    • Moriwak, Y.1    Yamamot, T.2    Higashin, K.3
  • 4
    • 0000656061 scopus 로고
    • Identification of the candidate ALS2 gene at chromosome 2q33 as a human aldehyde oxidase gene
    • Wright, R. M., Vaitaitis, G. M., Weigel, L. K., Repine, T. B., McManaman, J. L. and Repine, J. E.: Identification of the candidate ALS2 gene at chromosome 2q33 as a human aldehyde oxidase gene. Redox Rep., 1: 313-321 1995.
    • (1995) Redox Rep , vol.1 , pp. 313-321
    • Wright, R.M.1    Vaitaitis, G.M.2    Weigel, L.K.3    Repine, T.B.4    McManaman, J.L.5    Repine, J.E.6
  • 5
    • 0016281733 scopus 로고
    • A comparison of the distribution and electron acceptor specificities of xanthine oxidase and aldehyde oxidase
    • Krenitsky, T. A., Tuttle, J. V., Cattau, E. L. and Wang, P.: A comparison of the distribution and electron acceptor specificities of xanthine oxidase and aldehyde oxidase. Comp. Biochem. Physiol., B, 49: 687-703 1974.
    • (1974) Comp. Biochem. Physiol., B , vol.49 , pp. 687-703
    • Krenitsky, T.A.1    Tuttle, J.V.2    Cattau, E.L.3    Wang, P.4
  • 6
    • 33847709895 scopus 로고    scopus 로고
    • In vivo-in vitro relationship of methotrexate 7-hydroxylation by aldehyde oxidase in four different strain rats
    • Moriyasu, A., Sugihara, K., Nakatani, K., Ohta, S. and Kitamura, S.: In vivo-in vitro relationship of methotrexate 7-hydroxylation by aldehyde oxidase in four different strain rats. Drug Metab. Pharmacokinet., 21: 485-491 2006.
    • (2006) Drug Metab. Pharmacokinet , vol.21 , pp. 485-491
    • Moriyasu, A.1    Sugihara, K.2    Nakatani, K.3    Ohta, S.4    Kitamura, S.5
  • 7
    • 33744979094 scopus 로고    scopus 로고
    • Drug-metabolizing ability of molybdenum hydroxylases
    • Kitamura, S., Sugihara, K. and Ohta, S.: Drug-metabolizing ability of molybdenum hydroxylases. Drug Metab. Pharmacokinet., 21: 83-98 2006.
    • (2006) Drug Metab. Pharmacokinet , vol.21 , pp. 83
    • Kitamura, S.1    Sugihara, K.2    Ohta, S.3
  • 8
    • 0030058077 scopus 로고    scopus 로고
    • Involvement of mammalian liver cytosols and aldehyde oxidase in reductive metabolism of zonisamide
    • Sugihara, K., Kitamura, S. and Tatsumi, K.: Involvement of mammalian liver cytosols and aldehyde oxidase in reductive metabolism of zonisamide. Drug Metab. Dispos., 24: 199-202 1996.
    • (1996) Drug Metab. Dispos , vol.24 , pp. 199-202
    • Sugihara, K.1    Kitamura, S.2    Tatsumi, K.3
  • 9
    • 0028641302 scopus 로고
    • Two different enzymes are primarily responsible for retinoic acid synthesis in rabbit liver cytosol
    • Huang, D. Y. and Ichikawa, Y.: Two different enzymes are primarily responsible for retinoic acid synthesis in rabbit liver cytosol. Biochem. Biophys. Res. Commun., 205: 1278-1283 1994.
    • (1994) Biochem. Biophys. Res. Commun , vol.205 , pp. 1278-1283
    • Huang, D.Y.1    Ichikawa, Y.2
  • 10
    • 0004187830 scopus 로고
    • Molecular Neurobiology of Mammalian Brain
    • McGeer, E. J. and McGeer, P. L. eds, New York, Plenum Publishing Corp
    • McGeer, E. J. and McGeer, P. L. eds.: Molecular Neurobiology of Mammalian Brain. New York, Plenum Publishing Corp., 1978.
    • (1978)
  • 11
    • 0024727223 scopus 로고
    • Bacteriological variations in a medio-mineral water bottled in polyethylene terephthalate containers
    • De Fusco, R., Biscardi, D. and Mazzacca, F. R.: Bacteriological variations in a medio-mineral water bottled in polyethylene terephthalate containers. Ann. Ig., 1: 1255-1267 1989.
    • (1989) Ann. Ig , vol.1 , pp. 1255-1267
    • de Fusco, R.1    Biscardi, D.2    Mazzacca, F.R.3
  • 12
    • 0043138287 scopus 로고    scopus 로고
    • Green tea: Healing tonic
    • Alschuler, L.: Green tea: Healing tonic. Am. J. Nat. Med., 5: 28-31 1998.
    • (1998) Am. J. Nat. Med , vol.5 , pp. 28-31
    • Alschuler, L.1
  • 13
    • 0026771060 scopus 로고
    • Green tea composition, consumption, and polyphenol chemistry
    • Graham, H. N.: Green tea composition, consumption, and polyphenol chemistry. Prev. Med., 21: 334-350 1992.
    • (1992) Prev. Med , vol.21 , pp. 334-350
    • Graham, H.N.1
  • 14
    • 0036005963 scopus 로고    scopus 로고
    • Anti-invasive effects of green tea polyphenol epigallocatechin-3- gallate EGCG, a natural inhibitor of metallo and serine proteases
    • Benelli, R., Vene, R., Bisacchi, D., Garbisa, S. and Albini, A.: Anti-invasive effects of green tea polyphenol epigallocatechin-3- gallate EGCG, a natural inhibitor of metallo and serine proteases. Biol. Chem., 383: 101-105 2002.
    • (2002) Biol. Chem , vol.383 , pp. 101-105
    • Benelli, R.1    Vene, R.2    Bisacchi, D.3    Garbisa, S.4    Albini, A.5
  • 15
    • 0036282695 scopus 로고    scopus 로고
    • Mechanisms of chronic disease causation by nutritional factors and tobacco products and their prevention by tea polyphenols
    • Weisburger, J. H. and Chung, F. L.: Mechanisms of chronic disease causation by nutritional factors and tobacco products and their prevention by tea polyphenols. Food Chem. Toxicol., 40: 1145-1154 2002.
    • (2002) Food Chem. Toxicol , vol.40 , pp. 1145-1154
    • Weisburger, J.H.1    Chung, F.L.2
  • 16
    • 2442686532 scopus 로고    scopus 로고
    • Green tea supplementation ameliorates insulin resistance and increases glucose transporter IV content in a fructose-fed rat model
    • Wu, L. Y., Juan, C. C., Hwang, L. S., Hsu, Y. P., Ho, P. H. and Ho, L. T.: Green tea supplementation ameliorates insulin resistance and increases glucose transporter IV content in a fructose-fed rat model. Eur. J. Nutr., 43: 116-124 2004.
    • (2004) Eur. J. Nutr , vol.43 , pp. 116-124
    • Wu, L.Y.1    Juan, C.C.2    Hwang, L.S.3    Hsu, Y.P.4    Ho, P.H.5    Ho, L.T.6
  • 17
    • 33744723078 scopus 로고    scopus 로고
    • Nutraceuticals as anti-angiogenic agents: Hopes and reality
    • Dulak, J.: Nutraceuticals as anti-angiogenic agents: hopes and reality. J. Physiol. Pharmacol., 56Suppl. 1: 51-67 2005.
    • (2005) J. Physiol. Pharmacol , vol.56 , Issue.SUPPL. 1 , pp. 51-67
    • Dulak, J.1
  • 18
    • 0035512382 scopus 로고    scopus 로고
    • Herb-drug interactions: Review and assessment of report reliability
    • Fugh-Berman, A. and Ernst, E.: Herb-drug interactions: review and assessment of report reliability. Br. J. Clin. Pharmacol., 52: 587-595 2001.
    • (2001) Br. J. Clin. Pharmacol , vol.52 , pp. 587-595
    • Fugh-Berman, A.1    Ernst, E.2
  • 19
    • 0141611906 scopus 로고    scopus 로고
    • Effect of St. Johnös wort on drug metabolism by induction of cytochrome P450 3A4 enzyme
    • Markowitz, J. S., Donovan, J. L., DeVane, C. L., Taylor, R. M., Ruan, Y., Wang, J. S. and Chavin, K. D.: Effect of St. Johnös wort on drug metabolism by induction of cytochrome P450 3A4 enzyme. JAMA, 290: 1500-1504 2003.
    • (2003) JAMA , vol.290 , pp. 1500-1504
    • Markowitz, J.S.1    Donovan, J.L.2    Devane, C.L.3    Taylor, R.M.4    Ruan, Y.5    Wang, J.S.6    Chavin, K.D.7
  • 21
    • 0036324035 scopus 로고    scopus 로고
    • Effects of plant-derived phenols on rat liver cytochrome P450 2B1 activity
    • Huynh, H. T. and Teel, R. W.: Effects of plant-derived phenols on rat liver cytochrome P450 2B1 activity. Anticancer Res., 22: 1699-1703 2002.
    • (2002) Anticancer Res , vol.22 , pp. 1699-1703
    • Huynh, H.T.1    Teel, R.W.2
  • 22
    • 0035042496 scopus 로고    scopus 로고
    • Tea consumption modulates hepatic drug metabolizing enzymes in Wistar rats
    • Maliakal, P. P., Coville, P. F. and Wanwimolruk, S.: Tea consumption modulates hepatic drug metabolizing enzymes in Wistar rats. J. Pharm. Pharmacol., 53: 569-577 2001.
    • (2001) J. Pharm. Pharmacol , vol.53 , pp. 569-577
    • Maliakal, P.P.1    Coville, P.F.2    Wanwimolruk, S.3
  • 23
    • 0028077568 scopus 로고
    • Selective induction of rat hepatic CYP1 and CYP4 proteins and of peroxisomal proliferation by green tea
    • Bu-Abbas, A., Clifford, M. N., Walker, R. and Ioannides, C.: Selective induction of rat hepatic CYP1 and CYP4 proteins and of peroxisomal proliferation by green tea. Carcinogenesis, 15: 2575-2579 1994.
    • (1994) Carcinogenesis , vol.15 , pp. 2575-2579
    • Bu-Abbas, A.1    Clifford, M.N.2    Walker, R.3    Ioannides, C.4
  • 24
  • 25
    • 0001397278 scopus 로고
    • Preparation of 2-and 6-pyridones of N1-methylnicotinamide
    • Pullman, M. E. and Colowick, S. P.: Preparation of 2- and 6- pyridones of N1-methylnicotinamide. J. Biol. Chem., 206: 121-127 1954.
    • (1954) J. Biol. Chem , vol.206 , pp. 121-127
    • Pullman, M.E.1    Colowick, S.P.2
  • 26
    • 0023877336 scopus 로고
    • Simultaneous micro-determination of nicotinamide and its major metabolites, N1- methyl-2-pyridone-5-carboxamide and N1-methyl-4-pyridone-3- carboxamide, by high-performance liquid chromatography
    • Shibata, K., Kawada, T. and Iwai, K.: Simultaneous micro-determination of nicotinamide and its major metabolites, N1- methyl-2-pyridone-5-carboxamide and N1-methyl-4-pyridone-3- carboxamide, by high-performance liquid chromatography. J. Chromatogr., 424: 23-28 1988.
    • (1988) J. Chromatogr , vol.424 , pp. 23-28
    • Shibata, K.1    Kawada, T.2    Iwai, K.3
  • 29
    • 0023528062 scopus 로고
    • Molybdenum hydroxylases: Biological distribution and substrate-inhibitor specificity
    • Beedham, C.: Molybdenum hydroxylases: Biological distribution and substrate-inhibitor specificity. Prog. Med. Chem., 24: 85-127 1987.
    • (1987) Prog. Med. Chem , vol.24 , pp. 85-127
    • Beedham, C.1
  • 30
    • 0033525193 scopus 로고    scopus 로고
    • CDNA cloning, sequencing, and characterization of male and female rat liver aldehyde oxidase rAOX1
    • Wright, R. M., Clayton, D. A., Riley, M. G., McManaman, J. L. and Repine, J. E.: CDNA cloning, sequencing, and characterization of male and female rat liver aldehyde oxidase rAOX1. J. Biol. Chem., 274: 3878-3886 1999.
    • (1999) J. Biol. Chem , vol.274 , pp. 3878-3886
    • Wright, R.M.1    Clayton, D.A.2    Riley, M.G.3    McManaman, J.L.4    Repine, J.E.5
  • 32
    • 0034730637 scopus 로고    scopus 로고
    • Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase
    • Terao, M., Kurosaki, M., Saltini, G., Demontis, S., Marini, M., Salmona, M. and Garattini, E.: Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase. J. Biol. Chem., 275: 30690-30700 2000.
    • (2000) J. Biol. Chem , vol.275 , pp. 30690-30700
    • Terao, M.1    Kurosaki, M.2    Saltini, G.3    Demontis, S.4    Marini, M.5    Salmona, M.6    Garattini, E.7
  • 33
    • 33646815750 scopus 로고    scopus 로고
    • Large effects from small exposures. III. Endocrine mechanisms mediating effects of bisphenol A at levels of human exposure
    • Welshons, W. V., Nagel, S. C. and vom Saal, F. S.: Large effects from small exposures. III. Endocrine mechanisms mediating effects of bisphenol A at levels of human exposure. Endocrinology, 147Suppl.: S56-S69 2006.
    • (2006) Endocrinology , vol.147 , Issue.SUPPL.
    • Welshons, W.V.1    Nagel, S.C.2    vom Saal, F.S.3
  • 34
    • 1642539111 scopus 로고    scopus 로고
    • Potent inhibition of human liver aldehyde oxidase by raloxifene
    • Obach, R. S.: Potent inhibition of human liver aldehyde oxidase by raloxifene. Drug Metab. Dispos., 32: 89-97 2004.
    • (2004) Drug Metab. Dispos , vol.32 , pp. 89-97
    • Obach, R.S.1
  • 35
  • 36
    • 13544275101 scopus 로고    scopus 로고
    • Effect of high dose vitamin C on the steady-state pharmacokinetics of the protease inhibitor indinavir in healthy volunteers
    • Slain, D., Amsden, J. R., Khakoo, R. A., Fisher, M. A., Lalka, D. and Hobbs, G. R.: Effect of high dose vitamin C on the steady-state pharmacokinetics of the protease inhibitor indinavir in healthy volunteers. Pharmacotherapy, 25: 165-170 2005.
    • (2005) Pharmacotherapy , vol.25 , pp. 165-170
    • Slain, D.1    Amsden, J.R.2    Khakoo, R.A.3    Fisher, M.A.4    Lalka, D.5    Hobbs, G.R.6
  • 38
    • 0141989790 scopus 로고    scopus 로고
    • Effect of metabolic inhibition against CYP3A4 by catechins in bottled green tea drinks
    • Nakamura, T., Asada, E., Nagata, Y. and Kanazawa, H.: Effect of metabolic inhibition against CYP3A4 by catechins in bottled green tea drinks. Bunseki Kagaku, 52: 769-773 2003.
    • (2003) Bunseki Kagaku , vol.52 , pp. 769-773
    • Nakamura, T.1    Asada, E.2    Nagata, Y.3    Kanazawa, H.4
  • 40
    • 23944454203 scopus 로고    scopus 로고
    • Involvement of molybdenum hydroxylases in reductive metabolism of nitro polycyclic aromatic hydrocarbons in mammalian skin
    • Ueda, O., Sugihara, K., Ohta, S. and Kitamura, S.: Involvement of molybdenum hydroxylases in reductive metabolism of nitro polycyclic aromatic hydrocarbons in mammalian skin. Drug Metab. Dispos., 33: 1312-1318 2005.
    • (2005) Drug Metab. Dispos , vol.33 , pp. 1312-1318
    • Ueda, O.1    Sugihara, K.2    Ohta, S.3    Kitamura, S.4
  • 41
    • 78651151595 scopus 로고
    • Hepatic aldehyde oxidase II. Differential inhibition of electron transfer to various electron acceptors
    • Rajagopalan, K. V. and Handler, P.: Hepatic aldehyde oxidase II. Differential inhibition of electron transfer to various electron acceptors. J. Biol. Chem., 239: 2022-2026 1964.
    • (1964) J. Biol. Chem , vol.239 , pp. 2022-2026
    • Rajagopalan, K.V.1    Handler, P.2
  • 42
    • 78651147104 scopus 로고
    • Hepatic aldehyde oxidase. III. The substrate-binding site
    • Rajagopalan, K. V. and Handler, P.: Hepatic aldehyde oxidase. III. The substrate-binding site. J. Biol. Chem., 239: 2027-2035 1964.
    • (1964) J. Biol. Chem , vol.239 , pp. 2027-2035
    • Rajagopalan, K.V.1    Handler, P.2
  • 43
    • 0030058077 scopus 로고    scopus 로고
    • Involvement of mammalian liver cytosols and aldehyde oxidase in reductive metabolism of zonisamide
    • Sugihara, K., Kitamura, S. and Tatsumi, K.: Involvement of mammalian liver cytosols and aldehyde oxidase in reductive metabolism of zonisamide. Drug Metab. Dispos., 24: 199-202 1996.
    • (1996) Drug Metab. Dispos , vol.24 , pp. 199-202
    • Sugihara, K.1    Kitamura, S.2    Tatsumi, K.3
  • 44
    • 0033990931 scopus 로고    scopus 로고
    • Inter- species variation in the metabolism and inhibition of N-2'- dimethylaminoethyl«acridine-4-carboxamide DACA by aldehyde oxidase
    • Schofield, P. C., Robertson, I. G. C. and Paxton, J. W.: Inter- species variation in the metabolism and inhibition of N-2'- dimethylaminoethyl«acridine-4-carboxamide DACA by aldehyde oxidase. Biochem. Pharmacol., 59: 161-165 2000.
    • (2000) Biochem. Pharmacol , vol.59 , pp. 161-165
    • Schofield, P.C.1    Robertson, I.G.C.2    Paxton, J.W.3
  • 45
    • 4143091857 scopus 로고    scopus 로고
    • Green tea Camellia sinensis extract does not alter cytochrome p450 3A4 or 2D6 activity in healthy volunteers
    • Donovan, J. L., Chavin, K. D., Devane, C. L., Taylor, R. M., Wang, J. S., Ruan, Y. and Markowitz, J. S.: Green tea Camellia sinensis extract does not alter cytochrome p450 3A4 or 2D6 activity in healthy volunteers. Drug Metab. Dispos., 32: 906-908 2004.
    • (2004) Drug Metab. Dispos , vol.32 , pp. 906-908
    • Donovan, J.L.1    Chavin, K.D.2    Devane, C.L.3    Taylor, R.M.4    Wang, J.S.5    Ruan, Y.6    Markowitz, J.S.7
  • 46
    • 20444480574 scopus 로고    scopus 로고
    • Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in Healthy Individuals
    • Chow, H. H., Hakim, I. A., Vining, D. R., Crowell, J. A., Ranger-Moore, J., Chew, W. M., Celaya, C. A., Rodney, S. R., Hara, Y. and Alberts, D. S.: Effects of dosing condition on the oral bioavailability of green tea catechins after single-dose administration of Polyphenon E in healthy individuals. Clin. Cancer Res., 11: 4627-4633 2005.
    • (2005) Clin. Cancer Res , vol.11 , pp. 4627
    • Chow, H.H.1    Hakim, I.A.2    Vining, D.R.3    Crowell, J.A.4    Ranger-Moore, J.5    Chew, W.M.6    Celaya, C.A.7    Rodney, S.R.8    Hara, Y.9    Alberts, D.S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.