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Volumn 32, Issue 12, 2004, Pages 1434-1445

Evidence of significant contribution from CYP3A5 to hepatic drug metabolism

Author keywords

[No Author keywords available]

Indexed keywords

CARBAMAZEPINE; CYTOCHROME P450 3A4; CYTOCHROME P450 3A5; DEXTROMETHORPHAN; ERYTHROMYCIN; FLUNITRAZEPAM; ITRACONAZOLE; LIDOCAINE; MIDAZOLAM; TERFENADINE;

EID: 9444228347     PISSN: 00909556     EISSN: None     Source Type: Journal    
DOI: 10.1124/dmd.104.001313     Document Type: Article
Times cited : (176)

References (53)
  • 1
    • 0024412071 scopus 로고
    • Cytochrome P-450 hPCN3, a novel cytochrome P-450IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine
    • Aoyama T, Yamano S, Waxman DJ, Lapenson DP, Meyer UA, Fischer V, Tyndale R, Inaba T, Kalow W, Gelboin HV, et al. (1989) Cytochrome P-450 hPCN3, a novel cytochrome P-450IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine. J Biol Chem 264:10388-10395.
    • (1989) J Biol Chem , vol.264 , pp. 10388-10395
    • Aoyama, T.1    Yamano, S.2    Waxman, D.J.3    Lapenson, D.P.4    Meyer, U.A.5    Fischer, V.6    Tyndale, R.7    Inaba, T.8    Kalow, W.9    Gelboin, H.V.10
  • 3
    • 0024408814 scopus 로고
    • Lidocaine metabolism in human liver microsomes by cytochrome P450IIIA4
    • Bargetzi MJ, Aoyama T, Gonzalez FJ, and Meyer UA (1989) Lidocaine metabolism in human liver microsomes by cytochrome P450IIIA4. Clin Pharmacol Ther 46:521-527.
    • (1989) Clin Pharmacol Ther , vol.46 , pp. 521-527
    • Bargetzi, M.J.1    Aoyama, T.2    Gonzalez, F.J.3    Meyer, U.A.4
  • 4
    • 0142250945 scopus 로고    scopus 로고
    • Genotype-phenotype associations for common CYP3A4 and CYP3A5 variants in the basal and induced metabolism of midazolam in European- and African-American men and women
    • Floyd MD, Gervasini G, Masica AL, Mayo G, George AL Jr, Bhat K, Kim RB, and Wilkinson GR (2003) Genotype-phenotype associations for common CYP3A4 and CYP3A5 variants in the basal and induced metabolism of midazolam in European- and African-American men and women. Pharmacogenetics 13:595-606.
    • (2003) Pharmacogenetics , vol.13 , pp. 595-606
    • Floyd, M.D.1    Gervasini, G.2    Masica, A.L.3    Mayo, G.4    George Jr., A.L.5    Bhat, K.6    Kim, R.B.7    Wilkinson, G.R.8
  • 5
    • 0028912205 scopus 로고
    • Expression of cytochrome P450 3A5 in Escherichia coli: Effects of 5′ modification, purification, spectral characterization, reconstitution conditions and catalytic activities
    • Gillam EMJ, Guo Z, Ueng Y-F, Yamazaki H, Cock I, Reilly PEB, Hooper WD, and Guengerich FP (1995) Expression of cytochrome P450 3A5 in Escherichia coli: effects of 5′ modification, purification, spectral characterization, reconstitution conditions and catalytic activities. Arch Biochem Biophys 317:374-384.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 374-384
    • Gillam, E.M.J.1    Guo, Z.2    Ueng, Y.-F.3    Yamazaki, H.4    Cock, I.5    Reilly, P.E.B.6    Hooper, W.D.7    Guengerich, F.P.8
  • 7
    • 0036731724 scopus 로고    scopus 로고
    • Explaining interindividual variability of docetaxel pharmacokinetics and pharmacodynamics in Asians through phenotyping and genotyping strategies
    • Goh BC, Lee SC, Wang LZ, Fan L, Guo JY, Lamba J, Schuetz E, Lim R, Lim HL, Ong AB, et al. (2002) Explaining interindividual variability of docetaxel pharmacokinetics and pharmacodynamics in Asians through phenotyping and genotyping strategies. J Clin Oncol 20:3683-3690.
    • (2002) J Clin Oncol , vol.20 , pp. 3683-3690
    • Goh, B.C.1    Lee, S.C.2    Wang, L.Z.3    Fan, L.4    Guo, J.Y.5    Lamba, J.6    Schuetz, E.7    Lim, R.8    Lim, H.L.9    Ong, A.B.10
  • 8
    • 0028234586 scopus 로고
    • Regioselective biotransformation of midazolam by members of the human cytochrome P450 3A (CYP3A) subfamily
    • Gorski JC, Hall SD, Jones DR, VandenBranden M, and Wrighton SA (1994) Regioselective biotransformation of midazolam by members of the human cytochrome P450 3A (CYP3A) subfamily. Biochem Pharmacol 47:1643-1653.
    • (1994) Biochem Pharmacol , vol.47 , pp. 1643-1653
    • Gorski, J.C.1    Hall, S.D.2    Jones, D.R.3    VandenBranden, M.4    Wrighton, S.A.5
  • 9
    • 0030739468 scopus 로고    scopus 로고
    • Possible involvement of multiple cytochrome P450s in fentanyl and sufentanil metabolism as opposed to alfentanil
    • Guitton J, Buronfosse T, Desage M, Lepape A, Brazier JL, and Beaune P (1997) Possible involvement of multiple cytochrome P450s in fentanyl and sufentanil metabolism as opposed to alfentanil. Biochem Pharmacol 53:1613-1619.
    • (1997) Biochem Pharmacol , vol.53 , pp. 1613-1619
    • Guitton, J.1    Buronfosse, T.2    Desage, M.3    Lepape, A.4    Brazier, J.L.5    Beaune, P.6
  • 14
    • 0346992330 scopus 로고    scopus 로고
    • Progress towards prediction of human pharmacokinetic parameters from in vitro technologies
    • Houston JB and Galetin A (2003) Progress towards prediction of human pharmacokinetic parameters from in vitro technologies. Drug Metab Rev 35:393-415.
    • (2003) Drug Metab Rev , vol.35 , pp. 393-415
    • Houston, J.B.1    Galetin, A.2
  • 15
    • 0034105896 scopus 로고    scopus 로고
    • In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model
    • Houston JB and Kenworthy KE (2000) In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model. Drug Metab Dispos 28:246-254.
    • (2000) Drug Metab Dispos , vol.28 , pp. 246-254
    • Houston, J.B.1    Kenworthy, K.E.2
  • 17
    • 0029971798 scopus 로고    scopus 로고
    • Multiple forms of human P450 expressed in Saccharomyces cerevisiae. Systematic characterization and comparison with those of the rat
    • Imaoka S, Yamada T, Hiroi T, Hayashi K, Sakaki T, Yabusaki Y, and Funae Y (1996) Multiple forms of human P450 expressed in Saccharomyces cerevisiae. Systematic characterization and comparison with those of the rat. Biochem Pharmacol 51:1041-1050.
    • (1996) Biochem Pharmacol , vol.51 , pp. 1041-1050
    • Imaoka, S.1    Yamada, T.2    Hiroi, T.3    Hayashi, K.4    Sakaki, T.5    Yabusaki, Y.6    Funae, Y.7
  • 20
    • 0036707616 scopus 로고    scopus 로고
    • Differential oxidation of mifepristone by cytochromes P450 3A4 and 3A5: Selective inactivation of P450 3A4
    • Khan KK, He YQ, Correia MA, and Halpert JR (2002a) Differential oxidation of mifepristone by cytochromes P450 3A4 and 3A5: selective inactivation of P450 3A4. Drug Metab Dispos 30:985-990.
    • (2002) Drug Metab Dispos , vol.30 , pp. 985-990
    • Khan, K.K.1    He, Y.Q.2    Correia, M.A.3    Halpert, J.R.4
  • 21
    • 0036178095 scopus 로고    scopus 로고
    • Midazolam oxidation by cytochrome P450 3A4 and active-site mutants: An evaluation of multiple binding sites and of the metabolic pathway that leads to enzyme inactivation
    • Khan KK, He YQ, Domanski TL, and Halpert JR (2002b) Midazolam oxidation by cytochrome P450 3A4 and active-site mutants: an evaluation of multiple binding sites and of the metabolic pathway that leads to enzyme inactivation. Mol Pharmacol 61:495-506.
    • (2002) Mol Pharmacol , vol.61 , pp. 495-506
    • Khan, K.K.1    He, Y.Q.2    Domanski, T.L.3    Halpert, J.R.4
  • 23
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate- models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • Korzekwa KR, Krishnamachary N, Shou M, Ogai A, Parise RA, Rettie AE, Gonzalez FJ, and Tracy TS (1998) Evaluation of atypical cytochrome P450 kinetics with two-substrate-models: evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry 37:4137-4147.
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, N.2    Shou, M.3    Ogai, A.4    Parise, R.A.5    Rettie, A.E.6    Gonzalez, F.J.7    Tracy, T.S.8
  • 24
    • 0024373348 scopus 로고
    • Oxidation of midazolam and triazolam by human liver cytochrome P450IIIA4
    • Kronbach T, Mathys D, Umeno M, Gonzalez FJ, and Meyer UA (1989) Oxidation of midazolam and triazolam by human liver cytochrome P450IIIA4. Mol Pharmacol 36:89-96.
    • (1989) Mol Pharmacol , vol.36 , pp. 89-96
    • Kronbach, T.1    Mathys, D.2    Umeno, M.3    Gonzalez, F.J.4    Meyer, U.A.5
  • 26
    • 0034911153 scopus 로고    scopus 로고
    • Characterization of the NADPH-dependent metabolism of 17beta-estradiol to multiple metabolites by human liver microsomes and selectively expressed human cytochrome P450 3A4 and 3A5
    • Lee AJ, Kosh JW, Conney AH, and Zhu BT (2001) Characterization of the NADPH-dependent metabolism of 17beta-estradiol to multiple metabolites by human liver microsomes and selectively expressed human cytochrome P450 3A4 and 3A5. J Pharmacol Exp Ther 298: 420-432.
    • (2001) J Pharmacol Exp Ther , vol.298 , pp. 420-432
    • Lee, A.J.1    Kosh, J.W.2    Conney, A.H.3    Zhu, B.T.4
  • 30
    • 0031960329 scopus 로고    scopus 로고
    • Human cytochrome P450 3A (CYP3A) mediated midazolam metabolism: The effect of assay conditions and regioselective stimulation by alpha-naphthoflavone, terfenadine and testosterone
    • Maenpaa J, Hall SD, Ring BJ, Strom SC, and Wrighton SA (1998) Human cytochrome P450 3A (CYP3A) mediated midazolam metabolism: the effect of assay conditions and regioselective stimulation by alpha-naphthoflavone, terfenadine and testosterone. Pharmacogenetics 8:137-155.
    • (1998) Pharmacogenetics , vol.8 , pp. 137-155
    • Maenpaa, J.1    Hall, S.D.2    Ring, B.J.3    Strom, S.C.4    Wrighton, S.A.5
  • 31
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T and Sato R (1964a) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239:2370-2385.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2385
    • Omura, T.1    Sato, R.2
  • 32
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification and properties
    • Omura T and Sato R (1964b) The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification and properties. J Biol Chem 239:2379-2385.
    • (1964) J Biol Chem , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 34
    • 0030843652 scopus 로고    scopus 로고
    • Drug metabolism by Escherichia coli expressing human cytochromes P450
    • Parikh A, Gillam EM, and Guengerich FP (1997) Drug metabolism by Escherichia coli expressing human cytochromes P450. Nat Biotechnol 15:784-788.
    • (1997) Nat Biotechnol , vol.15 , pp. 784-788
    • Parikh, A.1    Gillam, E.M.2    Guengerich, F.P.3
  • 35
    • 0037974573 scopus 로고    scopus 로고
    • In vitro metabolism of midazolam, triazolam, nifedipine and testosterone by human liver microsomes and recombinant cytochromes p450: Role of cyp3a4 and cyp3a5
    • Patki KC, Von Moltke LL, and Greenblatt DJ (2003) In vitro metabolism of midazolam, triazolam, nifedipine and testosterone by human liver microsomes and recombinant cytochromes p450: role of cyp3a4 and cyp3a5. Drug Metab Dispos 31:938-944.
    • (2003) Drug Metab Dispos , vol.31 , pp. 938-944
    • Patki, K.C.1    Von Moltke, L.L.2    Greenblatt, D.J.3
  • 36
    • 27244462157 scopus 로고    scopus 로고
    • Covalent alteration of the CYP3A4 active site: Evidence for multiple substrate binding domains
    • Schrag ML and Wienkers LC (2001) Covalent alteration of the CYP3A4 active site: evidence for multiple substrate binding domains. Arch Biochem Biophys 391:49-55.
    • (2001) Arch Biochem Biophys , vol.391 , pp. 49-55
    • Schrag, M.L.1    Wienkers, L.C.2
  • 38
    • 0036892578 scopus 로고    scopus 로고
    • Pharmacokinetics of midazolam and 1′-hydroxymidazolam in Chinese with different CYP3A5 genotypes
    • Shih PS and Huang JD (2002) Pharmacokinetics of midazolam and 1′-hydroxymidazolam in Chinese with different CYP3A5 genotypes. Drug Metab Dispos 30:1491-1496.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1491-1496
    • Shih, P.S.1    Huang, J.D.2
  • 39
    • 0242332169 scopus 로고    scopus 로고
    • Impact of cytochrome p450 3A5 genetic polymorphism on tacrolimus doses and concentration-to-dose ratio in renal transplant recipients
    • Thervet E, Anglicheau D, King B, Schlageter MH, Cassinat B, Beaune P, Legendre C, and Daly AK (2003) Impact of cytochrome p450 3A5 genetic polymorphism on tacrolimus doses and concentration-to-dose ratio in renal transplant recipients. Transplantation 76:1233-1235.
    • (2003) Transplantation , vol.76 , pp. 1233-1235
    • Thervet, E.1    Anglicheau, D.2    King, B.3    Schlageter, M.H.4    Cassinat, B.5    Beaune, P.6    Legendre, C.7    Daly, A.K.8
  • 40
  • 47
    • 0031570724 scopus 로고    scopus 로고
    • Reconstitution of recombinant cytochrome P450 2CI0(2C9) and comparison with ytochrome P450 3A4 and other forms: Effects of cytochrome P450-P450 and cytochrome P450-b5 interactions
    • Yamazaki H, Gillam EM, Dong MS, Johnson WW, Guengerich FP, and Shimada T (1997) Reconstitution of recombinant cytochrome P450 2CI0(2C9) and comparison with ytochrome P450 3A4 and other forms: effects of cytochrome P450-P450 and cytochrome P450-b5 interactions. Arch Biochem Biophys 342:329-337.
    • (1997) Arch Biochem Biophys , vol.342 , pp. 329-337
    • Yamazaki, H.1    Gillam, E.M.2    Dong, M.S.3    Johnson, W.W.4    Guengerich, F.P.5    Shimada, T.6
  • 48
    • 0029926494 scopus 로고    scopus 로고
    • Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5
    • Yamazaki H, Johnson WW, Ueng YF, Shimada T, and Guengerich FP (1996) Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5. J Biol Chem 271:27438-27444.
    • (1996) J Biol Chem , vol.271 , pp. 27438-27444
    • Yamazaki, H.1    Johnson, W.W.2    Ueng, Y.F.3    Shimada, T.4    Guengerich, F.P.5
  • 50
    • 0036447583 scopus 로고    scopus 로고
    • Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli
    • Yamazaki H, Nakamura M, Komatsu T, Ohyama K, Hatanaka N, Asahi S, Shimada N, Guengerich FP, Shimada T, Nakajima M, et al. (2002) Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli. Protein Expression Purif 24:329-337.
    • (2002) Protein Expression Purif , vol.24 , pp. 329-337
    • Yamazaki, H.1    Nakamura, M.2    Komatsu, T.3    Ohyama, K.4    Hatanaka, N.5    Asahi, S.6    Shimada, N.7    Guengerich, F.P.8    Shimada, T.9    Nakajima, M.10
  • 51
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi Y and Masters BS (1976) Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography. J Biol Chem 251:5337-5344.
    • (1976) J Biol Chem , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.2


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