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Volumn 68, Issue 3, 2005, Pages 644-651

CYP2C9 genotype-dependent effects on in vitro drug-drug interactions: Switching of benzbromarone effect from inhibition to activation in the CYP2C9.3 variant

Author keywords

[No Author keywords available]

Indexed keywords

BENZBROMARONE; CYTOCHROME P450 2C9; FLURBIPROFEN;

EID: 23944487499     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.105.013763     Document Type: Article
Times cited : (43)

References (36)
  • 1
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes HJ, Arlotto MP, and Waterman MR (1991) Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc Natl Acad Sci USA 88:5597-5601.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 2
    • 0038691507 scopus 로고    scopus 로고
    • Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: Ligand stabilization and processing of the N-terminus and heme prosthetic group
    • Cheesman MJ, Baer BR, Zheng YM, Gillam EM, and Rettie AE (2003) Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: ligand stabilization and processing of the N-terminus and heme prosthetic group. Arch Biochem Biophys 416:17-24.
    • (2003) Arch Biochem Biophys , vol.416 , pp. 17-24
    • Cheesman, M.J.1    Baer, B.R.2    Zheng, Y.M.3    Gillam, E.M.4    Rettie, A.E.5
  • 3
    • 1842428730 scopus 로고    scopus 로고
    • Differential roles of Arg97, Asp293, and Arg108 in enzyme stability and substrate specificity of CYP2C9
    • Dickmann LJ, Locuson CW, Jones JP, and Rettie AE (2004) Differential roles of Arg97, Asp293, and Arg108 in enzyme stability and substrate specificity of CYP2C9. Mol Pharmacol 65:842-850.
    • (2004) Mol Pharmacol , vol.65 , pp. 842-850
    • Dickmann, L.J.1    Locuson, C.W.2    Jones, J.P.3    Rettie, A.E.4
  • 6
    • 1842866515 scopus 로고    scopus 로고
    • Quinidine and haloperidol as modifiers of CYP3A4 activity: Multisite kinetic model approach
    • Galetin A, Clarke SE, and Houston JB (2002) Quinidine and haloperidol as modifiers of CYP3A4 activity: multisite kinetic model approach. Drug Metab Dispos 30:1512-1522.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1512-1522
    • Galetin, A.1    Clarke, S.E.2    Houston, J.B.3
  • 7
    • 0030587544 scopus 로고    scopus 로고
    • Allelic variants of human cytochrome P450 2C9: Baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity and prochiral selectivity of the wild-type and I359L mutant forms
    • Haining RL, Hunter AP, Veronese ME, Trager WF, and Rettie AE (1996) Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity and prochiral selectivity of the wild-type and I359L mutant forms. Arch Biochem Biophys 333:447-458.
    • (1996) Arch Biochem Biophys , vol.333 , pp. 447-458
    • Haining, R.L.1    Hunter, A.P.2    Veronese, M.E.3    Trager, W.F.4    Rettie, A.E.5
  • 8
    • 0033574258 scopus 로고    scopus 로고
    • Enzymatic determinants of the substrate specificity of CYP2C9: Role of B'-C loop residues in providing the Pi-stacking anchor site for warfarin binding
    • Haining RL, Jones JP, Henne KR, Fisher MB, Koop DR, Trager WF, and Rettie AE (1999) Enzymatic determinants of the substrate specificity of CYP2C9: role of B'-C loop residues in providing the Pi-stacking anchor site for warfarin binding. Biochemistry 38:3285-3292.
    • (1999) Biochemistry , vol.38 , pp. 3285-3292
    • Haining, R.L.1    Jones, J.P.2    Henne, K.R.3    Fisher, M.B.4    Koop, D.R.5    Trager, W.F.6    Rettie, A.E.7
  • 11
    • 2642555502 scopus 로고    scopus 로고
    • Effector-mediated alteration of substrate orientation in cytochrome P450 2C9
    • Hummel MA, Gannett PM, Aguilar JS, and Tracy TS (2004b) Effector-mediated alteration of substrate orientation in cytochrome P450 2C9. Biochemistry 43:7207-7214.
    • (2004) Biochemistry , vol.43 , pp. 7207-7214
    • Hummel, M.A.1    Gannett, P.M.2    Aguilar, J.S.3    Tracy, T.S.4
  • 12
    • 0034956877 scopus 로고    scopus 로고
    • Dapsone activation of CYP2C9-mediated metabolism: Evidence for activation of multiple substrates and a two-site model
    • Hutzler JM, Hauer MJ, and Tracy TS (2001) Dapsone activation of CYP2C9-mediated metabolism: evidence for activation of multiple substrates and a two-site model. Drug Metab Dispos 29:1029-1034.
    • (2001) Drug Metab Dispos , vol.29 , pp. 1029-1034
    • Hutzler, J.M.1    Hauer, M.J.2    Tracy, T.S.3
  • 13
    • 0037325958 scopus 로고    scopus 로고
    • Activation of cytochrome P450 2C9-mediated metabolism: Mechanistic evidence in support of kinetic observations
    • Hutzler JM, Wienkers LC, Wahlstrom JL, Carlson TJ, and Tracy TS (2003) Activation of cytochrome P450 2C9-mediated metabolism: mechanistic evidence in support of kinetic observations. Arch Biochem Biophys 410:16-24.
    • (2003) Arch Biochem Biophys , vol.410 , pp. 16-24
    • Hutzler, J.M.1    Wienkers, L.C.2    Wahlstrom, J.L.3    Carlson, T.J.4    Tracy, T.S.5
  • 14
    • 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
  • 15
    • 0036263813 scopus 로고    scopus 로고
    • Cytochrome P450 2C9 Polymorphisms: A Comprehensive Review of the in-Vitro and Human Data
    • Lee CR, Goldstein JA, and Pieper JA (2002) Cytochrome P450 2C9 Polymorphisms: a Comprehensive Review of the in-Vitro and Human Data. Pharmacogenetics 12:251-263.
    • (2002) Pharmacogenetics , vol.12 , pp. 251-263
    • Lee, C.R.1    Goldstein, J.A.2    Pieper, J.A.3
  • 16
    • 2642518851 scopus 로고    scopus 로고
    • Quantitative binding models for CYP2C9 based on benzbromarone analogues
    • Locuson CW, Rock DA, and Jones JP (2004) Quantitative binding models for CYP2C9 based on benzbromarone analogues. Biochemistry 43:6948-6958.
    • (2004) Biochemistry , vol.43 , pp. 6948-6958
    • Locuson, C.W.1    Rock, D.A.2    Jones, J.P.3
  • 17
    • 0037636387 scopus 로고    scopus 로고
    • A new class of CYP2C9 inhibitors: Probing 2C9 specificity with high-affinity benzbromarone derivatives
    • Locuson CW, Wahlstrom JL, Rock DA, Rock DA, and Jones JP (2003) A new class of CYP2C9 inhibitors: probing 2C9 specificity with high-affinity benzbromarone derivatives. Drug Metab Dispos 31:967-971.
    • (2003) Drug Metab Dispos , vol.31 , pp. 967-971
    • Locuson, C.W.1    Wahlstrom, J.L.2    Rock, D.A.3    Rock, D.A.4    Jones, J.P.5
  • 18
    • 12244256555 scopus 로고    scopus 로고
    • Highthroughput screening assays for the assessment of CYP2C9*1, CYP2C9*2, and CYP2C9*3 metabolism using fluorogenic vivid substrates
    • Marks BD, Thompson DV, Goossens TA, and Trubetskoy OV (2004) Highthroughput screening assays for the assessment of CYP2C9*1, CYP2C9*2, and CYP2C9*3 metabolism using fluorogenic vivid substrates. J Biomol Screen 9:439-449.
    • (2004) J Biomol Screen , vol.9 , pp. 439-449
    • Marks, B.D.1    Thompson, D.V.2    Goossens, T.A.3    Trubetskoy, O.V.4
  • 19
    • 0017923171 scopus 로고
    • Nuclear relaxation measurements of the geometry of enzyme-bound substrates and analogs
    • Mildvan AS and Gupta RK (1978) Nuclear relaxation measurements of the geometry of enzyme-bound substrates and analogs. Methods Enzymol 49:322-359.
    • (1978) Methods Enzymol , vol.49 , pp. 322-359
    • Mildvan, A.S.1    Gupta, R.K.2
  • 22
    • 0030687597 scopus 로고    scopus 로고
    • The substrate binding site of human liver cytochrome P450 2C9: An NMR study
    • Poli-Scaife S, Attias R, Dansette PM, and Mansuy D (1997) The substrate binding site of human liver cytochrome P450 2C9: an NMR study. Biochemistry 36:12672-12682.
    • (1997) Biochemistry , vol.36 , pp. 12672-12682
    • Poli-Scaife, S.1    Attias, R.2    Dansette, P.M.3    Mansuy, D.4
  • 23
    • 0034548034 scopus 로고    scopus 로고
    • Orientation of caffeine within the active site of human cytochrome P450 1A2 based on NMR longitudinal (T1) relaxation measurements
    • Regal KA and Nelson SD (2000) Orientation of caffeine within the active site of human cytochrome P450 1A2 based on NMR longitudinal (T1) relaxation measurements. Arch Biochem Biophys 384:47-58.
    • (2000) Arch Biochem Biophys , vol.384 , pp. 47-58
    • Regal, K.A.1    Nelson, S.D.2
  • 24
    • 0036223375 scopus 로고    scopus 로고
    • Photochemically catalyzed generation of site-specific 8-nitroguanine adducts in DNA by the reaction of long-lived neutral guanine radicals with nitrogen dioxide
    • Shafirovich V, Mock S, Kolbanovskiy A, and Geacintov NE (2002) Photochemically catalyzed generation of site-specific 8-nitroguanine adducts in DNA by the reaction of long-lived neutral guanine radicals with nitrogen dioxide. Chem Res Toxicol 15:591-597.
    • (2002) Chem Res Toxicol , vol.15 , pp. 591-597
    • Shafirovich, V.1    Mock, S.2    Kolbanovskiy, A.3    Geacintov, N.E.4
  • 25
    • 0035910579 scopus 로고    scopus 로고
    • A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4
    • Shou M, Dai R, Cui D, Korzekwa KR, Baillie TA, and Rushmore TH (2001) A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4. J Biol Chem 276:2256-2262.
    • (2001) J Biol Chem , vol.276 , pp. 2256-2262
    • Shou, M.1    Dai, R.2    Cui, D.3    Korzekwa, K.R.4    Baillie, T.A.5    Rushmore, T.H.6
  • 26
  • 27
    • 0033564235 scopus 로고    scopus 로고
    • Sigmoidal kinetic model for two co-operative substrate-binding sites in a cytochrome P450 3A4 active site: An example of the metabolism of diazepam and its derivatives
    • Shou M, Mei Q, EttoreMWJr, Dai R, Baillie TA, and Rushmore TH (1999) Sigmoidal kinetic model for two co-operative substrate-binding sites in a cytochrome P450 3A4 active site: an example of the metabolism of diazepam and its derivatives. Biochem J 340:845-853.
    • (1999) Biochem J , vol.340 , pp. 845-853
    • Shou, M.1    Mei, Q.2    Ettore Jr., M.W.3    Dai, R.4    Baillie, T.A.5    Rushmore, T.H.6
  • 30
    • 0036206152 scopus 로고    scopus 로고
    • Polymorphic variants (CYP2C9*3 and CYP2C9*5) and the F114L active site mutation of CYP2C9: Effect on atypical kinetic metabolism profiles
    • Tracy TS, Hutzler JM, Haining RL, Rettie AE, Hummel MA, and Dickmann LJ (2002) Polymorphic variants (CYP2C9*3 and CYP2C9*5) and the F114L active site mutation of CYP2C9: effect on atypical kinetic metabolism profiles. Drug Metab Dispos 30:385-390.
    • (2002) Drug Metab Dispos , vol.30 , pp. 385-390
    • Tracy, T.S.1    Hutzler, J.M.2    Haining, R.L.3    Rettie, A.E.4    Hummel, M.A.5    Dickmann, L.J.6
  • 31
    • 0030601837 scopus 로고    scopus 로고
    • Studies of flurbiprofen 4′-hydroxylation - Additional evidence suggesting the sole involvement of cytochrome P450 2C9
    • Tracy TS, Marra C, Wrighton SA, Gonzalez FJ, and Korzekwa KR (1996) Studies of flurbiprofen 4′-hydroxylation - additional evidence suggesting the sole involvement of cytochrome P450 2C9. Biochem Pharmacol 52:1305-1309.
    • (1996) Biochem Pharmacol , vol.52 , pp. 1305-1309
    • Tracy, T.S.1    Marra, C.2    Wrighton, S.A.3    Gonzalez, F.J.4    Korzekwa, K.R.5
  • 32
    • 0029010518 scopus 로고
    • Role of cytochrome P450 2C9 and an allelic variant in the 4′-hydroxylation of (R)- and (S)-flurbiprofen
    • Tracy TS, Rosenbluth BW, Wrighton SA, Gonzalez FJ, and Korzekwa KR (1995) Role of cytochrome P450 2C9 and an allelic variant in the 4′- hydroxylation of (R)- and (S)-flurbiprofen. Biochem Pharmacol 49:1269-1275.
    • (1995) Biochem Pharmacol , vol.49 , pp. 1269-1275
    • Tracy, T.S.1    Rosenbluth, B.W.2    Wrighton, S.A.3    Gonzalez, F.J.4    Korzekwa, K.R.5
  • 34
    • 0036118686 scopus 로고    scopus 로고
    • Factors confounding the successful extrapolation of in vitro CYP3A inhibition information to the in vivo condition
    • Wienkers LC (2002) Factors confounding the successful extrapolation of in vitro CYP3A inhibition information to the in vivo condition. Eur J Pharm Sci 15:239-242.
    • (2002) Eur J Pharm Sci , vol.15 , pp. 239-242
    • Wienkers, L.C.1
  • 36
    • 0031757521 scopus 로고    scopus 로고
    • Comparative studies on the catalytic roles of cytochrome P450 2C9 and its Cys- and Leu-variants in the oxidation of warfarin, flurbiprofen and diclofenac by human liver microsomes
    • Yamazaki H, Inoue K, Chiba K, Ozawa N, Kawai T, Suzuki Y, Goldstein JA, Guengerich FP, and Shimada T (1998) Comparative studies on the catalytic roles of cytochrome P450 2C9 and its Cys- and Leu-variants in the oxidation of warfarin, flurbiprofen and diclofenac by human liver microsomes. Biochem Pharmacol 56:243-251.
    • (1998) Biochem Pharmacol , vol.56 , pp. 243-251
    • Yamazaki, H.1    Inoue, K.2    Chiba, K.3    Ozawa, N.4    Kawai, T.5    Suzuki, Y.6    Goldstein, J.A.7    Guengerich, F.P.8    Shimada, T.9


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