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Volumn 36, Issue 3, 2008, Pages 490-499

CYP3A4-mediated carbamazepine (CBZ) metabolism: Formation of a covalent CBZ-CYP3A4 adduct and alteration of the enzyme kinetic profile

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; CARBAMAZEPINE; CYTOCHROME P450; CYTOCHROME P450 3A4; ERYTHROMYCIN; GLUTATHIONE; N DEMETHYLASE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 40949102296     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.107.016501     Document Type: Article
Times cited : (59)

References (37)
  • 1
    • 34447133553 scopus 로고    scopus 로고
    • Time-dependent inactivation of P450 3A4 by raloxifene: Identification of Cys239 as the site of apoprotein alkylation
    • Baer BR, Wienkers LC, and Rock DA (2007) Time-dependent inactivation of P450 3A4 by raloxifene: identification of Cys239 as the site of apoprotein alkylation. Chem Res Toxicol 20:954-964.
    • (2007) Chem Res Toxicol , vol.20 , pp. 954-964
    • Baer, B.R.1    Wienkers, L.C.2    Rock, D.A.3
  • 2
    • 28144464500 scopus 로고    scopus 로고
    • Human in vitro glutathionyl and protein adducts of carbamazepine-10,11-epoxide, a stable and pharmacologically active metabolite of carbamazepine
    • Bu HZ, Kang P, Deese AJ, Zhao P, and Pool WF (2005) Human in vitro glutathionyl and protein adducts of carbamazepine-10,11-epoxide, a stable and pharmacologically active metabolite of carbamazepine. Drug Metab Dispos 33:1920-1924.
    • (2005) Drug Metab Dispos , vol.33 , pp. 1920-1924
    • Bu, H.Z.1    Kang, P.2    Deese, A.J.3    Zhao, P.4    Pool, W.F.5
  • 3
    • 33747736671 scopus 로고    scopus 로고
    • The ferrous-dioxygen intermediate in human cytochrome P450 3A4. Substrate dependence of formation and decay kinetics
    • Denisov IG, Grinkova YV, Baas BJ, and Sligar SG (2006) The ferrous-dioxygen intermediate in human cytochrome P450 3A4. Substrate dependence of formation and decay kinetics. J Biol Chem 281:23313-23318.
    • (2006) J Biol Chem , vol.281 , pp. 23313-23318
    • Denisov, I.G.1    Grinkova, Y.V.2    Baas, B.J.3    Sligar, S.G.4
  • 4
    • 33748802003 scopus 로고    scopus 로고
    • Structural basis for ligand promiscuity in cytochrome P450 3A4
    • Ekroos M and Sjogren T (2006) Structural basis for ligand promiscuity in cytochrome P450 3A4. Proc Natl Acad Sci U S A 103:13682-136876.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13682-136876
    • Ekroos, M.1    Sjogren, T.2
  • 5
    • 0029294584 scopus 로고
    • Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: Conformationally flexible docking by evolutionary programming
    • Gehlhaar DK, Verkhivker GM, Rejto PA, Sherman CJ, Fogel DB, Fogel LJ, and Freer ST (1995) Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming. Chem Biol 2:317-324.
    • (1995) Chem Biol , vol.2 , pp. 317-324
    • Gehlhaar, D.K.1    Verkhivker, G.M.2    Rejto, P.A.3    Sherman, C.J.4    Fogel, D.B.5    Fogel, L.J.6    Freer, S.T.7
  • 6
    • 0039012103 scopus 로고    scopus 로고
    • Reduced dimensionality in ligand-protein structure prediction: Covalent inhibitors of serine proteases and design of site-directed combinatorial libraries
    • Parrill AL and Reddy MR eds pp, ACS Press, Washington, DC
    • Gehlhaar D, Bouzida D, and Rejto PA (1999) Reduced dimensionality in ligand-protein structure prediction: covalent inhibitors of serine proteases and design of site-directed combinatorial libraries. ACS Symposium Series 719: Rational Drug Design. (Parrill AL and Reddy MR eds) pp 292-311, ACS Press, Washington, DC.
    • (1999) ACS Symposium Series 719: Rational Drug Design , pp. 292-311
    • Gehlhaar, D.1    Bouzida, D.2    Rejto, P.A.3
  • 7
    • 0032499691 scopus 로고    scopus 로고
    • Analysis of human cytochrome P450 3A4 cooperativity: Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics
    • Harlow GR and Halpert JR (1998) Analysis of human cytochrome P450 3A4 cooperativity: construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics. Proc Natl Acad Sci U S A 95:6636-6418.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6636-6418
    • Harlow, G.R.1    Halpert, J.R.2
  • 8
    • 0020061626 scopus 로고
    • Carbamazepine and hematological monitoring
    • Hart RG and Easton JD (1982) Carbamazepine and hematological monitoring. Ann Neurol 11:309-312.
    • (1982) Ann Neurol , vol.11 , pp. 309-312
    • Hart, R.G.1    Easton, J.D.2
  • 9
    • 0032534908 scopus 로고    scopus 로고
    • Identification of the heme-modified peptides from cumene hydroperoxide- inactivated cytochrome P450 3A4
    • He K, Bornheim LM, Falick AM, Maltby D, Yin H, Correia MA (1998) Identification of the heme-modified peptides from cumene hydroperoxide- inactivated cytochrome P450 3A4. Biochemistry 37:17448-17457.
    • (1998) Biochemistry , vol.37 , pp. 17448-17457
    • He, K.1    Bornheim, L.M.2    Falick, A.M.3    Maltby, D.4    Yin, H.5    Correia, M.A.6
  • 10
    • 0036377952 scopus 로고    scopus 로고
    • Carbamazepine-provoked hepatotoxicity and possible aetiopathological role of glutathione in the events. Retrospective review of old data and call for new investigation
    • Kalapos MP (2002) Carbamazepine-provoked hepatotoxicity and possible aetiopathological role of glutathione in the events. Retrospective review of old data and call for new investigation. Adverse Drug React Toxicol Rev 21:123-141.
    • (2002) Adverse Drug React Toxicol Rev , vol.21 , pp. 123-141
    • Kalapos, M.P.1
  • 11
    • 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 (2002) 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 61:495-5062.
    • (2002) Mol Pharmacol , vol.61 , pp. 495-5062
    • Khan, K.K.1    He, Y.Q.2    Domanski, T.L.3    Halpert, J.R.4
  • 12
    • 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
  • 13
    • 0031787340 scopus 로고    scopus 로고
    • Mechanisms of idiosyncratic hypersensitivity reactions to antiepileptic drugs
    • Leeder JS (1998) Mechanisms of idiosyncratic hypersensitivity reactions to antiepileptic drugs. Epilepsia 39(suppl 7):S8-S16.
    • (1998) Epilepsia , vol.39 , Issue.SUPPL. 7
    • Leeder, J.S.1
  • 14
    • 0030063547 scopus 로고    scopus 로고
    • Epitope mapping studies with human anti-cytochrome P450 3A antibodies
    • Leeder JS, Gaedigk A, Lu X, and Cook VA (1996) Epitope mapping studies with human anti-cytochrome P450 3A antibodies. Mol Pharmacol 49:234-243.
    • (1996) Mol Pharmacol , vol.49 , pp. 234-243
    • Leeder, J.S.1    Gaedigk, A.2    Lu, X.3    Cook, V.A.4
  • 15
    • 0030954347 scopus 로고    scopus 로고
    • Cytochrome P450 2C11: Escherichia coli expression, purification, functional characterization, and mechanism-based inactivation of the enzyme
    • Licad-Coles E, He K, Yin H, and Correia MA (1997) Cytochrome P450 2C11: Escherichia coli expression, purification, functional characterization, and mechanism-based inactivation of the enzyme. Arch Biochem Biophys 338:35-42.
    • (1997) Arch Biochem Biophys , vol.338 , pp. 35-42
    • Licad-Coles, E.1    He, K.2    Yin, H.3    Correia, M.A.4
  • 17
    • 0029926719 scopus 로고    scopus 로고
    • Bioactivation of carbamazepine in the rat in vivo. Evidence for the formation of reactive arene oxide(s)
    • Madden S, Maggs JL, and Park BK (1996) Bioactivation of carbamazepine in the rat in vivo. Evidence for the formation of reactive arene oxide(s). Drug Metab Dispos 24:469-479.
    • (1996) Drug Metab Dispos , vol.24 , pp. 469-479
    • Madden, S.1    Maggs, J.L.2    Park, B.K.3
  • 18
    • 0033668846 scopus 로고    scopus 로고
    • Marrone TJ, Luty BA, and Rose PW (1999) Discovering high-affinity ligands from the computationally predicted structures and affinities of small molecules bound to a target: a virtual screening approach. Virtual screening: an alternative or complement to high throughput screening?, in Proceedings of the Workshop New Approaches in Drug Design and Discovery, special topic Virtual Screening; 1999 March 15-18; Springer Netherlands, Schloâ Rauischholzhausen, Germany, pp 209-230.
    • Marrone TJ, Luty BA, and Rose PW (1999) Discovering high-affinity ligands from the computationally predicted structures and affinities of small molecules bound to a target: a virtual screening approach. Virtual screening: an alternative or complement to high throughput screening?, in Proceedings of the Workshop "New Approaches in Drug Design and Discovery," special topic "Virtual Screening;" 1999 March 15-18; Springer Netherlands, Schloâ Rauischholzhausen, Germany, pp 209-230.
  • 19
    • 0034756188 scopus 로고    scopus 로고
    • Differential selectivity in carbamazepineinduced inactivation of cytochrome P450 enzymes in rat and human liver
    • Masubuchi Y, Nakano T, Ose A, and Horie T (2001) Differential selectivity in carbamazepineinduced inactivation of cytochrome P450 enzymes in rat and human liver. Arch Toxicol 75:538-543.
    • (2001) Arch Toxicol , vol.75 , pp. 538-543
    • Masubuchi, Y.1    Nakano, T.2    Ose, A.3    Horie, T.4
  • 20
    • 0242276321 scopus 로고    scopus 로고
    • CYP3A4 and CYP3A7-mediated carbamazepine 10,11-epoxidation are activated by differential endogenous steroids
    • Nakamura H, Torimoto N, Ishii I, Ariyoshi N, Nakasa H, Ohmori S, and Kitada M (2003) CYP3A4 and CYP3A7-mediated carbamazepine 10,11-epoxidation are activated by differential endogenous steroids. Drug Metab Dispos 31:432-438.
    • (2003) Drug Metab Dispos , vol.31 , pp. 432-438
    • Nakamura, H.1    Torimoto, N.2    Ishii, I.3    Ariyoshi, N.4    Nakasa, H.5    Ohmori, S.6    Kitada, M.7
  • 22
    • 0036841947 scopus 로고    scopus 로고
    • Pathways of carbamazepine bioactivation in vitro I. Characterization of human cytochromes P450 responsible for the formation of 2- and 3-hydroxylated metabolites
    • Pearce RE, Vakkalagadda GR, and Leeder JS (2002) Pathways of carbamazepine bioactivation in vitro I. Characterization of human cytochromes P450 responsible for the formation of 2- and 3-hydroxylated metabolites. Drug Metab Dispos 30:1170-1179.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1170-1179
    • Pearce, R.E.1    Vakkalagadda, G.R.2    Leeder, J.S.3
  • 23
    • 28144440176 scopus 로고    scopus 로고
    • Pathways of carbamazepine bioactivation in vitro: II. The role of human cytochrome P450 enzymes in the formation of 2-hydroxyiminostilbene
    • Pearce RE, Uetrecht JP, and Leeder JS (2005) Pathways of carbamazepine bioactivation in vitro: II. The role of human cytochrome P450 enzymes in the formation of 2-hydroxyiminostilbene. Drug Metab Dispos 33:1819-1826.
    • (2005) Drug Metab Dispos , vol.33 , pp. 1819-1826
    • Pearce, R.E.1    Uetrecht, J.P.2    Leeder, J.S.3
  • 25
    • 0026676057 scopus 로고
    • The effect of enzyme induction on the cytochrome P450-mediated bioactivation of carbamazepine by mouse liver microsomes
    • Pirmohamed M, Kitteringham NR, Breckenridge AM, and Park BK (1992) The effect of enzyme induction on the cytochrome P450-mediated bioactivation of carbamazepine by mouse liver microsomes. Biochem Pharmacol 44:2307-2314.
    • (1992) Biochem Pharmacol , vol.44 , pp. 2307-2314
    • Pirmohamed, M.1    Kitteringham, N.R.2    Breckenridge, A.M.3    Park, B.K.4
  • 27
    • 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
  • 28
    • 0024208020 scopus 로고
    • Anticonvulsant hypersensitivity syndrome. In vitro risk assessment
    • Shear NH, Spielberg SP, Cannon M, and Miller M (1988) Anticonvulsant hypersensitivity syndrome. In vitro risk assessment. J Clin Invest 82:1826-1832.
    • (1988) J Clin Invest , vol.82 , pp. 1826-1832
    • Shear, N.H.1    Spielberg, S.P.2    Cannon, M.3    Miller, M.4
  • 29
    • 0028307539 scopus 로고
    • Activation of CYP3A4: Evidence for the simultaneous binding of two substrates in a cytochrome P450 active site
    • Shou M, Grogan J, Mancewicz JA, Krausz KW, Gonzalez FJ, Gelboin HV, and Korzekwa KR (1994) Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 33:6450-64554.
    • (1994) Biochemistry , vol.33 , pp. 6450-64554
    • Shou, M.1    Grogan, J.2    Mancewicz, J.A.3    Krausz, K.W.4    Gonzalez, F.J.5    Gelboin, H.V.6    Korzekwa, K.R.7
  • 30
    • 0031028518 scopus 로고    scopus 로고
    • Cooperativity in oxidations catalyzed by cytochrome P450 3A4
    • Ueng YF, Kuwabara T, Chun YJ, and Guengerich FP (1997) Cooperativity in oxidations catalyzed by cytochrome P450 3A4. Biochemistry 36:370-381.
    • (1997) Biochemistry , vol.36 , pp. 370-381
    • Ueng, Y.F.1    Kuwabara, T.2    Chun, Y.J.3    Guengerich, F.P.4
  • 31
    • 0031005752 scopus 로고    scopus 로고
    • Human cytochrome P450 3A4-catalyzed testosterone 6 beta-hydroxylation and erythromycin N-demethylation. Competition during catalysis
    • Wang RW, Newton DJ, Scheri TD, and Lu AY (1997) Human cytochrome P450 3A4-catalyzed testosterone 6 beta-hydroxylation and erythromycin N-demethylation. Competition during catalysis. Drug Metab Dispos 25:502-507.
    • (1997) Drug Metab Dispos , vol.25 , pp. 502-507
    • Wang, R.W.1    Newton, D.J.2    Scheri, T.D.3    Lu, A.Y.4
  • 36
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution
    • Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, and Johnson EF (2004) The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 279:38091- 38094.
    • (2004) J Biol Chem , vol.279 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 37
    • 4444268690 scopus 로고    scopus 로고
    • Mechanisms that regulate production of reactive oxygen species by cytochrome P450
    • Zangar RC, Davydov DR, and Verma S (2004) Mechanisms that regulate production of reactive oxygen species by cytochrome P450. Toxicol Appl Pharmacol 199:316-331.
    • (2004) Toxicol Appl Pharmacol , vol.199 , pp. 316-331
    • Zangar, R.C.1    Davydov, D.R.2    Verma, S.3


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