메뉴 건너뛰기




Volumn 25, Issue 11, 1997, Pages 1242-1248

Inactivation of cytochrome P450S 2B1, 2B4, 2B6, and 2B11 by arylalkynes

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC HYDROCARBON; CYTOCHROME P450; ERYTHROMYCIN; ETHOXYRESORUFIN DEETHYLASE; LIDOCAINE; NITROPHENOL; OXYGENASE; PENTOXYRESORUFIN; PHENOBARBITAL; PYRIDINE; TESTOSTERONE;

EID: 0030720486     PISSN: 00909556     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (39)

References (29)
  • 2
    • 0018937071 scopus 로고
    • Self-catalyzed inactivation of hepatic cytochrome P-450 by ethynyl substrates
    • P. R. Ortiz de Montellano, and K. L. Kunze: Self-catalyzed inactivation of hepatic cytochrome P-450 by ethynyl substrates. J. Biol. Chem. 255, 5578-5585 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 5578-5585
    • Ortiz De Montellano, P.R.1    Kunze, K.L.2
  • 4
    • 0024789979 scopus 로고
    • 2-Ethynylnaphthalene as a mechanism-based inactivator of the cytochrome P450 catalyzed N-oxidation of 2-naphthylamine
    • G. J. Hammons, W. L. Alworth, N. E. Hopkins, F. P. Guengerich, and F. F. Kadlubar: 2-Ethynylnaphthalene as a mechanism-based inactivator of the cytochrome P450 catalyzed N-oxidation of 2-naphthylamine. Chem. Res. Toxicol. 2, 367-374 (1989).
    • (1989) Chem. Res. Toxicol. , vol.2 , pp. 367-374
    • Hammons, G.J.1    Alworth, W.L.2    Hopkins, N.E.3    Guengerich, F.P.4    Kadlubar, F.F.5
  • 5
    • 0026468125 scopus 로고
    • Modification of cytochrome P450 1A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl
    • C. H. Yun, G. J. Hammons, G. Jones, M. V. Martin, N. E. Hopkins, W. L. Alworth, and F. P. Guengerich: Modification of cytochrome P450 1A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl. Biochemistry 31, 10556-10563 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10556-10563
    • Yun, C.H.1    Hammons, G.J.2    Jones, G.3    Martin, M.V.4    Hopkins, N.E.5    Alworth, W.L.6    Guengerich, F.P.7
  • 6
    • 0031021458 scopus 로고    scopus 로고
    • Aryl acetylenes as mechanism-based inhibitors of cytochrome P450-dependent monooxygenase enzymes
    • M. Foroozesh, G. Primrose, Z. Guo, L. C. Bell, W. L. Alworth, and F. P. Guengerich: Aryl acetylenes as mechanism-based inhibitors of cytochrome P450-dependent monooxygenase enzymes. Chem. Res. Toxicol. 10, 91-102 (1997).
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 91-102
    • Foroozesh, M.1    Primrose, G.2    Guo, Z.3    Bell, L.C.4    Alworth, W.L.5    Guengerich, F.P.6
  • 8
    • 0026726554 scopus 로고
    • Suicide inhibitors of cytochrome P450 1A1 and P450 2B1
    • N. E. Hopkins, M. K. Foroozesh, and W. L. Alworth: Suicide inhibitors of cytochrome P450 1A1 and P450 2B1. Biochem. Pharmacol. 44, 787-796 (1992).
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 787-796
    • Hopkins, N.E.1    Foroozesh, M.K.2    Alworth, W.L.3
  • 10
    • 0019523641 scopus 로고
    • Purification to homogeneity and characterization of a form of cytochrome P450 with high specificity for benzo[a]pyrene from β-naphthoflavone-pretreated rat liver microsomes
    • T. Saito, and H. W. Strobel: Purification to homogeneity and characterization of a form of cytochrome P450 with high specificity for benzo[a]pyrene from β-naphthoflavone-pretreated rat liver microsomes. J. Biol. Chem. 256, 984-988 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 984-988
    • Saito, T.1    Strobel, H.W.2
  • 11
    • 0017795019 scopus 로고
    • Purification and properties of NADPH-cytochrome P-450 reductase
    • H. W. Strobel, and J. D. Dignam: Purification and properties of NADPH-cytochrome P-450 reductase. Methods Enzymol. 52, 89-96 (1978).
    • (1978) Methods Enzymol. , vol.52 , pp. 89-96
    • Strobel, H.W.1    Dignam, J.D.2
  • 12
    • 0017833010 scopus 로고
    • Two forms of liver microsomal cytochrome P450, P450 LM2 and P450 LM4 (rabbit liver)
    • M. J. Coon, T. A. van der Hoeven, S. B. Dahl, and D. A. Haugen: Two forms of liver microsomal cytochrome P450, P450 LM2 and P450 LM4 (rabbit liver). Methods Enzymol. 52, 109-117 (1978).
    • (1978) Methods Enzymol. , vol.52 , pp. 109-117
    • Coon, M.J.1    Van Der Hoeven, T.A.2    Dahl, S.B.3    Haugen, D.A.4
  • 13
    • 0023351645 scopus 로고
    • Purification and characterization of the dog hepatic cytochrome P-450 isozyme responsible for the metabolism of 2,4,5,2′,4′,5′-hexachlorobiphenyl
    • D. B. Duignan, I. G. Sipes, T. B. Leonard, and J. R. Halpert: Purification and characterization of the dog hepatic cytochrome P-450 isozyme responsible for the metabolism of 2,4,5,2′,4′,5′-hexachlorobiphenyl. Arch. Biochem. Biophys. 255, 290-303 (1987).
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 290-303
    • Duignan, D.B.1    Sipes, I.G.2    Leonard, T.B.3    Halpert, J.R.4
  • 15
    • 0027374515 scopus 로고
    • A highly sensitive tool for the assay of cytochrome P450 enzyme activity in rat, dog, and man: Direct fluorescence of the deethylation of 7-ethoxy-4-trifluoromethylcoumarin
    • J. T. M. Buters, C. D. Schiller, and R. C. Chou: A highly sensitive tool for the assay of cytochrome P450 enzyme activity in rat, dog, and man: direct fluorescence of the deethylation of 7-ethoxy-4-trifluoromethylcoumarin. Biochem. Pharmacol. 46, 1577-1584 (1993).
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1577-1584
    • Buters, J.T.M.1    Schiller, C.D.2    Chou, R.C.3
  • 16
    • 0017847465 scopus 로고
    • An improved assay of 7-ethoxycoumarin O-deethylase activity: Induction of hepatic enzyme activity in C57BL/6J and DBA/2J mice by phenobarbital, 3-methylcholanthrene, and 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • W. F. Greenlee, and A. Poland: An improved assay of 7-ethoxycoumarin O-deethylase activity: induction of hepatic enzyme activity in C57BL/6J and DBA/2J mice by phenobarbital, 3-methylcholanthrene, and 2,3,7,8-tetrachlorodibenzo-p-dioxin. J. Pharmacol. Exp. Ther. 205, 596-605 (1978).
    • (1978) J. Pharmacol. Exp. Ther. , vol.205 , pp. 596-605
    • Greenlee, W.F.1    Poland, A.2
  • 17
    • 0021112308 scopus 로고
    • 19 steroids by 5 highly purified and reconstituted rat hepatic cytochrome P-450 isozymes
    • 19 steroids by 5 highly purified and reconstituted rat hepatic cytochrome P-450 isozymes. J. Biol. Chem. 258, 8839-8847 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 8839-8847
    • Wood, A.W.1    Ryan, D.E.2    Thomas, P.E.3    Levin, W.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U. K. Laemmli: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 277, 680-685 (1970).
    • (1970) Nature (Lond.) , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0028085833 scopus 로고
    • Regio- and stereo-selective metabolism of phenanthrene by twelve cDNA-expressed human, rodent, and rabbit cytochromes P-450
    • M. Shou, K. R. Korzekwa, K. W. Krausz, C. L. Crespi, F. J. Gonzalez, and H. V. Gelboin: Regio-and stereo-selective metabolism of phenanthrene by twelve cDNA-expressed human, rodent, and rabbit cytochromes P-450. Cancer Lett. 83, 305-313 (1994).
    • (1994) Cancer Lett. , vol.83 , pp. 305-313
    • Shou, M.1    Korzekwa, K.R.2    Krausz, K.W.3    Crespi, C.L.4    Gonzalez, F.J.5    Gelboin, H.V.6
  • 21
    • 0022419376 scopus 로고
    • Gene structure of a major form of phenobarbital-inducible cytochrome P-450 in rat liver
    • Y. Suwa, Y. Mizukami, K. Sogawa, and Y. Fujii-Kuriyama: Gene structure of a major form of phenobarbital-inducible cytochrome P-450 in rat liver. J. Biol. Chem. 260, 7980-7984 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 7980-7984
    • Suwa, Y.1    Mizukami, Y.2    Sogawa, K.3    Fujii-Kuriyama, Y.4
  • 22
    • 0012538590 scopus 로고
    • Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes
    • G. E. Tarr, S. D. Black, V. S. Fujita, and M. J. Coon: Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes. Proc. Natl. Acad. Sci. USA 80, 6552-6556 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6552-6556
    • Tarr, G.E.1    Black, S.D.2    Fujita, V.S.3    Coon, M.J.4
  • 23
    • 0024464027 scopus 로고
    • cDNA cloning and sequence and cDNA-directed expression of human P450 HB1: Identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver
    • S. Yamano, P. T. Nhamburo, T. Aoyama, U. A. Meyer, T. Inaba, W. Kalow, H. V. Gelboin, O. W. McBride, and F. J. Gonzalez: cDNA cloning and sequence and cDNA-directed expression of human P450 HB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver. Biochemistry 28, 7340-7348 (1989).
    • (1989) Biochemistry , vol.28 , pp. 7340-7348
    • Yamano, S.1    Nhamburo, P.T.2    Aoyama, T.3    Meyer, U.A.4    Inaba, T.5    Kalow, W.6    Gelboin, H.V.7    McBride, O.W.8    Gonzalez, F.J.9
  • 24
    • 0023766113 scopus 로고
    • 16α) of testosterone 16α-hydroxylase in mouse liver, chromosome localization, and cloning of P-450 cDNA
    • 16α) of testosterone 16α-hydroxylase in mouse liver, chromosome localization, and cloning of P-450 cDNA. Biochemistry 27, 6434-6443 (1988).
    • (1988) Biochemistry , vol.27 , pp. 6434-6443
    • Noshiro, M.1    Lakso, M.2    Kawajiri, K.3    Negishi, M.4
  • 25
    • 0025341142 scopus 로고
    • cDNA and deduced amino acid sequences of a dog hepatic cytochrome P450IIB responsible for the metabolism of 2,2′,4,4′,5,5′-hexachlorobiphenyl
    • P. E. Graves, G. A. Elhag, P. J. Ciaccio, D. P. Bourque, and J. R. Halpert: cDNA and deduced amino acid sequences of a dog hepatic cytochrome P450IIB responsible for the metabolism of 2,2′,4,4′,5,5′-hexachlorobiphenyl. Arch. Biochem. Biophys. 281, 106-115 (1990).
    • (1990) Arch. Biochem. Biophys. , vol.281 , pp. 106-115
    • Graves, P.E.1    Elhag, G.A.2    Ciaccio, P.J.3    Bourque, D.P.4    Halpert, J.R.5
  • 26
    • 0026569805 scopus 로고
    • Cytochromes P-450 in rats: Structures, functions, properties and relevant human forms
    • P. Soucek, and I. Gut: Cytochromes P-450 in rats: structures, functions, properties and relevant human forms. Xenobiotica 22, 83-103 (1992).
    • (1992) Xenobiotica , vol.22 , pp. 83-103
    • Soucek, P.1    Gut, I.2
  • 27
    • 0026542174 scopus 로고
    • Topological analysis of the active sites of cytochromes P450IIB4 (rabbit), P450 IIB10 (mouse), and P450 IIB11 (dog) by in situ rearrangement of phenyl-iron complexes
    • B. A. Swanson, J. R. Halpert, L. M. Bornheim, and P. R. Ortiz de Montellano: Topological analysis of the active sites of cytochromes P450IIB4 (rabbit), P450 IIB10 (mouse), and P450 IIB11 (dog) by in situ rearrangement of phenyl-iron complexes. Arch. Biochem. Biophys. 292, 42-46 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 42-46
    • Swanson, B.A.1    Halpert, J.R.2    Bornheim, L.M.3    Ortiz De Montellano, P.R.4
  • 29
    • 0028858960 scopus 로고
    • Cytochrome P450 inhibitors: Evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes
    • D. J. Newton, R. W. Wang, and A. Y. Lu: Cytochrome P450 inhibitors: evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes. Drug Metab. Dispos. 23, 154-158 (1995).
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 154-158
    • Newton, D.J.1    Wang, R.W.2    Lu, A.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.