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Volumn 24, Issue 7-8, 1998, Pages 1324-1330

Production of reactive oxygen species by microsomes enriched in specific human cytochrome P450 enzymes

Author keywords

CYP1A1; CYP1A2; CYP2B6; CYP3A4; Free radical; Human cytochrome P450s; Iron reduction; Reactive oxygen species; Superoxide anion

Indexed keywords

CYTOCHROME; CYTOCHROME P450; CYTOCHROME P450 1A1; CYTOCHROME P450 1A2; CYTOCHROME P450 2B6; CYTOCHROME P450 3 A 4; HEMOPROTEIN; LIVER ENZYME; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 0032077936     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00463-2     Document Type: Article
Times cited : (239)

References (42)
  • 2
    • 0026536546 scopus 로고
    • Cytochrome P450: Advances and prospects
    • Guengerich F. P. Cytochrome P450 Advances and prospects . FASEB J. 6:1992;667-668.
    • (1992) FASEB J. , vol.6 , pp. 667-668
    • Guengerich, F.P.1
  • 4
    • 0025784027 scopus 로고
    • Cytochrome P450: Multiplicity of isoforms, substrates and catalytic and regulatory mechanisms
    • Porter T. D., Coon M. J. Cytochrome P450 Multiplicity of isoforms, substrates and catalytic and regulatory mechanisms . J. Biol. Chem. 266:1991;13469-13472.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13469-13472
    • Porter, T.D.1    Coon, M.J.2
  • 5
    • 0025992864 scopus 로고
    • Oxidation of toxic and carcinogenic chemicals by human cytochrome P450 enzymes
    • Guengerich F. P., Shimada T. Oxidation of toxic and carcinogenic chemicals by human cytochrome P450 enzymes. Chem. Res. Toxicol. 4:1991;391-407.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 391-407
    • Guengerich, F.P.1    Shimada, T.2
  • 6
    • 0026651273 scopus 로고
    • Human cytochromes P450: Problems and prospects
    • Gonzalez F. Human cytochromes P450 Problems and prospects . TIPS Rev. 13:1992;346-352.
    • (1992) TIPS Rev. , vol.13 , pp. 346-352
    • Gonzalez, F.1
  • 7
    • 0025368387 scopus 로고
    • Five of 12 forms of vaccinia-expressed human hepatic cytochrome P450 metabolically activate aflatoxin B1
    • Aoyama T., Yamano S., Guzelian P. S., Gelboin H. V., Gonzalez F. J. Five of 12 forms of vaccinia-expressed human hepatic cytochrome P450 metabolically activate aflatoxin B1. Proc. Natl. Acad. Sci. USA. 87:1990;4790-4793.
    • (1990) Proc. Natl. Acad. Sci. USA. , vol.87 , pp. 4790-4793
    • Aoyama, T.1    Yamano, S.2    Guzelian, P.S.3    Gelboin, H.V.4    Gonzalez, F.J.5
  • 8
    • 0027369366 scopus 로고
    • Differential activation of cyclophosphamide and ifosphamide by cytochromes P-450 2B and 3A in human liver microsomes
    • Chang T. K. M., Weber G. F., Crespi C. L., Waxman D. J. Differential activation of cyclophosphamide and ifosphamide by cytochromes P-450 2B and 3A in human liver microsomes. Cancer Res. 53:1993;5629-5637.
    • (1993) Cancer Res. , vol.53 , pp. 5629-5637
    • Chang, T.K.M.1    Weber, G.F.2    Crespi, C.L.3    Waxman, D.J.4
  • 9
    • 0030239348 scopus 로고    scopus 로고
    • Catalytic activities and structure/function relationships of cytochrome P450 enzymes
    • Halkier B. A. Catalytic activities and structure/function relationships of cytochrome P450 enzymes. Phytochemistry. 43:1996;1-21.
    • (1996) Phytochemistry , vol.43 , pp. 1-21
    • Halkier, B.A.1
  • 10
    • 0018817225 scopus 로고
    • Oxygen activation by cytochrome P450
    • White R. E., Coon M. J. Oxygen activation by cytochrome P450. Ann. Rev. Biochem. 49:1980;315-356.
    • (1980) Ann. Rev. Biochem. , vol.49 , pp. 315-356
    • White, R.E.1    Coon, M.J.2
  • 11
    • 0028106174 scopus 로고
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains
    • Smith G. C. M., Tew D. G., Wolf C. R. Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. Proc. Natl. Acad. Sci. USA. 91:1994;8710-8714.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8710-8714
    • Smith, G.C.M.1    Tew, D.G.2    Wolf, C.R.3
  • 14
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillian E. M. J., Baba T., Kim B. R., Ohmori S., Guengerich F. P. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 305:1993;123-131.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillian, E.M.J.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 15
    • 0028057499 scopus 로고
    • Generation of reactive oxygen intermediates by human liver microsomes in the presence of NADPH or NADH
    • Rashba-Step J., Cederbaum A. I. Generation of reactive oxygen intermediates by human liver microsomes in the presence of NADPH or NADH. Molec. Pharmacol. 45:1994;150-157.
    • (1994) Molec. Pharmacol. , vol.45 , pp. 150-157
    • Rashba-Step, J.1    Cederbaum, A.I.2
  • 16
    • 0024546914 scopus 로고
    • Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P450
    • Ekstrom G., Ingelman-Sundberg M. Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P450. Biochem. Pharmacol. 38:1989;1313-1319.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 1313-1319
    • Ekstrom, G.1    Ingelman-Sundberg, M.2
  • 18
    • 0021138883 scopus 로고
    • On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P450
    • Gorsky L. D., Koop D. R., Coon M. J. On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P450. J. Biol. Chem. 259:1984;6812-6817.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6812-6817
    • Gorsky, L.D.1    Koop, D.R.2    Coon, M.J.3
  • 22
    • 0024464027 scopus 로고
    • CDNA cloning and sequence and cDNA-directed expression of human P450 II B1: Identification of a normal and two variant cDNAs derived from CYP 2B locus on chromosome 19 and differential expression of the II B mRNAs in human liver
    • Yamano S., Nhamburo P. T., Aoyama T., Meyer U. A., Inaba T., Kalow W., Gelboin H. V., McBride O. W., Gonzalez F. J. cDNA cloning and sequence and cDNA-directed expression of human P450 II B1: identification of a normal and two variant cDNAs derived from CYP 2B locus on chromosome 19 and differential expression of the II B mRNAs in human liver. Biochemistry. 28:1989;7340-7348.
    • (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
  • 23
    • 0023858226 scopus 로고
    • Human P450 PCN1. Sequence, chromosome localization and direct evidence through cDNA expression that P450 PCN1 is nifedipine oxidase
    • Gonzalez F. J., Schmid B. J., Umeno M., McBride O. W., Hardwick J. P., Meyer U. R. S. A., Gelboin H. V., Idle J. R. Human P450 PCN1. Sequence, chromosome localization and direct evidence through cDNA expression that P450 PCN1 is nifedipine oxidase. DNA. 7:1988;79-86.
    • (1988) DNA , vol.7 , pp. 79-86
    • Gonzalez, F.J.1    Schmid, B.J.2    Umeno, M.3    McBride, O.W.4    Hardwick, J.P.5    Meyer, U.R.S.A.6    Gelboin, H.V.7    Idle, J.R.8
  • 24
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. J. Biol. Chem. 239:1964;2379-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 25
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization and kinetic studies
    • Phillips A. H., Langdon R. G. Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization and kinetic studies. J. Biol. Chem. 237:1962;2652-2660.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 26
    • 0025087596 scopus 로고
    • Sensitive and rapid quantitation of oxygen reactive species in rat synaptosomes
    • Lebel C., Bondy S. C. Sensitive and rapid quantitation of oxygen reactive species in rat synaptosomes. Neurochem. Int. 17:1990;435-440.
    • (1990) Neurochem. Int. , vol.17 , pp. 435-440
    • Lebel, C.1    Bondy, S.C.2
  • 27
    • 0031128377 scopus 로고    scopus 로고
    • Inhibition of ferritin-stimulated microsomal production of reactive oxygen intermediates by nitric oxide
    • Puntarulo S., Cederbaum A. I. Inhibition of ferritin-stimulated microsomal production of reactive oxygen intermediates by nitric oxide. Arch. Biochem. Biophys. 340:1997;19-26.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 19-26
    • Puntarulo, S.1    Cederbaum, A.I.2
  • 28
    • 0023682012 scopus 로고
    • Comparison of the ability of ferric complexes to catalyze microsomal chemiluminescence, lipid peroxidation and hydroxyl radical generation
    • Puntarulo S., Cederbaum A. I. Comparison of the ability of ferric complexes to catalyze microsomal chemiluminescence, lipid peroxidation and hydroxyl radical generation. Arch. Biochem. Biophys. 264:1988;482-491.
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 482-491
    • Puntarulo, S.1    Cederbaum, A.I.2
  • 29
    • 0020188453 scopus 로고
    • Oxidase and oxygenase function of the microsomal cytochrome P-450 monooxygenase system
    • Kuthan H., Ullrich V. Oxidase and oxygenase function of the microsomal cytochrome P-450 monooxygenase system. Eur. J. Biochem. 126:1982;583-588.
    • (1982) Eur. J. Biochem. , vol.126 , pp. 583-588
    • Kuthan, H.1    Ullrich, V.2
  • 30
    • 0001067564 scopus 로고
    • Low level chemiluminescence in biological systems
    • Pryor W.A. San Diego: Academic Press
    • Cadenas E., Boveris A., Chance B. Low level chemiluminescence in biological systems. Pryor W. A. Free Radicals in Biology. Vol. 6:1984;211-247 Academic Press, San Diego.
    • (1984) Free Radicals in Biology , vol.6 , pp. 211-247
    • Cadenas, E.1    Boveris, A.2    Chance, B.3
  • 32
    • 0026710009 scopus 로고
    • The role of iron in oxygen-mediated toxicities
    • Ryan T. P., Aust S. D. The role of iron in oxygen-mediated toxicities. Crit. Rev. Toxicol. 32:1992;119-141.
    • (1992) Crit. Rev. Toxicol. , vol.32 , pp. 119-141
    • Ryan, T.P.1    Aust, S.D.2
  • 33
  • 35
    • 0027375275 scopus 로고
    • Molecular recognition in cytochrome P-450. Mechanism for the control of uncoupling reactions
    • Loida P. J., Sligar S. G. Molecular recognition in cytochrome P-450. Mechanism for the control of uncoupling reactions. Biochemistry. 32:1993;11530-11538.
    • (1993) Biochemistry , vol.32 , pp. 11530-11538
    • Loida, P.J.1    Sligar, S.G.2
  • 36
    • 0029962091 scopus 로고    scopus 로고
    • 1-Hydroxyethyl radical formation during NADPH- and NADH-dependent oxidation of ethanol by human liver microsomes
    • Rao D. N. R., Yang M.-X., Lasker J. M., Cederbaum A. I. 1-Hydroxyethyl radical formation during NADPH- and NADH-dependent oxidation of ethanol by human liver microsomes. Molec. Pharmacol. 49:1996;814-821.
    • (1996) Molec. Pharmacol. , vol.49 , pp. 814-821
    • Rao, D.N.R.1    Yang, M.-X.2    Lasker, J.M.3    Cederbaum, A.I.4
  • 37
    • 0028948688 scopus 로고
    • 5 on the stoichiometry of P4502E1-catalyzed reactions
    • 5 on the stoichiometry of P4502E1-catalyzed reactions . Arch. Biochem. Biophys. 317:1995;504-513.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 504-513
    • Patten, C.J.1    Koch, P.2
  • 39
    • 0025757011 scopus 로고
    • Comparison of levels of several human microsomal cytochrome P450 enzymes and epoxide hydrolase in normal and disease state using immunochemical analysis of surgical liver samples
    • Guengerich F. P., Turvy C. G. Comparison of levels of several human microsomal cytochrome P450 enzymes and epoxide hydrolase in normal and disease state using immunochemical analysis of surgical liver samples. J. Pharmacol. Exp. Ther. 256:1991;1189-1194.
    • (1991) J. Pharmacol. Exp. Ther. , vol.256 , pp. 1189-1194
    • Guengerich, F.P.1    Turvy, C.G.2
  • 40
    • 0028237729 scopus 로고
    • Inter-individual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens, and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians
    • Shimada T., Yamazaki H., Minura M., Inui Y., Guengerich F. P. Inter-individual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens, and toxic chemicals studies with liver microsomes of 30 Japanese and 30 Caucasians . J. Pharmacol. Exp. Ther. 270:1994;414-423.
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Minura, M.3    Inui, Y.4    Guengerich, F.P.5
  • 42
    • 0027077438 scopus 로고
    • Characterization of human lung microsomal cytochrome P-4501A1 and its role in the oxidation of chemical carcinogens
    • Shimada T., Yun C. H., Yamazaki H., Gautier J. C., Beaune P. H., Guengerich F. P. Characterization of human lung microsomal cytochrome P-4501A1 and its role in the oxidation of chemical carcinogens. Molec. Pharmacol. 41:1992;856-864.
    • (1992) Molec. Pharmacol. , vol.41 , pp. 856-864
    • Shimada, T.1    Yun, C.H.2    Yamazaki, H.3    Gautier, J.C.4    Beaune, P.H.5    Guengerich, F.P.6


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