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Volumn 383, Issue 10, 2002, Pages 1587-1592

Fast regulation of cytochrome P450 activities by phosphorylation and consequences for drug metabolism and toxicity

Author keywords

cAMP; Drug metabolism; P450; Phosphorylation; Regulation

Indexed keywords

2 AMINOANTHRACENE; 2 FLUORENYLAMINE; ADENOSINE TRIPHOSPHATE; AROMATIC AMIDE; AROMATIC AMINE; CARCINOGEN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLOPHOSPHAMIDE; CYTOCHROME P450; CYTOCHROME P450 2B1; CYTOCHROME P450 2B2; CYTOCHROME P450 2E1; FLUORENYLACETOHYDROXAMIC ACID; GLUCAGON; HORMONE; IFOSFAMIDE; ISOENZYME; N (2 FLUORENYL)ACETAMIDE; OKADAIC ACID; OXAZAPHOSPHORINE DERIVATIVE; PHENOBARBITAL; PHOSPHODIESTERASE INHIBITOR; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROMUTAGEN; PROTEIN KINASE INHIBITOR; THEOPHYLLINE; UNINDEXED DRUG; UNSPECIFIC MONOOXYGENASE; VANADIC ACID; DRUG;

EID: 0036805785     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.179     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0024587565 scopus 로고
    • Phosphorylation of carcinogen metabolizing enzymes: Regulation of the phosphorylation status of the major phenobarbital inducible cytochromes P-450 in hepatocytes
    • Bartlomowicz, B., Waxman, D. J., Utesch, D., Oesch, F., and Friedberg, T. (1989a). Phosphorylation of carcinogen metabolizing enzymes: regulation of the phosphorylation status of the major phenobarbital inducible cytochromes P-450 in hepatocytes. Carcinogenesis 10, 225-228.
    • (1989) Carcinogenesis , vol.10 , pp. 225-228
    • Bartlomowicz, B.1    Waxman, D.J.2    Utesch, D.3    Oesch, F.4    Friedberg, T.5
  • 2
    • 0024550971 scopus 로고
    • Regio- and stereoselective regulation of monooxygenase activities by isoenzyme-selective phosphorylation of cytochrome P450
    • Bartlomowicz, B., Friedberg, T., Utesch, D., Molitor, E., Platt, K., and Oesch, F. (1989b). Regio- and stereoselective regulation of monooxygenase activities by isoenzyme-selective phosphorylation of cytochrome P450. Biochem. Biophys. Res. Commun. 160, 46-52.
    • (1989) Biochem. Biophys. Res. Commun , vol.160 , pp. 46-52
    • Bartlomowicz, B.1    Friedberg, T.2    Utesch, D.3    Molitor, E.4    Platt, K.5    Oesch, F.6
  • 3
    • 0032479307 scopus 로고    scopus 로고
    • Identification of the binding site on cytochrome P450 2B4 for cytochromes b5 and cytochrome P450 reductase
    • Bridges, A., Gruenke, L., Chang, Y. T., Vakser, I. A., Loew, G., and Waskell, L. (1998). Identification of the binding site on cytochrome P450 2B4 for cytochromes b5 and cytochrome P450 reductase. J. Biol. Chem. 273, 17036-17049.
    • (1998) J. Biol. Chem , vol.273 , pp. 17036-17049
    • Bridges, A.1    Gruenke, L.2    Chang, Y.T.3    Vakser, I.A.4    Loew, G.5    Waskell, L.6
  • 4
    • 0028936342 scopus 로고
    • Intratumoral activation and enhanced chemotherapeutic effect of oxazaphosphorines following cytochrome P-450 gene transfer: Development of a combined chemotherapy/cancer gene therapy strategy
    • Chen, L., and Waxman, D. J. (1995). Intratumoral activation and enhanced chemotherapeutic effect of oxazaphosphorines following cytochrome P-450 gene transfer: development of a combined chemotherapy/cancer gene therapy strategy. Cancer Res. 55, 581-589.
    • (1995) Cancer Res , vol.55 , pp. 581-589
    • Chen, L.1    Waxman, D.J.2
  • 5
    • 0029897684 scopus 로고    scopus 로고
    • Sensitization of human breast cancer cells to cyclophosphamide and ifosfamide by transfer of a liver cytochrome P450 gene
    • Chen, L., Waxman, D. J., Chen, D., and Kufe, D. W. (1996). Sensitization of human breast cancer cells to cyclophosphamide and ifosfamide by transfer of a liver cytochrome P450 gene. Cancer Res. 56, 1331-1340.
    • (1996) Cancer Res , vol.56 , pp. 1331-1340
    • Chen, L.1    Waxman, D.J.2    Chen, D.3    Kufe, D.W.4
  • 6
    • 0026773423 scopus 로고
    • Hormone- and substrate-regulated intracellular degradation of cytochrome P450 (2E1) involving MgATP-activated rapid proteolysis in the endoplasmic reticulum membranes
    • Eliasson, E., Mkrtchian, S., and Ingelman-Sundberg, M. (1992). Hormone- and substrate-regulated intracellular degradation of cytochrome P450 (2E1) involving MgATP-activated rapid proteolysis in the endoplasmic reticulum membranes. J. Biol. Chem. 267, 15765-15769.
    • (1992) J. Biol. Chem , vol.267 , pp. 15765-15769
    • Eliasson, E.1    Mkrtchian, S.2    Ingelman-Sundberg, M.3
  • 8
    • 0020094054 scopus 로고
    • Regulatory mechanisms in the control of protein kinases
    • Flockhart, D. A., and Corbin, J. D. (1982). Regulatory mechanisms in the control of protein kinases. CRC Crit. Rev. Biochem. 12, 133-186.
    • (1982) CRC Crit. Rev. Biochem , vol.12 , pp. 133-186
    • Flockhart, D.A.1    Corbin, J.D.2
  • 9
    • 0023402354 scopus 로고
    • Search for cell culture systems with diverse xenobiotic-metabolizing activities and their use in toxicological studies
    • Glatt, H. R., Gemperlein, I., Turchi, G., Heinritz, H., Doehmer, J., and Oesch, F. (1987). Search for cell culture systems with diverse xenobiotic-metabolizing activities and their use in toxicological studies. Mol. Toxicol. 1, 313-334.
    • (1987) Mol. Toxicol , vol.1 , pp. 313-334
    • Glatt, H.R.1    Gemperlein, I.2    Turchi, G.3    Heinritz, H.4    Doehmer, J.5    Oesch, F.6
  • 10
    • 0029006401 scopus 로고
    • Escherichia coli expression of site-directed mutants of cytochrome P450 2B1 from six substrate recognition sites: Substrate specificity and inhibitor selectivity studies
    • He, Y. Q., He, Y. A., and Halpert, J. R. (1995). Escherichia coli expression of site-directed mutants of cytochrome P450 2B1 from six substrate recognition sites: substrate specificity and inhibitor selectivity studies. Chem. Res. Toxicol. 8, 574-579.
    • (1995) Chem. Res. Toxicol , vol.8 , pp. 574-579
    • He, Y.Q.1    He, Y.A.2    Halpert, J.R.3
  • 11
    • 0023461586 scopus 로고
    • Inverse relationship between cytochrome P-450 phosphorylation and complexation with cytochrome b5
    • Jansson, I., Epstein, P. M., Bains, S., and Schenkman, J. B. (1987). Inverse relationship between cytochrome P-450 phosphorylation and complexation with cytochrome b5. Arch. Biochem. Biophys. 259, 441-448.
    • (1987) Arch. Biochem. Biophys , vol.259 , pp. 441-448
    • Jansson, I.1    Epstein, P.M.2    Bains, S.3    Schenkman, J.B.4
  • 12
    • 0011225035 scopus 로고
    • Mechanism of ethanol- and acetone-dependent induction of cytochromes P-450
    • Proceedings of 6th International Conference, Vienna, I. Schuster, ed. (London/New York/Philadelphia: Taylor and Francis)
    • Johansson, I., Eliasson, E., Johansson, A., Hagbjörk, A.-L., Lindros, K., and Ingelman-Sundberg, M. (1989). Mechanism of ethanol- and acetone-dependent induction of cytochromes P-450. In: Cytochrome P-450: Biochemistry and Biophysics, Proceedings of 6th International Conference, Vienna, I. Schuster, ed. (London/New York/Philadelphia: Taylor and Francis), pp. 592-595.
    • (1989) Cytochrome P-450: Biochemistry and Biophysics , pp. 592-595
    • Johansson, I.1    Eliasson, E.2    Johansson, A.3    Hagbjörk, A.-L.4    Lindros, K.5    Ingelman-Sundberg, M.6
  • 13
    • 0024507004 scopus 로고
    • Posttranslational modification of hepatic cytochrome P-450. Phosphorylation of phenobarbital-inducible P-450 forms PB-4 (IIB1) and PB-5 (IIB2) in isolated rat hepatocytes and in vivo
    • Koch, J. A., and Waxman, D. J. (1989). Posttranslational modification of hepatic cytochrome P-450. Phosphorylation of phenobarbital-inducible P-450 forms PB-4 (IIB1) and PB-5 (IIB2) in isolated rat hepatocytes and in vivo. Biochemistry 28, 3145-3152.
    • (1989) Biochemistry , vol.28 , pp. 3145-3152
    • Koch, J.A.1    Waxman, D.J.2
  • 14
    • 0018337894 scopus 로고
    • Phosphorylation-dephosphorylation of enzymes
    • Krebs, E. G., and Beavo, J. A. (1979). Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48, 923-959.
    • (1979) Annu. Rev. Biochem , vol.48 , pp. 923-959
    • Krebs, E.G.1    Beavo, J.A.2
  • 15
    • 0030963222 scopus 로고    scopus 로고
    • Molecular modelling of mammalian CYP2B isoforms and their interaction with substrates, inhibitors and redox partners
    • Lewis, D. F., and Lake B. G. (1997). Molecular modelling of mammalian CYP2B isoforms and their interaction with substrates, inhibitors and redox partners. Xenobiotica 5, 443-478.
    • (1997) Xenobiotica , vol.5 , pp. 443-478
    • Lewis, D.F.1    Lake, B.G.2
  • 16
    • 0029993999 scopus 로고    scopus 로고
    • Gene therapy for malignant gliomas using replication incompetent retroviral and adenoviral vectors encoding the cytochrome P450 2B1 gene together with cyclophosphamide
    • Manome, Y., Wen, P. Y., Chen, L., Tanaka, T., Dong, Y., Yamazoe, M., Hirshowitz, A., Kufe, D. W., and Fine, H. A. (1996). Gene therapy for malignant gliomas using replication incompetent retroviral and adenoviral vectors encoding the cytochrome P450 2B1 gene together with cyclophosphamide. Gene Ther. 3, 513-520.
    • (1996) Gene Ther , vol.3 , pp. 513-520
    • Manome, Y.1    Wen, P.Y.2    Chen, L.3    Tanaka, T.4    Dong, Y.5    Yamazoe, M.6    Hirshowitz, A.7    Kufe, D.W.8    Fine, H.A.9
  • 17
    • 0029658746 scopus 로고    scopus 로고
    • Involvement of cytochrome b5 in the metabolism of tetrachlorobiphenyls catalyzed by CYP2B1 and CYP1A1
    • Matsusue, K., Arioshi, N., Oguri, K., Koga, N., and Yoshimura, H. (1996). Involvement of cytochrome b5 in the metabolism of tetrachlorobiphenyls catalyzed by CYP2B1 and CYP1A1. Chemosphere 32, 517-523.
    • (1996) Chemosphere , vol.32 , pp. 517-523
    • Matsusue, K.1    Arioshi, N.2    Oguri, K.3    Koga, N.4    Yoshimura, H.5
  • 18
    • 0028260789 scopus 로고
    • Essential role of His163 of cytochrome P450 1A2 in catalytic functions associated with cytochrome b5
    • Mayuzumi, H., Shimizu, T., Sambongi, C., Hiroya, K., and Hatano, M. (1994). Essential role of His163 of cytochrome P450 1A2 in catalytic functions associated with cytochrome b5. Arch. Biochem. Biophys. 310, 367-372.
    • (1994) Arch. Biochem. Biophys , vol.310 , pp. 367-372
    • Mayuzumi, H.1    Shimizu, T.2    Sambongi, C.3    Hiroya, K.4    Hatano, M.5
  • 19
    • 0022253112 scopus 로고
    • The site of cyclic AMP-dependent protein kinase catalyzed phosphorylation of cytochrome P-450 LM2
    • Müller, R., Schmidt, W. E., and Stier, A. (1985). The site of cyclic AMP-dependent protein kinase catalyzed phosphorylation of cytochrome P-450 LM2. FEBS Lett. 187, 21-24.
    • (1985) FEBS Lett , vol.187 , pp. 21-24
    • Müller, R.1    Schmidt, W.E.2    Stier, A.3
  • 20
    • 0025149212 scopus 로고
    • Modulation of the control of mutagenic metabolites derived from cyclophosphamide and ifosfamide by stimulation of protein kinase A
    • Oesch-Bartlomowicz, B., Vogel, S., Arens, H.-J., and Oesch, F. (1990). Modulation of the control of mutagenic metabolites derived from cyclophosphamide and ifosfamide by stimulation of protein kinase A. Mutat. Res. 232, 305-312.
    • (1990) Mutat. Res , vol.232 , pp. 305-312
    • Oesch-Bartlomowicz, B.1    Vogel, S.2    Arens, H.-J.3    Oesch, F.4
  • 21
    • 0030805966 scopus 로고    scopus 로고
    • Control of the mutagenicity of aromatic amines by protein kinases and phosphatases
    • Oesch-Bartlomowicz, B., Arens, H. J., Richter, B., Hengstler, J. G., and Oesch, F. (1997). Control of the mutagenicity of aromatic amines by protein kinases and phosphatases. Arch. Toxicol. 71, 601-611.
    • (1997) Arch. Toxicol , vol.71 , pp. 601-611
    • Oesch-Bartlomowicz, B.1    Arens, H.J.2    Richter, B.3    Hengstler, J.G.4    Oesch, F.5
  • 23
    • 0035545910 scopus 로고    scopus 로고
    • cAMP-dependent phosphorylation of CYP2B1 as a functional switch for cyclophosphamide activation and its hormonal control in vitro and in vivo
    • Oesch-Bartlomowicz, B., Richter, B., Becker, R., Vogel, S., Padma, P. R., Hengstler, J. G., and Oesch, F. (2001). cAMP-dependent phosphorylation of CYP2B1 as a functional switch for cyclophosphamide activation and its hormonal control in vitro and in vivo. Int. J. Cancer 94, 733-742.
    • (2001) Int. J. Cancer , vol.94 , pp. 733-742
    • Oesch-Bartlomowicz, B.1    Richter, B.2    Becker, R.3    Vogel, S.4    Padma, P.R.5    Hengstler, J.G.6    Oesch, F.7
  • 24
    • 0028024546 scopus 로고
    • Interaction between cytochrome P450 2B1 and cytochrome b5: Inhibition by synthetic peptides indicates a role for P450 residues Lys-122 and Arg-125
    • Omata, Y., Sakamoto, H., Robinson, R. C., Pincus, M. R., and Friedman, F. K. (1994). Interaction between cytochrome P450 2B1 and cytochrome b5: inhibition by synthetic peptides indicates a role for P450 residues Lys-122 and Arg-125. Biochem. Biophys. Res. Commun. 201, 1090-1095.
    • (1994) Biochem. Biophys. Res. Commun , vol.201 , pp. 1090-1095
    • Omata, Y.1    Sakamoto, H.2    Robinson, R.C.3    Pincus, M.R.4    Friedman, F.K.5
  • 25
    • 0030611724 scopus 로고    scopus 로고
    • Control of the mutagenicity of arylamines by protein kinases and phosphatases. II. Lack of response of rat liver N-acetyl transferases to phosphorylation modulators
    • Padma, P. R., Oesch-Bartlomowicz, B., Hengstler, J. G., and Oesch, F. (1997). Control of the mutagenicity of arylamines by protein kinases and phosphatases. II. Lack of response of rat liver N-acetyl transferases to phosphorylation modulators. Arch. Toxicol. 71, 655-659.
    • (1997) Arch. Toxicol , vol.71 , pp. 655-659
    • Padma, P.R.1    Oesch-Bartlomowicz, B.2    Hengstler, J.G.3    Oesch, F.4
  • 26
    • 0024401458 scopus 로고
    • Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450
    • Pyerin W., and Taniguchi, H. (1989). Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450. EMBO J. 8, 3003-3010.
    • (1989) EMBO J , vol.8 , pp. 3003-3010
    • Pyerin, W.1    Taniguchi, H.2
  • 27
    • 0020640860 scopus 로고
    • Phosphorylation of cytochrome-P-450-dependent monooxygenase components
    • Pyerin, W., Wolf, C. R., Kinzel, V., Kübler, D., and Oesch, F. (1983). Phosphorylation of cytochrome-P-450-dependent monooxygenase components. Carcinogenesis 4, 573-576.
    • (1983) Carcinogenesis , vol.4 , pp. 573-576
    • Pyerin, W.1    Wolf, C.R.2    Kinzel, V.3    Kübler, D.4    Oesch, F.5
  • 29
    • 0027524747 scopus 로고
    • Benzene metabolism by reconstituted cytochromes P450 2B1 and 2E1 and its modulation by cytochrome b5, microsomal epoxide hydrolase and glutathione transferases: Evidence for an important role of microsomal epoxide hydrolase in the formation of hydroquinone
    • Snyder, R., Chepiga, T., Yang, C. S., Thomas, H., Platt, K., and Oesch, F. (1993). Benzene metabolism by reconstituted cytochromes P450 2B1 and 2E1 and its modulation by cytochrome b5, microsomal epoxide hydrolase and glutathione transferases: evidence for an important role of microsomal epoxide hydrolase in the formation of hydroquinone. Toxicol. Appl. Pharmacol. 122, 172-81.
    • (1993) Toxicol. Appl. Pharmacol , vol.122 , pp. 172-181
    • Snyder, R.1    Chepiga, T.2    Yang, C.S.3    Thomas, H.4    Platt, K.5    Oesch, F.6
  • 30
    • 0028118315 scopus 로고
    • Application of 3-dimensional homology modeling of cytochrome P450 2B1 for interpretation of site-directed mutagenesis results
    • Szklarz, G. D., Ornstein, R. L., and Halpert, J. R. (1994). Application of 3-dimensional homology modeling of cytochrome P450 2B1 for interpretation of site-directed mutagenesis results. J. Biomol. Struct. Dyn. 12, 61-78.
    • (1994) J. Biomol. Struct. Dyn , vol.12 , pp. 61-78
    • Szklarz, G.D.1    Ornstein, R.L.2    Halpert, J.R.3
  • 31
    • 0021919348 scopus 로고
    • Conversion of hepatic microsomal cytochrome P-450 to P-420 upon phosphorylation by cyclic AMP-dependent protein kinase
    • Taniguchi, H., Pyerin, W., and Stier, A. (1985). Conversion of hepatic microsomal cytochrome P-450 to P-420 upon phosphorylation by cyclic AMP-dependent protein kinase. Biochem. Pharmacol. 34, 1835-1837.
    • (1985) Biochem. Pharmacol , vol.34 , pp. 1835-1837
    • Taniguchi, H.1    Pyerin, W.2    Stier, A.3
  • 32
    • 0028832191 scopus 로고
    • Diffusible cytotoxic metabolites contribute to the in vitro bystander effect associated with the cyclophosphamide/cytochrome P4502B1 cancer gene therapy paradigm
    • Wei, M. X., Tamiya, T., Rhee, R. J., Breakefield, X. O., and Chiocca, E. A. (1995). Diffusible cytotoxic metabolites contribute to the in vitro bystander effect associated with the cyclophosphamide/cytochrome P4502B1 cancer gene therapy paradigm. Clin. Cancer Res. 1, 1171-1177.
    • (1995) Clin. Cancer Res , vol.1 , pp. 1171-1177
    • Wei M., X.1    Tamiya, T.2    Rhee, R.J.3    Breakefield, X.O.4    Chiocca, E.A.5
  • 33
    • 0029671251 scopus 로고    scopus 로고
    • Roles of cytochrome b5 in the oxidation of testosterone and nifedipine by recombinant cytochrome P450 3A4 and by human liver microsomes
    • Yamazaki, H., Nakano, M., Imai, Y., Ueng, Y. F., Guengerich, F. P., and Shimada, T. (1996a). Roles of cytochrome b5 in the oxidation of testosterone and nifedipine by recombinant cytochrome P450 3A4 and by human liver microsomes. Arch. Biochem. Biophys. 325, 174-182.
    • (1996) Arch. Biochem. Biophys , vol.325 , pp. 174-182
    • Yamazaki, H.1    Nakano, M.2    Imai, Y.3    Ueng, Y.F.4    Guengerich, F.P.5    Shimada, T.6
  • 34
    • 0030602654 scopus 로고    scopus 로고
    • Requirements for cytochrome b5 in the oxidation of 7-ethoxycoumarin, chlorzoxazone, aniline and N-nitrosodimethylamine by recombinant cytochrome P450 2E1 and by human liver microsomes
    • Yamazaki, H., Nakano, M. Gillam, E. M., Bell, L. C., Guengerich, F. P., and Shimada, T. (1996b). Requirements for cytochrome b5 in the oxidation of 7-ethoxycoumarin, chlorzoxazone, aniline and N-nitrosodimethylamine by recombinant cytochrome P450 2E1 and by human liver microsomes. Biochem. Pharmacol. 52, 301-309.
    • (1996) Biochem. Pharmacol , vol.52 , pp. 301-309
    • Yamazaki, H.1    Nakano, M.2    Gillam, E.M.3    Bell, L.C.4    Guengerich, F.P.5    Shimada, T.6
  • 35
    • 0032529219 scopus 로고    scopus 로고
    • Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid
    • Yun, C. H., Ahn, T., and Guengerich, F. P. (1998). Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid. Arch. Biochem. Biophys. 356, 229-238.
    • (1998) Arch. Biochem. Biophys , vol.356 , pp. 229-238
    • Yun, C.H.1    Ahn, T.2    Guengerich, F.P.3


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