메뉴 건너뛰기




Volumn 10, Issue 8, 1996, Pages 809-818

Induction of cytochrome P4501A1: A model for analyzing mammalian gene transcription

Author keywords

Ah receptor; basic helix loop helix proteins; chromatin structure; dioxin; protein DNA interactions

Indexed keywords

AROMATIC HYDROCARBON; CYTOCHROME P450; TRANSCRIPTION FACTOR;

EID: 0030163010     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.8.8666157     Document Type: Review
Times cited : (226)

References (44)
  • 1
    • 0020431144 scopus 로고
    • Induction of microsomal enzymes by foreign compounds and carcinogenesis by polycyclic aromatic hydrocarbons
    • Conney, A. H. (1982) Induction of microsomal enzymes by foreign compounds and carcinogenesis by polycyclic aromatic hydrocarbons. Cancer Res. 42, 4875-4917
    • (1982) Cancer Res. , vol.42 , pp. 4875-4917
    • Conney, A.H.1
  • 2
    • 0016228330 scopus 로고
    • Arene oxides: A new aspect of drug metabolism
    • Jerina, D. M., and Daly, J. W. (1974) Arene oxides: A new aspect of drug metabolism. Science 185, 573-582
    • (1974) Science , vol.185 , pp. 573-582
    • Jerina, D.M.1    Daly, J.W.2
  • 3
    • 0019074870 scopus 로고
    • Benzo(a)pyrene metabolism, activation, and carcinogenesis: Role and regulation of mixed-function oxidases and related enzymes
    • Gelboin, H. V. (1980) Benzo(a)pyrene metabolism, activation, and carcinogenesis: Role and regulation of mixed-function oxidases and related enzymes. Physiol. Rev. 60, 1107-1166
    • (1980) Physiol. Rev. , vol.60 , pp. 1107-1166
    • Gelboin, H.V.1
  • 4
    • 0025055648 scopus 로고
    • Enzyme induction in the cytochrome P450 system
    • Okey, A. B. (1990) Enzyme induction in the cytochrome P450 system. Pharmacol. Ther. 45, 241-298
    • (1990) Pharmacol. Ther. , vol.45 , pp. 241-298
    • Okey, A.B.1
  • 5
    • 0020010617 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin and related aromatic hydrocarbons: Examination of the mechanism of toxicity
    • Poland, A., and Knudson, J. C. (1982) 2,3,7,8-Tetrachlorodibenzo-p-dioxin and related aromatic hydrocarbons: examination of the mechanism of toxicity. Annu. Rev. Pharmacol. Toxicol. 22, 517-554
    • (1982) Annu. Rev. Pharmacol. Toxicol. , vol.22 , pp. 517-554
    • Poland, A.1    Knudson, J.C.2
  • 6
    • 0028303135 scopus 로고
    • Molecular biology of the aromatic hydrocarbon (dioxin) receptor
    • Okey, A. B., Riddick, D. S., and Harper, P. A. (1994) Molecular biology of the aromatic hydrocarbon (dioxin) receptor. Trends Pharrnacol. Sci. 15, 226-232
    • (1994) Trends Pharrnacol. Sci. , vol.15 , pp. 226-232
    • Okey, A.B.1    Riddick, D.S.2    Harper, P.A.3
  • 7
    • 0027458138 scopus 로고
    • The AH-receptor: Genetics, structure and function
    • Swanson, H. I., and Bradfield, C. A. (1993) The AH-receptor: genetics, structure and function. Pharmacogenetics 3, 213-230
    • (1993) Pharmacogenetics , vol.3 , pp. 213-230
    • Swanson, H.I.1    Bradfield, C.A.2
  • 8
    • 0028987872 scopus 로고
    • The aryl hydrocarbon receptor complex
    • Hankinson, O. (1995) The aryl hydrocarbon receptor complex. Annu. Rev. Pharmacol. Toxicol. 35, 307-340
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 307-340
    • Hankinson, O.1
  • 9
    • 0022555425 scopus 로고
    • Comparative toxicology and mechanism of action of polychlorinated dibenzo-p-dioxins and dibenzofurans
    • Safe, S. H. (1986) Comparative toxicology and mechanism of action of polychlorinated dibenzo-p-dioxins and dibenzofurans. Annu. Rev. Pharmacol. Toxicol. 26, 371-399
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 371-399
    • Safe, S.H.1
  • 10
    • 0028174982 scopus 로고
    • Carcinogenicity of TCDD: Experimental, mechanistic, and epidemiological evidence
    • Huff, J., Lucier, G., and Tritsher, A. (1994) Carcinogenicity of TCDD: experimental, mechanistic, and epidemiological evidence. Annu. Rev. Pharmacol. Toxicol. 34, 343-372
    • (1994) Annu. Rev. Pharmacol. Toxicol. , vol.34 , pp. 343-372
    • Huff, J.1    Lucier, G.2    Tritsher, A.3
  • 11
    • 0025333289 scopus 로고
    • Evolution of the P450 gene superfamily
    • Gonzalez, F. J., and Nebert, D. W. (1990) Evolution of the P450 gene superfamily. Trends Genet. 6, 182-186
    • (1990) Trends Genet. , vol.6 , pp. 182-186
    • Gonzalez, F.J.1    Nebert, D.W.2
  • 14
    • 0027521742 scopus 로고
    • Mechanistic aspects of dioxin action
    • Whitlock, J. P., Jr. (1993) Mechanistic aspects of dioxin action. Chem. Res. Toxicol. 6, 754-763
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 754-763
    • Whitlock Jr., J.P.1
  • 15
    • 0026644794 scopus 로고
    • Protein-DNA interactions at a dioxin-responsive enhancer: Mutational analysis of the DNA-binding site for the liganded Ah receptor
    • Shen, E. S., and Whitlock, J. P., Jr. (1992) Protein-DNA interactions at a dioxin-responsive enhancer: mutational analysis of the DNA-binding site for the liganded Ah receptor. J. Biol. Chem. 267, 6815-6819
    • (1992) J. Biol. Chem. , vol.267 , pp. 6815-6819
    • Shen, E.S.1    Whitlock Jr., J.P.2
  • 16
    • 0027208834 scopus 로고
    • Consequences of heteromeric interactions among helix-loop-helix proteins
    • Kadesch, T. (1993) Consequences of heteromeric interactions among helix-loop-helix proteins. Cell Growth Differ. 4, 49-55
    • (1993) Cell Growth Differ. , vol.4 , pp. 49-55
    • Kadesch, T.1
  • 17
    • 0025051172 scopus 로고
    • Functional analysis of the transcriptional promoter for the CYP1A1 gene
    • Jones, K. W., and Whitlock, J. P., Jr. (1990) Functional analysis of the transcriptional promoter for the CYP1A1 gene. Mol. Cell. Biol. 10, 5098-5105
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5098-5105
    • Jones, K.W.1    Whitlock Jr., J.P.2
  • 18
    • 0028207310 scopus 로고
    • The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa lclc7 cells by immunfluorescence microscopy
    • Pollenz, R. S., Sattler, C. A., Poland, A. (1993) The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa lclc7 cells by immunfluorescence microscopy. Mol. Pharmacol. 45, 428-438
    • (1993) Mol. Pharmacol. , vol.45 , pp. 428-438
    • Pollenz, R.S.1    Sattler, C.A.2    Poland, A.3
  • 19
    • 0026631538 scopus 로고
    • Dual roles of the 90 kDA heat shock protein hsp90 in modulating functional activities of the dioxin receptor
    • Pongratz, I., Mason, G. G. F., and Poellinger, L. (1992) Dual roles of the 90 kDA heat shock protein hsp90 in modulating functional activities of the dioxin receptor. J. Biol. Chem. 267, 13728-13734
    • (1992) J. Biol. Chem. , vol.267 , pp. 13728-13734
    • Pongratz, I.1    Mason, G.G.F.2    Poellinger, L.3
  • 20
    • 0028077887 scopus 로고
    • The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system
    • Carver, L.A., Jackiw, V., and Bradfield, C. A. (1994) The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system. J. Biol. Chem. 269, 30109-30112
    • (1994) J. Biol. Chem. , vol.269 , pp. 30109-30112
    • Carver, L.A.1    Jackiw, V.2    Bradfield, C.A.3
  • 22
    • 0027304728 scopus 로고
    • Transformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90kDa heat-shock protein and increased affinity for 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Henry, E. C., and Gasciewicz, T. A. (1993) Transformation of the aryl hydrocarbon receptor to a DNA-binding form is accompanied by release of the 90kDa heat-shock protein and increased affinity for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Biochem. J. 294, 95-101
    • (1993) Biochem. J. , vol.294 , pp. 95-101
    • Henry, E.C.1    Gasciewicz, T.A.2
  • 23
    • 0028296576 scopus 로고
    • A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor
    • McGuire, J., Whitelaw, M. L., Pongratz, I., Gustafsson, J.-A., and Poellinger, L. (1994) A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor. Mol. Cell. Biol. 14, 2438-2446
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2438-2446
    • McGuire, J.1    Whitelaw, M.L.2    Pongratz, I.3    Gustafsson, J.-A.4    Poellinger, L.5
  • 24
    • 0026625037 scopus 로고
    • Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor
    • Reyes, H., Reisz-Porszasz, S., and Hankinson, O. (1992) Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 256, 1193-1195
    • (1992) Science , vol.256 , pp. 1193-1195
    • Reyes, H.1    Reisz-Porszasz, S.2    Hankinson, O.3
  • 25
    • 0027442864 scopus 로고
    • A factor binding to the xenobiotic responsive element (XRE) of P-450IA1 gene consists of at least two helix-loop-helix proteins, Ah receptor and Arnt
    • Matsushita, N., Sogawa, K., Ema, M., Yoshida, A., and Fujii-Kuriyama, Y. (1993) A factor binding to the xenobiotic responsive element (XRE) of P-450IA1 gene consists of at least two helix-loop-helix proteins, Ah receptor and Arnt. J. Biol. Chem. 268, 21002-21006.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21002-21006
    • Matsushita, N.1    Sogawa, K.2    Ema, M.3    Yoshida, A.4    Fujii-Kuriyama, Y.5
  • 26
    • 0027323931 scopus 로고
    • Role of the aryl hydrocarbon receptor nuclear translocator protein in aryl hydrocarbon (dioxin) receptor action
    • Probst, M. R., Reisz-Porszasz, S., Agbunag, V., Ong, M. S., and Hankinson, O. (1993) Role of the aryl hydrocarbon receptor nuclear translocator protein in aryl hydrocarbon (dioxin) receptor action. Mol. Pharmacol. 44, 511-518
    • (1993) Mol. Pharmacol. , vol.44 , pp. 511-518
    • Probst, M.R.1    Reisz-Porszasz, S.2    Agbunag, V.3    Ong, M.S.4    Hankinson, O.5
  • 27
    • 0027403810 scopus 로고
    • Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor
    • Whitelaw, M., Pongratz, I., Wilhelmsson, A., Gustafsson, J.-Å., and Poellinger, L. (1993) Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. Mol. Cell. Biol. 13, 2504-2514
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2504-2514
    • Whitelaw, M.1    Pongratz, I.2    Wilhelmsson, A.3    Gustafsson, J.-Å.4    Poellinger, L.5
  • 28
    • 0027169125 scopus 로고
    • In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition
    • Dolwick, K. M., Swanson, H. I., and Bradfield, C. A. (1993) In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition. Proc. Natl. Acad. Sci. USA 90, 8566-8570
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8566-8570
    • Dolwick, K.M.1    Swanson, H.I.2    Bradfield, C.A.3
  • 29
    • 0028908504 scopus 로고
    • Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence
    • Bacsi, S. C., Reisz-Porszasz, S., and Hankinson, O. (1995) Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence. Mol Pharmacol. 47, 432-438
    • (1995) Mol Pharmacol. , vol.47 , pp. 432-438
    • Bacsi, S.C.1    Reisz-Porszasz, S.2    Hankinson, O.3
  • 30
    • 0029017976 scopus 로고
    • Protein-protein interaction via PAS domains: Role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex
    • Lindebro, M. C., Poellinger, L., and Whitelaw, M. L. (1995) Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. EMBO J. 14, 3528-3539
    • (1995) EMBO J. , vol.14 , pp. 3528-3539
    • Lindebro, M.C.1    Poellinger, L.2    Whitelaw, M.L.3
  • 31
    • 0028079988 scopus 로고
    • Potent transactivation domains of the Ah receptor and the Ah receptor nuclear translocator map to their carboxyl termini
    • Jain, S., Dolwick, K. M., Schmidt, J. V., and Bradfield, C. A. (1994) Potent transactivation domains of the Ah receptor and the Ah receptor nuclear translocator map to their carboxyl termini. J. Biol. Chem. 269, 31518-31524
    • (1994) J. Biol. Chem. , vol.269 , pp. 31518-31524
    • Jain, S.1    Dolwick, K.M.2    Schmidt, J.V.3    Bradfield, C.A.4
  • 32
    • 0028113007 scopus 로고
    • Transcriptional activation function of the mouse Ah receptor nuclear translocator
    • Li, H., Dong, L., and Whitlock, J. P., Jr. (1994) Transcriptional activation function of the mouse Ah receptor nuclear translocator. J. Biol. Chem. 269, 28098-28105
    • (1994) J. Biol. Chem. , vol.269 , pp. 28098-28105
    • Li, H.1    Dong, L.2    Whitlock Jr., J.P.3
  • 33
    • 0028144972 scopus 로고
    • Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)
    • Reisz-Porszasz, S., Probst, M. R., Fukunaga, B. N., and Hankinson, O. (1994) Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT). Mol. Cell. Biol 14, 6075-6086
    • (1994) Mol. Cell. Biol , vol.14 , pp. 6075-6086
    • Reisz-Porszasz, S.1    Probst, M.R.2    Fukunaga, B.N.3    Hankinson, O.4
  • 34
    • 0027942089 scopus 로고
    • Identification of transactivation and repressive functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: Inducible versus constitutive modes of regulation
    • Whitelaw, M., Gustafsson, J.-Å., and Poellinger, L. (1994) Identification of transactivation and repressive functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation. Mol. Cell. Biol. 14, 8343-8355
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8343-8355
    • Whitelaw, M.1    Gustafsson, J.-Å.2    Poellinger, L.3
  • 35
    • 0029019489 scopus 로고
    • Transcriptional activation by the mouse Ah receptor, Interplay between multiple stimulatory and inhibitory functions
    • Ma, Q., Dong, L., and Whitlock, J. P., Jr. (1995) Transcriptional activation by the mouse Ah receptor, Interplay between multiple stimulatory and inhibitory functions. J. Biol. Chem. 270, 12697-12703
    • (1995) J. Biol. Chem. , vol.270 , pp. 12697-12703
    • Ma, Q.1    Dong, L.2    Whitlock Jr., J.P.3
  • 36
    • 0027473240 scopus 로고
    • Cross-coupling of signal transduction pathways: The dioxin receptor mediates induction of cytochrome P4501A1 expression via a protein kinase C mechanism
    • Berghard, A., Gradin, K., Pongratz, I., Whitelaw, M., and Poellinger, L. (1993) Cross-coupling of signal transduction pathways: the dioxin receptor mediates induction of cytochrome P4501A1 expression via a protein kinase C mechanism. Mol. Cell. Biol. 13, 677-689
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 677-689
    • Berghard, A.1    Gradin, K.2    Pongratz, I.3    Whitelaw, M.4    Poellinger, L.5
  • 37
    • 0028239906 scopus 로고
    • Role of chromatin structure in the regulation of transcription by RNA polymerase II
    • Paranjape, S. M., Kamakaka, R. T., and Kadonaga, J. T. (1994) Role of chromatin structure in the regulation of transcription by RNA polymerase II. Annu. Rev. Biochem. 63, 265-297
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 265-297
    • Paranjape, S.M.1    Kamakaka, R.T.2    Kadonaga, J.T.3
  • 38
    • 0026457834 scopus 로고
    • Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin
    • Morgan, J. E., and Whitlock, J. P., Jr. (1992) Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin. Proc. Natl. Acad. Sci. USA 89, 11622-11626
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11622-11626
    • Morgan, J.E.1    Whitlock Jr., J.P.2
  • 39
    • 0026653368 scopus 로고
    • Mechanism of dioxin action: Ah receptor-mediated increase in promoter accessibility in vivo
    • Wu, L., and Whitlock, J. P., Jr. (1992) Mechanism of dioxin action: Ah receptor-mediated increase in promoter accessibility in vivo. Proc. Natl. Acad. Sci. USA 89, 4811-4815
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4811-4815
    • Wu, L.1    Whitlock Jr., J.P.2
  • 40
    • 0027255780 scopus 로고
    • Mechanism of dioxin action: Receptor-enhancer interactions in intact cells
    • Wu, L., and Whitlock, J. P., Jr. (1993) Mechanism of dioxin action: receptor-enhancer interactions in intact cells. Nucleic Acids Res. 21, 119-125
    • (1993) Nucleic Acids Res. , vol.21 , pp. 119-125
    • Wu, L.1    Whitlock Jr., J.P.2
  • 41
    • 0029034448 scopus 로고
    • Dioxin induces localized, graded changes in chromatin structure: Implications for CYP1A1 gene transcription
    • Okino, S. T., and Whitlock, J. P., Jr. (1995) Dioxin induces localized, graded changes in chromatin structure: implications for CYP1A1 gene transcription. Mol. Cell. Biol. 15, 3714-3721
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3714-3721
    • Okino, S.T.1    Whitlock Jr., J.P.2
  • 42
    • 0029655655 scopus 로고    scopus 로고
    • Dioxin-induced CYP1A1 transcription in vivo: Ah receptor mediates transactivation, enhancer-promoter communication, and changes in chromatin structure
    • Ko, H. P., Okino, S. T., Ma, Q., and Whitlock, J. P., Jr. (1996) Dioxin-induced CYP1A1 transcription in vivo: Ah receptor mediates transactivation, enhancer-promoter communication, and changes in chromatin structure. Mol. Cell. Biol. 16, 430-436
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 430-436
    • Ko, H.P.1    Okino, S.T.2    Ma, Q.3    Whitlock Jr., J.P.4
  • 44
    • 0026376260 scopus 로고
    • Proposed role of drug-metabolizing enzymes: Regulation of steady-state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions
    • Nebert, D. W. (1991) Proposed role of drug-metabolizing enzymes: regulation of steady-state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions. Mol Endocrinol. 5, 1203-1214
    • (1991) Mol Endocrinol. , vol.5 , pp. 1203-1214
    • Nebert, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.