메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 311-317

Molecular mechanisms of AhR functions in the regulation of cytochrome P450 genes

(2)  Fujii Kuriyama, Y a   Mimura, J a  

a NONE

Author keywords

Aryl hydrocarbon receptor; Coactivator; Cytochrome P450; Gene regulation; Transcription factor

Indexed keywords

2 (1' H INDOLE 3' CARBONYL)THIAZOLE 4 CARBOXYLIC ACID METHYL ESTER; 2,3,7,8 TETRACHLORODIBENZO PARA DIOXIN; 2,3,7,8 TETRACHLORODIBENZOFURAN; 3 METHYLCHOLANTHRENE; 6 FORMYLINDOLO[3,2 B]CARBAZOLE; AROMATIC HYDROCARBON RECEPTOR; BILIRUBIN; BILIVERDIN; CARBAZOLE DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; CIS ACTING ELEMENT; CYTOCHROME P450; INDOLEACETIC ACID; LIPOXIN A; TRANS ACTING FACTOR; TRYPTAMINE; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 27544434863     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.162     Document Type: Review
Times cited : (243)

References (53)
  • 1
    • 27544493437 scopus 로고    scopus 로고
    • D.R. Nelson, http://drnelson.utmem.edu/CytochromeP450.html.
    • Nelson, D.R.1
  • 2
    • 9044254525 scopus 로고    scopus 로고
    • P450 superfamily: Update on new sequences, gene mapping, accession numbers and nomenclature
    • D.R. Nelson P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature Pharmacogenetics 6 1996 1 42
    • (1996) Pharmacogenetics , vol.6 , pp. 1-42
    • Nelson, D.R.1
  • 3
    • 0034655747 scopus 로고    scopus 로고
    • Regulation of cytochrome P450 (CYP) by nuclear receptors
    • P. Honkakoski, and M. Negishi Regulation of cytochrome P450 (CYP) by nuclear receptors Biochem. J. 347 2000 321 337
    • (2000) Biochem. J. , vol.347 , pp. 321-337
    • Honkakoski, P.1    Negishi, M.2
  • 4
    • 0033199499 scopus 로고    scopus 로고
    • P450 gene induction by structurally diverse xenochemicals: Contral role of nuclear receptors CAR, PXR and PPAR
    • D.J. Waxman P450 gene induction by structurally diverse xenochemicals: contral role of nuclear receptors CAR, PXR and PPAR Arch. Biochem. Biophys. 369 1999 11 23
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 11-23
    • Waxman, D.J.1
  • 5
  • 6
    • 0037450429 scopus 로고    scopus 로고
    • Functional role of AhR in the expression of toxic effects by TCDD
    • J. Mimura, and Y. Fujii-Kuriyama Functional role of AhR in the expression of toxic effects by TCDD Biochim. Biophys. Acta 1619 2003 263 268
    • (2003) Biochim. Biophys. Acta , vol.1619 , pp. 263-268
    • Mimura, J.1    Fujii-Kuriyama, Y.2
  • 7
    • 0037225752 scopus 로고    scopus 로고
    • Study of P450 function using gene knockout and transgenic mice
    • F.J. Gonzalez, and S. Kimura Study of P450 function using gene knockout and transgenic mice Arch. Biochem. Biophys. 409 2003 153 158
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 153-158
    • Gonzalez, F.J.1    Kimura, S.2
  • 8
    • 9944247695 scopus 로고    scopus 로고
    • Coordinate transcriptional regulation of bile acid homeostasis and drug metabolism
    • J.J. Floranta, and G.A. Kullak-Ublick Coordinate transcriptional regulation of bile acid homeostasis and drug metabolism Arch. Biochem. Biophys. 433 2005 397 412
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 397-412
    • Floranta, J.J.1    Kullak-Ublick, G.A.2
  • 9
    • 9944255780 scopus 로고    scopus 로고
    • Role of coactivators in transcriptional activation of the aryl hydrocarbon receptor
    • O. Hankinson Role of coactivators in transcriptional activation of the aryl hydrocarbon receptor Arch. Biochem. Biophys. 433 2005 379 386
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 379-386
    • Hankinson, O.1
  • 10
    • 0036799870 scopus 로고    scopus 로고
    • The nuclear pregnane X receptor: A key regulator of xenobiotic metabolism
    • S.A. Kliewer, B. Goodwin, and T.M. Willson The nuclear pregnane X receptor: a key regulator of xenobiotic metabolism Endocr. Rev. 23 2002 687 702
    • (2002) Endocr. Rev. , vol.23 , pp. 687-702
    • Kliewer, S.A.1    Goodwin, B.2    Willson, T.M.3
  • 11
    • 3042726385 scopus 로고    scopus 로고
    • CAR, driving into the future
    • K. Swales, and M. Negishi CAR, driving into the future Mol. Endocr. 18 2004 1589 1598
    • (2004) Mol. Endocr. , vol.18 , pp. 1589-1598
    • Swales, K.1    Negishi, M.2
  • 12
    • 0032707445 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome P-450 induction by xenobiotics: An expanded role for nulear hormone receptors
    • Ü. Savas, K.J. Griffin, and E.F. Johnson Molecular mechanisms of cytochrome P-450 induction by xenobiotics: an expanded role for nulear hormone receptors Mol. Pharmachol. 56 1999 851 857
    • (1999) Mol. Pharmachol. , vol.56 , pp. 851-857
    • Savas, Ü.1    Griffin, K.J.2    Johnson, E.F.3
  • 13
    • 0030582844 scopus 로고    scopus 로고
    • Analysis of structural requirements for Ah receptor antagonist activity: Ellipticines, flavones and related compounds
    • T.A. Gasiewicz, A.S. Kende, G. Rucci, B. Whitney, and J.J. Willey Analysis of structural requirements for Ah receptor antagonist activity: ellipticines, flavones and related compounds Biochem. Pharmacol. 52 1996 1787 1803
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 1787-1803
    • Gasiewicz, T.A.1    Kende, A.S.2    Rucci, G.3    Whitney, B.4    Willey, J.J.5
  • 15
    • 0037145023 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptors: Diversity and evolution
    • M.E. Hahn Aryl hydrocarbon receptors: diversity and evolution Chem. Biol. Interact. 141 2002 131 160
    • (2002) Chem. Biol. Interact. , vol.141 , pp. 131-160
    • Hahn, M.E.1
  • 17
  • 18
    • 0033535843 scopus 로고    scopus 로고
    • Lipoxin A4: A new class of ligand for the Ah receptor
    • C.M. Schaldach, J. Riby, and L.F. Bjeldanes Lipoxin A4: a new class of ligand for the Ah receptor Biochemistry 38 1999 7594 7600
    • (1999) Biochemistry , vol.38 , pp. 7594-7600
    • Schaldach, C.M.1    Riby, J.2    Bjeldanes, L.F.3
  • 19
    • 0031895561 scopus 로고    scopus 로고
    • Rapid and transient induction of CYP1A1 gene expression in human cells by the tryptophan photoproduct 6-formyl indolo[3,2-b]carbazole
    • Y.D. Wei, H. Helleberg, U. Rannug, and A. Rannug Rapid and transient induction of CYP1A1 gene expression in human cells by the tryptophan photoproduct 6-formyl indolo[3,2-b]carbazole Chem. Biol. Interact. 110 1998 39 55
    • (1998) Chem. Biol. Interact. , vol.110 , pp. 39-55
    • Wei, Y.D.1    Helleberg, H.2    Rannug, U.3    Rannug, A.4
  • 20
    • 0028116593 scopus 로고
    • Suspension-mediated induction of Hepa 1c1c7 CYP1a-1 expression dependent on the Ah receptor signal transduction palthway
    • C.M. Sadek, and B.L. Allen-Hoffmann Suspension-mediated induction of Hepa 1c1c7 CYP1a-1 expression dependent on the Ah receptor signal transduction palthway J. Biol. Chem. 269 1994 31505 31509
    • (1994) J. Biol. Chem. , vol.269 , pp. 31505-31509
    • Sadek, C.M.1    Allen-Hoffmann, B.L.2
  • 21
    • 0028178381 scopus 로고
    • Cytochrome P450 1A1 is rapidly induced in normal humen keratinocytes in the absence of xenobiotics
    • C.M. Sadek, and B.L. Allen-Hoffmann Cytochrome P450 1A1 is rapidly induced in normal humen keratinocytes in the absence of xenobiotics J. Biol. Chem. 269 1994 16067 16074
    • (1994) J. Biol. Chem. , vol.269 , pp. 16067-16074
    • Sadek, C.M.1    Allen-Hoffmann, B.L.2
  • 22
    • 4444358405 scopus 로고    scopus 로고
    • Disruption of cell-cell contact maximally but transiently activates AhR-mediated transcription in 10T1/2 fibroblasts
    • Y.C. Cho, W. Zheng, and C.R. Jefcoate Disruption of cell-cell contact maximally but transiently activates AhR-mediated transcription in 10T1/2 fibroblasts Toxicol. Appl. Pharmacol. 199 2004 220 238
    • (2004) Toxicol. Appl. Pharmacol. , vol.199 , pp. 220-238
    • Cho, Y.C.1    Zheng, W.2    Jefcoate, C.R.3
  • 23
    • 1842418966 scopus 로고    scopus 로고
    • Cell density regulates intracellar localization of aryl hydrocarbon receptor
    • T. Ikuta, Y. Kobayashi, and K. Kawajiri Cell density regulates intracellar localization of aryl hydrocarbon receptor J. Biol. Chem. 279 2004 19209 19216
    • (2004) J. Biol. Chem. , vol.279 , pp. 19209-19216
    • Ikuta, T.1    Kobayashi, Y.2    Kawajiri, K.3
  • 24
    • 0037145022 scopus 로고    scopus 로고
    • Role of the aryl hydrocarbon receptor in cell cycle regulation
    • A. Puga, Y. Xia, and C. Elferink Role of the aryl hydrocarbon receptor in cell cycle regulation Chem. Biol. Interact. 141 2002 117 130
    • (2002) Chem. Biol. Interact. , vol.141 , pp. 117-130
    • Puga, A.1    Xia, Y.2    Elferink, C.3
  • 26
    • 4644356710 scopus 로고    scopus 로고
    • Regulation of aryl hydrocarbon receptor signal transduction by protein tyrosine kinases
    • M. Backlund, and M. Ingelman-Sundberg Regulation of aryl hydrocarbon receptor signal transduction by protein tyrosine kinases Cell. Signal. 17 2005 39 48
    • (2005) Cell. Signal. , vol.17 , pp. 39-48
    • Backlund, M.1    Ingelman-Sundberg, M.2
  • 27
    • 0023665615 scopus 로고
    • Characterization of xenobiotic responsive elements upstreams from the drug-metabolizing cytochrome P450C: A similarity to glucocarticoid regulatory elements
    • A. Fujisawa-Sehara, K. Sogawa, M. Yamane, and Y. Fujii-Kuriyama Characterization of xenobiotic responsive elements upstreams from the drug-metabolizing cytochrome P450C: a similarity to glucocarticoid regulatory elements Nucleic Acids. Res. 15 1987 4179 4191
    • (1987) Nucleic Acids. Res. , vol.15 , pp. 4179-4191
    • Fujisawa-Sehara, A.1    Sogawa, K.2    Yamane, M.3    Fujii-Kuriyama, Y.4
  • 28
    • 0026644794 scopus 로고
    • Protein-DNA interactions at a dioxin-responsive enhancer. Mutational analysis of the DNA-binding site for the liganded Ah receptor
    • E.S. Shen, and J.P. Whitlock Jr. Protein-DNA interactions at a dioxin-responsive enhancer. Mutational analysis of the DNA-binding site for the liganded Ah receptor J. Biol. Chem. 267 1992 6815 6819
    • (1992) J. Biol. Chem. , vol.267 , pp. 6815-6819
    • Shen, E.S.1    Whitlock Jr., J.P.2
  • 29
    • 0032570685 scopus 로고    scopus 로고
    • Characterization of the mouse CYP1B1 gene Identification of an enhancer region that directs aryl hydrocarbon receptor-mediated constitutive and induced expression
    • L. Zhang, U. Sawas, D.L. Alexander, and C.R. Jefcoate Characterization of the mouse CYP1B1 gene Identification of an enhancer region that directs aryl hydrocarbon receptor-mediated constitutive and induced expression J. Biol. Chem. 273 1998 5174 5183
    • (1998) J. Biol. Chem. , vol.273 , pp. 5174-5183
    • Zhang, L.1    Sawas, U.2    Alexander, D.L.3    Jefcoate, C.R.4
  • 30
    • 0032980422 scopus 로고    scopus 로고
    • A novel positive regulatory element that enhances hamster CYP2A8 gene expression mediated by xenobiotic responsive element
    • K. Kurose, M. Tohkin, and M. Fukuhara A novel positive regulatory element that enhances hamster CYP2A8 gene expression mediated by xenobiotic responsive element Mol. Pharmacol. 55 1999 279 287
    • (1999) Mol. Pharmacol. , vol.55 , pp. 279-287
    • Kurose, K.1    Tohkin, M.2    Fukuhara, M.3
  • 32
    • 0035136070 scopus 로고    scopus 로고
    • Organization of the CYP1A cluster on human chromosome 15: Implication for gene regulation
    • J. Corchero, S. Pimprole, S. Kimura, and F.J. Gonzalez Organization of the CYP1A cluster on human chromosome 15: implication for gene regulation Pharmacogenetics 11 2001 1 6
    • (2001) Pharmacogenetics , vol.11 , pp. 1-6
    • Corchero, J.1    Pimprole, S.2    Kimura, S.3    Gonzalez, F.J.4
  • 36
    • 0037637542 scopus 로고    scopus 로고
    • The basic helix-loop-helix-PAS protein ARNT functions as a potent coactivator of estrogen receptor-dependent transcription
    • S. Brunnberg, K. Pettersson, E. Rydin, J. Matthews, A. Hanberg, and I. Pongratz The basic helix-loop-helix-PAS protein ARNT functions as a potent coactivator of estrogen receptor-dependent transcription Proc. Natl. Acad. Sci. USA 100 2003 6517 6522
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6517-6522
    • Brunnberg, S.1    Pettersson, K.2    Rydin, E.3    Matthews, J.4    Hanberg, A.5    Pongratz, I.6
  • 37
    • 13444283747 scopus 로고    scopus 로고
    • Transcription factor NF2d9 (LBP-1a) interacts with the positive regulatory element for the xenobiotic responsive element
    • K. Kurose, M. Tohkin, and R. Hasegawa Transcription factor NF2d9 (LBP-1a) interacts with the positive regulatory element for the xenobiotic responsive element Biochim. Biophys. Acta 1727 2005 141 144
    • (2005) Biochim. Biophys. Acta , vol.1727 , pp. 141-144
    • Kurose, K.1    Tohkin, M.2    Hasegawa, R.3
  • 38
    • 15844389899 scopus 로고    scopus 로고
    • Cooperative interaction between AhR.Arnt and Sp1 for drug-inducible expression of CYP1A1 gene
    • A. Kobayashi, K. Sogawa, and Y. Fujii-Kuriyama Cooperative interaction between AhR.Arnt and Sp1 for drug-inducible expression of CYP1A1 gene J. Biol. Chem. 271 1996 12310 123106
    • (1996) J. Biol. Chem. , vol.271 , pp. 12310-123106
    • Kobayashi, A.1    Sogawa, K.2    Fujii-Kuriyama, Y.3
  • 39
    • 0017145975 scopus 로고
    • Stereospecific, high affinity binding of 2,3,7,8-tetrachlorodibenzo-p- dioxin by hepatic cytosol. Evidence that the binding species is receptor for induction of aryl hydrocarbon hydroxylase
    • A. Poland, E. Glober, and A.S. Kende Stereospecific, high affinity binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin by hepatic cytosol. Evidence that the binding species is receptor for induction of aryl hydrocarbon hydroxylase J. Biol. Chem. 251 1976 4936 4946
    • (1976) J. Biol. Chem. , vol.251 , pp. 4936-4946
    • Poland, A.1    Glober, E.2    Kende, A.S.3
  • 40
    • 2442745398 scopus 로고
    • A DNA-binding factor specific for xenobiotic responsive elements of P-450c gene exists as a cryptic form in cytoplasm: Its possible translocation to nucleus
    • A. Fujisawa-Sehara, M. Yamane, and Y. Fujii-Kuriyama A DNA-binding factor specific for xenobiotic responsive elements of P-450c gene exists as a cryptic form in cytoplasm: its possible translocation to nucleus Proc. Natl. Acad. Sci. USA 85 1988 7486 7490
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7486-7490
    • Fujisawa-Sehara, A.1    Yamane, M.2    Fujii-Kuriyama, Y.3
  • 42
    • 0026725943 scopus 로고
    • Cloning of Ah-receptor cDNA reveals a distinctive ligand-activated transcription factor
    • K.M. Burbach, A. Poland, and C.A. Bradfield Cloning of Ah-receptor cDNA reveals a distinctive ligand-activated transcription factor Proc. Natl. Acad. Sci. USA 89 1992 8185 8189
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8185-8189
    • Burbach, K.M.1    Poland, A.2    Bradfield, C.A.3
  • 43
    • 0030667728 scopus 로고    scopus 로고
    • CBP/p300 function as possible transcriptional coactivator of Ah receptor nuclear translocator (Arnt)
    • A. Kobayashi, K Numayama-Tsuruta, K. Sogawa, and Y. Fujii-Kuriyama CBP/p300 function as possible transcriptional coactivator of Ah receptor nuclear translocator (Arnt) J. Biochem. 122 1997 703 710
    • (1997) J. Biochem. , vol.122 , pp. 703-710
    • Kobayashi, A.1    Numayama-Tsuruta, K.2    Sogawa, K.3    Fujii-Kuriyama, Y.4
  • 44
    • 0033324251 scopus 로고    scopus 로고
    • Nuclear receptor coactivator SRC-1 interacts with the Q-rich subdomain of the AhR and modulates its transactivation potential
    • M.B. Kumar, and G.H. Perdew Nuclear receptor coactivator SRC-1 interacts with the Q-rich subdomain of the AhR and modulates its transactivation potential Gene Expr. 8 1999 273 286
    • (1999) Gene Expr. , vol.8 , pp. 273-286
    • Kumar, M.B.1    Perdew, G.H.2
  • 46
    • 0026457834 scopus 로고
    • Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin
    • J.E. Morgan, and J.P. Whitlock Jr. Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin Proc. Natl. Acad. Sci. USA 89 1992 11622 11626
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11622-11626
    • Morgan, J.E.1    Whitlock Jr., J.P.2
  • 47
    • 0037023766 scopus 로고    scopus 로고
    • Functional involvement of the Brahma/SWI2-related gene 1 protein in cytochrome P4501A1 transcription mediated by the aryl hydrocarbon receptor complex
    • S. Wang, and O. Hankinson Functional involvement of the Brahma/SWI2-related gene 1 protein in cytochrome P4501A1 transcription mediated by the aryl hydrocarbon receptor complex J. Biol. Chem. 277 2002 11821 11827
    • (2002) J. Biol. Chem. , vol.277 , pp. 11821-11827
    • Wang, S.1    Hankinson, O.2
  • 48
    • 1842640322 scopus 로고    scopus 로고
    • Role of mediator in transcriptional activation by the aryl hydrocarbon receptor
    • S. Wang, K. Ge, R.G. Roeder, and O. Hankinson Role of mediator in transcriptional activation by the aryl hydrocarbon receptor J. Biol. Chem. 279 2004 13593 13600
    • (2004) J. Biol. Chem. , vol.279 , pp. 13593-13600
    • Wang, S.1    Ge, K.2    Roeder, R.G.3    Hankinson, O.4
  • 49
    • 0037145007 scopus 로고    scopus 로고
    • The mechanism of AH receptor protein down-regulation (degradation) and its impact on AH receptor-mediated gene regulation
    • R.S. Pollenz The mechanism of AH receptor protein down-regulation (degradation) and its impact on AH receptor-mediated gene regulation Chem. Biol. Interact. 141 2002 41 61
    • (2002) Chem. Biol. Interact. , vol.141 , pp. 41-61
    • Pollenz, R.S.1
  • 50
    • 0033214443 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor imported into the nucleus following ligand binding is rapidly degraded via the cytoplasmic proteasome following nuclear export
    • N.A. Davarinos, and R.S. Pollenz Aryl hydrocarbon receptor imported into the nucleus following ligand binding is rapidly degraded via the cytoplasmic proteasome following nuclear export J. Biol. Chem. 274 1999 28708 28715
    • (1999) J. Biol. Chem. , vol.274 , pp. 28708-28715
    • Davarinos, N.A.1    Pollenz, R.S.2
  • 51
    • 0033579570 scopus 로고    scopus 로고
    • Degradation of the basic helix-loop-helix/Per-ARNT-Sim homology domain dioxin receptor via the ubiquitin/proteasome pathway
    • B.J. Roberts, and M.L. Whitelaw Degradation of the basic helix-loop-helix/Per-ARNT-Sim homology domain dioxin receptor via the ubiquitin/proteasome pathway J. Biol. Chem. 274 1999 36351 36356
    • (1999) J. Biol. Chem. , vol.274 , pp. 36351-36356
    • Roberts, B.J.1    Whitelaw, M.L.2
  • 52
    • 0141704410 scopus 로고    scopus 로고
    • Defining the role for XAP2 in stabilization of the dioxin receptor
    • M.J. Lees, D.J. Peet, and M.L. Whitelaw Defining the role for XAP2 in stabilization of the dioxin receptor J. Biol. Chem. 278 2003 35878 35888
    • (2003) J. Biol. Chem. , vol.278 , pp. 35878-35888
    • Lees, M.J.1    Peet, D.J.2    Whitelaw, M.L.3
  • 53
    • 0032899367 scopus 로고    scopus 로고
    • Identification of a novel mechanism of regulation of Ah (dioxin) receptor function
    • J. Mimura, M. Ema, K. Sogawa, and Y. Fujii-Kuriyama Identification of a novel mechanism of regulation of Ah (dioxin) receptor function Genes Dev. 13 1999 20 25
    • (1999) Genes Dev. , vol.13 , pp. 20-25
    • Mimura, J.1    Ema, M.2    Sogawa, K.3    Fujii-Kuriyama, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.