Aryl Hydrocarbon Receptor-Mediated Signal Transduction

References

• Hutzinger O., Blumich M. J., Berg M. V. D., Olie K. Sources of fate of PCDDs and PCDFs: an overview. Chemosphere 1985; 14: 581
   Web of Science ®Google Scholar
• Vanden Heuvel J. P., Lucier G. Environmental toxicology of polychlorinated dibenzo-p-dioxins and polyehlorinated dibenzofurans. Environ. Health Perspect. 1983; 100: 189
   Google Scholar
• Safe S. Polychlorinated biphenyls (PCBs) and poly-brominated biphenyls (PBBs): biochemistry, toxicology and mechanism of action. CRC Crir. Rev. Toxicol. 1984; 13: 319
   Google Scholar
• Skene S. A., Dewhurst I. C., Greenber M. Polychlorinated dibenzo-p-dioxins and polychlorinated dibenzofurans: the risk to human health. A review. Human Toxicol. 1989; 8: 173
   PubMedGoogle Scholar
• Rappe C., Andersson R., Bergqvist P. A., Brobede C., Hansson M., Kjeller L. O., Lindstrom G., Marklund S., Nygren M., Swanson S. E., Tysklind M., Wiber K. Overview on environmental fate of chlorinated dioxins and dibenzofurans. Sources. levels and isometric patterns in various matrices. Chemosphere 1987; 16: 1603
   Web of Science ®Google Scholar
• Safe S., Hutzinger O. PCDDs and PCDFs: sources and environmental impact. Polychlorinated Dibenzo-p-dioxins and -furans (PCDDs/PCDFs): Sources and Environmental Impact. Epidemiology, Mechanisms of Action. Health Risks. Springer-Verlag, Heidelberg 1990; 1
   Google Scholar
• Cook P. M., W., K. D., Walker M. K., Peterson R. E. Bioacumulation and toxicity of TCDD and related compounds in aquatic ecosystems. Banbury Report 35: Biological Basis for Risk Assessment of Dioxins and Related Compounds, M. A. Gallo, R. J. Scheuplein, K. A. Van Der Heijden. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 1991; 143
   Google Scholar
• Poland A., Knutson J. C. 2,3.7,8-Tetrachloro-dibenzo-p-dioxin and related halogenated aromatic hydrocarbons: examination of the mechanism of toxicity. Annit. Rev. Pharmacol. Toxicol. 1982; 22: 517
   PubMed Web of Science ®Google Scholar
• Safe S. H. Comparative toxicology and mechanism of action of polychlorinated dibenzo-p-dioxins and dibenzofurans. Anna. Rev. Pharmacol. Toxicol. 1986; 26: 371
   PubMed Web of Science ®Google Scholar
• Goldstein J. A., Safe S. Mechanism of action and structure-activity relationships for the chlorinated dibenzo-p-dioxins and related compounds. Halo-gented Biphenyls. Naphthalenes. Dibenzodioxins and Related Compounds, R. D. Kimbrough, A. A. Jensen. Elsevier-North Holland, Amsterdam 1989
   Google Scholar
• Poellinger L., Göttlicher M., Gustafsson J. Å. The dioxin and peroxisome proliferator-acti-vated receptors: nuclear receptors in search of endogenous ligands. TiPS. 1992; 13: 241
   PubMed Web of Science ®Google Scholar
• Whitlock J. P. The regulation of cytochrome P-450 gene expression. Annu. Rev. Pharmacol. Toxicol. 1986; 26: 333
   PubMed Web of Science ®Google Scholar
• Whitlock J. P. The regulation of gene expression by 2.3.7.8-tetrachlorodibenzo-p-dioxin. Pharmacol. Rev. 1987; 39: 147
   PubMed Web of Science ®Google Scholar
• Burbach K. M., Poland A., Bradfield C. A. Cloning of the Ah receptor cDNA reveals a distinctive ligand-acti vated transcription factor. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 8185
   PubMed Web of Science ®Google Scholar
• Carver L. A., Hogenesch J. B., Bradfield C. A. Tissue specific expression of the rat Ah-recep-tor and ARNT mRNAs. Nucleic Acids Res. 1994; 22: 3038
   PubMed Web of Science ®Google Scholar
• Dolwick K. M., Schmidt J. V., Carver L. A., Swanson H. I., Bradfield C. A. Cloning and expression of a human Ah receptor cDNA. Mol. Pharmacol 1993; 44: 911
   PubMed Web of Science ®Google Scholar
• Cuthill S., Wilhelmsson A., Poellinger L. Role of the ligand in intracellular receptor function: receptor affinity determines activationin vitro of the latent dioxin receptor to a DNA-binding form. Mol. Cell Biol. 1991; 11: 401
   PubMedGoogle Scholar
• Poland A., Glover E., Bradfield C. Characterization of polyclonal antibodies to the Ah receptor prepared by immunization with a synthetic peptide hapten. Mol. Pharmacol 1991; 39: 20
   PubMed Web of Science ®Google Scholar
• Ema M., Sogawa K., Watanabe Y., Chujoh Y., Matsushita N., Gotoh O., Funae Y., Fujii-Kuriyama Y. cDNA cloning and structure of mouse putative Ah receptor. Biochem. Biophys. Res. Commun. 1992; 184: 246
   PubMed Web of Science ®Google Scholar
• Nebert D. W., Goujon F. ML, Gielen J. E. Aryl hydrocarbon hydroxylase induction by polycy-clic hydrocarbons is a simple autosomal dominant trait in the mouse. Nature New Biol 1972; 236: 107
   PubMedGoogle Scholar
• Thomas P. E., Kouri R. E., Hutton J. J. The genetics of aryi hydrocarbon hydroxylase induction in mice: a single gene difference between C57BL/6J and DBA/2J. Biochem. Genet. 1972; 6: 157
   PubMed Web of Science ®Google Scholar
• Nebert D. W., Gelboin H. V. The in vivo and in vitro induction of aryl hydrocarbon hydroxylase in mammalian cells of different species, tissues, strains, and developmental and hormonal states. Arch, of Biochem. Biophys. 1969; 134: 76
   PubMed Web of Science ®Google Scholar
• Green M. C. Nomenclature of genetically determined biochemical variants in mice. Biochem. Genet. 1973; 9: 369
   Google Scholar
• Poland A., Glover E. Chlorinated dibenzo-p-dioxins: potent inducers of d-aminolevulinic acid synthetase and aryl hydrocarbon hydroxylase. II. A study of the structure activity relationship. Mol. Pharmacol. 1973; 9: 737
   Web of Science ®Google Scholar
• Poland A., Greenlee W. F., Kende A. S. Studies on the mechanism of action of the chlorinated dibenzo-p-dioxins and related compounds. Ann. N. Y. Acad. Sci. 1979; 30: 214
   Google Scholar
• Poland A., Glover E., Kende A. S. Stereo specific, high-affinity binding of 2,3,7,8-tetrachlorodi-benzo-p-dioxin by hepatic cytosol. J. Biol. Chem. 1976; 251: 4936
   PubMed Web of Science ®Google Scholar
• Landers J. P., Bunce N. J. The Ah receptor and the mechanism of dioxin toxicity. Biochem. J. 1991; 276: 273
   PubMed Web of Science ®Google Scholar
• Safe S., Astroff B., Harris M., Zacharewski T., Dickerson R., Romkes M., Biegel L. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) and related compounds as antiestrogens: characterization and mechanism of action. Pharmacol. Toxicol 1991; 69: 400
   PubMedGoogle Scholar
• Rowlands C., Krishnan V., Wang X., Santostefano M., Safe S., Miller W. R., Langdon S. Characterization of the aryl hydrocarbon receptor and aryl hydrocarbon responsiveness in human ovarian carcinoma cell lines. Cancer Res. 1993; 53: 1802
   Google Scholar
• Ema M., Matsushita N., Sogawa K., Ariyama T., Inazawa J., Nemoto T., Ota M., Oshimura M., Fujii-Kuriyama Y. Human aryl hydrocarbon receptor: function expression and chromosomal assignment to 7p21. J. Biochem. 1994; 116: 845
   PubMed Web of Science ®Google Scholar
• Poland A., Glover E. Genetic expression of aryl hydrocarbon hydroxylase by 2,3,7,8-tetrachloro-dibenzo-p-dioxin: evidence for a receptor mutation in genetically non-responsive mice. Mol. Pharmacol. 1975; 11: 389
   Web of Science ®Google Scholar
• Nebert D. W. The Ah locus: genetic differences in toxicity, cancer, mutation, and birth defects. CRC Crit. Rev. Toxicol 1989; 20: 153
   Google Scholar
• Poellinger L., Lund J., Gillner M., Gustafsson J. Å. The receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin: similarities and dissimilarities with steroid hormone receptors. Molecular Mechanisms of Steroid Hormone Action, V. K. Moudgil. Walter de Gruyter & Co., Berlin 1985
   Google Scholar
• Wang G. L., Jiang B. H., Rue E. A., Semenza G. L. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-pas heterodimer regulated by cellular O2 tension. Proc. Natl. Acad. Sci. U.S.A. 1995; 92: 5510
   PubMed Web of Science ®Google Scholar
• Reyes H., Reiz-Porszasz S., Hankinson O. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 1992; 256: 1193
   PubMed Web of Science ®Google Scholar
• Huang Z. J., Edery J. I., Robash M. PAS is a dimerization domain common toDrosophila Period and several transcription factors. Nature 1993; 364: 259
   PubMed Web of Science ®Google Scholar
• Nambu J. R., Lewis J. O., Wharton K. A., Crews S. T. TheDrosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development. Cell 1991; 67: 1157
   PubMed Web of Science ®Google Scholar
• Kadesch T. Helix-loop-helix proteins in the regulation of immunoglobulin gene transcription. Immun. Today 1992; 13: 31
   PubMedGoogle Scholar
• Kadesch T. Consequences of heteromeric interactions among helix-loop-helix proteins. Cell Growth Diff. 1993; 4: 49
   PubMedGoogle Scholar
• Littlewood T. D., Evan G. I. Transcription factors 2: helix-loop-helix. Protein Profde 1994; 1: 639
   Google Scholar
• Edmondson D. G., Olson E. N. Helix-loop-helix proteins as regulators of muscle-specific transcription. J. Biol. Chem. 1993; 268: 755
   PubMed Web of Science ®Google Scholar
• Murre C., Bain G., van Dijk M. A., Engel I., Furnari B. A., Massari M. E., Matthews J. R., Quong M. W., Rivera R. R., Stuiver M. H. Structure and function of helix-loop-helix proteins. Biochim. et Biophy. Acta 1994; 1218: 129
   PubMed Web of Science ®Google Scholar
• Hoffman E. C., Reyes H., Chu F. F., Sander F., Conley L. H., Brooks B. A., Hankinson O. Cloning of a factor required for activity of the Ah (dioxin) receptor. Science 1991; 252: 954
   PubMed Web of Science ®Google Scholar
• Pollenz R. S., Sattler C. A., Poland A. The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa lclc7 cells by immunofluorescence microscopy. Mol. Pharmacol. 1994; 45: 428
   PubMed Web of Science ®Google Scholar
• Takahashi J. S. Circadian clock genes are ticking. Science 1992; 258: 238
   PubMed Web of Science ®Google Scholar
• Wang G. L., Semenza G. L. Purification and characterization of hypoxia-inducible factor 1,7. Biol. Chem. 1995; 270: 1230
   Google Scholar
• Perego M., Cole S. P., Burbulys D., Trach K., Hoch J. A. Characterization of the gene for a protein kinase which phosphorylates the sporulation-regulatory proteins SpoOA and SpoOF of Bacillus subtilis. J. Bacteriol 1989; 171: 6187
   PubMed Web of Science ®Google Scholar
• Safe S. H. The aryl hydrocarbon (Ah) receptor. ISI Atlas Sci. Pharmacol 1988; 2: 78
   Google Scholar
• Okey A. B. The Ah receptor: mediator of the toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and related compounds. Toxicol. Lett 1994; 70: 1
   PubMed Web of Science ®Google Scholar
• Poellinger L., Lund J., Gillner M., Hansson L. A., Gustafsson J. Å. Physiochemical characterization of specific and nonspecific polyaromatic hydrocarbon binders in rat and mouse liver cytosol. J. Biol. Chem. 1983; 258: 13535
   PubMed Web of Science ®Google Scholar
• Poland A., Glover E. Variation in the molecular mass of the Ah receptor among vertabrate species and strains of rats. Biochem. Biophys. Res. Commun. 1987; 146: 1439
   PubMed Web of Science ®Google Scholar
• Gasiewicz T. A., Rucci G. Cytosolic receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Evidence for a homologous nature among various mammalian species. Mol. Pharmacol 1984; 26: 90
   PubMed Web of Science ®Google Scholar
• Cuthill S., Poellinger L., Gustafsson J. A. The receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in the mouse hepatoma cell line Hepa lclc7. A comparison with the glucocorticoid receptor and the mouse and rat hepatic dioxin receptors. J. Biol. Chem. 1987; 262: 3477
   PubMed Web of Science ®Google Scholar
• Denison M. S., Vella L. M., Okey A. B. Structure and function of the Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Species differences in the molecular properties of the receptors from mouse and rat hepatic cytosols. J. Biol Chem. 1986; 261: 3987
   PubMed Web of Science ®Google Scholar
• Wilhelmsson A., Wikström A. C., Poellinger L. Polyanionic properties of the receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. J. Biol. Chem. 1986; 261: 13456
   PubMed Web of Science ®Google Scholar
• Denison M., Vella L. The hepatic Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Species differences in subunit dissociation. Arch. Biochem. Biophys. 1990; 277: 382
   Google Scholar
• Henry E. C., Rucci G., Gasiewicz T. A. Characterization of multiple forms of the Ah receptor: comparison of species and tissues. Biochemistry 1989; 28: 6430
   PubMed Web of Science ®Google Scholar
• Prokipcak R. D., Okey A. B. Physicochemical characterization of the nuclear form of Ah receptor from mouse hepatoma cells exposed in culture to 2.3.7,8-tetrachlorodibenzo-p-dioxin. Arch. Biochem. Biophys. 1988; 267: 811
   PubMedGoogle Scholar
• Prokipcak R. D., Denison M. S., Okey A. B. Nuclear Ah receptor from mouse hepatoma cells: effect of partial proteolysis on relative molecular mass and DNA-binding properties. Arch. Biochem. Biophys. 1990; 283: 476
   Google Scholar
• Perdew G. H. Association of the Ah receptor with the 90-kDa heat shock protein. J. Biol. Chem. 1988; 263: 13802
   PubMed Web of Science ®Google Scholar
• Denis V I., Cuthill S., Wikstrom A. C., Poellinger L., Gustafsson J. Å. Association of the dioxin receptor with the Mr 90,000 heat shock protein: a structural kinship with the glucocorticoid receptor. Biochem. Biophys. Res. Commun. 1988; 155: 801
   PubMedGoogle Scholar
• Chen H. S., Perdew G. H. Subunit composition of the heteromeric cytosolic aryi hydrocarbon receptor complex. J. Biol. Chem. 1994; 269: 27554
   PubMed Web of Science ®Google Scholar
• Hannah R. R., Nebert D. W., Eisen H. J. Regulatory gene product of the Ah complex. Comparison of 2.3.7.8-tetrachlorodibenzo-p-dioxin and 3-methylcholanthrene binding to several moiteies in mouse liver cytosol. J. Biol. Chem. 1981; 256: 4584
   PubMedGoogle Scholar
• Okey A. B., Bondy G. P., Mason M. E., Nebert D. W., Forster-Gibson C. J., Dufresne M. J. Temperature-dependent cytosol-to-nucleus translocation of the Ah receptor for 2.3,7.8-tetrachlorodibenzo-p-dioxin in continuous cell culture. J. Biol. Chem. 1980; 255: 11415
   PubMed Web of Science ®Google Scholar
• Whitlock J., Jr., Galeazzi D. R. 2.3.7.8 Tetrachlorodibenzo-p-dioxin receptors in wild type and variant mouse hepatoma cells. Nuclear location and strength of nuclear binding. J. Biol. Chem. 1984; 259: 980
   PubMed Web of Science ®Google Scholar
• Denison M. S., Harper P. A., Okey A. B. Ah receptor for 2,3.7.8-tetrachlorodibenzo-p-dioxin. Codistribution of unoccupied receptor with cytosolic marker enzymes during fractionation of mouse liver. rat liver, and cultured Hepa lclc7 cells. Eur. J. Biochem. 1986; 155: 223
   Google Scholar
• Gudas J. M., Karenlampi S. O., Hankinson O. Intracellular location of the Ah receptor. J. Cell. Physiol 1986; 128: 441
   PubMed Web of Science ®Google Scholar
• Hord N. G., Perdew G. H. Physicochemical and immunoeytochemical analysis of the aryl hydrocarbon receptor nuclear translocator: characterization of two monoclonal antibodies to the aryl hydrocarbon receptor nuclear translocator. Mol Pharmacol. 1994; 46: 618
   PubMed Web of Science ®Google Scholar
• Greenlee W. F., Poland A. Nuclear uptake of 2,3,7,8-tetrachlorodibenzo-p-dioxin in C57B1/6J and DBA/2J mice. J. Biol. Chem. 1979; 254: 9814
   PubMed Web of Science ®Google Scholar
• Whitelaw M., Pongratz I., Wilhelmsson A., Gustafsson J. Å., Poellinger L. Ligand-de-pendent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. Mol. Cell. Biol. 1993; 13: 2504
   PubMed Web of Science ®Google Scholar
• Denison M. S., Yao E. F. Characterization of the interaction of transformed rat hepatic cytosolic Ah receptor with a dioxin responsive transcriptional enhancer. Arch. Biochem. Biophys. 1991; 284: 158
   PubMedGoogle Scholar
• Wilhelmsson A., Cuthill S., Denis M., Wikstrom A. C., Gustafsson J. Å., Poellinger L. The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein. EMBO J. 1990; 9: 69
   PubMed Web of Science ®Google Scholar
• Perdew G. H., Whitelaw M. L. Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000. J. Biol. Chem. 1991; 266: 6708
   PubMed Web of Science ®Google Scholar
• McGuire J., Whitelaw M. L., Pongratz I., Gustafsson J. Å., Poellinger L. A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor. Mol. Cell. Biol 1994; 14: 2438
   PubMed Web of Science ®Google Scholar
• Nebert D. W., Gonzalez F. J. P450 genes: structure, evolution and regulation. Annu. Rev. Biochem. 1987; 56: 945
   PubMed Web of Science ®Google Scholar
• Tukey R. H., Hannah R. R., Negishi M., Nebert D. W., Eisen H. J. The Ah locus: correlation of intranuclear appearance of inducer-receptor complex with induction of cytochrome P-450 mRNA. Cell 1982; 31: 275
   PubMed Web of Science ®Google Scholar
• Israel D. I., Whitlock J. P., Jr. Regulation of cytochrome Pl-450 gene transcription by 2,3,7,8-tetrachlorodibezo-p-dioxin in wild type and variant mouse hepatoma cells. J. Biol. Chem. 1984; 259: 5400
   PubMed Web of Science ®Google Scholar
• Sogawa K., Fujisawa-Sehara A., Yamane M., Fuji-Kuriyama Y. Location of regulatory elements responsible for drug induction in the rat cytochrome P-450c gene. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 8044
   PubMed Web of Science ®Google Scholar
• Denison M. S., Fisher J. M., Whitlock J. P., Jr. The DNA recognition site for the dioxin-Ah receptor complex. J. Biol. Chem. 1988; 263: 17221
   PubMed Web of Science ®Google Scholar
• Israel D. I., Whitlock J. P., Jr. Induction of mRNA specific for cytochrome Pl-450 in wild type and variant mouse hepatoma cells. J. Biol Chem. 1983; 258: 10390
   PubMed Web of Science ®Google Scholar
• Fujisawa-Sehara A., Sogawa K., Yamane V I., Fuji-Kuriyama Y. Characterization of xenobiotic responsive elements upstream from the drug-metabolizing cytochrome P-450c gene. A similarity to glucocorticoid regulatory elements. Nucleic Acids Res. 1987; 15: 4179
   PubMed Web of Science ®Google Scholar
• Gonzalez F. J., Nebert D. W. Autoregulation plus upstream positive and negative control regions associated with transcriptional activation of the mouse cytochrome PI -450 gene. Nucleic Acids Res. 1985; 13: 7269
   PubMed Web of Science ®Google Scholar
• Jones P. B., Galeazzi D. R., Fisher J. M., Whitlock J. P., Jr. Control of cytochrome PI-450 gene expression by dioxin. Science 1985; 227: 1499
   PubMed Web of Science ®Google Scholar
• Jones P. B. C., Durrin L. K., Galeazzi D. R., Whitlock J. P., Jr. Control of cytochrome PI-450 gene expression: Analysis of a dioxin-responsive enhancer system. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 2802
   PubMed Web of Science ®Google Scholar
• Denison M. S., Fisher J. M., Whitlock J. P., Jr. Protein-DNA interaction at recognition sites for the dioxin-Ah receptor complex. J. Biol. Chem. 1989; 264: 16478
   PubMed Web of Science ®Google Scholar
• Henry E. C., Rucci G., Gasiewicz T. A. Purification to homogeneity of the heteromeric DNA-binding form of the aryl hydrocarbon receptor from rat liver. Mol. Pharmacol 1994; 46: 1022
   Google Scholar
• Ireland R. C., Li S. Y., Dougherty J. J. The DNA binding of purified Ah receptor heterodimer is regulated by redox conditions. Arch. Biochem. Biophys. 1995; 319: 470
   Google Scholar
• Elferink C. J., Whitlock J., Jr. Dioxin-depen-dent, DNA sequence-specific binding of a multiprotein complex containing the Ah receptor. Receptor 1994; 4: 157
   Google Scholar
• Swanson H. I., Tullis K., Denison M. S. Binding of transformed Ah receptor complex to a dioxin responsive transcriptional enhancer: evidence for two distinct heteromeric DNA-binding forms. Biochemistry 1993; 32: 12841
   Google Scholar
• Okino S. T., Pendurthi U. R., Tukey R. H. 2,3,7,8-Tetrachlorodibenzo-p-dioxin induces the nuclear translocation of two XRE binding proteins in mice. Pharmacogenetics 1993; 3: 101
   Google Scholar
• Perdew G. H., Holenback C. E. Evidence for two functionally distinct forms of the human Ah receptor. J. Biochem. Toxicol. 1995; 10: 95
   Google Scholar
• Chan W. K., Chu R. Y., Jain S., Reddy J. K., Bradfield C. A. Baculovirus expression of the Ah receptor and Ah receptor nuclear translocator – evidence for additional dioxin responsive element-binding species and factors required for signaling. J. Biol. Chem. 1994; 269: 26464
   Google Scholar
• Hines R. N., Mathis J. M., Jacob C. S. Identification of multiple regulatory elements on the human cytochrome P450IA1 gene. Carcinogenesis 1988; 9: 1599
   PubMed Web of Science ®Google Scholar
• Shen E. S., Whitlock J. P., Jr. Protein-DNA interactions at the dioxin-responsive enhancer. J. Biol. Chem. 1992; 267: 6815
   PubMed Web of Science ®Google Scholar
• Lusska A., Shen E., Whitlock J., Jr. Protein-DNA interactions at a dioxin-responsive enhancer. Analysis of six bona fide DNA-binding sites for the liganded Ah receptor. J. Biol. Chem. 1993; 268: 6575
   PubMed Web of Science ®Google Scholar
• Yao E. F., Denison M. S. DNA sequence determinants for binding of transformed Ah receptor to a dioxin-responsive enhancer. Biochemistry 1992; 31: 5060
   PubMed Web of Science ®Google Scholar
• Shen E. S., Whitlock J. P., Jr. The potential role of DNA methylation in the response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. J. Biol. Chem. 1989; 264: 17754
   PubMedGoogle Scholar
• Whitlock J. P., Jr. Genetic and molecular aspects of 2,3,7,8-tetrachlorodibenzo-p-dioxin action. Annu. Rev. Pharmacol. Toxicol 1990; 30: 251
   PubMed Web of Science ®Google Scholar
• Lamb P., McKnight S. L. Diversity and specificity in transcriptional regulation: the benefits of heterotypic dimerization. Trends Biol. Sci. 1991; 16: 417
   PubMedGoogle Scholar
• Bacsi S. G., Reiszporszasz S., Hankinson O. Orientation of the heterodimeric aryl hydrocarbon (dioxin) receptor complex on its asymmetric DNA recognition sequence. Mol. Pharmacol 1995; 47: 432
   PubMed Web of Science ®Google Scholar
• Swanson H. I., Chan W. K., Bradfield C. A. DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins. J. Biol. Chem. 1995; 270: 26292
   PubMed Web of Science ®Google Scholar
• Berghard A., Gradin K., Toftgard R. Serum and extracellular calcium modulate induction of cytochrome P-450IA1 in human keratinocytes. J. Biol. Chem. 1990; 265: 21086
   PubMedGoogle Scholar
• Okino S. T., Pendurthi U. R., Tukey R. H. Phorbol esters inhibit the dioxin receptor-mediated transcriptional activation of the mouse Cypla-1 and CypIa-2 genes by 2,3,7,8-tetrachlorodibenzo-α-dioxin. J. Biol Chem. 1992; 267: 6991
   PubMedGoogle Scholar
• Carrier F., Owens R. A., Nebert D. W., Puga A. Dioxin-dependent activation of murineCypla-1 gene transcription requires protein kinase C-depen-dent phosphorylation. Mol. Cell. Biol 1992; 12: 1856
   PubMed Web of Science ®Google Scholar
• Berghard A., Gradin K., Pongratz I., Whitelaw M., Poellinger L. Cross-coupling of signal transduction pathways: the dioxin receptor mediates induction of cytochrome P-450IA1 expression via a protein kinase C-dependent mechanism. Mol. Cell. Biol 1993; 13: 677
   PubMed Web of Science ®Google Scholar
• Pongratz I., Stromstedt P. E., Mason G. G., Poellinger L. Inhibition of the specific DNA binding activity of the dioxin receptor by phosphatase treatment. J. Biol. Chem. 1991; 266: 16813
   PubMed Web of Science ®Google Scholar
• Schafer M. W., Madhukar B. V., Swanson H. I., Tullis K., Denison M. W. Protein kinase C is not involved in Ah receptor transformation and DNA binding. Arch. Biochem. Biophys. 1993; 307: 267
   Google Scholar
• Dolwick K. M., Swanson H. I., Bradfield C. A. In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition. Proc. Natl. Acad. Sci. U.S.A. 1993; 90: 8566
   PubMed Web of Science ®Google Scholar
• Mahon M. J., Gasiewicz T. A. Ah receptor phosphorylation – localization of phosphorylation sites to the c-terminal half of the protein. Arch. Biochem. Biophys. 1995; 318: 166
   Google Scholar
• Davis R. L., Cheng P. F., Lasser A. B., Weintraub H. The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation. Cell 1990; 60: 733
   PubMedGoogle Scholar
• Voronova A., Baltimore D. Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 4722
   PubMed Web of Science ®Google Scholar
• Anthony-Cahill S. J., Benfeild P. A., Fairman R., Wasserman Z. R., Brenner S. L., Stafford W. F., III, Altenbach C., Hubbell W. L., DeGrado W. F. Molecular characterization of helix-loop-helix peptides. Science 1992; 255: 979
   PubMed Web of Science ®Google Scholar
• Reisz-Porszasz S., Probst M. R., Fukunaga B. N., Hankinson O. Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT). Mol. Cell. Biol. 1994; 14: 6075
   PubMed Web of Science ®Google Scholar
• Antonsson C., Whitelaw M. L., McGuire J., Gustafsson J. Å., Poellinger L. Distinct roles of the molecular chaperone hsp90 in modulating di-oxin receptor function via the basic helix-loop-helix and PAS domains. Mol. Cell. Biol. 1995; 15: 756
   PubMed Web of Science ®Google Scholar
• Lindebro M. C., Poellinger L., Whitelaw M. I. Protein-protein interaction via pas domains – role of the pas domain in positive and negative regulation of the bhh/pas dioxin receptor-arnt transcription factor complex. EMBO J. 1995; 14: 3528
   PubMed Web of Science ®Google Scholar
• Whitelaw M. L., Göttlicher M., Gustafsson J. Å., Poellinger L. Definition of a novel ligand binding domain of a nuclear bHLH receptor: co-localization of ligand and hsp90 binding activities within the regulable inactivation domain of the dioxin receptor. EMBO J. 1993; 12: 4169
   PubMed Web of Science ®Google Scholar
• Coumailleau P., Poellinger L., Gustafsson J. Å., Whitelaw M. L. Definition of a minimal domain of the dioxin receptor that is associated with hsp90 and maintains wild type ligand binding affinity and specificity. J. Biol. Chem. 1995; 270: 25291
   PubMed Web of Science ®Google Scholar
• Blackwood E. M., Eisenman R. N. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 1991; 251: 1211
   PubMed Web of Science ®Google Scholar
• Chen Y. H., Riby J., Srivastava P., Bartholomew J., Denison M., Bjeldanes L. Regulation of cyp 1 a 1 by indolof 3,2-b] carbazole in murine hepatoma cells. J. Biol. Chem. 1995; 270: 22548
   PubMedGoogle Scholar
• Gillner M., Bergman J., Cambillan C., Fernstrom B., Gustafsson J. Å. Interactions of indoles with specific binding sites for 2,3,7.8-tetrachlo-rodibenzo-p-dioxin in rat liver. Mol. Pharmacol. 1985; 28: 357
   PubMed Web of Science ®Google Scholar
• Kleman M. I., Overvik E., Mason G. G., Gustafsson J. Å. In vitro activation of the dioxin receptor to a DNA-binding form by food-borne heterocyclic amines. Carcinogenesis 1992; 13: 1619
   PubMed Web of Science ®Google Scholar
• Rannug A., Rannug U., Rosenkranz H. S., Winqvist L., Westerholm R., Agurell E., Grafstrom A. K. Certain photooxidized derivatives of tryptophan bind with very high affinity to the Ah receptor and are likely to be endogenous signal substances. J. Biol. Chem. 1987; 262: 15422
   PubMed Web of Science ®Google Scholar
• Gillner M., Bergman J., Cambillau C., Gustafsson J. Å. Interactions of rutaecarpine alkaloids with specific binding sites for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver. Carcinogenesis 1989; 10: 651
   PubMed Web of Science ®Google Scholar
• Knutson J. C., Poland A. Keratinization of mouse teratoma cell line XB produced by 2,3,7,8-tetrachlorodibenzo-p-dioxin: an in vitro model of toxicity. Cell 1980; 22: 27
   PubMed Web of Science ®Google Scholar
• Whitlock J., Jr. Mechanistic aspects of dioxin action. Chem. Res. Toxicol. 1993; 6: 754
   PubMed Web of Science ®Google Scholar
• Fernandezsalguero P., Pineau T., Hilbert D. M., McPhail T., Lee S., Kimura S., Nebert D. W., Rudikoff S., Ward J. M., Gonzalez F. J. Immune system impairment and hepatic fibrosis in mice lacking the dioxin-binding Ah receptor. Science 1995; 268: 722
   Google Scholar
• Tukey R. H., Nebert D. W. Regulation of mouse cytochrome P3–450 by the Ah receptor. Studies with a P3–450 cDNA clone. Biochemistry; 1984; 23: 6003
   PubMed Web of Science ®Google Scholar
• Safe S., Safe L. Synthesis and characterization of twenty-two purified polychlorinated dibenzofuran congeners. J. Agric. Food Chem. 1984; 32: 68
   Google Scholar
• Piskorska-Pliszczynska J., Keys B., Safe S., Newman M. S. The cytosolic binding affinities and AHH induction potencies of 29 polynuclear aromatic hydrocarbons. Toxicol. Lett. 1986; 34: 67
   PubMed Web of Science ®Google Scholar
• Gillner M., Bergman J., Cambillau C., Alexandersson M L, Fernstrom B., Gustafsson J. Å. Interactions of indolo[3,2-b] carbazoles and related polycy-clic aromatic hydrocarbons with specific binding sites for 2,3,7.8-tetrachlorodibenzo-p-dioxin in rat liver. Mol. Pharmacol 1993; AA: 336
   Google Scholar
• Waller C. L., McKinney J. D. Three-dimensional quantitative structure-activity relationships of dioxins and dioxin-like compounds – model validation and Ah receptor characterization. Chem. Res. Toxicol 1995; 8: 847
   PubMed Web of Science ®Google Scholar
• Poland A., Palen D., Glover E. Analysis of the four alleles of the murine aryl hydrocarbon receptor. Mol. Pharmacol 1994; 46: 915
   PubMed Web of Science ®Google Scholar
• Poland A., Glover E. Comparison of 2,3,7,8-tetrachlorodibenzo-p-dioxin, a potent inducer of aryl hydrocarbon hydroxylase, with 3-methylcholanthrene. Mol. Pharmacol 1974; 10: 349
   PubMed Web of Science ®Google Scholar
• Okey A. B., Vella L. M., Harper P. A. Detec tion and characterization of a low affinity form of cytosolic Ah receptor in livers of mice nonresponsive to induction of cytochrome PI -450 by 3-methylcholanthrene. Mol. Pharmacol 1989; 35: 823
   PubMed Web of Science ®Google Scholar
• Ema M., Ohe N., Suzuki M., Mimura J., Sogawa K., Ikawa S., Fujii-Kuriyama Y. Dioxin binding activities of polymorphic forms of mouse and human aryl hydrocarbon receptors. J. Biol. Chem. 1994; 269: 27337
   PubMed Web of Science ®Google Scholar
• Harper P. A., Golas C. L., Okey A. B. Characterization of the Ah receptor and aryl hydrocarbon hydroxylase induction by 2,3,7,8-tetrachlorodibenzo-p-dioxin and benz(a)anthracene in the human A431 squamous cell carcinoma line. Cancer Research 1988; 48: 2388
   PubMed Web of Science ®Google Scholar
• Smith D. F., Toft D. O. Steroid receptors and their associated proteins. Mol. Endocrinol. 1993; 7: 4
   PubMed Web of Science ®Google Scholar
• Pratt W. B. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 1993; 268: 21455
   PubMed Web of Science ®Google Scholar
• Pongratz I., Mason G. G., Poellinger L. Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity. J. Biol. Chem. 1992; 267: 13728
   PubMed Web of Science ®Google Scholar
• Whitelaw M. L., McGuire J., Picard D., Gustafsson J. Å., Poellinger L. Heat shock protein hsp90 regulates dioxin receptor function in vivo. Proc. Natl. Acad. Set U.S.A. 1995; 92: 4437
   PubMed Web of Science ®Google Scholar
• Carver L. A., Jackiw V., Bradfield C. A. The 90-kda heat shock protein is essential for Ah receptor signaling in a yeast expression system. J. Biol. Chem. 1994; 269: 30109
   PubMed Web of Science ®Google Scholar
• Whitelaw M. L., Gustafsson J. Å., Poellinger L. Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation. Mol. Cell. Biol 1994; 14: 8343
   PubMed Web of Science ®Google Scholar
• Li H., Dong L. Q., Whitlock J. P. Transcriptional activation function of the mouse Ah receptor nuclear translocator. J. Biol. Chem. 1994; 269: 28098
   PubMed Web of Science ®Google Scholar
• Jain S., Dolwick K. M., Schmidt J. V., Bradfield C. A. Potent transactivation domains of the Ah receptor and the Ah receptor nuclear translocator map to their carboxyl termini. J. Biol. Chem. 1994; 269: 31518
   PubMed Web of Science ®Google Scholar
• Ma Q., Dong L. Q., Whitlock J. P. Transcriptional activation by the mouse Ah receptor – interplay between multiple stimulatory and inhibitory functions. J. Biol. Chem. 1995; 270: 12697
   PubMed Web of Science ®Google Scholar
• Rowlands J. C., McEwan I. J., Gustafsson J. Å. Transactivation by the human dioxin receptor and ARNT proteins: direct interactions with basal transcription factors. Mol. Pharmacol 1996; 50: 538
   PubMed Web of Science ®Google Scholar
• Sogawa K., Iwabuchi K., Abe H., Fujiikuriyama Y. Transcriptional activation domains of the Ah receptor and Ah receptor nuclear translocator. J. Cancer Res. Clin. Oncol 1995; 121: 612
   PubMedGoogle Scholar
• Ptashne M. How eukaryotic transcriptional activators work. Nature 1988; 335: 683
   PubMed Web of Science ®Google Scholar
• Tjian R., Maniatis T. Transcriptional activation: a complex puzzle with few easy pieces. Cell 1994; 11: 5
   Google Scholar
• Croston G. E., Kadonaga J. T. Role of chromatin structure in the regulation of transcription by RNA polymerase II. Curr. Opin. Cell Biol 1993; 5: 417
   PubMed Web of Science ®Google Scholar
• Svaren J., Hörz W. Histones, nucleosomes and transcription. Curr. Opin. Genet. Dev. 1993; 3: 219
   PubMedGoogle Scholar
• Durrin L. K., Whitlock J. P., Jr. In situ pro-tein-DNA interactions at a dioxin-responsive enhancer associated with the cytochrome PI-450 gene. Mol. Cell. Biol 1987; 1: 3008
   Google Scholar
• Elferink C. J., Gasiewicz T. A., Whitlock J. P., Jr. Protein-DNA interactions at a dioxin-responsive enhancer: evidence that the transformed Ah receptor is heteromeric. J. Biol. Chem. 1990; 265: 20708
   PubMed Web of Science ®Google Scholar
• Morgan J. E., Whitlock J., Jr. Transcription-dependent and transcription-independent nucleosome disruption induced by dioxin. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 11622
   PubMed Web of Science ®Google Scholar
• Wu L., Whitlock J., Jr. Mechanism of dioxin action: receptor-enhancer interactions in intact cells. Nucleic Acids Res. 1993; 21: 119
   PubMed Web of Science ®Google Scholar
• Wu L., Whitlock J., Jr. Mechanism of dioxin action: Ah receptor-mediated increase in promoter accessibility in vivo. Proc. Natl Acad. Sci. U.S.A. 1992; 89: 4811
   PubMed Web of Science ®Google Scholar
• Okino S. T., Whitlock J. P. Dioxin induces localized, graded changes in chromatin structure – implications forcyplal gene transcription. Mol. Cell. Biol 1995; 15: 3714
   PubMed Web of Science ®Google Scholar
• Wen L. P., Koeiman N., Whitlock J., Jr. Dioxin-inducible, Ah receptor-dependent transcription in vitro. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 8545
   PubMedGoogle Scholar
• Zawel L., Reinberg D. Common themes in assembly and function of eukaryotic transcription complexes. Annu. Rev. Biochem. 1995; 64: 533
   PubMedGoogle Scholar
• Goodrich J. A., Tjian R. TBP-TAF complexes: selectivity factors for eukaryotic transcription. Curr. Opin. Cell Biol 1994; 6: 403
   PubMedGoogle Scholar
• Sayre M. H., Tschochner H., Romberg R. D. Reconstitution of transcription with five purified initiation factors and RNA polymerase II from, Saccha-romyces cerevisiae. J. Biol. Chem. 1992; 267: 23376
   PubMedGoogle Scholar
• McEwan I. J., Wright A. P., Dahlman-Wright K., Carlstedt-Duke J., Gustafsson J. Å. Direct interaction of the tau 1 transactivation domain of the human glucocorticoid receptor with the basal transcriptional machinery. Mol. Cell. Biol 1993; 13: 399
   PubMed Web of Science ®Google Scholar
• McEwan I. J., Almlof T., Wikstrom A. C., Dahlman-Wright K., Wright A. P., Gustafsson J. Å. The glucocorticoid receptor functions at multiple steps during transcription initiation by RNA polymerase II. J. Biol. Chem. 1994; 269: 25629
   PubMedGoogle Scholar
• Robertson R. W., Zhang L., Pasco D. S., Fagan J. B. Aryl hydrocarbon-induced interactions at multiple DNA elements of diverse sequence – a multicomponent mechanism for activation of cytochrome P4501A1 (CYP1A1) gene transcription. Nucleic Acids Res. 1994; 22: 1741
   PubMedGoogle Scholar
• Jones K. W., Whitlock J. P., Jr. Functional analysis of the transcriptional promoter for theCYPIAI gene. Mol. Cell. Biol. 1990; 10: 5098
   PubMed Web of Science ®Google Scholar
• Watson A. J., Hankinson O. Dioxin- and Ah receptor-dependent protein binding to xenobiotic responsive elements and G-rich DNA studied byin vivo footprinting. J. Biol. Chem. 1992; 266: 6874
   Google Scholar
• Fisher J. M., Wu L., Denison M. S., Whitlock J. P., Jr. Organization and function of a dioxin-responsive enhancer. J. Biol. Chem. 1990; 265: 9676
   PubMedGoogle Scholar
• Boucher P. D., Piechocki M. P., Hines R. N. Partial characterization of the human CYP1 Al negatively acting transcription factor and mutational analysis of its cognate DNA recognition sequence. Mol. Cell. Biol. 1995; 15: 5144
   PubMed Web of Science ®Google Scholar
• Sterling K., Weaver J., Ho K. L., Xu L. C., Bresnick E. Rat CYP1A1 negative reguiatory element: biological activity and interaction with a protein from liver and hepatoma cells. Mol. Pharmacol. 1993; 44: 560
   PubMed Web of Science ®Google Scholar
• Gradin K., Wilhelmsson A., Poellinger L., Berghard A. Nonnresponsiveness of normal human fibroblasts to dioxin correlates with the presence of a constitutive xenobiotic response element-binding factor. J. Biol. Chem. 1993; 268: 4061
   PubMed Web of Science ®Google Scholar
• Watson A. J., Weir-Brown K. I., Bannister R. M., Chu F. F., Reisz-Porszasz S., Fuji-Kuriyama Y., Sogawa K., Hankinson O. Mechanism of action of a repressor of dioxin-dependent induction of Cyplal gene transcription. Mol. Cell. Biol. 1992; 12: 2115
   PubMed Web of Science ®Google Scholar
• Carrier F., Chang C. Y., Duh J. L., Nebert D. W., Puga A. Interaction of the regulatory domains of the murine Cyplal gene with two DNA-binding proteins in addition to the Ah receptor and the Ah receptor nuclear translocator (ARNT). Biochem. Pharmacol. 1994; 48: 1767
   PubMedGoogle Scholar
• Parkinson A. Biotransformation of xenobiotics. Cassarett & Doull's Toxicology: The Basic Science of Poisons, C. D. Klaassen. McGraw-Hill, New York 1996; 113
   Google Scholar
• Quattrochi L. C., Vu T., Tukey R. H. The human CYP1A2 gene and induction by 3-methyl-cholanthrene. J. Biol. Chem. 1994; 269: 6949
   PubMed Web of Science ®Google Scholar
• Quattrochi L. C., Tukey R. H. The human cytochrome CyplA2 gene contains regulatory elements responsive to 3-methylcholanthrene. Mol. Pharmacol. 1989; 36: 66
   PubMed Web of Science ®Google Scholar
• Tritscher A. M., Seacat A. M., Yager J. D., Groopman J. D., Miller B. D., Bell D., Sutter T. R., Lucier G. W. Increased oxidative DNA damage in livers of 2.3.7.8-tetraehlorodibenzo-p-di-oxin treated intact but not ovariectomized rats. Cancer Lett. 1996; 98: 219
   PubMed Web of Science ®Google Scholar
• Sutter T. R., Tang Y. ML, Hayes C. L., Wo Y. Y., Jabs. E. W., Li X., Yin H., Cody C. W., Greenlee W. F. Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. J. Biol. Chem. 1994; 269: 13092
   PubMed Web of Science ®Google Scholar
• Savas U., Bhattacharyya K. K., Christou M L, Alexander D. L., Jefcoate C. R. Mouse cytochrome P-450EF, representative of a new IB subfamily of cytochrome P-450s. Cloning, sequence determination, and tissue expression. J. Biol. Chem. 1994; 269: 14905
   PubMed Web of Science ®Google Scholar
• Bhattacharyya K. K., Brake P. B., Fjtom S. E., Otto S. A., Jefcoate C. R. Identification of a rat adrenal cytochrome P450 active in polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a unique tissue-specific pattern of hormonal and aryl hydrocarbon receptor-linked regulation. J. Biol. Chem. 1995; 270: 11595
   PubMed Web of Science ®Google Scholar
• Walker N. J., Gastel J. A., Costa L. T., Clark G. C., Lucier G. W., Sutter T. R. Rat cyp 1 b 1 – an adrenal cytochrome p450 that exhibits sex-dependent expression in livers and kidneys of tcdd-treated animals. Carcinogenesis 1995; 16: 1319
   PubMedGoogle Scholar
• Rushmore T. H., King R. G., Paulson K. E., Pickett C. B. Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 3826
   PubMed Web of Science ®Google Scholar
• Rushmore T. H., Pickett C. B. Transcriptional regulation of the rat glutathione S-transferase Ya subunit gene. Characterization of a xenobiotic-responsive element controlling inducible expression by phenolic antioxidants. J. Biol. Chem. 1990; 265: 14648
   PubMed Web of Science ®Google Scholar
• Paulson K. E., Darnell J., Jr., Rushmore T., Pickett C. B. Analysis of the upstream elements of the xenobiotic compound-inducible and positionally regulated glutathione S-transferase Ya gene. Mol. Cell. Biol. 1990; 10: 1841
   PubMed Web of Science ®Google Scholar
• Pimental R. A., Liang B., Yee G. K., Wilhelmsson A., Poellinger L., Paulson K. E. Dioxin receptor and C/EBP regulate the function of the glutatione S-transferase Ya gene xenobiotic response element. Mol. Cell. Biol. 1993; 13: 4365
   PubMed Web of Science ®Google Scholar
• Friling R. S., Bergelson S., Daniel V. Two adjacent AP-1 -like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 668
   PubMed Web of Science ®Google Scholar
• Nguyen T., Rushmore T. H., Pickett C. B. Transcriptional regulation of a rat liver glutathione S-transferase Ya subunit gene. Analysis of the antioxidant response element and its activation by the phorbol ester 12–0-tetradecanoy phorbol-13-acetate. J. Biol. Chem. 1994; 269: 13656
   PubMed Web of Science ®Google Scholar
• Xiao G. H., Pinaire J. A., Rodrigues A. D., Prough R. A. Regulation of the Ah gene battery via Ah receptor-dependent and independent processes in cultured adult rat hepatocytes. Drug Metah. Dispos. 1995; 23: 642
   PubMed Web of Science ®Google Scholar
• Takimoto K., Lindahl R., Pitot H. C. Regulation of 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible expression of aldehyde dehydrogenase in hepatoma cells. Arch. Biochem. Biophys. 1992; 298: 493
   Google Scholar
• Hempel J., Harper K., Lindahl R. Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-di-oxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mito-chondria. Biochemistry 1989; 28: 1160
   PubMed Web of Science ®Google Scholar
• Takimoto K., Lindahl R., Dunn T. J., Pitot H. C. Structure of the 5' flanking region of class 3 aldehyde dehydrogenase in the rat. Arch. Biochem. Biophys. 1994; 312: 539
   PubMed Web of Science ®Google Scholar
• Kumaki K., Jensen N. M., Shire J. G., Nebert D. W. Genetic differences in induction of cytosol reduced-NAD(P):menadione oxidoreductase and microsomal aryl hydrocarbon hydroxylase in the mouse. J. Biol. Chem. 1977; 252: 157
   PubMed Web of Science ®Google Scholar
• Williams J. B., Wang R., Lu A. Y., Pickett C. B. Rat liver DT-diaphorase: regulation of functional mRNA levels by 3-methylcholanthrene, trans-stilbene oxide, and phenobarbital. Arch. Biochem. Biophys. 1984; 232: 408
   PubMed Web of Science ®Google Scholar
• Favreau L. V., Pickett C. B. Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants. J. Biol. Chem. 1991; 266: 4556
   PubMed Web of Science ®Google Scholar
• Favreau L. V., Pickett C. B. Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Characterization of a DNA-protein interaction at the antioxidant responsive element and induction by 12-O-tetradecanoylphorbol 13-acetate. J. Biol. Chem. 1993; 268: 19875
   PubMed Web of Science ®Google Scholar
• Sutter T. R., Guzman K., Dold K. M., Greenlee W. F. Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta. Science 1991; 254: 415
   PubMed Web of Science ®Google Scholar
• Cousin E., Medcalf R. L., Bergonzelli G. E., Kruithof E. K. Regulatory elements involved in constitutive and phorbol ester-inducible expression of the plasminogen activator inhibitor type 2 gene promoter. Nucleic Acids Res. 1991; 19: 3881
   PubMedGoogle Scholar
• Choi E. J., Toscano D. G., Ryan J. A., Riedel N., Toscano W. A., Jr. Dioxin induces transforming growth factor-a in human keratinocytes. J. Biol. Chem. 1991; 266: 9591
   PubMedGoogle Scholar
• Gaido K. W., Maness S. C., Leonard L. S., Greenlee W. F. 2,3,7,8-Tetrachlorodibenzo-p-di-oxin-dependent regulation of transforming growth factors-alpha and -beta 2 expression in a human keratinocyte cell line involves both transcriptional and post-transcriptional control. J. Biol. Chem. 1992; 267: 24591
   PubMed Web of Science ®Google Scholar
• Puga A., Nebert D. W., Carrier F. Dioxin induces expression ofc-fos andc-jun proto-oncogenes and a large increase in transcription factor AP-1. DNA Cell Biol 1992; 11: 269
   PubMed Web of Science ®Google Scholar
• Safe S. H. Modulation of gene expression and endocrine response pathways by 2,3,7,8-tetrachlorodibenzo-p-dioxin and related compounds. Pharmacol. Therap. 1995; 67: 247
   PubMed Web of Science ®Google Scholar
• Philips A., Chalbos D., Rochefort H. Estradiol increases and anti-estrogens antagonize the growth factor-induced activator protein-1 activity in MCF-7 breast cancer cells without affectingc-fos andc-jun synthesis. J. Biol. Chem. 1993; 268: 14103
   PubMedGoogle Scholar
• Zacharewski T. R., Bondy K. L., McDonell P., Wu Z. F. Antiestrogenic effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin on 17 beta-estradiol-induced pS2 expression. Cancer Res. 1994; 54: 2707
   PubMed Web of Science ®Google Scholar
• Krishnan V., Porter W., Santostefano M., Wang X. H., Safe S. Molecular mechanism of inhibition of estrogen-induced cathepsin D gene expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in MCF-7 cells. Mol. Cell. Biol 1995; 15: 6710
   PubMed Web of Science ®Google Scholar
• Krishnan V., Wang X., Safe S. Estrogen receptor-Spl complexes mediate estrogen-induced cathepsin D gene expression in MCF-7 human breast cancer cells. J. Biol. Chem. 1994; 269: 15912
   PubMedGoogle Scholar
• Nunez A., Berry M., Imler J., Chambon P. The 5' flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumor promoter (TPA), thec-Ha-ras oncoprotein and the c-jun protein. EMBO J. 1989; 8: 823
   PubMed Web of Science ®Google Scholar
• Rowlands J. C., Wang X., Safe S. 2,3,7,8-Tetrachlorodibenzo-p-dioxin inhibition of nuclear AP-1 binding in MCF-7 human breast cancer cells. Organohalogen Compounds 1992; 10: 201
   Google Scholar
• Astroff B., Eldridge B., Safe S. Inhibition of 17P-estradiol-induced and constitutive expression of the cellular protooncogene c-Fos by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in the female rat uterus. Toxicol. Lett 1991; 56: 305
   PubMed Web of Science ®Google Scholar
• Olson E. N. Myo D family: a paradigm for development?. Genes Dev. 1990; 4: 1454
   PubMed Web of Science ®Google Scholar
• Weintraub H., Dwarki V. J., Verma I., Davis R., HoIIenberg S., Snider L., Lasser A., Tapscott S. J. Muscle-specific transcriptional activation by MyoD. Genes Dev. 1991; 5: 1377
   PubMed Web of Science ®Google Scholar
• Emerson C. P. Myogenesis and development control genes. Curr. Opin. Cell Biol 1990; 2: 1065
   PubMedGoogle Scholar
• Blackwell T. K., Weintraub H. Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection. Science 1990; 250: 1104
   PubMed Web of Science ®Google Scholar
• Wright W. E., Binder M., Funk W. Cyclic amplification and selection of targets (CASTing) for the myogenin consensus binding site. Mol. Cell. Biol 1991; 11: 4104
   PubMed Web of Science ®Google Scholar
• Halazonetis T. D., Kandil A. N. Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco Rl. Science 1992; 255: 464
   PubMedGoogle Scholar
• Dang C. V., Dolde C., Gillison M. C., Kato G. J. Discrimination between related DNA sites by a single amino acid residue of Myc-related basic helix-loop-helix proteins. Proc. Nail. Acad. Sci. U.S.A. 1992; 89: 559
   Google Scholar
• Fisher F., Coding C. R. Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif. EM BO J. 1992; 11: 4103
   PubMedGoogle Scholar
• Ferre-ĎAmare A. R., Prendergast G. C., Ziff E. B., Burley S. K. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 1993; 363: 38
   Google Scholar
• Ferre-D'Amare A. R., Pognonec P., Roeder R. G., Burley S. K. Structure and function of the b/ HLH/Z domain of USF. EMBO J. 1994; 13: 180
   PubMedGoogle Scholar
• Gregor P., Sawadogo M., Roeder R. G. The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer. Genes Dew. 1990; 4: 1730
   PubMed Web of Science ®Google Scholar
• Antonsson C., Arulampalam V., Whitelaw M. L., Pettersson S., Poellinger L. Constitutive function of the basic hclix-loop-helix/PAS factor Arnt. Regulation of target promoters via the E box motif. J. Biol. Chem. 1995; 210: 13968
   Google Scholar
• Sogawa K., Nakano R., Kobayashi A., Kikuchi Y., Ohe N., Matsushita N., Fujii-Kuriyama Y. Possible function of Ah receptor nuclear translocator (Arnt) homodimer in transcriptional regulation. Proc Natl. Acad. Sciences U.S.A. 1995; 92: 1936
   PubMed Web of Science ®Google Scholar
• Semenza G. L., Roth P. H., Fang H. ML, Wang G. L. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J. Biol. Chem. 1994; 269: 23757
   PubMed Web of Science ®Google Scholar
• Lindeman G. J., Harris A. W., Bath M. L., Eisenman R. N., Adams J. M. Overexpressed max is not oncogenic and attenuates myc-induced lymphoproliferation and lymphomagenesis in transgenic mice. Oncogene 1995; 10: 1013
   PubMedGoogle Scholar
• Lahoz E. G., Xu L., Schreiber-Agus N., DePinho R. A. Suppression of Myc, but not Ela, transformation activity by Max-associated proteins, Mad and Mxil. Proc. Natl. Acad. Sci. U.S.A. 1994; 91: 5503
   PubMedGoogle Scholar