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Volumn 49, Issue 2, 1996, Pages 276-287

Regulation of CYP4A expression in rat by dehydroepiandrosterone and thyroid hormone

Author keywords

[No Author keywords available]

Indexed keywords

PRASTERONE; THYROID HORMONE;

EID: 0030040908     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (32)

References (55)
  • 2
    • 0024385160 scopus 로고
    • The rat clofibrate-inducible CYP4A subfamily. II. cDNA sequence of IVA3, mapping of the cyp4a locus to mouse chromosome 4 and coordinate and tissue specific regulation of the CYP4A genes
    • Kimura, S., J. P Hardwick, C. A. Kozak, and F. J. Gonzalez. The rat clofibrate-inducible CYP4A subfamily. II. cDNA sequence of IVA3, mapping of the cyp4a locus to mouse chromosome 4 and coordinate and tissue specific regulation of the CYP4A genes DNA 8:517-525 (1989).
    • (1989) DNA , vol.8 , pp. 517-525
    • Kimura, S.1    Hardwick, J.P.2    Kozak, C.A.3    Gonzalez, F.J.4
  • 3
    • 0024350111 scopus 로고
    • The rat clofibrate-inducible CYP4A gene subfamily. I. Complete intron and exon sequences of the CYP4A1 and CYP4A2 genes, unique exon organization and identification of a conserved 16 bp upstream element
    • Kimura, S., N. Hamoka, E. Matsunaga, and F. J. Gonzalez. The rat clofibrate-inducible CYP4A gene subfamily. I. Complete intron and exon sequences of the CYP4A1 and CYP4A2 genes, unique exon organization and identification of a conserved 16 bp upstream element. DNA 8:503-516 (1989).
    • (1989) DNA , vol.8 , pp. 503-516
    • Kimura, S.1    Hamoka, N.2    Matsunaga, E.3    Gonzalez, F.J.4
  • 4
    • 0015337156 scopus 로고
    • Cytochrome P450K of rat kidney cortex microsomes: Its involvement in fatty acid ω-and (ω-1)-hydroxylation
    • Ellim, A., S V. Jakobsson, J B. Schenkman, and S. Orrenius. Cytochrome P450K of rat kidney cortex microsomes: its involvement in fatty acid ω-and (ω-1)-hydroxylation. Arch. Biochem. Biophys. 150:64-72 (1972).
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 64-72
    • Ellim, A.1    Jakobsson, S.V.2    Schenkman, J.B.3    Orrenius, S.4
  • 5
    • 0025063441 scopus 로고
    • Clofibrate-inducible rat hepatic P450s IVA1 and IVA3 catalyze the ω- and (ω-1)-hydroxylation of fatty acids and the ω-hydroxylation of prostaglandin E1 and F2a
    • Aoyama, T., J. P. Hardwick, S. Imaoka, Y. Funae, H. V. Gelboin, and F. J. Gonzalez. Clofibrate-inducible rat hepatic P450s IVA1 and IVA3 catalyze the ω- and (ω-1)-hydroxylation of fatty acids and the ω-hydroxylation of prostaglandin E1 and F2a. J. Lipid. Res. 31:1477-1482 (1990).
    • (1990) J. Lipid. Res. , vol.31 , pp. 1477-1482
    • Aoyama, T.1    Hardwick, J.P.2    Imaoka, S.3    Funae, Y.4    Gelboin, H.V.5    Gonzalez, F.J.6
  • 6
    • 0027422899 scopus 로고
    • Expression of rabbit cytochromes P4504A which catalyze the omega-hydroxylation of arachidonic acid, fatty acids, and prostaglandins
    • Roman, L. J., C. N. Palmer, J. E. Clark, A. S. Muerhoff, K. J. Griffin, E. F. Johnson, and B. S. Masters. Expression of rabbit cytochromes P4504A which catalyze the omega-hydroxylation of arachidonic acid, fatty acids, and prostaglandins. Arch. Biochem. Biophys. 307:57-65 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 57-65
    • Roman, L.J.1    Palmer, C.N.2    Clark, J.E.3    Muerhoff, A.S.4    Griffin, K.J.5    Johnson, E.F.6    Masters, B.S.7
  • 7
    • 0023522829 scopus 로고
    • The effect of peroxisome proliferators on microsomal, peroxisomal, and mitochondrial enzyme activities in the liver and kidney
    • Hawkins, J. M., W. E Jones, F W. Bonner, and G. G. Gibson. The effect of peroxisome proliferators on microsomal, peroxisomal, and mitochondrial enzyme activities in the liver and kidney. Drug Metab. Rev. 18:441-615 (1988).
    • (1988) Drug Metab. Rev. , vol.18 , pp. 441-615
    • Hawkins, J.M.1    Jones, W.E.2    Bonner, F.W.3    Gibson, G.G.4
  • 8
    • 0026467676 scopus 로고
    • Peroxisome proliferation and hepatocarcinogenesis
    • Reddy, J. K., and M. S. Rao. Peroxisome proliferation and hepatocarcinogenesis. IARC Sci. Publ. 116:225-235(1992).
    • (1992) IARC Sci. Publ. , vol.116 , pp. 225-235
    • Reddy, J.K.1    Rao, M.S.2
  • 10
    • 0018865153 scopus 로고
    • Effects of fat content in the diet on hepatic peroxisomes of the rat
    • Ishii, H., N. Fukumori, S. Horie, and T. Suga. Effects of fat content in the diet on hepatic peroxisomes of the rat. Biochim. Biophys. Acta 617:1-11 (1980).
    • (1980) Biochim. Biophys. Acta , vol.617 , pp. 1-11
    • Ishii, H.1    Fukumori, N.2    Horie, S.3    Suga, T.4
  • 12
    • 0020965193 scopus 로고
    • Effect of cold adaptation on liver peroxisomes and peroxisomal oxidative activities of rat: A morphometric/stereologic and biochemical study
    • Pollera, M., T. Locci Cubeddu, and E. Bergammi. Effect of cold adaptation on liver peroxisomes and peroxisomal oxidative activities of rat: a morphometric/stereologic and biochemical study. Arch. Int. Physiol. Biochim. 91: 35-42 (1983).
    • (1983) Arch. Int. Physiol. Biochim. , vol.91 , pp. 35-42
    • Pollera, M.1    Locci Cubeddu, T.2    Bergammi, E.3
  • 14
    • 0028308486 scopus 로고
    • Induction of microsomal and peroxisomal enzymes by dehydroepiandrosterone and its reduced metabolite in rats
    • Prough, R. A., S. J. Webb, H.-Q. Wu, D. P. Lapenson, and D. J. Waxman. Induction of microsomal and peroxisomal enzymes by dehydroepiandrosterone and its reduced metabolite in rats. Cancer Res. 54:2878-2886 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 2878-2886
    • Prough, R.A.1    Webb, S.J.2    Wu, H.-Q.3    Lapenson, D.P.4    Waxman, D.J.5
  • 15
    • 0025132245 scopus 로고
    • Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
    • Issemann, I., and S. Green. Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators. Nature (Lond.) 347:645-650 (1990).
    • (1990) Nature (Lond.) , vol.347 , pp. 645-650
    • Issemann, I.1    Green, S.2
  • 16
    • 0025726848 scopus 로고
    • Two cis-acting regulatory sequences in the peroxisome proliferator-responsive enhancer region of rat acyl-CoA oxidase gene
    • Osumi, T., J. K. Wen, and T. Hashimoto. Two cis-acting regulatory sequences in the peroxisome proliferator-responsive enhancer region of rat acyl-CoA oxidase gene. Biochem. Biophys. Res Commun. 175:866-871 (1991).
    • (1991) Biochem. Biophys. Res Commun. , vol.175 , pp. 866-871
    • Osumi, T.1    Wen, J.K.2    Hashimoto, T.3
  • 17
    • 0026541591 scopus 로고
    • The mouse peroxisome proliferator activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene
    • Tugwood, J. D., I. Issemann, R. G. Anderson, K. R. Bundell, W. L. McPheat, and S. Green, The mouse peroxisome proliferator activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene. EMBO J. 11:433-439 (1992)
    • (1992) EMBO J. , vol.11 , pp. 433-439
    • Tugwood, J.D.1    Issemann, I.2    Anderson, R.G.3    Bundell, K.R.4    McPheat, W.L.5    Green, S.6
  • 18
    • 0026730908 scopus 로고
    • The peroxisome proliferator-activated receptor mediates the induction of CYP4A6, a cytochrome P450 fatty acid omega-hydroxylase, by clofibric acid
    • Muerhoff, A. S., K. J. Griffin, and E. F. Johnson. The peroxisome proliferator-activated receptor mediates the induction of CYP4A6, a cytochrome P450 fatty acid omega-hydroxylase, by clofibric acid. J. Biol. Chem. 267: 19051-19053 (1992)
    • (1992) J. Biol. Chem. , vol.267 , pp. 19051-19053
    • Muerhoff, A.S.1    Griffin, K.J.2    Johnson, E.F.3
  • 19
    • 0027265115 scopus 로고
    • Characterization of protein-DNA interactions within the peroxisome proliferator-responsive element of the rat hydratasedehydrogenase gene
    • Zhang, B., S. L. Marcus, K. S. Miyata, S. Subramani, J. P. Capone, and R. A. Rachubinski. Characterization of protein-DNA interactions within the peroxisome proliferator-responsive element of the rat hydratasedehydrogenase gene. J. Biol. Chem. 268:12939-12945 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 12939-12945
    • Zhang, B.1    Marcus, S.L.2    Miyata, K.S.3    Subramani, S.4    Capone, J.P.5    Rachubinski, R.A.6
  • 20
    • 0027415913 scopus 로고
    • Enantioselective activation of the peroxisome proliferator-activated receptor
    • Boie, Y., M. Adam, T. H. Rushmore, and B. P. Kennedy. Enantioselective activation of the peroxisome proliferator-activated receptor. J. Biol. Chem. 268:5530-5534 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 5530-5534
    • Boie, Y.1    Adam, M.2    Rushmore, T.H.3    Kennedy, B.P.4
  • 21
    • 0025763402 scopus 로고
    • Induction of hepatic mitochondrial glycerophosphate dehydrogenase in rats by dehydroepiandrosterone
    • Su, C. Y., and H. Lardy. Induction of hepatic mitochondrial glycerophosphate dehydrogenase in rats by dehydroepiandrosterone. J. Biochem. Tokyo 110:207-213 (1991).
    • (1991) J. Biochem. Tokyo , vol.110 , pp. 207-213
    • Su, C.Y.1    Lardy, H.2
  • 22
    • 0024813413 scopus 로고
    • Thyroid hormone-mediated transcriptional activation of the rat liver malic enzyme gene by dehydroepiandrosterone
    • Song, M. K., D. Grieco, J. E. Rail, and V. M. Nikodem. Thyroid hormone-mediated transcriptional activation of the rat liver malic enzyme gene by dehydroepiandrosterone. J. Biol. Chem. 264:18981-18985 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 18981-18985
    • Song, M.K.1    Grieco, D.2    Rail, J.E.3    Nikodem, V.M.4
  • 23
    • 0027229302 scopus 로고
    • 20-Hydroxyeicosatetraenoic acid is an endothelium-dependent vasoconstrictor in rabbit arteries
    • Escalante, B., K. Omata, W. Sessa, S. G. Lee, J. R. Falck, and M. L. Schwartzman. 20-Hydroxyeicosatetraenoic acid is an endothelium-dependent vasoconstrictor in rabbit arteries. Eur. J. Pharmacol. 235:1-7 (1993).
    • (1993) Eur. J. Pharmacol. , vol.235 , pp. 1-7
    • Escalante, B.1    Omata, K.2    Sessa, W.3    Lee, S.G.4    Falck, J.R.5    Schwartzman, M.L.6
  • 24
    • 0028087299 scopus 로고
    • Effects of 17-octadecynoic acid, a suicide-substrate inhibitor of cytochrome P450 fatty acid ω-hydroxylase, on renal function in rats
    • Zou, A.-P., Y.-H. Ma, Z.-H. Sui, P. R. Ortiz de Montellano, J. E. Clark, B. S. S. Masters, and R. J. Roman. Effects of 17-octadecynoic acid, a suicide-substrate inhibitor of cytochrome P450 fatty acid ω-hydroxylase, on renal function in rats. J. Pharmacol. Exp Ther. 268:474-481 (1994).
    • (1994) J. Pharmacol. Exp Ther. , vol.268 , pp. 474-481
    • Zou, A.-P.1    Ma, Y.-H.2    Sui, Z.-H.3    Ortiz De Montellano, P.R.4    Clark, J.E.5    Masters, B.S.S.6    Roman, R.J.7
  • 25
    • 0025214061 scopus 로고
    • Cytochrome P-450 arachidonate metabolites in rat kidney: Characterization and hemodynamic responses
    • Takahashi, K., J. H. Capdevila, A. Karara, J. R. Falck, H. R. Jacobson, and K. F. Badr. Cytochrome P-450 arachidonate metabolites in rat kidney: characterization and hemodynamic responses. Am. J. Physiol. 258:F781-F7S9 (1990).
    • (1990) Am. J. Physiol. , vol.258
    • Takahashi, K.1    Capdevila, J.H.2    Karara, A.3    Falck, J.R.4    Jacobson, H.R.5    Badr, K.F.6
  • 26
    • 0022423216 scopus 로고
    • Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family
    • Fort, P., L. Marty, M. Piechaczyk, S el Sabrouty, C. Dani, P. Jeanteur, and J. M. Blanchard. Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family Nucleic Acids Res. 13:1431-1442 (1985).
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1431-1442
    • Fort, P.1    Marty, L.2    Piechaczyk, M.3    El Sabrouty, S.4    Dani, C.5    Jeanteur, P.6    Blanchard, J.M.7
  • 28
    • 0020288407 scopus 로고
    • Cloning of DNA complementary to rat liver NADPH-eytochrome c (P450) oxidoreductase and cytochrome P450b mRNAs: Evidence that phenobarbital augments transcription of specific genes
    • Gonzalez, F. J., and C. B. Kasper. Cloning of DNA complementary to rat liver NADPH-eytochrome c (P450) oxidoreductase and cytochrome P450b mRNAs: evidence that phenobarbital augments transcription of specific genes. J. Biol Chem. 257:5962-5988 (1982).
    • (1982) J. Biol Chem. , vol.257 , pp. 5962-5988
    • Gonzalez, F.J.1    Kasper, C.B.2
  • 29
    • 0026707675 scopus 로고
    • Sex-specific growth hormone-regulated transcription of the cytoehrome P450 2C11 and 2C12
    • Sundseth, S. S., J. A. Alberta, and D. J. Waxman. Sex-specific growth hormone-regulated transcription of the cytoehrome P450 2C11 and 2C12. J. Biol. Chem. 267:3907-3914 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 3907-3914
    • Sundseth, S.S.1    Alberta, J.A.2    Waxman, D.J.3
  • 30
    • 0000317492 scopus 로고
    • Methods for the elevation of hepatic microsomal mixed function oxidase levels and cytochrome P450
    • Remmer, H., H. Greim, J. B. Schenkman, and R. W. Estabrook. Methods for the elevation of hepatic microsomal mixed function oxidase levels and cytochrome P450. Methods Enzymol. 10:703-708 (1967).
    • (1967) Methods Enzymol. , vol.10 , pp. 703-708
    • Remmer, H.1    Greim, H.2    Schenkman, J.B.3    Estabrook, R.W.4
  • 32
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y., and B. S. S. Masters. Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251:5337-5344 (1976).
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2
  • 33
    • 0019742075 scopus 로고
    • Assay of peroxisomal β-oxidation of fatty acids
    • Lazarow, P. B. Assay of peroxisomal β-oxidation of fatty acids. Methods Enzymol. 72:315-319 (1981).
    • (1981) Methods Enzymol. , vol.72 , pp. 315-319
    • Lazarow, P.B.1
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227:680-685 (1970).
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets:procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets:procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 36
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159 (1987).
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 37
    • 0022555902 scopus 로고
    • Insulin enhances transcription of the tyrosine aminotransferase gene in rat liver
    • Lee, K.-L., K. R. Isham, A. Johnson, A., and F. T. Keene. Insulin enhances transcription of the tyrosine aminotransferase gene in rat liver. Arch. Biochem. Biophys. 248:679-683 (1986).
    • (1986) Arch. Biochem. Biophys. , vol.248 , pp. 679-683
    • Lee, K.-L.1    Isham, K.R.2    A. Johnson, A.3    Keene, F.T.4
  • 38
    • 0001190006 scopus 로고
    • Identification of newly transcribed RNA
    • (F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. D. Seidman, J. A. Smith, and K. Stuhl, eds.). John Wiley and Sons, New York
    • Greenberg, M.E. and T. P. Bender. Identification of newly transcribed RNA, in Current Protocols (F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. D. Seidman, J. A. Smith, and K. Stuhl, eds.). John Wiley and Sons, New York, 4:10.1-4:11 (1994).
    • (1994) Current Protocols
    • Greenberg, M.E.1    Bender, T.P.2
  • 39
    • 0019226759 scopus 로고
    • Phenotypic stability of adult rat hepatocytes in monolayer culture
    • Bissell, D. M., and P. S. Guzelian. Phenotypic stability of adult rat hepatocytes in monolayer culture. Ann. N. Y. Acad. Sci. 349:85-98 (1980).
    • (1980) Ann. N. Y. Acad. Sci. , vol.349 , pp. 85-98
    • Bissell, D.M.1    Guzelian, P.S.2
  • 40
    • 0021355534 scopus 로고
    • Induction of cytochrome P-450 by glucocorticoids in rat liver. I. Evidence that glucocorticoids and pregnenolone 16α-carbonitrile regulate de novo synthesis of a common form of cytochrome P-450 in cultures of adult rat hepatocytes and in the liver in vivo
    • Schuetz, E. G., S. A. Wrighton, J. L. Barwick, and P. S. Guzelian. Induction of cytochrome P-450 by glucocorticoids in rat liver. I. Evidence that glucocorticoids and pregnenolone 16α-carbonitrile regulate de novo synthesis of a common form of cytochrome P-450 in cultures of adult rat hepatocytes and in the liver in vivo. J. Biol. Chem. 259:1999-2006 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 1999-2006
    • Schuetz, E.G.1    Wrighton, S.A.2    Barwick, J.L.3    Guzelian, P.S.4
  • 41
    • 0029076781 scopus 로고
    • Regulation of the Ah gene battery via Ah receptor-dependent and independent processes in cultured adult rat hepatocytes
    • Xiao, G.-H., J. A. Pinaire, A. D. Rodrigues, and R. A. Prough. Regulation of the Ah gene battery via Ah receptor-dependent and independent processes in cultured adult rat hepatocytes. Drug Metab. Dispos. 23: 642-650 (1995).
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 642-650
    • Xiao, G.-H.1    Pinaire, J.A.2    Rodrigues, A.D.3    Prough, R.A.4
  • 42
    • 0001742515 scopus 로고
    • Dehydroepiandrosterone induces enzymes that permit thermogenesis and decrease metabolic efficiency
    • (H. Lardy and F. Stratman, eds.). Elsevier Science, New York
    • Lardy, H., C.-Y. Su, N. Kneer, and S. Wielgus. Dehydroepiandrosterone induces enzymes that permit thermogenesis and decrease metabolic efficiency, in Hormones, Thermogenesis, and Obesity (H. Lardy and F. Stratman, eds.). Elsevier Science, New York, 415-426 (1989).
    • (1989) Hormones, Thermogenesis, and Obesity , pp. 415-426
    • Lardy, H.1    Su, C.-Y.2    Kneer, N.3    Wielgus, S.4
  • 43
    • 0024596341 scopus 로고
    • Hypophysectomy differentially alters P-450 protein levels and enzyme activities in rat liver: Pituitary control of hepatic NADPH cytochrome P-450 reductase
    • Waxman, D. J., J J. Morrissey, and G. A. LeBlanc. Hypophysectomy differentially alters P-450 protein levels and enzyme activities in rat liver: pituitary control of hepatic NADPH cytochrome P-450 reductase Mol. Pharmacol. 35:519-525 (1989).
    • (1989) Mol. Pharmacol. , vol.35 , pp. 519-525
    • Waxman, D.J.1    Morrissey, J.J.2    LeBlanc, G.A.3
  • 44
    • 0027460223 scopus 로고
    • Role of thyroid state on induction by ciprofibrate of laurate hydroxylase and peroxisomal enzymes in rat liver microsomes
    • Pacot, C., M. Charmoillaux, H. Goudonnet, R. C. Truehot, and N. Latruffe. Role of thyroid state on induction by ciprofibrate of laurate hydroxylase and peroxisomal enzymes in rat liver microsomes. Biochem Pharmacol. 45:1437-1446 (1993).
    • (1993) Biochem Pharmacol. , vol.45 , pp. 1437-1446
    • Pacot, C.1    Charmoillaux, M.2    Goudonnet, H.3    Truehot, R.C.4    Latruffe, N.5
  • 46
    • 0026093207 scopus 로고
    • Tyromimetic effect of peroxisomal proliferators in rat liver
    • Hertz, R., R. Aurbach, T. Hashimoto, and J. Bar-Tana. Tyromimetic effect of peroxisomal proliferators in rat liver. Biochem. J. 274:745-751 (1991).
    • (1991) Biochem. J. , vol.274 , pp. 745-751
    • Hertz, R.1    Aurbach, R.2    Hashimoto, T.3    Bar-Tana, J.4
  • 47
    • 0025000063 scopus 로고
    • Pretranslational control by thyroid hormone of rat liver steroid 5α-reductase and comparison to the thyroid dependence of two growth hormone-regulated CYP2C mRNAs
    • Ram, P. A., and D. J. Waxman. Pretranslational control by thyroid hormone of rat liver steroid 5α-reductase and comparison to the thyroid dependence of two growth hormone-regulated CYP2C mRNAs. J. Biol. Chem. 265:19223-19229 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 19223-19229
    • Ram, P.A.1    Waxman, D.J.2
  • 48
    • 0025870577 scopus 로고
    • Difference in the susceptibility of two phenobarbital-inducible forms, P450IIB1 and P450IIB2, to thyroid hormone and growth hormone-induced suppression in rat liver: Phenobarbital-inducible P450IIB2 suppression by thyroid hormone acting directly, but not through the pituitary system
    • Murayama, N., M. Shimada, Y. Yamazoe, and R. Kato. Difference in the susceptibility of two phenobarbital-inducible forms, P450IIB1 and P450IIB2, to thyroid hormone and growth hormone-induced suppression in rat liver: phenobarbital-inducible P450IIB2 suppression by thyroid hormone acting directly, but not through the pituitary system. Mol. Pharmacol. 39:811-817 (1991).
    • (1991) Mol. Pharmacol. , vol.39 , pp. 811-817
    • Murayama, N.1    Shimada, M.2    Yamazoe, Y.3    Kato, R.4
  • 49
    • 0027255726 scopus 로고
    • Induction of peroxisomal fatty acid β-oxidation and liver fatty acid-binding protein by peroxisome proliferators
    • Kaikaus, R. M., W. K. Chan, N. Lysenko, R. Ray, P. R. Ortiz de Montellano, and N. M. Bass. Induction of peroxisomal fatty acid β-oxidation and liver fatty acid-binding protein by peroxisome proliferators. J. Biol. Chem 268:9593-9603 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 9593-9603
    • Kaikaus, R.M.1    Chan, W.K.2    Lysenko, N.3    Ray, R.4    Ortiz De Montellano, P.R.5    Bass, N.M.6
  • 50
    • 0025801795 scopus 로고
    • Effect of cytochrome P450 arachidonate metabolites on ion transport in rabbit kidney loop of Henle
    • Escalante, B., D. Erlij, J. R. Falck, and J. C. McGiff. Effect of cytochrome P450 arachidonate metabolites on ion transport in rabbit kidney loop of Henle. Science (Washington D. C.) 251:799-802 (1991).
    • (1991) Science (Washington D. C.) , vol.251 , pp. 799-802
    • Escalante, B.1    Erlij, D.2    Falck, J.R.3    McGiff, J.C.4
  • 52
    • 0026781117 scopus 로고
    • Thyroid hormone inhibits thyrotropin gene expression via a position-independent negative L-thiodothyronine-responsive element
    • Carr, F. E., L. L. Kaseem, and N. C. Wong. Thyroid hormone inhibits thyrotropin gene expression via a position-independent negative L-thiodothyronine-responsive element. J. Biol. Chem. 267:18689-18694 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 18689-18694
    • Carr, F.E.1    Kaseem, L.L.2    Wong, N.C.3
  • 53
    • 0028025348 scopus 로고
    • Characteristics of a negative thyroid hormone response element
    • Carr, F. E., and N. C. W. Wong. Characteristics of a negative thyroid hormone response element. J. Biol. Chem. 269:4175-4179 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4175-4179
    • Carr, F.E.1    Wong, N.C.W.2
  • 54
    • 0029053917 scopus 로고
    • Thyroid hormone receptor homodimers can function as ligand-sensitive repressors
    • Piedrafita, F. J., I. Bendik, M. A. Ortiz, and M. Pfahl. Thyroid hormone receptor homodimers can function as ligand-sensitive repressors. Mol. Endocrinol. 9:563-578 (1995).
    • (1995) Mol. Endocrinol. , vol.9 , pp. 563-578
    • Piedrafita, F.J.1    Bendik, I.2    Ortiz, M.A.3    Pfahl, M.4
  • 55
    • 0028355391 scopus 로고
    • Peroxisome proliferator-activated receptors: Finding the orphan a home
    • Green, S., and W. Wahli. Peroxisome proliferator-activated receptors: finding the orphan a home. Mol. Cell. Endocrinol. 100:149-153 (1994).
    • (1994) Mol. Cell. Endocrinol. , vol.100 , pp. 149-153
    • Green, S.1    Wahli, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.