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Volumn 10, Issue 2, 2005, Pages 1678-1692

Kinase/phosphatase regulation of CYP7A1

Author keywords

AMP activated protein kinase (AMPK); Bile Acids; Biochemistry; c Jun N terminal kinase (JNK); Cross Talk; CYP7A1; Extracellular regulated kinase (ERK); Review; Signal Transduction

Indexed keywords

BILE ACID; CHOLESTEROL 7ALPHA MONOOXYGENASE; CYTOCHROME P450 7A1; CYTOCHROME P450 ISOENZYME; HEPATOCYTE NUCLEAR FACTOR 4ALPHA; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PHOSPHOTRANSFERASE; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 17244375261     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1652     Document Type: Article
Times cited : (7)

References (172)
  • 1
    • 0030819160 scopus 로고    scopus 로고
    • Cell-cell interactions in the regulation of the expression of hepatic enzymes
    • Gebhardt R. & F. Gaunitz: Cell-cell interactions in the regulation of the expression of hepatic enzymes. Cell Biol Toxicol 13, 263-273 (1997)
    • (1997) Cell Biol Toxicol , vol.13 , pp. 263-273
    • Gebhardt, R.1    Gaunitz, F.2
  • 2
    • 0031595548 scopus 로고    scopus 로고
    • Cholesterol 7alpha-hydroxylase (CYP7A): Patterns of messenger RNA expression during rat liver development
    • Massimi M., S. R. Lear, S. L. Huling, A. L. Jones & S. K. Erickson: Cholesterol 7alpha-hydroxylase (CYP7A): patterns of messenger RNA expression during rat liver development. Hepatology 28, 1064-1072 (1998)
    • (1998) Hepatology , vol.28 , pp. 1064-1072
    • Massimi, M.1    Lear, S.R.2    Huling, S.L.3    Jones, A.L.4    Erickson, S.K.5
  • 3
    • 0028278187 scopus 로고
    • Identification and characterization of a putative bile acid-responsive element in cholesterol 7 alpha-hydroxylase gene promoter
    • Chiang J. Y. & D. Stroup: Identification and characterization of a putative bile acid-responsive element in cholesterol 7 alpha-hydroxylase gene promoter. J Biol Chem 269, 17502-17507 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 17502-17507
    • Chiang, J.Y.1    Stroup, D.2
  • 4
    • 0028868818 scopus 로고
    • Hormonal regulation of the cholesterol 7 alpha-hydroxylase gene (CYP7)
    • Crestani M., D. Stroup & J. Y. Chiang: Hormonal regulation of the cholesterol 7 alpha-hydroxylase gene (CYP7). J Lipid Res 36, 2419-2432 (1995)
    • (1995) J Lipid Res , vol.36 , pp. 2419-2432
    • Crestani, M.1    Stroup, D.2    Chiang, J.Y.3
  • 5
    • 0029834337 scopus 로고    scopus 로고
    • Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene (CYP7A) in HepG2 cells
    • Wang D. P., D. Stroup, M. Marrapodi, M. Crestani, G. Galli & J. Y. Chiang: Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene (CYP7A) in HepG2 cells. J Lipid Res 37, 1831-1841 (1996)
    • (1996) J Lipid Res , vol.37 , pp. 1831-1841
    • Wang, D.P.1    Stroup, D.2    Marrapodi, M.3    Crestani, M.4    Galli, G.5    Chiang, J.Y.6
  • 6
    • 0025269939 scopus 로고
    • Cloning and regulation of cholesterol 7alpha-hydroxylase, the rate-limiting enzyme in bile acid biosynthesis
    • Jelinek D. F., S. Andersson, C. A. Slaughter & D. W. Russell: Cloning and regulation of cholesterol 7alpha-hydroxylase, the rate-limiting enzyme in bile acid biosynthesis. J Biol Chem 265, 8190-8197 (1990)
    • (1990) J Biol Chem , vol.265 , pp. 8190-8197
    • Jelinek, D.F.1    Andersson, S.2    Slaughter, C.A.3    Russell, D.W.4
  • 7
    • 0025353861 scopus 로고
    • Regulation of cholesterol 7 alpha-hydroxylase in the liver. Cloning, sequencing, and regulation of cholesterol 7 alpha-hydroxylase mRNA
    • Li Y. C., D. P. Wang & J. Y. Chiang: Regulation of cholesterol 7 alpha-hydroxylase in the liver. Cloning, sequencing, and regulation of cholesterol 7 alpha-hydroxylase mRNA. J Biol Chem 265, 12012-12019 (1990)
    • (1990) J Biol Chem , vol.265 , pp. 12012-12019
    • Li, Y.C.1    Wang, D.P.2    Chiang, J.Y.3
  • 8
    • 0025046139 scopus 로고
    • Hepatic P-450 cholesterol 7alpha-hydroxylase. Regulation in vivo at the protein and mRNA level in response to mevalonate, diurnal rhythm, and bile acid feedback
    • Sundseth S. S. & D. J. Waxman: Hepatic P-450 cholesterol 7alpha-hydroxylase. Regulation in vivo at the protein and mRNA level in response to mevalonate, diurnal rhythm, and bile acid feedback. J Biol Chem 265, 15090-15095 (1990)
    • (1990) J Biol Chem , vol.265 , pp. 15090-15095
    • Sundseth, S.S.1    Waxman, D.J.2
  • 9
    • 0027242111 scopus 로고
    • Transcriptional regulation of the gene encoding cholesterol 7 alpha- hydroxylase in the rat
    • published erratum appears in Gene 1994 Apr 20;141(2):309-10
    • Hoekman M. F., J. M. Rientjes, J. Twisk, R. J. Planta, H. M. Princen & W. H. Mager: Transcriptional regulation of the gene encoding cholesterol 7 alpha- hydroxylase in the rat [published erratum appears in Gene 1994 Apr 20;141(2):309-10]. Gene 130, 217-223 (1993)
    • (1993) Gene , vol.130 , pp. 217-223
    • Hoekman, M.F.1    Rientjes, J.M.2    Twisk, J.3    Planta, R.J.4    Princen, H.M.5    Mager, W.H.6
  • 10
    • 0028239336 scopus 로고
    • Effects of bile acids and steroid/thyroid hormones on the expression of cholesterol 7 alpha-hydroxylase mRNA and the CYP7 gene in HepG2 cells
    • Crestani M., W. G. Karam & J. Y. Chiang: Effects of bile acids and steroid/thyroid hormones on the expression of cholesterol 7 alpha-hydroxylase mRNA and the CYP7 gene in HepG2 cells. Biochem Biophys Res Commun 198, 546-553 (1994)
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 546-553
    • Crestani, M.1    Karam, W.G.2    Chiang, J.Y.3
  • 11
    • 0028233386 scopus 로고
    • Regulation of cholesterol 7 alpha-hydroxylase gene expression in Hep-G2 cells. Effect of serum, bile salts, and coordinate and noncoordinate regulation with other sterol-responsive genes
    • Taniguchi T., J. Chen & A. D. Cooper: Regulation of cholesterol 7 alpha-hydroxylase gene expression in Hep-G2 cells. Effect of serum, bile salts, and coordinate and noncoordinate regulation with other sterol-responsive genes. J Biol Chem 269, 10071-10078 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 10071-10078
    • Taniguchi, T.1    Chen, J.2    Cooper, A.D.3
  • 12
    • 0029160030 scopus 로고
    • Adenovirus-mediated transfer of a gene encoding cholesterol 7 alpha- hydroxylase into hamsters increases hepatic enzyme activity and reduces plasma total and low density lipoprotein cholesterol
    • Spady D. K., J. A. Cuthbert, M. N. Willard & R. S. Meidell: Adenovirus-mediated transfer of a gene encoding cholesterol 7 alpha- hydroxylase into hamsters increases hepatic enzyme activity and reduces plasma total and low density lipoprotein cholesterol. J Clin Invest 96, 700-709 (1995)
    • (1995) J Clin Invest , vol.96 , pp. 700-709
    • Spady, D.K.1    Cuthbert, J.A.2    Willard, M.N.3    Meidell, R.S.4
  • 13
    • 0031023181 scopus 로고    scopus 로고
    • Characterization of hepatic-specific regulatory elements in the promoter region of the human cholesterol 7alpha-hydroxylase gene
    • Cooper A. D., J. Chen, M. J. Botelho-Yetkinler, Y. Cao, T. Taniguchi & B. Levy-Wilson: Characterization of hepatic-specific regulatory elements in the promoter region of the human cholesterol 7alpha-hydroxylase gene. J Biol Chem 272, 3444-3452 (1997)
    • (1997) J Biol Chem , vol.272 , pp. 3444-3452
    • Cooper, A.D.1    Chen, J.2    Botelho-Yetkinler, M.J.3    Cao, Y.4    Taniguchi, T.5    Levy-Wilson, B.6
  • 14
  • 15
    • 0028961238 scopus 로고
    • Structural aspects of bile acids involved in the regulation of cholesterol 7 alpha-hydroxylase and sterol 27-hydroxylase
    • Twisk J., M. F. Hoekman, L. M. Muller, T. Iida, T. Tamaru, A. Ijzerman, W. H. Mager & H. M. Princen: Structural aspects of bile acids involved in the regulation of cholesterol 7 alpha-hydroxylase and sterol 27-hydroxylase. Eur J Biochem 228, 596-604 (1995)
    • (1995) Eur J Biochem , vol.228 , pp. 596-604
    • Twisk, J.1    Hoekman, M.F.2    Muller, L.M.3    Iida, T.4    Tamaru, T.5    Ijzerman, A.6    Mager, W.H.7    Princen, H.M.8
  • 16
    • 0030870025 scopus 로고    scopus 로고
    • Identification of a bile acid response element in the cholesterol 7 alpha-hydroxylase gene CYP7A
    • Stroup D., M. Crestani & J. Y. Chiang: Identification of a bile acid response element in the cholesterol 7 alpha-hydroxylase gene CYP7A. Am J Physiol 273, G508-517 (1997)
    • (1997) Am J Physiol , vol.273
    • Stroup, D.1    Crestani, M.2    Chiang, J.Y.3
  • 17
    • 17244379921 scopus 로고
    • The Bile Acid Reponse of Cholesterol 7alpha-hydroxylase Gene Proximal Promoter May Not be Mediated Through One Element
    • Stroup D. & J. Y. L. Chiang: The Bile Acid Reponse of Cholesterol 7alpha-hydroxylase Gene Proximal Promoter May Not be Mediated Through One Element. Advances in Gene Technology: Protein Engineering and Structural Biology 6, 76 (1995)
    • (1995) Advances in Gene Technology: Protein Engineering and Structural Biology , vol.6 , pp. 76
    • Stroup, D.1    Chiang, J.Y.L.2
  • 18
    • 0033954261 scopus 로고    scopus 로고
    • HNF4 and COUP-TFII interact to modulate transcription of the cholesterol 7alpha-hydroxylase gene (CYP7A1)
    • Stroup D. & J. Y. Chiang: HNF4 and COUP-TFII interact to modulate transcription of the cholesterol 7alpha-hydroxylase gene (CYP7A1). J Lipid Res 41, 1-11 (2000)
    • (2000) J Lipid Res , vol.41 , pp. 1-11
    • Stroup, D.1    Chiang, J.Y.2
  • 19
    • 0032501401 scopus 로고    scopus 로고
    • Basic transcription element binding protein (BTEB) transactivates the cholesterol 7 alpha-hydroxylase gene (CYP7A)
    • Foti D., D. Stroup & J. Y. Chiang: Basic transcription element binding protein (BTEB) transactivates the cholesterol 7 alpha-hydroxylase gene (CYP7A). Biochem Biophys Res Commun 253, 109-113 (1998)
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 109-113
    • Foti, D.1    Stroup, D.2    Chiang, J.Y.3
  • 20
    • 0033536005 scopus 로고    scopus 로고
    • CPF: An orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene
    • Nitta M., S. Ku, C. Brown, A. Y. Okamoto & B. Shan: CPF: an orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene. Proc Natl Acad Sci U S A 96, 6660-6665 (1999)
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6660-6665
    • Nitta, M.1    Ku, S.2    Brown, C.3    Okamoto, A.Y.4    Shan, B.5
  • 21
    • 0036668184 scopus 로고    scopus 로고
    • Bile acid regulation of gene expression: Roles of nuclear hormone receptors
    • Chiang J. Y.: Bile acid regulation of gene expression: roles of nuclear hormone receptors. Endocr Rev 23, 443-463 (2002)
    • (2002) Endocr Rev , vol.23 , pp. 443-463
    • Chiang, J.Y.1
  • 22
    • 0037790917 scopus 로고    scopus 로고
    • The enzymes, regulation, and genetics of bile acid synthesis
    • Russell D. W.: The enzymes, regulation, and genetics of bile acid synthesis. Annu Rev Biochem 72, 137-174 (2003)
    • (2003) Annu Rev Biochem , vol.72 , pp. 137-174
    • Russell, D.W.1
  • 23
    • 1242269851 scopus 로고    scopus 로고
    • Regulation of bile acid synthesis: Pathways, nuclear receptors, and mechanisms
    • Chiang J. Y.: Regulation of bile acid synthesis: pathways, nuclear receptors, and mechanisms. J Hepatol 40, 539-551 (2004)
    • (2004) J Hepatol , vol.40 , pp. 539-551
    • Chiang, J.Y.1
  • 24
    • 0029666289 scopus 로고    scopus 로고
    • Disruption of cholesterol 7alpha-hydroxylase gene in mice. I. Postnatal lethality reversed by bile acid and vitamin supplementation
    • Ishibashi S., M. Schwarz, P. K. Frykman, J. Herz & D. W. Russell: Disruption of cholesterol 7alpha-hydroxylase gene in mice. I. Postnatal lethality reversed by bile acid and vitamin supplementation. J Biol Chem 271, 18017-18023 (1996)
    • (1996) J Biol Chem , vol.271 , pp. 18017-18023
    • Ishibashi, S.1    Schwarz, M.2    Frykman, P.K.3    Herz, J.4    Russell, D.W.5
  • 25
    • 0033386688 scopus 로고    scopus 로고
    • Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene CYP7B1
    • Wu Z., K. O. Martin, N. B. Javitt & J. Y. Chiang: Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene CYP7B1. J Lipid Res 40, 2195-2203 (1999)
    • (1999) J Lipid Res , vol.40 , pp. 2195-2203
    • Wu, Z.1    Martin, K.O.2    Javitt, N.B.3    Chiang, J.Y.4
  • 26
    • 0034595650 scopus 로고    scopus 로고
    • Expression cloning of an oxysterol 7alpha-hydroxylase selective for 24-hydroxycholesterol
    • Li-Hawkins J., E. G. Lund, A. D. Bronson & D. W. Russell: Expression cloning of an oxysterol 7alpha-hydroxylase selective for 24-hydroxycholesterol. J Biol Chem 275, 16543-16549 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 16543-16549
    • Li-Hawkins, J.1    Lund, E.G.2    Bronson, A.D.3    Russell, D.W.4
  • 28
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P450 sterol 27-hydroxylase, a bile acid biosynthetic enzyme
    • Anderson S., D. L. Davis, H. Dahlback, H. Jornvall & D. W. Russell: Cloning, structure, and expression of the mitochondrial cytochrome P450 sterol 27-hydroxylase, a bile acid biosynthetic enzyme. J Biol Chem 264, 8222-8229 (1989)
    • (1989) J Biol Chem , vol.264 , pp. 8222-8229
    • Anderson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4    Russell, D.W.5
  • 29
    • 0028003885 scopus 로고
    • Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1alpha- hydroxylation of 25-hydroxyvitamin D3
    • Axen E., H. Postlind, H. Sjoberg & K. Wikvall: Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1alpha- hydroxylation of 25-hydroxyvitamin D3. Proc Natl Acad Sci USA 91, 10014-10018 (1994)
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10014-10018
    • Axen, E.1    Postlind, H.2    Sjoberg, H.3    Wikvall, K.4
  • 30
    • 0344011516 scopus 로고    scopus 로고
    • Ontogenesis and regulation of cholesterol metabolism in the central nervous system of the mouse
    • Quan G., C. Xie, J. M. Dietschy & S. D. Turley: Ontogenesis and regulation of cholesterol metabolism in the central nervous system of the mouse. Brain Res Dev Brain Res 146, 87-98 (2003)
    • (2003) Brain Res Dev Brain Res , vol.146 , pp. 87-98
    • Quan, G.1    Xie, C.2    Dietschy, J.M.3    Turley, S.D.4
  • 31
    • 0035914368 scopus 로고    scopus 로고
    • Antiepileptic drugs increase plasma levels of 4beta-hydroxycholesterol in humans: Evidence for involvement of cytochrome p450 3A4
    • Bodin K., L. Bretillon, Y. Aden, L. Bertilsson, U. Broome, C. Einarsson & U. Diczfalusy: Antiepileptic drugs increase plasma levels of 4beta-hydroxycholesterol in humans: evidence for involvement of cytochrome p450 3A4. J Biol Chem 276, 38685-38689 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 38685-38689
    • Bodin, K.1    Bretillon, L.2    Aden, Y.3    Bertilsson, L.4    Broome, U.5    Einarsson, C.6    Diczfalusy, U.7
  • 32
    • 0034762627 scopus 로고    scopus 로고
    • Alternate pathways of bile acid synthesis in the cholesterol 7alpha-hydroxylase knockout mouse are not upregulated by either cholesterol or cholestyramine feeding
    • Schwarz M., D. W. Russell, J. M. Dietschy & S. D. Turley: Alternate pathways of bile acid synthesis in the cholesterol 7alpha-hydroxylase knockout mouse are not upregulated by either cholesterol or cholestyramine feeding. J Lipid Res 42, 1594-1603 (2001)
    • (2001) J Lipid Res , vol.42 , pp. 1594-1603
    • Schwarz, M.1    Russell, D.W.2    Dietschy, J.M.3    Turley, S.D.4
  • 33
    • 0037178894 scopus 로고    scopus 로고
    • Differences in the regulation of the classical and the alternative pathway for bile acid synthesis in human liver. No coordinate regulation of CYP7A1 and CYP27A1
    • Bjorkhem I., Z. Araya, M. Rudling, B. Angelin, C. Einarsson & K. Wikvall: Differences in the regulation of the classical and the alternative pathway for bile acid synthesis in human liver. No coordinate regulation of CYP7A1 and CYP27A1. J Biol Chem 277, 26804-26807 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 26804-26807
    • Bjorkhem, I.1    Araya, Z.2    Rudling, M.3    Angelin, B.4    Einarsson, C.5    Wikvall, K.6
  • 34
    • 1242342009 scopus 로고    scopus 로고
    • Cholesterol feeding of mice expressing cholesterol 7alpha-hydroxylase increases bile acid pool size despite decreased enzyme activity
    • Tiemann M., Z. Han, R. Soccio, J. Bollineni, S. Shefer, E. Sehayek & J. L. Breslow: Cholesterol feeding of mice expressing cholesterol 7alpha-hydroxylase increases bile acid pool size despite decreased enzyme activity. Proc Natl Acad Sci U S A 101, 1846-1851 (2004)
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1846-1851
    • Tiemann, M.1    Han, Z.2    Soccio, R.3    Bollineni, J.4    Shefer, S.5    Sehayek, E.6    Breslow, J.L.7
  • 35
    • 0028068796 scopus 로고
    • Atherosclerosis and sterol 27-hydroxylase: Evidence for a role of this enzyme in elimination of cholesterol from human macrophages
    • Bjorkhem I., O. Andersson, U. Diczfalusy, B. Sevastik, R.-j. Xiu, C. Duan & E. Lund: Atherosclerosis and sterol 27-hydroxylase: evidence for a role of this enzyme in elimination of cholesterol from human macrophages. Proc Natl Acad Sci USA 91, 8592-8596 (1994)
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8592-8596
    • Bjorkhem, I.1    Andersson, O.2    Diczfalusy, U.3    Sevastik, B.4    Xiu, R.-J.5    Duan, C.6    Lund, E.7
  • 36
    • 0034595445 scopus 로고    scopus 로고
    • Disruption of the oxysterol 7alpha-hydroxylase gene in mice
    • Li-Hawkins J., E. G. Lund, S. D. Turley & D. W. Russell: Disruption of the oxysterol 7alpha-hydroxylase gene in mice. J Biol Chem 275, 16536-16542 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 16536-16542
    • Li-Hawkins, J.1    Lund, E.G.2    Turley, S.D.3    Russell, D.W.4
  • 38
    • 0034671509 scopus 로고    scopus 로고
    • Disruption of the sterol 27-hydroxylase gene in mice results in hepatomegaly and hypertriglyceridemia. Reversal by cholic acid feeding
    • Repa J. J., E. G. Lund, J. D. Horton, E. Leitersdorf, D. W. Russell, J. M. Dietschy & S. D. Turley: Disruption of the sterol 27-hydroxylase gene in mice results in hepatomegaly and hypertriglyceridemia. Reversal by cholic acid feeding. J Biol Chem 275, 39685-39692 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 39685-39692
    • Repa, J.J.1    Lund, E.G.2    Horton, J.D.3    Leitersdorf, E.4    Russell, D.W.5    Dietschy, J.M.6    Turley, S.D.7
  • 39
    • 2342573009 scopus 로고    scopus 로고
    • The role of corepressors in transcriptional regulation by nuclear hormone receptors
    • Privalsky M. L.: The role of corepressors in transcriptional regulation by nuclear hormone receptors. Annu Rev Physiol 66, 315-360 (2004)
    • (2004) Annu Rev Physiol , vol.66 , pp. 315-360
    • Privalsky, M.L.1
  • 40
    • 3242888465 scopus 로고    scopus 로고
    • Gene silencing by nuclear orphan receptors
    • Zhang Y. & M. L. Dufau: Gene silencing by nuclear orphan receptors. Vitam Horm 68, 1-48 (2004)
    • (2004) Vitam Horm , vol.68 , pp. 1-48
    • Zhang, Y.1    Dufau, M.L.2
  • 41
    • 0035141324 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis
    • Hayhurst G. P., Y. H. Lee, G. Lambert, J. M. Ward & F. J. Gonzalez: Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis. Mol Cell Biol 21, 1393-1403. (2001)
    • (2001) Mol Cell Biol , vol.21 , pp. 1393-1403
    • Hayhurst, G.P.1    Lee, Y.H.2    Lambert, G.3    Ward, J.M.4    Gonzalez, F.J.5
  • 42
    • 0030695445 scopus 로고    scopus 로고
    • The maturity-onset diabetes of the young (MODY1) transcription factor HNF4alpha regulates expression of genes required for glucose transport and metabolism
    • Stoffel M. & S. A. Duncan: The maturity-onset diabetes of the young (MODY1) transcription factor HNF4alpha regulates expression of genes required for glucose transport and metabolism. Proc Natl Acad Sci U S A 94, 13209-13214 (1997)
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13209-13214
    • Stoffel, M.1    Duncan, S.A.2
  • 43
    • 0033556695 scopus 로고    scopus 로고
    • Extinction of alpha1-antitrypsin expression in cell hybrids is independent of HNF1alpha and HNF4 and involves both promoter and internal DNA sequences
    • Bulla G. A.: Extinction of alpha1-antitrypsin expression in cell hybrids is independent of HNF1alpha and HNF4 and involves both promoter and internal DNA sequences. Nucleic Acids Res 27, 1190-1197 (1999)
    • (1999) Nucleic Acids Res , vol.27 , pp. 1190-1197
    • Bulla, G.A.1
  • 44
    • 0034213689 scopus 로고    scopus 로고
    • Fatty acyl-CoAs inhibit retinoic acid-induced apoptosis in Hep3B cells
    • Wan Y. J., Y. Cai, C. Cowan & T. R. Magee: Fatty acyl-CoAs inhibit retinoic acid-induced apoptosis in Hep3B cells. Cancer Lett 154, 19-27 (2000)
    • (2000) Cancer Lett , vol.154 , pp. 19-27
    • Wan, Y.J.1    Cai, Y.2    Cowan, C.3    Magee, T.R.4
  • 45
    • 0030877342 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4
    • Viollet B., A. Kahn & M. Raymondjean: Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4. Mol Cell Biol 17, 4208-4219 (1997)
    • (1997) Mol Cell Biol , vol.17 , pp. 4208-4219
    • Viollet, B.1    Kahn, A.2    Raymondjean, M.3
  • 47
    • 0033324782 scopus 로고    scopus 로고
    • The phosphoenolpyruvate carboxykinase gene glucocorticoid response unit: Identification of the functional domains of accessory factors HNF3 beta (hepatic nuclear factor-3 beta) and HNF4 and the necessity of proper alignment of their cognate binding sites
    • Wang J. C., P. E. Stromstedt, T. Sugiyama & D. K. Granner: The phosphoenolpyruvate carboxykinase gene glucocorticoid response unit: identification of the functional domains of accessory factors HNF3 beta (hepatic nuclear factor-3 beta) and HNF4 and the necessity of proper alignment of their cognate binding sites. Mol Endocrinol 13, 604-618 (1999)
    • (1999) Mol Endocrinol , vol.13 , pp. 604-618
    • Wang, J.C.1    Stromstedt, P.E.2    Sugiyama, T.3    Granner, D.K.4
  • 48
    • 0032553439 scopus 로고    scopus 로고
    • SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4
    • Wang J. C., J. M. Stafford & D. K. Granner: SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. J Biol Chem 273, 30847-30850 (1998)
    • (1998) J Biol Chem , vol.273 , pp. 30847-30850
    • Wang, J.C.1    Stafford, J.M.2    Granner, D.K.3
  • 49
    • 0034964730 scopus 로고    scopus 로고
    • Maturity-Onset Diabetes of the Young Type 1 (MODY1)-Associated Mutations R154X and E276Q in Hepatocyte Nuclear Factor 4alpha (HNF4alpha) Gene Impair Recruitment of p300, a Key Transcriptional Coactivator
    • Eeckhoute J., P. Formstecher & B. Laine: Maturity-Onset Diabetes of the Young Type 1 (MODY1)-Associated Mutations R154X and E276Q in Hepatocyte Nuclear Factor 4alpha (HNF4alpha) Gene Impair Recruitment of p300, a Key Transcriptional Coactivator. Mol Endocrinol 15, 1200-1210. (2001)
    • (2001) Mol Endocrinol , vol.15 , pp. 1200-1210
    • Eeckhoute, J.1    Formstecher, P.2    Laine, B.3
  • 51
    • 0032941790 scopus 로고    scopus 로고
    • Functional study of the E276Q mutant hepatocyte nuclear factor-4alpha found in type 1 maturity-onset diabetes of the young: Impaired synergy with chicken ovalbumin upstream promoter transcription factor II on the hepatocyte nuclear factor-1 promoter
    • Suaud L., Y. Hemimou, P. Formstecher & B. Laine: Functional study of the E276Q mutant hepatocyte nuclear factor-4alpha found in type 1 maturity-onset diabetes of the young: impaired synergy with chicken ovalbumin upstream promoter transcription factor II on the hepatocyte nuclear factor-1 promoter. Diabetes 48, 1162-1167. (1999)
    • (1999) Diabetes , vol.48 , pp. 1162-1167
    • Suaud, L.1    Hemimou, Y.2    Formstecher, P.3    Laine, B.4
  • 54
    • 0035834771 scopus 로고    scopus 로고
    • Transcriptional regulation of the human sterol 12alpha-hydroxylase gene (CYP8B1): Roles of heaptocyte nuclear factor 4alpha in mediating bile acid repression
    • Zhang M. & J. Y. Chiang: Transcriptional regulation of the human sterol 12alpha-hydroxylase gene (CYP8B1): roles of heaptocyte nuclear factor 4alpha in mediating bile acid repression. J Biol Chem 276, 41690-41699 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 41690-41699
    • Zhang, M.1    Chiang, J.Y.2
  • 55
    • 0035102247 scopus 로고    scopus 로고
    • Developmental expression patterns of FTZ-F1 homologues in zebrafish (Danio rerio)
    • von Hofsten J., I. Jones, J. Karlsson & P. E. Olsson: Developmental expression patterns of FTZ-F1 homologues in zebrafish (Danio rerio). Gen Comp Endocrinol 121, 146-155. (2001)
    • (2001) Gen Comp Endocrinol , vol.121 , pp. 146-155
    • Von Hofsten, J.1    Jones, I.2    Karlsson, J.3    Olsson, P.E.4
  • 56
    • 2342459110 scopus 로고    scopus 로고
    • LRH-1: An orphan nuclear receptor involved in development, metabolism and steroidogenesis
    • Fayard E., J. Auwerx & K. Schoonjans: LRH-1: an orphan nuclear receptor involved in development, metabolism and steroidogenesis. Trends Cell Biol 14, 250-260 (2004)
    • (2004) Trends Cell Biol , vol.14 , pp. 250-260
    • Fayard, E.1    Auwerx, J.2    Schoonjans, K.3
  • 57
    • 0033597891 scopus 로고    scopus 로고
    • Activation of the promoter of the orphan receptor SHP by orphan receptors that bind DNA as monomers
    • Lee Y. K., K. L. Parker, H. S. Choi & D. D. Moore: Activation of the promoter of the orphan receptor SHP by orphan receptors that bind DNA as monomers. J Biol Chem 274, 20869-20873 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 20869-20873
    • Lee, Y.K.1    Parker, K.L.2    Choi, H.S.3    Moore, D.D.4
  • 58
    • 0035909521 scopus 로고    scopus 로고
    • HBV integrants of hepatocellular carcinoma cell lines contain an active enhancer
    • Shamay M., R. Agami & Y. Shaul: HBV integrants of hepatocellular carcinoma cell lines contain an active enhancer. Oncogene 20, 6811-6819. (2001)
    • (2001) Oncogene , vol.20 , pp. 6811-6819
    • Shamay, M.1    Agami, R.2    Shaul, Y.3
  • 59
    • 0032724603 scopus 로고    scopus 로고
    • The nuclear receptor fetoprotein transcription factor is coexpressed with its target gene HNF-3beta in the developing murine liver, intestine and pancreas
    • Rausa F. M., L. Galarneau, L. Belanger & R. H. Costa: The nuclear receptor fetoprotein transcription factor is coexpressed with its target gene HNF-3beta in the developing murine liver, intestine and pancreas. Mech Dev 89, 185-188 (1999)
    • (1999) Mech Dev , vol.89 , pp. 185-188
    • Rausa, F.M.1    Galarneau, L.2    Belanger, L.3    Costa, R.H.4
  • 61
    • 0034625419 scopus 로고    scopus 로고
    • Alpha 1-fetoprotein transcription factor is required for the expression of sterol 12alpha -hydroxylase, the specific enzyme for cholic acid synthesis. Potential role in the bile acid-mediated regulation of gene transcription
    • del Castillo-Olivares A. & G. Gil: Alpha 1-fetoprotein transcription factor is required for the expression of sterol 12alpha -hydroxylase, the specific enzyme for cholic acid synthesis. Potential role in the bile acid-mediated regulation of gene transcription. J Biol Chem 275, 17793-17799. (2000)
    • (2000) J Biol Chem , vol.275 , pp. 17793-17799
    • Del Castillo-Olivares, A.1    Gil, G.2
  • 62
    • 0141835531 scopus 로고    scopus 로고
    • Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 (LRH-1) by the orphan small heterodimer partner (SHP)
    • Lee Y. K. & D. D. Moore: Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 (LRH-1) by the orphan small heterodimer partner (SHP). J Biol Chem 19, 19 (2001)
    • (2001) J Biol Chem , vol.19 , pp. 19
    • Lee, Y.K.1    Moore, D.D.2
  • 65
    • 0037155163 scopus 로고    scopus 로고
    • Differential effects of sterol regulatory binding proteins 1 and 2 on sterol 12 alpha-hydroxylase. SREBP-2 suppresses the sterol 12 alpha-hydroxylase promoter
    • del Castillo-Olivares A. & G. Gil: Differential effects of sterol regulatory binding proteins 1 and 2 on sterol 12 alpha-hydroxylase. SREBP-2 suppresses the sterol 12 alpha-hydroxylase promoter. J Biol Chem 277, 6750-6757 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 6750-6757
    • Del Castillo-Olivares, A.1    Gil, G.2
  • 66
    • 0035657634 scopus 로고    scopus 로고
    • Nuclear receptor-mediated repression of human cholesterol 7alpha- hydroxylase gene transcription by bile acids
    • Chen W., E. Owsley, Y. Yang, D. Stroup & J. Y. Chiang: Nuclear receptor-mediated repression of human cholesterol 7alpha- hydroxylase gene transcription by bile acids. J Lipid Res 42, 1402-1412. (2001)
    • (2001) J Lipid Res , vol.42 , pp. 1402-1412
    • Chen, W.1    Owsley, E.2    Yang, Y.3    Stroup, D.4    Chiang, J.Y.5
  • 67
    • 0034666027 scopus 로고    scopus 로고
    • Role of FXR and FTF in bile acid-mediated suppression of cholesterol 7alpha-hydroxylase transcription
    • del Castillo-Olivares A. & G. Gil: Role of FXR and FTF in bile acid-mediated suppression of cholesterol 7alpha-hydroxylase transcription. Nucleic Acids Res 28, 3587-3593. (2000)
    • (2000) Nucleic Acids Res , vol.28 , pp. 3587-3593
    • Del Castillo-Olivares, A.1    Gil, G.2
  • 68
    • 0035470833 scopus 로고    scopus 로고
    • Suppression of sterol 12alpha-hydroxylase transcription by the short heterodimer partner: Insights into the repression mechanism
    • del Castillo-Olivares A. & G. Gil: Suppression of sterol 12alpha-hydroxylase transcription by the short heterodimer partner: insights into the repression mechanism. Nucleic Acids Res 29, 4035-4042. (2001)
    • (2001) Nucleic Acids Res , vol.29 , pp. 4035-4042
    • Del Castillo-Olivares, A.1    Gil, G.2
  • 69
    • 0037044581 scopus 로고    scopus 로고
    • Suppression of cholesterol 7alpha-hydroxylase transcription and bile acid synthesis by an alpha1-antitrypsin peptide via interaction with alpha1-fetoprotein transcription factor
    • Gerbod-Giannone M. C., A. Del Castillo-Olivares, S. Janciauskiene, G. Gil & P. B. Hylemon: Suppression of cholesterol 7alpha-hydroxylase transcription and bile acid synthesis by an alpha1-antitrypsin peptide via interaction with alpha1-fetoprotein transcription factor. J Biol Chem 277, 42973-42980 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 42973-42980
    • Gerbod-Giannone, M.C.1    Del Castillo-Olivares, A.2    Janciauskiene, S.3    Gil, G.4    Hylemon, P.B.5
  • 70
    • 0037169541 scopus 로고    scopus 로고
    • Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 by the orphan small heterodimer partner
    • Lee Y. K. & D. D. Moore: Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 by the orphan small heterodimer partner. J Biol Chem 277, 2463-2467 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 2463-2467
    • Lee, Y.K.1    Moore, D.D.2
  • 71
    • 0037071854 scopus 로고    scopus 로고
    • On the mechanism of bile acid inhibition of rat sterol 12alpha-hydroxylase gene (CYP8B1) transcription: Roles of alpha-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha
    • Yang Y., M. Zhang, G. Eggertsen & J. Y. Chiang: On the mechanism of bile acid inhibition of rat sterol 12alpha-hydroxylase gene (CYP8B1) transcription: roles of alpha-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha. Biochim Biophys Acta 1583, 63-73. (2002)
    • (2002) Biochim Biophys Acta , vol.1583 , pp. 63-73
    • Yang, Y.1    Zhang, M.2    Eggertsen, G.3    Chiang, J.Y.4
  • 73
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf D. J. & R. M. Evans: The RXR heterodimers and orphan receptors. Cell 83, 841-850 (1995)
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 76
    • 0033026760 scopus 로고    scopus 로고
    • Endogenous bile acids are ligands for the nuclear receptor FXR/BAR
    • Wang H., J. Chen, K. Hollister, L. C. Sowers & B. M. Forman: Endogenous bile acids are ligands for the nuclear receptor FXR/BAR. Mol Cell 3, 543-553 (1999)
    • (1999) Mol Cell , vol.3 , pp. 543-553
    • Wang, H.1    Chen, J.2    Hollister, K.3    Sowers, L.C.4    Forman, B.M.5
  • 77
    • 0034163857 scopus 로고    scopus 로고
    • Catabolites of Cholesterol Synthesis Pathways and Forskolin as Activators of the Farnesoid X-Activated Nuclear Receptor
    • Howard W. R., J. A. Pospisil, E. Njolito & D. J. Noonan: Catabolites of Cholesterol Synthesis Pathways and Forskolin as Activators of the Farnesoid X-Activated Nuclear Receptor. Toxicol Appl Pharmacol 163, 195-202 (2000)
    • (2000) Toxicol Appl Pharmacol , vol.163 , pp. 195-202
    • Howard, W.R.1    Pospisil, J.A.2    Njolito, E.3    Noonan, D.J.4
  • 78
    • 0030835838 scopus 로고    scopus 로고
    • Activators of the nuclear hormone receptors PPARalpha and FXR accelerate the development of the fetal epidermal permeability barrier
    • Hanley K., Y. Jiang, D. Crumrine, N. M. Bass, R. Appel, P. M. Elias, M. L. Williams & K. R. Feingold: Activators of the nuclear hormone receptors PPARalpha and FXR accelerate the development of the fetal epidermal permeability barrier. J Clin Invest 100, 705-712 (1997)
    • (1997) J Clin Invest , vol.100 , pp. 705-712
    • Hanley, K.1    Jiang, Y.2    Crumrine, D.3    Bass, N.M.4    Appel, R.5    Elias, P.M.6    Williams, M.L.7    Feingold, K.R.8
  • 80
    • 0034664729 scopus 로고    scopus 로고
    • Targeted disruption of the nuclear receptor FXR/BAR impairs bile acid and lipid homeostasis
    • Sinal C. J., M. Tohkin, M. Miyata, J. M. Ward, G. Lambert & F. J. Gonzalez: Targeted disruption of the nuclear receptor FXR/BAR impairs bile acid and lipid homeostasis. Cell 102, 731-744 (2000)
    • (2000) Cell , vol.102 , pp. 731-744
    • Sinal, C.J.1    Tohkin, M.2    Miyata, M.3    Ward, J.M.4    Lambert, G.5    Gonzalez, F.J.6
  • 81
    • 0033570028 scopus 로고    scopus 로고
    • Identification of a bile acid-responsive element in the human ileal bile acid-binding protein gene. Involvement of the farnesoid X receptor/9-cis- retinoic acid receptor heterodimer
    • Grober J., I. Zaghini, H. Fujii, S. A. Jones, S. A. Kliewer, T. M. Willson, T. Ono & P. Besnard: Identification of a bile acid-responsive element in the human ileal bile acid-binding protein gene. Involvement of the farnesoid X receptor/9-cis-retinoic acid receptor heterodimer. J Biol Chem 274, 29749-29754 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 29749-29754
    • Grober, J.1    Zaghini, I.2    Fujii, H.3    Jones, S.A.4    Kliewer, S.A.5    Willson, T.M.6    Ono, T.7    Besnard, P.8
  • 82
    • 0034671526 scopus 로고    scopus 로고
    • The farnesoid X-activated receptor mediates bile acid activation of phospholipid transfer protein gene expression
    • Urizar N. L., D. H. Dowhan & D. D. Moore: The farnesoid X-activated receptor mediates bile acid activation of phospholipid transfer protein gene expression. J Biol Chem (2000)
    • (2000) J Biol Chem
    • Urizar, N.L.1    Dowhan, D.H.2    Moore, D.D.3
  • 84
  • 85
    • 0036009146 scopus 로고    scopus 로고
    • Regulation of cholesterol-7alpha-hydroxylase. Barely missing a shp
    • Davis R. A., J. H. Miyake, T. Y. Hui & N. J. Spann: Regulation of cholesterol-7alpha-hydroxylase. Barely missing a shp. J Lipid Res 43, 533-543 (2002)
    • (2002) J Lipid Res , vol.43 , pp. 533-543
    • Davis, R.A.1    Miyake, J.H.2    Hui, T.Y.3    Spann, N.J.4
  • 86
    • 17244371470 scopus 로고    scopus 로고
    • Liver receptor homologue-1 mediates species-and cell line-specific bile acid dependent negative feedback regulation of the apical sodium-dependent bile acid transporter
    • Chen F., L. Ma, P. A. Dawson, C. J. Sinai, E. Sehayek, F. J. Gonzalez, J. Breslow, M. Ananthanarayanan & B. L. Shneider: Liver receptor homologue-1 mediates species-and cell line-specific bile acid dependent negative feedback regulation of the apical sodium-dependent bile acid transporter. J Biol Chem (2002)
    • (2002) J Biol Chem
    • Chen, F.1    Ma, L.2    Dawson, P.A.3    Sinai, C.J.4    Sehayek, E.5    Gonzalez, F.J.6    Breslow, J.7    Ananthanarayanan, M.8    Shneider, B.L.9
  • 88
    • 1642273187 scopus 로고    scopus 로고
    • Integration of hormone signaling in the regulation of human 25(OH)D3 24-hydroxylase transcription
    • Barletta F., P. Dhawan & S. Christakos: Integration of hormone signaling in the regulation of human 25(OH)D3 24-hydroxylase transcription. Am J Physiol Endocrinol Metab 286, E598-608 (2004)
    • (2004) Am J Physiol Endocrinol Metab , vol.286
    • Barletta, F.1    Dhawan, P.2    Christakos, S.3
  • 89
    • 0038587678 scopus 로고    scopus 로고
    • PPARgamma coactivator-1 alpha expression during thyroid hormone- and contractile activity-induced mitochondrial adaptations
    • Irrcher I., P. J. Adhihetty, T. Sheehan, A. M. Joseph & D. A. Hood: PPARgamma coactivator-1 alpha expression during thyroid hormone- and contractile activity-induced mitochondrial adaptations. Am J Physiol Cell Physiol 284, C1669-1677 (2003)
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Irrcher, I.1    Adhihetty, P.J.2    Sheehan, T.3    Joseph, A.M.4    Hood, D.A.5
  • 90
    • 0346118926 scopus 로고    scopus 로고
    • PGC-1alpha activates CYP7A1 and bile acid biosynthesis
    • Shin D. J., J. A. Campos, G. Gil & T. F. Osborne: PGC-1alpha activates CYP7A1 and bile acid biosynthesis. J Biol Chem 278, 50047-50052 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 50047-50052
    • Shin, D.J.1    Campos, J.A.2    Gil, G.3    Osborne, T.F.4
  • 91
    • 0345374578 scopus 로고    scopus 로고
    • Minireview: Malonyl CoA, AMP-activated protein kinase, and adiposity
    • Ruderman N. B., A. K. Saha & E. W. Kraegen: Minireview: malonyl CoA, AMP-activated protein kinase, and adiposity. Endocrinology 144, 5166-5171 (2003)
    • (2003) Endocrinology , vol.144 , pp. 5166-5171
    • Ruderman, N.B.1    Saha, A.K.2    Kraegen, E.W.3
  • 92
    • 0036386911 scopus 로고    scopus 로고
    • Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle
    • Terada S., M. Goto, M. Kato, K. Kawanaka, T. Shimokawa & I. Tabata: Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle. Biochem Biophys Res Commun 296, 350-354 (2002)
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 350-354
    • Terada, S.1    Goto, M.2    Kato, M.3    Kawanaka, K.4    Shimokawa, T.5    Tabata, I.6
  • 93
    • 0036151709 scopus 로고    scopus 로고
    • Activation of the Raf-1/MEK/ERK cascade by bile acids occurs via the epidermal growth factor receptor in primary rat hepatocytes
    • Rao Y. P., E. J. Studer, R. T. Stravitz, S. Gupta, L. Qiao, P. Dent & P. B. Hylemon: Activation of the Raf-1/MEK/ERK cascade by bile acids occurs via the epidermal growth factor receptor in primary rat hepatocytes. Hepatology 35, 307-314 (2002)
    • (2002) Hepatology , vol.35 , pp. 307-314
    • Rao, Y.P.1    Studer, E.J.2    Stravitz, R.T.3    Gupta, S.4    Qiao, L.5    Dent, P.6    Hylemon, P.B.7
  • 94
    • 0030583286 scopus 로고    scopus 로고
    • The opposing effects of retinoic acid and phorbol esters converge to a common response element in the promoter of the rat cholesterol 7 alpha- hydroxylase gene (CYP7A)
    • Crestani M., A. Sadeghpour, D. Stroup, G. Galli & J. Y. Chiang: The opposing effects of retinoic acid and phorbol esters converge to a common response element in the promoter of the rat cholesterol 7 alpha- hydroxylase gene (CYP7A). Biochem Biophys Res Commun 225, 585-592 (1996)
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 585-592
    • Crestani, M.1    Sadeghpour, A.2    Stroup, D.3    Galli, G.4    Chiang, J.Y.5
  • 95
    • 0035903105 scopus 로고    scopus 로고
    • The negative effects of bile acids and tumor necrosis factor-alpha on the transcription of cholesterol 7alpha-hydroxylase gene (CYP7A1) converge to hepatic nuclear factor-4: A novel mechanism of feedback regulation of bile acid synthesis mediated by nuclear receptors
    • De Fabiani E., N. Mitro, A. C. Anzulovich, A. Pinelli, G. Galli & M. Crestani: The negative effects of bile acids and tumor necrosis factor-alpha on the transcription of cholesterol 7alpha-hydroxylase gene (CYP7A1) converge to hepatic nuclear factor-4: a novel mechanism of feedback regulation of bile acid synthesis mediated by nuclear receptors. J Biol Chem 276, 30708-30716 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 30708-30716
    • De Fabiani, E.1    Mitro, N.2    Anzulovich, A.C.3    Pinelli, A.4    Galli, G.5    Crestani, M.6
  • 97
    • 0035844156 scopus 로고    scopus 로고
    • Down-regulation of cholesterol 7alpha-hydroxylase (CYP7A1) gene expression by bile acids in primary rat hepatocytes is mediated by the c-Jun N-terminal kinase pathway
    • Gupta S., R. T. Stravitz, P. Dent & P. B. Hylemon: Down-regulation of cholesterol 7alpha-hydroxylase (CYP7A1) gene expression by bile acids in primary rat hepatocytes is mediated by the c-Jun N-terminal kinase pathway J Biol Chem 276, 15816-15822 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 15816-15822
    • Gupta, S.1    Stravitz, R.T.2    Dent, P.3    Hylemon, P.B.4
  • 98
    • 8744264023 scopus 로고    scopus 로고
    • The functional consequences of cross-talk between the vitamin D receptor and ERK signaling pathways are cell-specific
    • Narayanan R., V. A. Sepulveda, M. Falzon & N. L. Weigel: The functional consequences of cross-talk between the vitamin D receptor and ERK signaling pathways are cell-specific. J Biol Chem 279, 47298-47310 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 47298-47310
    • Narayanan, R.1    Sepulveda, V.A.2    Falzon, M.3    Weigel, N.L.4
  • 100
    • 0036787839 scopus 로고    scopus 로고
    • Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1
    • Desclozeaux M., I. N. Krylova, F. Horn, R. J. Fletterick & H. A. Ingraham: Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1. Mol Cell Biol 22, 7193-7203 (2002)
    • (2002) Mol Cell Biol , vol.22 , pp. 7193-7203
    • Desclozeaux, M.1    Krylova, I.N.2    Horn, F.3    Fletterick, R.J.4    Ingraham, H.A.5
  • 101
    • 0037155837 scopus 로고    scopus 로고
    • Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes
    • Aoki H., P. M. Kang, J. Hampe, K. Yoshimura, T. Noma, M. Matsuzaki & S. Izumo: Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes. J Biol Chem 277, 10244-10250 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 10244-10250
    • Aoki, H.1    Kang, P.M.2    Hampe, J.3    Yoshimura, K.4    Noma, T.5    Matsuzaki, M.6    Izumo, S.7
  • 102
    • 0034889129 scopus 로고    scopus 로고
    • Cross-talk between proinflammatory transcription factors and glucocorticoids
    • Adcock I. M. & G. Caramori: Cross-talk between proinflammatory transcription factors and glucocorticoids. Immunol Cell Biol 79, 376-384 (2001)
    • (2001) Immunol Cell Biol , vol.79 , pp. 376-384
    • Adcock, I.M.1    Caramori, G.2
  • 103
    • 1242294416 scopus 로고    scopus 로고
    • Deoxycholic acid activates the c-Jun N-terminal kinase pathway via FAS receptor activation in primary hepatocytes. Role of acidic sphingomyelinase- mediated ceramide generation in FAS receptor activation
    • Gupta S., R. Natarajan, S. G. Payne, E. J. Studer, S. Spiegel, P. Dent & P. B. Hylemon: Deoxycholic acid activates the c-Jun N-terminal kinase pathway via FAS receptor activation in primary hepatocytes. Role of acidic sphingomyelinase-mediated ceramide generation in FAS receptor activation. J Biol Chem 279, 5821-5828 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 5821-5828
    • Gupta, S.1    Natarajan, R.2    Payne, S.G.3    Studer, E.J.4    Spiegel, S.5    Dent, P.6    Hylemon, P.B.7
  • 104
    • 0026311501 scopus 로고
    • The effect of spices on cholesterol 7 alpha-hydroxylase activity and on serum and hepatic cholesterol levels in the rat
    • Srinivasan K. & K. Sambaiah: The effect of spices on cholesterol 7 alpha-hydroxylase activity and on serum and hepatic cholesterol levels in the rat. Int J Vitam Nutr Res 61, 364-369 (1991)
    • (1991) Int J Vitam Nutr Res , vol.61 , pp. 364-369
    • Srinivasan, K.1    Sambaiah, K.2
  • 105
    • 1442274948 scopus 로고    scopus 로고
    • Inhibiting Src family tyrosine kinase activity blocks glutamate signalling to ERK1/2 and Akt/PKB but not JNK in cultured striatal neurones
    • Crossthwaite A. J., H. Valli & R. J. Williams: Inhibiting Src family tyrosine kinase activity blocks glutamate signalling to ERK1/2 and Akt/PKB but not JNK in cultured striatal neurones. J Neurochem 88, 1127-1139 (2004)
    • (2004) J Neurochem , vol.88 , pp. 1127-1139
    • Crossthwaite, A.J.1    Valli, H.2    Williams, R.J.3
  • 106
    • 0035860761 scopus 로고    scopus 로고
    • ERKs regulate cyclic AMP-induced steroid synthesis through transcription of the steroidogenic acute regulatory (StAR) gene
    • Gyles S. L., C. J. Burns, B. J. Whitehouse, D. Sugden, P. J. Marsh, S. J. Persaud & P. M. Jones: ERKs regulate cyclic AMP-induced steroid synthesis through transcription of the steroidogenic acute regulatory (StAR) gene. J Biol Chem 276, 34888-34895 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 34888-34895
    • Gyles, S.L.1    Burns, C.J.2    Whitehouse, B.J.3    Sugden, D.4    Marsh, P.J.5    Persaud, S.J.6    Jones, P.M.7
  • 107
    • 4644353365 scopus 로고    scopus 로고
    • Bile acids induce mitochondrial ROS, which promote activation of receptor tyrosine kinases and signaling pathways in rat hepatocytes
    • Fang Y., S. I. Han, C. Mitchell, S. Gupta, E. Studer, S. Grant, P. B. Hylemon & P. Dent: Bile acids induce mitochondrial ROS, which promote activation of receptor tyrosine kinases and signaling pathways in rat hepatocytes. Hepatology 40, 961-971 (2004)
    • (2004) Hepatology , vol.40 , pp. 961-971
    • Fang, Y.1    Han, S.I.2    Mitchell, C.3    Gupta, S.4    Studer, E.5    Grant, S.6    Hylemon, P.B.7    Dent, P.8
  • 108
    • 0017809387 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme a reductase: Regulation of enzymatic activity by phosphorylation and dephosphorylation
    • Beg Z. H., J. A. Stonik & H. B. Brewer, Jr.: 3-Hydroxy-3- methylglutaryl coenzyme A reductase: regulation of enzymatic activity by phosphorylation and dephosphorylation. Proc Natl Acad Sci U S A 75, 3678-3682. (1978)
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3678-3682
    • Beg, Z.H.1    Stonik, J.A.2    Brewer Jr., H.B.3
  • 109
    • 0023259133 scopus 로고
    • Modulation of the enzymic activity of 3-hydroxy-3-methylglutaryl coenzyme a reductase by multiple kinase systems involving reversible phosphorylation: A review
    • Beg Z. H., J. A. Stonik & H. B. Brewer, Jr.: Modulation of the enzymic activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase by multiple kinase systems involving reversible phosphorylation: a review. Metabolism 36, 900-917. (1987)
    • (1987) Metabolism , vol.36 , pp. 900-917
    • Beg, Z.H.1    Stonik, J.A.2    Brewer Jr., H.B.3
  • 110
    • 0025310576 scopus 로고
    • Regulation of HMG-CoA reductase: Identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver
    • Clarke P. R. & D. G. Hardie: Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. Embo J 9, 2439-2446. (1990)
    • (1990) Embo J , vol.9 , pp. 2439-2446
    • Clarke, P.R.1    Hardie, D.G.2
  • 111
    • 0027985194 scopus 로고
    • Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: A major regulator of lipid metabolism in mammals
    • Aguan K., J. Scott, C. G. See & N. H. Sarkar: Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals. Gene 149, 345-350 (1994)
    • (1994) Gene , vol.149 , pp. 345-350
    • Aguan, K.1    Scott, J.2    See, C.G.3    Sarkar, N.H.4
  • 112
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale S., W. A. Wilson, A. M. Edelman & D. G. Hardie: Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett 361, 191-195. (1995)
    • (1995) FEBS Lett , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 113
    • 0019082502 scopus 로고
    • In vivo regulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme a reductase: Enzyme phosphorylation as an early regulatory response after intragastric administration of mevalonolactone
    • Arebalo R. E., J. E. Hardgrave, B. J. Noland & T. J. Scallen: In vivo regulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase: enzyme phosphorylation as an early regulatory response after intragastric administration of mevalonolactone. Proc Natl Acad Sci U S A 77, 6429-6433. (1980)
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 6429-6433
    • Arebalo, R.E.1    Hardgrave, J.E.2    Noland, B.J.3    Scallen, T.J.4
  • 115
    • 0035029874 scopus 로고    scopus 로고
    • Effect of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside infusion on in vivo glucose and lipid metabolism in lean and obese Zucker rats
    • Bergeron R., S. F. Previs, G. W. Cline, P. Perret, R. R. Russell, 3rd, L. H. Young & G. I. Shulman: Effect of 5-aminoimidazole-4-carboxamide-1-beta- D-ribofuranoside infusion on in vivo glucose and lipid metabolism in lean and obese Zucker rats. Diabetes 50, 1076-1082 (2001)
    • (2001) Diabetes , vol.50 , pp. 1076-1082
    • Bergeron, R.1    Previs, S.F.2    Cline, G.W.3    Perret, P.4    Russell III, R.R.5    Young, L.H.6    Shulman, G.I.7
  • 117
    • 17244371929 scopus 로고
    • Protein kinase C activation/cellular redistribution and cholesterol 7alpha-hydroxylase mRNA repression by bile acids in rat hepatocytes
    • Stravitz R. T., Y. Rao, Z. R. Vlahcevic, E. C. Gurley & P. B. Hylemon: Protein kinase C activation/cellular redistribution and cholesterol 7alpha-hydroxylase mRNA repression by bile acids in rat hepatocytes. Hepatology 22, 239A (1995)
    • (1995) Hepatology , vol.22
    • Stravitz, R.T.1    Rao, Y.2    Vlahcevic, Z.R.3    Gurley, E.C.4    Hylemon, P.B.5
  • 118
    • 0034074153 scopus 로고    scopus 로고
    • 5-aminoimidazole-4-carboxamide riboside mimics the effects of insulin on the expression of the 2 key gluconeogenic genes PEPCK and glucose-6-phosphatase
    • Lochhead P. A., I. P. Salt, K. S. Walker, D. G. Hardie & C. Sutherland: 5-aminoimidazole-4-carboxamide riboside mimics the effects of insulin on the expression of the 2 key gluconeogenic genes PEPCK and glucose-6-phosphatase. Diabetes 49, 896-903 (2000)
    • (2000) Diabetes , vol.49 , pp. 896-903
    • Lochhead, P.A.1    Salt, I.P.2    Walker, K.S.3    Hardie, D.G.4    Sutherland, C.5
  • 119
    • 0035406121 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor-4alpha involved in type 1 maturity-onset diabetes of the young is a novel target of amp-activated protein kinase
    • Leclerc I., C. Lenzner, L. Gourdon, S. Vaulont, A. Kahn & B. Viollet: Hepatocyte nuclear factor-4alpha involved in type 1 maturity-onset diabetes of the young is a novel target of amp-activated protein kinase. Diabetes 50, 1515-1521. (2001)
    • (2001) Diabetes , vol.50 , pp. 1515-1521
    • Leclerc, I.1    Lenzner, C.2    Gourdon, L.3    Vaulont, S.4    Kahn, A.5    Viollet, B.6
  • 121
    • 0037023379 scopus 로고    scopus 로고
    • Bile Acid secreted by male sea lamprey that acts as a sex pheromone
    • Li W., A. P. Scott, M. J. Siefkes, H. Yan, Q. Liu, S. S. Yun & D. A. Gage: Bile Acid secreted by male sea lamprey that acts as a sex pheromone. Science 296, 138-141 (2002)
    • (2002) Science , vol.296 , pp. 138-141
    • Li, W.1    Scott, A.P.2    Siefkes, M.J.3    Yan, H.4    Liu, Q.5    Yun, S.S.6    Gage, D.A.7
  • 122
    • 0029874172 scopus 로고    scopus 로고
    • Regulation of bile acid synthesis by estradiol and progesterone in primary cultures of rat hepatocytes
    • Chico Y., O. Fresnedo, K. Botham, M. Lacort & B. Ochoa: Regulation of bile acid synthesis by estradiol and progesterone in primary cultures of rat hepatocytes. Exp Clin Endocrinol Diabetes 104, 137-144 (1996)
    • (1996) Exp Clin Endocrinol Diabetes , vol.104 , pp. 137-144
    • Chico, Y.1    Fresnedo, O.2    Botham, K.3    Lacort, M.4    Ochoa, B.5
  • 123
    • 0031847175 scopus 로고    scopus 로고
    • Effect of metformin on bile salt circulation and intestinal motility in type 2 diabetes mellitus
    • Scarpello J. H., E. Hodgson & H. C. Hewlett: Effect of metformin on bile salt circulation and intestinal motility in type 2 diabetes mellitus. Diabet Med 15, 651-656 (1998)
    • (1998) Diabet Med , vol.15 , pp. 651-656
    • Scarpello, J.H.1    Hodgson, E.2    Hewlett, H.C.3
  • 124
    • 0037424532 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase enhances CYP17 transcription via MKP-1 activation in H295R human adrenocortical cells
    • Sewer M. B. & M. R. Waterman: cAMP-dependent protein kinase enhances CYP17 transcription via MKP-1 activation in H295R human adrenocortical cells. J Biol Chem 278, 8106-8111 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 8106-8111
    • Sewer, M.B.1    Waterman, M.R.2
  • 125
    • 1242291934 scopus 로고    scopus 로고
    • Bile acids enhance the activity of the insulin receptor and glycogen synthase in primary rodent hepatocytes
    • Han S. I., E. Studer, S. Gupta, Y. Fang, L. Qiao, W. Li, S. Grant, P. B. Hylemon & P. Dent: Bile acids enhance the activity of the insulin receptor and glycogen synthase in primary rodent hepatocytes. Hepatology 39, 456-463 (2004)
    • (2004) Hepatology , vol.39 , pp. 456-463
    • Han, S.I.1    Studer, E.2    Gupta, S.3    Fang, Y.4    Qiao, L.5    Li, W.6    Grant, S.7    Hylemon, P.B.8    Dent, P.9
  • 126
    • 0037405649 scopus 로고    scopus 로고
    • Bile acid regulation of C/EBPbeta, CREB, and c-Jun function, via the extracellular signal-regulated kinase and c-Jun NH2-terminal kinase pathways, modulates the apoptotic response of hepatocytes
    • Qiao L., S. I. Han, Y. Fang, J. S. Park, S. Gupta, D. Gilfor, G. Amorino, K. Valerie, L. Sealy, J. F. Engelhardt, S. Grant, P. B. Hylemon & P. Dent: Bile acid regulation of C/EBPbeta, CREB, and c-Jun function, via the extracellular signal-regulated kinase and c-Jun NH2-terminal kinase pathways, modulates the apoptotic response of hepatocytes. Mol Cell Biol 23, 3052-3066 (2003)
    • (2003) Mol Cell Biol , vol.23 , pp. 3052-3066
    • Qiao, L.1    Han, S.I.2    Fang, Y.3    Park, J.S.4    Gupta, S.5    Gilfor, D.6    Amorino, G.7    Valerie, K.8    Sealy, L.9    Engelhardt, J.F.10    Grant, S.11    Hylemon, P.B.12    Dent, P.13
  • 127
    • 0346422479 scopus 로고    scopus 로고
    • Bile acids up-regulate death receptor 5/TRAIL-receptor 2 expression via a c-Jun N-terminal kinase-dependent pathway involving Sp1
    • Higuchi H., A. Grambihler, A. Canbay, S. F. Bronk & G. J. Gores: Bile acids up-regulate death receptor 5/TRAIL-receptor 2 expression via a c-Jun N-terminal kinase-dependent pathway involving Sp1. J Biol Chem 279, 51-60 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 51-60
    • Higuchi, H.1    Grambihler, A.2    Canbay, A.3    Bronk, S.F.4    Gores, G.J.5
  • 129
    • 0036241214 scopus 로고    scopus 로고
    • Taurolithocholic acid-3 sulfate induces CD95 trafficking and apoptosis in a c-Jun N-terminal kinase-dependent manner
    • Graf D., A. K. Kurz, R. Fischer, R. Reinehr & D. Haussinger: Taurolithocholic acid-3 sulfate induces CD95 trafficking and apoptosis in a c-Jun N-terminal kinase-dependent manner. Gastroenterology 122, 1411-1427 (2002)
    • (2002) Gastroenterology , vol.122 , pp. 1411-1427
    • Graf, D.1    Kurz, A.K.2    Fischer, R.3    Reinehr, R.4    Haussinger, D.5
  • 130
    • 0036211298 scopus 로고    scopus 로고
    • Inhibition of the MAPK and PI3K pathways enhances UDCA-induced apoptosis in primary rodent hepatocytes
    • Qiao L., A. Yacoub, E. Studer, S. Gupta, X. Y. Pei, S. Grant, P. B. Hylemon & P. Dent: Inhibition of the MAPK and PI3K pathways enhances UDCA-induced apoptosis in primary rodent hepatocytes. Hepatology 35, 779-789 (2002)
    • (2002) Hepatology , vol.35 , pp. 779-789
    • Qiao, L.1    Yacoub, A.2    Studer, E.3    Gupta, S.4    Pei, X.Y.5    Grant, S.6    Hylemon, P.B.7    Dent, P.8
  • 132
    • 0035895651 scopus 로고    scopus 로고
    • Cytoprotection by Jun kinase during nitric oxide-induced cardiac myocyte apoptosis
    • Andreka P., J. Zang, C. Dougherty, T. I. Slepak, K. A. Webster & N. H. Bishopric: Cytoprotection by Jun kinase during nitric oxide-induced cardiac myocyte apoptosis. Circ Res 88, 305-312 (2001)
    • (2001) Circ Res , vol.88 , pp. 305-312
    • Andreka, P.1    Zang, J.2    Dougherty, C.3    Slepak, T.I.4    Webster, K.A.5    Bishopric, N.H.6
  • 133
    • 0028820158 scopus 로고
    • Recruitment of hepatocyte nuclear factor 4 into specific intranuclear compartiments depends on tyrosine phosphorylation that affects its DNA-binding and transactivation potential
    • Ktistaki E., T. Ktistaki, E. Papadogeorgaki & I. Talianidis: Recruitment of hepatocyte nuclear factor 4 into specific intranuclear compartiments depends on tyrosine phosphorylation that affects its DNA-binding and transactivation potential. Proc Natl Acad Sci USA 92, 9876-9880 (1995)
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9876-9880
    • Ktistaki, E.1    Ktistaki, T.2    Papadogeorgaki, E.3    Talianidis, I.4
  • 134
    • 0032868388 scopus 로고    scopus 로고
    • Negative cyclic AMP response elements in the promoter of the L-type pyruvate kinase gene
    • Gourdon L., D. Q. Lou, M. Raymondjean, M. Vasseur-Cognet & A. Kahn: Negative cyclic AMP response elements in the promoter of the L-type pyruvate kinase gene. FEBS Lett 459, 9-14 (1999)
    • (1999) FEBS Lett , vol.459 , pp. 9-14
    • Gourdon, L.1    Lou, D.Q.2    Raymondjean, M.3    Vasseur-Cognet, M.4    Kahn, A.5
  • 135
    • 0031127252 scopus 로고    scopus 로고
    • Serine/threonine phosphorylation of orphan receptor hepatocyte nuclear factor 4
    • Jiang G., L. Nepomuceno, Q. Yang & F. M. Sladek: Serine/threonine phosphorylation of orphan receptor hepatocyte nuclear factor 4. Arch Biochem Biophys 340, 1-9 (1997)
    • (1997) Arch Biochem Biophys , vol.340 , pp. 1-9
    • Jiang, G.1    Nepomuceno, L.2    Yang, Q.3    Sladek, F.M.4
  • 136
    • 0042847434 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates HNF4alpha transcriptional activity by inhibiting dimer formation and decreasing protein stability
    • Hong Y. H., U. S. Varanasi, W. Yang & T. Leff: AMP-activated protein kinase regulates HNF4alpha transcriptional activity by inhibiting dimer formation and decreasing protein stability. J Biol Chem 278, 27495-27501 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 27495-27501
    • Hong, Y.H.1    Varanasi, U.S.2    Yang, W.3    Leff, T.4
  • 137
    • 0037200089 scopus 로고    scopus 로고
    • Interleukin-1 beta-mediated suppression of RXR:RAR transactivation of the Ntcp promoter is JNK-dependent
    • Li D., T. L. Zimmerman, S. Thevananther, H. Y. Lee, J. M. Kurie & S. J. Karpen: Interleukin-1 beta-mediated suppression of RXR:RAR transactivation of the Ntcp promoter is JNK-dependent. J Biol Chem 111, 31416-31422 (2002)
    • (2002) J Biol Chem , vol.111 , pp. 31416-31422
    • Li, D.1    Zimmerman, T.L.2    Thevananther, S.3    Lee, H.Y.4    Kurie, J.M.5    Karpen, S.J.6
  • 139
    • 0019839708 scopus 로고
    • Reversible activation-inactivation of cholesterol 7alpha-hydroxylase possibly due to phosphorylation-dephosphorylation
    • Sanghvi A., E. Grassi, V. Warty, W. Diven, C. Wight & R. Lester: Reversible activation-inactivation of cholesterol 7alpha-hydroxylase possibly due to phosphorylation-dephosphorylation. Biochem Biophys Res Commun 103, 886-892 (1981)
    • (1981) Biochem Biophys Res Commun , vol.103 , pp. 886-892
    • Sanghvi, A.1    Grassi, E.2    Warty, V.3    Diven, W.4    Wight, C.5    Lester, R.6
  • 140
    • 0020490558 scopus 로고
    • Rat liver cholesterol 7alpha-hydroxylase: Modulation of enzyme activity by changes in phosphorylation state
    • Goodwin C. D., B. W. Cooper & S. Margolis: Rat liver cholesterol 7alpha-hydroxylase: Modulation of enzyme activity by changes in phosphorylation state. J Biol Chem 257, 4469-4472 (1982)
    • (1982) J Biol Chem , vol.257 , pp. 4469-4472
    • Goodwin, C.D.1    Cooper, B.W.2    Margolis, S.3
  • 141
    • 0344952865 scopus 로고
    • Regulation of three key enzymes in cholesterol metabolism by phosphorylation/dephosphorylation
    • Scallen T. J. & A. Sanghvi: Regulation of three key enzymes in cholesterol metabolism by phosphorylation/dephosphorylation. Proc Natl Acad Sci U S A 80, 2477-2480 (1983)
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 2477-2480
    • Scallen, T.J.1    Sanghvi, A.2
  • 142
    • 0029658444 scopus 로고    scopus 로고
    • Cholesterol 7alpha-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation
    • Nguyen L. B., S. Shefer, G. Salen, J. Y. Chiang & M. Patel: Cholesterol 7alpha-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation. Hepatology 24, 1468-1474 (1996)
    • (1996) Hepatology , vol.24 , pp. 1468-1474
    • Nguyen, L.B.1    Shefer, S.2    Salen, G.3    Chiang, J.Y.4    Patel, M.5
  • 143
    • 0022742564 scopus 로고
    • Evidence against in vitro modulation of rat liver cholesterol 7 alpha- hydroxylase activity by phosphorylation-dephosphorylation: Comparison with hydroxymethylglutaryl CoA reductase
    • Berglund L., I. Bjorkhem, B. Angelin & K. Einarsson: Evidence against in vitro modulation of rat liver cholesterol 7 alpha- hydroxylase activity by phosphorylation-dephosphorylation: comparison with hydroxymethylglutaryl CoA reductase. Acta Chem Scand [B] 40, 457-461 (1986)
    • (1986) Acta Chem Scand [B] , vol.40 , pp. 457-461
    • Berglund, L.1    Bjorkhem, I.2    Angelin, B.3    Einarsson, K.4
  • 144
    • 0025050504 scopus 로고
    • Structure of the rat gene encoding cholesterol 7alpha-hydroxylase
    • Jelinek D. & D. W. Russell: Structure of the rat gene encoding
    • (1990) Biochemistry , vol.29 , pp. 7781-7785
    • Jelinek, D.1    Russell, D.W.2
  • 145
    • 0025353861 scopus 로고
    • Regulation of cholesterol 7alpha-hydroxylase in the liver: Cloning, sequencing and regulation of cholesterol 7alpha-hydroxylase mRNA
    • Li Y. C., D. P. Wang & J. Y. L. Chiang: Regulation of cholesterol 7alpha-hydroxylase in the liver: Cloning, sequencing and regulation of cholesterol 7alpha-hydroxylase mRNA. J Biol Chem 265, 12012-12019 (1990)
    • (1990) J Biol Chem , vol.265 , pp. 12012-12019
    • Li, Y.C.1    Wang, D.P.2    Chiang, J.Y.L.3
  • 146
    • 0028300020 scopus 로고
    • Cholesterol and bile acid regulate cholesterol 7alpha-hydroxylase expression at the transcriptional level in culture and in transgenic mice
    • Ramirez M. I., D. Karaoglu, D. Haro, C. Barillas, R. Bashirzadeh & G. Gil: Cholesterol and bile acid regulate cholesterol 7alpha-hydroxylase expression at the transcriptional level in culture and in transgenic mice. Mol Cell Biol 14, 2809-2821 (1994)
    • (1994) Mol Cell Biol , vol.14 , pp. 2809-2821
    • Ramirez, M.I.1    Karaoglu, D.2    Haro, D.3    Barillas, C.4    Bashirzadeh, R.5    Gil, G.6
  • 147
    • 0027242111 scopus 로고
    • Transcriptional regulation of the gene encoding cholesterol 7alpha-hydroxylase in the rat
    • Hoekman M. F. M., J. M. J. Rientjes, J. Twisk, R. J. Planta. II. M. G. Princen & W. H. Mager: Transcriptional regulation of the gene encoding cholesterol 7alpha-hydroxylase in the rat. Gene 130, 217-223 (1993)
    • (1993) Gene , vol.130 , pp. 217-223
    • Hoekman, M.F.M.1    Rientjes, J.M.J.2    Twisk, J.3    Planta, R.J.4    Princen, H.M.G.5    Mager, W.H.6
  • 148
    • 0028239336 scopus 로고
    • Effects of bile acids and steroid/thyroid hormones on the expression of cholesterol 7alpha-hydroxylase mRNA and the CYP7 gene in HepG2 cells
    • Crestani M., W. G. Karam & J. Y. L. Chiang: Effects of bile acids and steroid/thyroid hormones on the expression of cholesterol 7alpha-hydroxylase mRNA and the CYP7 gene in HepG2 cells. Biochem Biophys Res Commun 198, 546-553 (1994)
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 546-553
    • Crestani, M.1    Karam, W.G.2    Chiang, J.Y.L.3
  • 149
    • 0028233386 scopus 로고
    • Regulation of cholesterol 7alpha-hydroxylase gene expression in HepG2 cells
    • Taniguchi T., J. Chen & A. D. Cooper: Regulation of cholesterol 7alpha-hydroxylase gene expression in HepG2 cells. J Biol Chem 269, 10071-10078 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 10071-10078
    • Taniguchi, T.1    Chen, J.2    Cooper, A.D.3
  • 150
    • 0029834337 scopus 로고    scopus 로고
    • Transcriptional regulation of the human cholesterol 7alpha-hydroxylase gene (Cyp7A) in HepG2 cells
    • Wang D.-P., D. Stroup, M. Marrapodi, M. Crestani, G. Galli & J. Y. L. Chiang: Transcriptional regulation of the human cholesterol 7alpha-hydroxylase gene (Cyp7A) in HepG2 cells. J Lipid Research 37, 1831-1841 (1996)
    • (1996) J Lipid Research , vol.37 , pp. 1831-1841
    • Wang, D.-P.1    Stroup, D.2    Marrapodi, M.3    Crestani, M.4    Galli, G.5    Chiang, J.Y.L.6
  • 151
    • 0031023181 scopus 로고    scopus 로고
    • Characterization of hepatic-specific regulatory elements in the promoter region of the human cholesterol 7alpha-hydroxylase gene
    • Cooper A. D., J. Chen, M. J. Botelho-Yetkinler, Y. Cao, T. Taniguchi & B. Levy-Wilson: Characterization of hepatic-specific regulatory elements in the promoter region of the human cholesterol 7alpha-hydroxylase gene. J Biol Chem 272, 3444-3452 (1997)
    • (1997) J Biol Chem , vol.272 , pp. 3444-3452
    • Cooper, A.D.1    Chen, J.2    Botelho-Yetkinler, M.J.3    Cao, Y.4    Taniguchi, T.5    Levy-Wilson, B.6
  • 153
    • 0028224484 scopus 로고
    • Effect of different bile salts on the steady-state mRNA levels and transcriptional activity of cholesterol 7α-hydroxylase
    • Pandak W. M., Z. R. Vlahcevic, D. M. Heuman, K. S. Redford, J. Y. L. Chiang & P. B. Hylemon: Effect of different bile salts on the steady-state mRNA levels and transcriptional activity of cholesterol 7α-hydroxylase. Hepatology 19, 941-947 (1994)
    • (1994) Hepatology , vol.19 , pp. 941-947
    • Pandak, W.M.1    Vlahcevic, Z.R.2    Heuman, D.M.3    Redford, K.S.4    Chiang, J.Y.L.5    Hylemon, P.B.6
  • 154
    • 0030721593 scopus 로고    scopus 로고
    • The 3′-untranslated region of the mouse cholesterol 7alpha-hydroxylase mRNA contains elements responsive to post-transcriptional regulation by bile acids
    • Agellon L. B. & S. K. Cheema: The 3′-untranslated region of the mouse cholesterol 7alpha-hydroxylase mRNA contains elements responsive to post-transcriptional regulation by bile acids. Biochem J 328, 393-399 (1997)
    • (1997) Biochem J , vol.328 , pp. 393-399
    • Agellon, L.B.1    Cheema, S.K.2
  • 155
    • 0022510474 scopus 로고
    • Modulation of reconstituted cholesterol 7 alpha-hydroxylase by phosphatase and protein kinase
    • Tang P. M. & J. Y. L. Chiang: Modulation of reconstituted cholesterol 7 alpha-hydroxylase by phosphatase and protein kinase. Biochem Biophys Res Commun 134, 797-802 (1986)
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 797-802
    • Tang, P.M.1    Chiang, J.Y.L.2
  • 156
    • 0029658444 scopus 로고    scopus 로고
    • Cholesterol 7alpha-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation
    • Nguyen L. B., S. Shefer, G. Salen, J. Y. Chiang, L, & M. Patel: Cholesterol 7alpha-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation. Hepatology 24, 1468-1474 (1996)
    • (1996) Hepatology , vol.24 , pp. 1468-1474
    • Nguyen, L.B.1    Shefer, S.2    Salen, G.3    Chiang, J.Y.4    Patel, M.5
  • 157
    • 0028845251 scopus 로고
    • 5′-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
    • Hawley S. A., M. A. Selbert, E. G. Goldstein, A. M. Edelman, D. Carling & D. G. Hardie: 5′-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J Biol Chem 270, 27186-27191 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 27186-27191
    • Hawley, S.A.1    Selbert, M.A.2    Goldstein, E.G.3    Edelman, A.M.4    Carling, D.5    Hardie, D.G.6
  • 158
    • 0023576868 scopus 로고
    • Effect of diabetes on partially purified hepatic cholesterol 7 alpha- hydroxylase, the rate-limiting enzyme of bile acid biosynthesis
    • Hassan A. S. & B. L. Ventling: Effect of diabetes on partially purified hepatic cholesterol 7 alpha- hydroxylase, the rate-limiting enzyme of bile acid biosynthesis. Res Commun Chem Pathol Pharmacol 58, 41-51 (1987)
    • (1987) Res Commun Chem Pathol Pharmacol , vol.58 , pp. 41-51
    • Hassan, A.S.1    Ventling, B.L.2
  • 159
    • 0036887723 scopus 로고    scopus 로고
    • Steroid and sterol 7-hydroxylation: Ancient pathways
    • Lathe R.: Steroid and sterol 7-hydroxylation: ancient pathways. Steroids 67, 967-977 (2002)
    • (2002) Steroids , vol.67 , pp. 967-977
    • Lathe, R.1
  • 160
    • 0038623782 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid reduces apoptosis and protects against neurological injury after acute hemorrhagic stroke in rats
    • Rodrigues C. M., S. Sola, Z. Nan, R. E. Castro, P. S. Ribeiro, W. C. Low & C. J. Steer: Tauroursodeoxycholic acid reduces apoptosis and protects against neurological injury after acute hemorrhagic stroke in rats. Proc Natl Acad Sci U S A 100, 6087-6092 (2003)
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6087-6092
    • Rodrigues, C.M.1    Sola, S.2    Nan, Z.3    Castro, R.E.4    Ribeiro, P.S.5    Low, W.C.6    Steer, C.J.7
  • 161
    • 0036677435 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease
    • Keene C. D., C. M. Rodrigues, T. Eich, M. S. Chhabra, C. J. Steer & W. C. Low: Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc Natl Acad Sci U S A 99, 10671-10676 (2002)
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10671-10676
    • Keene, C.D.1    Rodrigues, C.M.2    Eich, T.3    Chhabra, M.S.4    Steer, C.J.5    Low, W.C.6
  • 163
    • 0018159006 scopus 로고
    • Altered bile in diabetic diarrhoea
    • Molloy A. M. & G. H. Tomkin: Altered bile in diabetic diarrhoea. Br Med J 2, 1462-1463 (1978)
    • (1978) Br Med J , vol.2 , pp. 1462-1463
    • Molloy, A.M.1    Tomkin, G.H.2
  • 165
    • 0030002526 scopus 로고    scopus 로고
    • Pathophysiology and treatment of diabetic diarrhea
    • Nakamura T., T. Suda & M. Kon: Pathophysiology and treatment of diabetic diarrhea. J Smooth Muscle Res 32, 27-42 (1996)
    • (1996) J Smooth Muscle Res , vol.32 , pp. 27-42
    • Nakamura, T.1    Suda, T.2    Kon, M.3
  • 166
    • 0021268887 scopus 로고
    • Evidence for the presence of non-lipoprotein factors in diabetic serum capable of stimulating rat hepatic cholesterol-7 alpha-hydroxylase in vitro
    • Subbiah M. T. & R. L. Yunker: Evidence for the presence of non-lipoprotein factors in diabetic serum capable of stimulating rat hepatic cholesterol-7 alpha-hydroxylase in vitro. Biochem Biophys Res Commun 121, 743-748 (1984)
    • (1984) Biochem Biophys Res Commun , vol.121 , pp. 743-748
    • Subbiah, M.T.1    Yunker, R.L.2
  • 167
    • 0031010251 scopus 로고    scopus 로고
    • Hepatobiliary excretion of bile acids and rose bengal in streptozotocin-induced and genetic diabetic rats
    • Stone J. L., J. B. Braunstein, T. M. Beaty, R. A. Sanders & J. B. Watkins, 3rd: Hepatobiliary excretion of bile acids and rose bengal in streptozotocin-induced and genetic diabetic rats. J Pharmacol Exp Ther 281, 412-419 (1997)
    • (1997) J Pharmacol Exp Ther , vol.281 , pp. 412-419
    • Stone, J.L.1    Braunstein, J.B.2    Beaty, T.M.3    Sanders, R.A.4    Watkins III, J.B.5
  • 168
    • 0028965012 scopus 로고
    • Insulin suppresses bile acid synthesis in cultured rat hepatocytes by down-regulation of cholesterol 7 alpha-hydroxylase and sterol 27- hydroxylase gene transcription
    • Twisk J., M. F. Hoekman, E. M. Lehmann, P. Meijer, W. H. Mager & H. M. Princen: Insulin suppresses bile acid synthesis in cultured rat hepatocytes by down-regulation of cholesterol 7 alpha-hydroxylase and sterol 27- hydroxylase gene transcription. Hepatology 21, 501-510 (1995)
    • (1995) Hepatology , vol.21 , pp. 501-510
    • Twisk, J.1    Hoekman, M.F.2    Lehmann, E.M.3    Meijer, P.4    Mager, W.H.5    Princen, H.M.6
  • 169
    • 0035850402 scopus 로고    scopus 로고
    • The continuing epidemics of obesity and diabetes in the United States
    • Mokdad A. H., B. A. Bowman, E. S. Ford, F. Vinicor, J. S. Marks & J. P. Koplan: The continuing epidemics of obesity and diabetes in the United States. Jama 286, 1195-1200 (2001)
    • (2001) Jama , vol.286 , pp. 1195-1200
    • Mokdad, A.H.1    Bowman, B.A.2    Ford, E.S.3    Vinicor, F.4    Marks, J.S.5    Koplan, J.P.6
  • 170
    • 0039568973 scopus 로고    scopus 로고
    • Major cardiovascular disease (CVD) during 1997-1999 and major CVD hospital discharge rates in 1997 among women with diabetes - United States
    • Major cardiovascular disease (CVD) during 1997-1999 and major CVD hospital discharge rates in 1997 among women with diabetes - United States. MMWR Morb Mortal Wkly Rep 50, 948-954 (2001)
    • (2001) MMWR Morb Mortal Wkly Rep , vol.50 , pp. 948-954
  • 171
    • 0034116811 scopus 로고    scopus 로고
    • Health care and health status and outcomes for patients with type 2 diabetes
    • Harris M. I.: Health care and health status and outcomes for patients with type 2 diabetes. Diabetes Care 23, 754-758 (2000)
    • (2000) Diabetes Care , vol.23 , pp. 754-758
    • Harris, M.I.1
  • 172
    • 0031016436 scopus 로고    scopus 로고
    • Cholesterol absorption, synthesis, and LDL metabolism in NIDDM
    • Gylling H. & T. A. Miettinen: Cholesterol absorption, synthesis, and LDL metabolism in NIDDM. Diabetes Care 20, 90-95 (1997)
    • (1997) Diabetes Care , vol.20 , pp. 90-95
    • Gylling, H.1    Miettinen, T.A.2


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