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Volumn 117, Issue 2, 1999, Pages 433-452

Signal transduction and hepatocellular bile acid transport: Cross talk between bile acids and second messengers

Author keywords

[No Author keywords available]

Indexed keywords

CHENODEOXYCHOLIC ACID; CHOLIC ACID; CYCLIC AMP; DEOXYCHOLIC ACID; GLUCAGON; LITHOCHOLIC ACID; PROTEIN KINASE C; VASOPRESSIN;

EID: 0032800486     PISSN: 00165085     EISSN: None     Source Type: Journal    
DOI: 10.1053/gast.1999.0029900433     Document Type: Article
Times cited : (57)

References (218)
  • 2
    • 85095943964 scopus 로고
    • Barrier function of epithelia
    • D. Powell Barrier function of epithelia Am J Physiol 241 1981 G275 G288
    • (1981) Am J Physiol , vol.241 , pp. G275-G288
    • Powell, D.1
  • 3
    • 0023715186 scopus 로고
    • The epithelial tight junction: structure, function and preliminary biochemical characterization
    • B. Stevenson J. Anderson J. Bullivant The epithelial tight junction: structure, function and preliminary biochemical characterization Mol Cell Biochem 83 1988 129 145
    • (1988) Mol Cell Biochem , vol.83 , pp. 129-145
    • Stevenson, B.1    Anderson, J.2    Bullivant, J.3
  • 4
    • 85025739140 scopus 로고
    • Canalicular bile salt-independent bile formation: concepts and clues from electrolyte transport in rat liver
    • J. Graf Canalicular bile salt-independent bile formation: concepts and clues from electrolyte transport in rat liver Am J Physiol 244 1983 G233 G246
    • (1983) Am J Physiol , vol.244 , pp. G233-G246
    • Graf, J.1
  • 7
    • 0021192714 scopus 로고
    • Chemistry and enterohepatic circulation of bile acids
    • A.F. Hofmann Chemistry and enterohepatic circulation of bile acids Hepatology 4 suppl 5 1984 4S 14S
    • (1984) Hepatology , vol.4 , Issue.suppl 5 , pp. 4S-14S
    • Hofmann, A.F.1
  • 8
    • 0027374704 scopus 로고
    • Comparative binding of bile acids to serum lipoproteins and albumin
    • S. Ceryak B. Bouscarel H. Fromm Comparative binding of bile acids to serum lipoproteins and albumin J Lipid Res 34 1993 1661 1674
    • (1993) J Lipid Res , vol.34 , pp. 1661-1674
    • Ceryak, S.1    Bouscarel, B.2    Fromm, H.3
  • 9
    • 0000382851 scopus 로고
    • Bile acid content of human serum. II. The binding of cholanic acids by human plasma proteins
    • D. Rudman F.E. Kendall Bile acid content of human serum. II. The binding of cholanic acids by human plasma proteins J Clin Invest 36 1957 538 542
    • (1957) J Clin Invest , vol.36 , pp. 538-542
    • Rudman, D.1    Kendall, F.E.2
  • 10
    • 0021736958 scopus 로고
    • Hepatic bile flow
    • R.C. Strange Hepatic bile flow Physiol Rev 64 1984 1055 1102
    • (1984) Physiol Rev , vol.64 , pp. 1055-1102
    • Strange, R.C.1
  • 11
    • 0025162155 scopus 로고
    • Signaling through phosphatidylcholine breakdown
    • J.H. Exton Signaling through phosphatidylcholine breakdown J Biol Chem 265 1990 1 4
    • (1990) J Biol Chem , vol.265 , pp. 1-4
    • Exton, J.H.1
  • 12
    • 0021334519 scopus 로고
    • Guanine nucleotide-binding regulatory proteins and dual control of adenylate cyclase
    • A.G. Gilman Guanine nucleotide-binding regulatory proteins and dual control of adenylate cyclase J Clin Invest 73 1984 1 14
    • (1984) J Clin Invest , vol.73 , pp. 1-14
    • Gilman, A.G.1
  • 13
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumor promotion
    • Y. Nishizuka The role of protein kinase C in cell surface signal transduction and tumor promotion Nature 308 1984 693 698
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 14
    • 0023882264 scopus 로고
    • The transport of bile acids in liver cells
    • M. Frimmer K. Ziegler The transport of bile acids in liver cells Biochim Biophys Acta 947 1988 75 99
    • (1988) Biochim Biophys Acta , vol.947 , pp. 75-99
    • Frimmer, M.1    Ziegler, K.2
  • 15
    • 0020420242 scopus 로고
    • Bile salt-binding polypeptides in plasma membranes of hepatocytes revealed by photoaffinity labeling
    • W. Kramer U. Bickel H.P. Buscher G. Kurz Bile salt-binding polypeptides in plasma membranes of hepatocytes revealed by photoaffinity labeling Eur J Biochem 129 1982 13 24
    • (1982) Eur J Biochem , vol.129 , pp. 13-24
    • Kramer, W.1    Bickel, U.2    Buscher, H.P.3    Kurz, G.4
  • 16
    • 0022981885 scopus 로고
    • Purification and reconstitution of the bile acid transport system from hepatocyte sinusoidal plasma membranes
    • P. Von Dippe M. Ananthanarayanan P. Drain D. Levy Purification and reconstitution of the bile acid transport system from hepatocyte sinusoidal plasma membranes Biochim Biophys Acta 862 1986 352 360
    • (1986) Biochim Biophys Acta , vol.862 , pp. 352-360
    • Von Dippe, P.1    Ananthanarayanan, M.2    Drain, P.3    Levy, D.4
  • 17
    • 0028231206 scopus 로고
    • Molecular cloning, chromosomal localization, and functional characterization of a human liver Na+/bile acid cotransporter
    • +/bile acid cotransporter J Clin Invest 93 1994 1326 1331
    • (1994) J Clin Invest , vol.93 , pp. 1326-1331
    • Hagenbuch, B.1    Meier, P.J.2
  • 19
    • 0018968775 scopus 로고
    • Identification, purification and partial characterization of an organic anion binding protein from rat liver cell plasma membrane
    • A.W. Wolkoff C.T. Chung Identification, purification and partial characterization of an organic anion binding protein from rat liver cell plasma membrane J Clin Invest 65 1980 1152 1161
    • (1980) J Clin Invest , vol.65 , pp. 1152-1161
    • Wolkoff, A.W.1    Chung, C.T.2
  • 20
    • 0023106660 scopus 로고
    • Role of plasma membrane ligand-binding proteins in the hepatocellular uptake of albumin-bound organic anions
    • P.D. Berk B.J. Potter W. Stremmel Role of plasma membrane ligand-binding proteins in the hepatocellular uptake of albumin-bound organic anions Hepatology 7 1987 165 176
    • (1987) Hepatology , vol.7 , pp. 165-176
    • Berk, P.D.1    Potter, B.J.2    Stremmel, W.3
  • 22
    • 0030460988 scopus 로고    scopus 로고
    • Assignment of the human organic anion transporting polypeptide (OATP) gene to chromosome 12p12 by fluorescence in situ hybridization
    • G.A. Kullak Ublick U. Beuers P.J. Meier H. Domdey G. Paumgartner Assignment of the human organic anion transporting polypeptide (OATP) gene to chromosome 12p12 by fluorescence in situ hybridization J Hepatol 25 1996 985 987
    • (1996) J Hepatol , vol.25 , pp. 985-987
    • Kullak Ublick, G.A.1    Beuers, U.2    Meier, P.J.3    Domdey, H.4    Paumgartner, G.5
  • 23
    • 0020966926 scopus 로고
    • Characterization of the bile acid transport system in normal and transformed hepatocytes: photoaffinity labeling of the taurocholate carrier protein
    • P. Von Dippe D. Levy Characterization of the bile acid transport system in normal and transformed hepatocytes: photoaffinity labeling of the taurocholate carrier protein J Biol Chem 258 1983 8896 8901
    • (1983) J Biol Chem , vol.258 , pp. 8896-8901
    • Von Dippe, P.1    Levy, D.2
  • 24
    • 0029905444 scopus 로고    scopus 로고
    • Effects of submicellar bile salt concentrations on biological membrane permeability to low molecular weight non-ionic solutes
    • A. Albalak M.L. Zeidel S.D. Zucker A.A. Jackson J.M. Donovan Effects of submicellar bile salt concentrations on biological membrane permeability to low molecular weight non-ionic solutes Biochemistry 35 1996 7936 7945
    • (1996) Biochemistry , vol.35 , pp. 7936-7945
    • Albalak, A.1    Zeidel, M.L.2    Zucker, S.D.3    Jackson, A.A.4    Donovan, J.M.5
  • 25
    • 0021092211 scopus 로고
    • (Na,K)-ATPase-mediated cation pumping in cultured rat hepatocytes. Rapid modulation by alanine and taurocholate transport and characterization of its relationship to intracellular sodium concentration
    • R.W. Van Dyke B.F. Scharschmidt (Na,K)-ATPase-mediated cation pumping in cultured rat hepatocytes. Rapid modulation by alanine and taurocholate transport and characterization of its relationship to intracellular sodium concentration J Biol Chem 258 1983 12912 12919
    • (1983) J Biol Chem , vol.258 , pp. 12912-12919
    • Van Dyke, R.W.1    Scharschmidt, B.F.2
  • 27
    • 0018241710 scopus 로고
    • Cytochemical localization of Na+,K+-ATPase in the rat hepatocyte
    • +-ATPase in the rat hepatocyte J Clin Invest 62 1978 1104 1108
    • (1978) J Clin Invest , vol.62 , pp. 1104-1108
    • Blitzer, B.L.1    Boyer, J.L.2
  • 28
    • 0025780035 scopus 로고
    • Role of chloride and intracellular pH on the activity of the rat hepatocyte organic anion transporter
    • A.D. Min K.L. Johansen C.G. Campbell A.W. Wolkoff Role of chloride and intracellular pH on the activity of the rat hepatocyte organic anion transporter J Clin Invest 87 1991 1496 1502
    • (1991) J Clin Invest , vol.87 , pp. 1496-1502
    • Min, A.D.1    Johansen, K.L.2    Campbell, C.G.3    Wolkoff, A.W.4
  • 32
    • 0028891443 scopus 로고
    • The role of sodium in the uptake of ursodeoxycholic acid in isolated hamster hepatocytes
    • B. Bouscarel R. Nussbaum H. Dubner H. Fromm The role of sodium in the uptake of ursodeoxycholic acid in isolated hamster hepatocytes Hepatology 21 1995 145 154
    • (1995) Hepatology , vol.21 , pp. 145-154
    • Bouscarel, B.1    Nussbaum, R.2    Dubner, H.3    Fromm, H.4
  • 33
    • 0024519221 scopus 로고
    • The role of cytoplasmic proteins in hepatic bile acid transport
    • A. Stolz H. Takikawa M. Ookhtens N. Kaplowitz The role of cytoplasmic proteins in hepatic bile acid transport Annu Rev Physiol 51 1989 161 176
    • (1989) Annu Rev Physiol , vol.51 , pp. 161-176
    • Stolz, A.1    Takikawa, H.2    Ookhtens, M.3    Kaplowitz, N.4
  • 34
    • 0026604953 scopus 로고
    • Monensin action on the Golgi complex in perfused rat liver: evidence against bile salt vesicular transport
    • M.O. Reynier I. Abou Hashieh C. Crotte N. Carbuccia B. Richard A. Gerolami Monensin action on the Golgi complex in perfused rat liver: evidence against bile salt vesicular transport Gastroenterology 102 1992 2024 2032
    • (1992) Gastroenterology , vol.102 , pp. 2024-2032
    • Reynier, M.O.1    Abou Hashieh, I.2    Crotte, C.3    Carbuccia, N.4    Richard, B.5    Gerolami, A.6
  • 35
    • 0025250504 scopus 로고
    • Role of intracellular organelles in the hepatic transport of bile acids
    • S. Erlinger Role of intracellular organelles in the hepatic transport of bile acids Biomed Pharmacother 44 1990 409 416
    • (1990) Biomed Pharmacother , vol.44 , pp. 409-416
    • Erlinger, S.1
  • 36
    • 0023954159 scopus 로고
    • Role of the hepatocyte microtubular system in the excretion of bile salts and biliary lipid: implications for intracellular vesicular transport
    • J.M. Crawford C.A. Berken J.L. Gollan Role of the hepatocyte microtubular system in the excretion of bile salts and biliary lipid: implications for intracellular vesicular transport J Lipid Res 29 1988 144 156
    • (1988) J Lipid Res , vol.29 , pp. 144-156
    • Crawford, J.M.1    Berken, C.A.2    Gollan, J.L.3
  • 37
    • 0028019458 scopus 로고
    • Fluorescent choleretic and cholestatic bile salts take different paths across the hepatocyte: transcytosis of glycolithocholate leads to an extensive redistribution of annexin II
    • J.C. Wilton G.M. Matthews R.D. Burgoyne C.O. Mills J.K. Chipman R. Coleman Fluorescent choleretic and cholestatic bile salts take different paths across the hepatocyte: transcytosis of glycolithocholate leads to an extensive redistribution of annexin II J Cell Biol 127 1994 401 410
    • (1994) J Cell Biol , vol.127 , pp. 401-410
    • Wilton, J.C.1    Matthews, G.M.2    Burgoyne, R.D.3    Mills, C.O.4    Chipman, J.K.5    Coleman, R.6
  • 38
    • 0018944339 scopus 로고
    • Influence of colchicine and phalloidin on bile secretion and hepatic ultrastructure in the rat. Possible interaction between microtubules and microfilaments
    • M. Dubin M. Maurice G. Feldmann S. Erlinger Influence of colchicine and phalloidin on bile secretion and hepatic ultrastructure in the rat. Possible interaction between microtubules and microfilaments Gastroenterology 79 1980 646 654
    • (1980) Gastroenterology , vol.79 , pp. 646-654
    • Dubin, M.1    Maurice, M.2    Feldmann, G.3    Erlinger, S.4
  • 39
    • 0027159022 scopus 로고
    • Involvement of microtubules in the swelling-induced stimulation of transcellular taurocholate transport in perfused rat liver
    • D. Haussinger N. Saha C. Hallbrucker F. Lang W. Gerok Involvement of microtubules in the swelling-induced stimulation of transcellular taurocholate transport in perfused rat liver Bio-chem J 291 1993 355 360
    • (1993) Bio-chem J , vol.291 , pp. 355-360
    • Haussinger, D.1    Saha, N.2    Hallbrucker, C.3    Lang, F.4    Gerok, W.5
  • 40
    • 0023806390 scopus 로고
    • Immunoper-oxidase localization of bile salts in rat liver cells. Evidence for a role of the Golgi apparatus in bile salt transport
    • Y. Lamri A. Roda M. Dumont G. Feldmann S. Erlinger Immunoper-oxidase localization of bile salts in rat liver cells. Evidence for a role of the Golgi apparatus in bile salt transport J Clin Invest 82 1988 1173 1182
    • (1988) J Clin Invest , vol.82 , pp. 1173-1182
    • Lamri, Y.1    Roda, A.2    Dumont, M.3    Feldmann, G.4    Erlinger, S.5
  • 41
    • 84955519043 scopus 로고
    • Intracellular bile acid transport in rat liver as visualized by electron micro-scope autoradiography using a bile acid analogue
    • F.J. Suchy W.F. Balistreri J. Hung P. Miller S.A. Garfield Intracellular bile acid transport in rat liver as visualized by electron micro-scope autoradiography using a bile acid analogue Am J Physiol 245 1983 G681 G689
    • (1983) Am J Physiol , vol.245 , pp. G681-G689
    • Suchy, F.J.1    Balistreri, W.F.2    Hung, J.3    Miller, P.4    Garfield, S.A.5
  • 42
    • 0019533699 scopus 로고
    • Hepatic bile salt transport. A review of subcellular binding sites
    • RC. Strange Hepatic bile salt transport. A review of subcellular binding sites Biochem Soc Trans 9 1981 170 174
    • (1981) Biochem Soc Trans , vol.9 , pp. 170-174
    • Strange, RC.1
  • 43
    • 0030731742 scopus 로고    scopus 로고
    • Osmodependent dynamic localization of the multidrug resistance protein 2 in the rat hepatocyte canalicular membrane
    • R. Kubitz D. D'urso D. Keppler D. Haussinger Osmodependent dynamic localization of the multidrug resistance protein 2 in the rat hepatocyte canalicular membrane Gastroenterology 113 1997 1438 1442
    • (1997) Gastroenterology , vol.113 , pp. 1438-1442
    • Kubitz, R.1    D'urso, D.2    Keppler, D.3    Haussinger, D.4
  • 44
    • 0028789248 scopus 로고
    • Vesicle targeting to the apical domain regulates bile excretory function in isolated rat hepatocyte couplets
    • J.L. Boyer C.J. Soroka Vesicle targeting to the apical domain regulates bile excretory function in isolated rat hepatocyte couplets Gastroenterology 109 1995 1600 1611
    • (1995) Gastroenterology , vol.109 , pp. 1600-1611
    • Boyer, J.L.1    Soroka, C.J.2
  • 46
    • 0026044685 scopus 로고
    • ATP-dependent transport of taurocholate across the hepatocyte canalicular membrane mediated by a 110-kDa glycoprotein binding ATP and bile salt
    • M. Müller T. Ishikawa U. Berger C. Klünemann L. Lucka A. Schreyer C. Kannicht W. Reutter G. Kurz D. Keppler ATP-dependent transport of taurocholate across the hepatocyte canalicular membrane mediated by a 110-kDa glycoprotein binding ATP and bile salt J Biol Chem 266 1991 18920 18926
    • (1991) J Biol Chem , vol.266 , pp. 18920-18926
    • Müller, M.1    Ishikawa, T.2    Berger, U.3    Klünemann, C.4    Lucka, L.5    Schreyer, A.6    Kannicht, C.7    Reutter, W.8    Kurz, G.9    Keppler, D.10
  • 47
    • 0024602082 scopus 로고
    • Voltage-driven, taurocholate-dependent secretion in isolated hepatocyte couplets
    • S.A. Weinman J. Graf J.L. Boyer Voltage-driven, taurocholate-dependent secretion in isolated hepatocyte couplets Am J Physiol 256 1989 G826 G832
    • (1989) Am J Physiol , vol.256 , pp. G826-G832
    • Weinman, S.A.1    Graf, J.2    Boyer, J.L.3
  • 48
    • 0027390262 scopus 로고
    • The rat liver ecto-ATPase is also a canalicular bile acid transport protein
    • C.J. Sippel F.J. Suchy M. Ananthanarayanan D.H. Perlmutter The rat liver ecto-ATPase is also a canalicular bile acid transport protein J Biol Chem 268 1993 2083 2091
    • (1993) J Biol Chem , vol.268 , pp. 2083-2091
    • Sippel, C.J.1    Suchy, F.J.2    Ananthanarayanan, M.3    Perlmutter, D.H.4
  • 49
    • 0027984777 scopus 로고
    • Hepatocellular transport of bile acids. Evidence for distinct subcellular localizations of electrogenic and ATP-dependent taurocholate transport in rat hepatocytes
    • C. Kast B. Stieger K.H. Winterhalter P.J. Meier Hepatocellular transport of bile acids. Evidence for distinct subcellular localizations of electrogenic and ATP-dependent taurocholate transport in rat hepatocytes J Biol Chem 269 1994 5179 5186
    • (1994) J Biol Chem , vol.269 , pp. 5179-5186
    • Kast, C.1    Stieger, B.2    Winterhalter, K.H.3    Meier, P.J.4
  • 50
    • 0021328118 scopus 로고
    • Taurocholate transport by rat liver canalicular membrane vesicles. Evidence for the presence of an Na+-independent transport system
    • +-independent transport system J Clin Invest 73 1984 659 663
    • (1984) J Clin Invest , vol.73 , pp. 659-663
    • Inoue, M.1    Kinne, R.2    Tran, T.3    Arias, I.M.4
  • 51
  • 52
    • 0025991571 scopus 로고
    • Rat liver canalicular membrane vesicles contain an ATP-dependent bile acid transport system
    • T. Nishida Z. Gatmaitan M. Che I.M. Arias Rat liver canalicular membrane vesicles contain an ATP-dependent bile acid transport system Proc Natl Acad Sci USA 88 1991 6590 6594
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6590-6594
    • Nishida, T.1    Gatmaitan, Z.2    Che, M.3    Arias, I.M.4
  • 53
    • 0026529394 scopus 로고
    • ATP-dependent bile-salt transport in canalicular rat liver plasma-membrane vesicles
    • B. Stieger B. O'Neill P.J. Meier ATP-dependent bile-salt transport in canalicular rat liver plasma-membrane vesicles Biochem J 284 1992 67 74
    • (1992) Biochem J , vol.284 , pp. 67-74
    • Stieger, B.1    O'Neill, B.2    Meier, P.J.3
  • 54
    • 0024363567 scopus 로고
    • Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase. The primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein I
    • S.H. Lin G. Guidotti Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase. The primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein I J Biol Chem 264 1989 14408 14414
    • (1989) J Biol Chem , vol.264 , pp. 14408-14414
    • Lin, S.H.1    Guidotti, G.2
  • 55
    • 0028070766 scopus 로고
    • Bile acid transport by the rat liver canalicular bile acid transport/ecto-ATPase protein is dependent on ATP but not on its own ecto-ATPase activity
    • C.J. Sippel M.J. Mccollum D.H. Perlmutter Bile acid transport by the rat liver canalicular bile acid transport/ecto-ATPase protein is dependent on ATP but not on its own ecto-ATPase activity J Biol Chem 269 1994 2800 2826
    • (1994) J Biol Chem , vol.269 , pp. 2800-2826
    • Sippel, C.J.1    Mccollum, M.J.2    Perlmutter, D.H.3
  • 56
    • 0025328628 scopus 로고
    • The cell adhesion molecule Cell-CAM 105 is an ecto-ATPase and a member of the immunoglobulin superfamily
    • M. Aurivillius O.C. Hansen M.B. Lazrek E. Bock B. Obrink The cell adhesion molecule Cell-CAM 105 is an ecto-ATPase and a member of the immunoglobulin superfamily FEBS Lett 264 1990 267 269
    • (1990) FEBS Lett , vol.264 , pp. 267-269
    • Aurivillius, M.1    Hansen, O.C.2    Lazrek, M.B.3    Bock, E.4    Obrink, B.5
  • 57
    • 0030753125 scopus 로고    scopus 로고
    • Molecular aspects of hepatobiliary transport
    • M. Muller P.L. Jansen Molecular aspects of hepatobiliary transport Am J Physiol 272 1997 G1285 G1303
    • (1997) Am J Physiol , vol.272 , pp. G1285-G1303
    • Muller, M.1    Jansen, P.L.2
  • 58
    • 0029022589 scopus 로고
    • Identification of a sister gene to P-glycoprotein
    • S. Childs R.L. Yeh E. Georges V. Ling Identification of a sister gene to P-glycoprotein Cancer Res 55 1995 2029 2034
    • (1995) Cancer Res , vol.55 , pp. 2029-2034
    • Childs, S.1    Yeh, R.L.2    Georges, E.3    Ling, V.4
  • 59
    • 0029849789 scopus 로고    scopus 로고
    • The canalicular conjugate export pump encoded by the cmrp/cmoat gene
    • D. Keppler J. Kartenbeck The canalicular conjugate export pump encoded by the cmrp/cmoat gene J.L. Boyer R.K. Ockner Progress in liver diseases 1996 Saunders Philadelphia 55 67
    • (1996) , pp. 55-67
    • Keppler, D.1    Kartenbeck, J.2
  • 60
    • 0025637082 scopus 로고
    • Disorders of calcium and phosphorus homeostasis
    • J.M. Gertner Disorders of calcium and phosphorus homeostasis Pediatr Clin North Am 37 1990 1441 1465
    • (1990) Pediatr Clin North Am , vol.37 , pp. 1441-1465
    • Gertner, J.M.1
  • 61
    • 85119808597 scopus 로고
    • Ionized calcium in pathological human bile
    • D.J. Sutor L.I. Wilkie M.J. Jackson Ionized calcium in pathological human bile J Clin Pathol 258 1980 C755 C786
    • (1980) J Clin Pathol , vol.258 , pp. C755-C786
    • Sutor, D.J.1    Wilkie, L.I.2    Jackson, M.J.3
  • 63
    • 0025017972 scopus 로고
    • Intracellular calcium storage organelles in non-muscle cells: heterogeneity and functional assignment
    • J. Meldolesi L. Madeddu T. Pozzan Intracellular calcium storage organelles in non-muscle cells: heterogeneity and functional assignment Biochim Biophys Acta 1055 1990 130 140
    • (1990) Biochim Biophys Acta , vol.1055 , pp. 130-140
    • Meldolesi, J.1    Madeddu, L.2    Pozzan, T.3
  • 64
    • 0025292743 scopus 로고
    • Mechanism by which mitochondria transport calcium
    • T.E. Gunter D.R. Pfeiffer Mechanism by which mitochondria transport calcium Am J Physiol 258 1990 C755 C786
    • (1990) Am J Physiol , vol.258 , pp. C755-C786
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 65
    • 0028022714 scopus 로고
    • Purification of activated and heterotrimeric forms of Gq proteins
    • J.L. Blank J.H. Exton Purification of activated and heterotrimeric forms of Gq proteins Methods Enzymol 237 1994 174 181
    • (1994) Methods Enzymol , vol.237 , pp. 174-181
    • Blank, J.L.1    Exton, J.H.2
  • 66
    • 0031309403 scopus 로고    scopus 로고
    • Regulation of phosphoinositide phospholipases by G-proteins
    • J.H. Exton Regulation of phosphoinositide phospholipases by G-proteins Adv Exp Med Biol 400A 1997 3 8
    • (1997) Adv Exp Med Biol , vol.400A , pp. 3-8
    • Exton, J.H.1
  • 67
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • M.J. Berridge Inositol trisphosphate and calcium signalling Nature 361 1993 315 325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 68
    • 0028208759 scopus 로고
    • Phosphoinositide phospholipases and G proteins in hormone action
    • J.H. Exton Phosphoinositide phospholipases and G proteins in hormone action Annu Rev Physiol 56 1994 349 369
    • (1994) Annu Rev Physiol , vol.56 , pp. 349-369
    • Exton, J.H.1
  • 69
    • 0344203380 scopus 로고
    • Inositol trisphosphate and diacylglycerol as intracellular second messengers in liver
    • J.R. Williamson R.H. Cooper S.K. Joseph A.P. Thomas Inositol trisphosphate and diacylglycerol as intracellular second messengers in liver Am J Physiol 248 1985 C203 C216
    • (1985) Am J Physiol , vol.248 , pp. C203-C216
    • Williamson, J.R.1    Cooper, R.H.2    Joseph, S.K.3    Thomas, A.P.4
  • 70
    • 0024605461 scopus 로고
    • Hepatic adenosine trisphosphate-dependent Ca2+-transport is mediated by distinct carriers on rat basolateral and canalicular membrane
    • 2+-transport is mediated by distinct carriers on rat basolateral and canalicular membrane J Clin Invest 83 1989 1319 1325
    • (1989) J Clin Invest , vol.83 , pp. 1319-1325
    • Blitzer, B.L.1    Hostetler, B.R.2    Scott, K.A.3
  • 72
    • 0022336164 scopus 로고
    • Role of extracellular Ca2+ in hepatic bile formation and taurocholate transport
    • 2+ in hepatic bile formation and taurocholate transport Am J Physiol 249 1985 G711 G718
    • (1985) Am J Physiol , vol.249 , pp. G711-G718
    • Anwer, M.S.1    Clayton, L.M.2
  • 73
    • 0022100519 scopus 로고
    • Characterization of calcium-deprivation-induced cholestasis in the perfused rat liver
    • J. Reichen F. Berr M. Le G.H. Warren Characterization of calcium-deprivation-induced cholestasis in the perfused rat liver Am J Physiol 249 1985 G48 G57
    • (1985) Am J Physiol , vol.249 , pp. G48-G57
    • Reichen, J.1    Berr, F.2    Le, M.3    Warren, G.H.4
  • 74
    • 0017640046 scopus 로고
    • Isolated rat liver needs calcium to make bile
    • C.A. Owen Isolated rat liver needs calcium to make bile Proc Soc Exp Biol Med 155 1977 314 317
    • (1977) Proc Soc Exp Biol Med , vol.155 , pp. 314-317
    • Owen, C.A.1
  • 75
    • 0023805067 scopus 로고
    • Biliary calcium and bile acid secretion in intact and TPTX rats with varying plasma calcium concentration
    • L. Limlomwongse C. Deachapunya N. Krishnamra Biliary calcium and bile acid secretion in intact and TPTX rats with varying plasma calcium concentration Dig Dis Sci 33 1988 685 691
    • (1988) Dig Dis Sci , vol.33 , pp. 685-691
    • Limlomwongse, L.1    Deachapunya, C.2    Krishnamra, N.3
  • 76
    • 0019596801 scopus 로고
    • Deleterious effects of calcium deprivation on freshly isolated hepatocytes
    • J.W. Edmondson N.U. Bang Deleterious effects of calcium deprivation on freshly isolated hepatocytes Am J Physiol 241 1981 C3 C8
    • (1981) Am J Physiol , vol.241 , pp. C3-C8
    • Edmondson, J.W.1    Bang, N.U.2
  • 77
    • 0023874241 scopus 로고
    • Comparative investigations on the uptake of phallotoxins, bile acids, bovine lactoperoxidase and horseradish peroxidase into rat hepatocytes in suspension and in cell cultures
    • E. Petzinger M. Frimmer Comparative investigations on the uptake of phallotoxins, bile acids, bovine lactoperoxidase and horseradish peroxidase into rat hepatocytes in suspension and in cell cultures Biochim Biophys Acta 937 1988 135 144
    • (1988) Biochim Biophys Acta , vol.937 , pp. 135-144
    • Petzinger, E.1    Frimmer, M.2
  • 79
    • 0027295492 scopus 로고
    • Role of intracellular calcium and protein kinases in the activation of hepatic Na+/taurocho-late cotransport by cyclic AMP
    • +/taurocho-late cotransport by cyclic AMP J Biol Chem 268 1993 17734 17741
    • (1993) J Biol Chem , vol.268 , pp. 17734-17741
    • Grune, S.1    Engelking, L.R.2    Anwer, M.S.3
  • 80
    • 0026593068 scopus 로고
    • Intracellular calcium-mediated activation of hepatic Na+/H+ exchange by arginine vasopressin and phenylephrine
    • + exchange by arginine vasopressin and phenylephrine Hepatology 15 1992 134 143
    • (1992) Hepatology , vol.15 , pp. 134-143
    • Anwer, M.S.1    Atkinson, J.M.2
  • 81
    • 0026609658 scopus 로고
    • Effects of Ca2+ agonists on cytosolic Ca2+ in isolated hepatocytes and on bile secretion in the isolated perfused rat liver
    • 2+ in isolated hepatocytes and on bile secretion in the isolated perfused rat liver Hepatology 15 1992 107 116
    • (1992) Hepatology , vol.15 , pp. 107-116
    • Nathanson, M.H.1    Gautam, A.2    Bruck, R.3    Isales, C.M.4    Boyer, J.L.5
  • 82
    • 0029047024 scopus 로고
    • Hormone-induced bile flow and hepatobiliary calcium fluxes are attenuated in the perfused liver of rats made cholestatic with ethynylestradiol in vivo and with phalloidin in vitro
    • Y. Hamada A. Karjalainen F.L. Bygrave Hormone-induced bile flow and hepatobiliary calcium fluxes are attenuated in the perfused liver of rats made cholestatic with ethynylestradiol in vivo and with phalloidin in vitro Hepatology 21 1995 1455 1464
    • (1995) Hepatology , vol.21 , pp. 1455-1464
    • Hamada, Y.1    Karjalainen, A.2    Bygrave, F.L.3
  • 83
    • 0022249097 scopus 로고
    • Regulation of canalicular bile formation by α-adrenergic action and by external ATP in the isolated perfused rat liver
    • H. Krell H. Jaeschke E. Pfaff Regulation of canalicular bile formation by α-adrenergic action and by external ATP in the isolated perfused rat liver Biochem Biophys Res Commun 131 1985 139 145
    • (1985) Biochem Biophys Res Commun , vol.131 , pp. 139-145
    • Krell, H.1    Jaeschke, H.2    Pfaff, E.3
  • 84
    • 0023270781 scopus 로고
    • Cholestasis and changes in the microcirculation of perfused rat liver caused by the calcium ionophore A-23187 and type I antiarhythmic drugs
    • T. Akerboom R. Lenzen I. Schneider H. Sies Cholestasis and changes in the microcirculation of perfused rat liver caused by the calcium ionophore A-23187 and type I antiarhythmic drugs Biochem Pharmacol 36 1987 3037 3042
    • (1987) Biochem Pharmacol , vol.36 , pp. 3037-3042
    • Akerboom, T.1    Lenzen, R.2    Schneider, I.3    Sies, H.4
  • 85
    • 0028360703 scopus 로고
    • Vasopressin and phorbol-12,13-dibutyrate inhibit glucagon- or cyclic AMP-stimulated taurocholate uptake in isolated rat hepatocytes
    • A. Divald E. Simpser S.E. Fisher P.I. Karl Vasopressin and phorbol-12,13-dibutyrate inhibit glucagon- or cyclic AMP-stimulated taurocholate uptake in isolated rat hepatocytes Hepatology 20 1994 159 165
    • (1994) Hepatology , vol.20 , pp. 159-165
    • Divald, A.1    Simpser, E.2    Fisher, S.E.3    Karl, P.I.4
  • 86
    • 85119808508 scopus 로고    scopus 로고
    • Mechanism of inhibition of cyclic AMP-induced stimulation of Na+/taurocholate cotransport by okadaic acid (abstr)
    • +/taurocholate cotransport by okadaic acid (abstr) Hepatology 26 1997 131A
    • (1997) Hepatology , vol.26 , pp. 131A
    • Mukhopadhyay, S.1    Anwer, M.S.2
  • 87
    • 0024470828 scopus 로고
    • Compartmental modeling of the hepatic transport of taurocholate in the rat in vivo
    • X. Deroubaix T. Coche E. Depiereux E. Feytmans Compartmental modeling of the hepatic transport of taurocholate in the rat in vivo Am J Physiol 257 1989 G210 G220
    • (1989) Am J Physiol , vol.257 , pp. G210-G220
    • Deroubaix, X.1    Coche, T.2    Depiereux, E.3    Feytmans, E.4
  • 88
    • 0026063777 scopus 로고
    • Saturation of hepatic transport of taurocholate in rats in vivo
    • X. Deroubaix T. Coche E. Depiereux E. Feytmans Saturation of hepatic transport of taurocholate in rats in vivo Am J Physiol 260 1991 G189 G196
    • (1991) Am J Physiol , vol.260 , pp. G189-G196
    • Deroubaix, X.1    Coche, T.2    Depiereux, E.3    Feytmans, E.4
  • 89
    • 0026059257 scopus 로고
    • Compartmental analysis of steady-state taurocholate transport kinetics by isolated rat hepatocytes
    • T. Coche E. Deroubaix E. Depereux E. Feytmans Compartmental analysis of steady-state taurocholate transport kinetics by isolated rat hepatocytes Hepatology 13 1991 1203 1214
    • (1991) Hepatology , vol.13 , pp. 1203-1214
    • Coche, T.1    Deroubaix, E.2    Depereux, E.3    Feytmans, E.4
  • 92
    • 85119810332 scopus 로고    scopus 로고
    • Schwartz LR, Schwenk M, Pfaff E, Greim M. Cholestatic steroid hormones inhibit taurocholate uptake by isolated hepatocytes at low concentrations. Naunyn Schmiedebergs Arch Pharmacol 2977;26:2433-2437.
  • 93
    • 0028064311 scopus 로고
    • Papaverine inhibits bile acid excretion in isolated perfused rat liver
    • T. Kumai M. Hoshino T. Hayakawa K. Higashi Papaverine inhibits bile acid excretion in isolated perfused rat liver Hepatology 20 1994 692 699
    • (1994) Hepatology , vol.20 , pp. 692-699
    • Kumai, T.1    Hoshino, M.2    Hayakawa, T.3    Higashi, K.4
  • 94
    • 0031887099 scopus 로고    scopus 로고
    • Effect of ethanol on intracellular vesicular transport from Golgi to the apical cell membrane: role of phosphatidylinositol 3-kinase and phospholipase A2 in Golgi transport vesicles association and fusion with the apical membrane
    • A. Slomiany P. Nowak E. Piotrowski B.L. Slomiany Effect of ethanol on intracellular vesicular transport from Golgi to the apical cell membrane: role of phosphatidylinositol 3-kinase and phospholipase A2 in Golgi transport vesicles association and fusion with the apical membrane Alcohol Clin Exp Res 22 1998 167 175
    • (1998) Alcohol Clin Exp Res , vol.22 , pp. 167-175
    • Slomiany, A.1    Nowak, P.2    Piotrowski, E.3    Slomiany, B.L.4
  • 95
    • 0027320960 scopus 로고
    • Inhibition by cyclosporin A of adeno-sine triphosphate-dependent transport from the hepatocyte into bile [see comments]
    • M. Kadmon C. Klunemann M. Bohme T. Ishikawa K. Gorgas G. Otto C. Herfarth D. Keppler Inhibition by cyclosporin A of adeno-sine triphosphate-dependent transport from the hepatocyte into bile [see comments] Gastroenterology 104 1993 1507 1514
    • (1993) Gastroenterology , vol.104 , pp. 1507-1514
    • Kadmon, M.1    Klunemann, C.2    Bohme, M.3    Ishikawa, T.4    Gorgas, K.5    Otto, G.6    Herfarth, C.7    Keppler, D.8
  • 97
    • 0032558588 scopus 로고    scopus 로고
    • Molecular pathogenesis of cholestasis
    • M. Trauner P.J. Meier J.L. Boyer Molecular pathogenesis of cholestasis N Engl J Med 339 1998 1217 1227
    • (1998) N Engl J Med , vol.339 , pp. 1217-1227
    • Trauner, M.1    Meier, P.J.2    Boyer, J.L.3
  • 98
    • 0023920968 scopus 로고
    • Stimulation of taurocholate and glycocholate efflux from the rat hepatocyte by arginine vasopressin
    • W.F. Kuhn D.A. Gewirtz Stimulation of taurocholate and glycocholate efflux from the rat hepatocyte by arginine vasopressin Am J Physiol 254 1988 G732 G740
    • (1988) Am J Physiol , vol.254 , pp. G732-G740
    • Kuhn, W.F.1    Gewirtz, D.A.2
  • 99
    • 0021236565 scopus 로고
    • Induction of taurocholate release from isolated rat hepatocytes in suspension by α-adrenergic agents and vasopressin: implication for control of bile secretion
    • D.A. Gewirtz J.K. Randolph I.D. Goldman Induction of taurocholate release from isolated rat hepatocytes in suspension by α-adrenergic agents and vasopressin: implication for control of bile secretion Hepatology 4 1984 205 212
    • (1984) Hepatology , vol.4 , pp. 205-212
    • Gewirtz, D.A.1    Randolph, J.K.2    Goldman, I.D.3
  • 100
    • 0023942043 scopus 로고
    • Bile canalicular contraction in the isolated hepatocyte doublet is related to an increase in cytosolic free calcium ion concentration
    • S. Watanabe M. Tomono M. Takeuchi T. Kitamura M. Hirose A. Miyazaki T. Namihisa Bile canalicular contraction in the isolated hepatocyte doublet is related to an increase in cytosolic free calcium ion concentration Liver 8 1988 178 183
    • (1988) Liver , vol.8 , pp. 178-183
    • Watanabe, S.1    Tomono, M.2    Takeuchi, M.3    Kitamura, T.4    Hirose, M.5    Miyazaki, A.6    Namihisa, T.7
  • 101
    • 0025190626 scopus 로고
    • Receptor-mediated stimulation of taurocholate efflux from the rat hepatocyte and the ex vivo perfused rat liver
    • W.F. Kuhn D.M. Heuman Z.R. Vlahcevic D.A. Gewirtz Receptor-mediated stimulation of taurocholate efflux from the rat hepatocyte and the ex vivo perfused rat liver Eur J Pharmacol 175 1990 117 128
    • (1990) Eur J Pharmacol , vol.175 , pp. 117-128
    • Kuhn, W.F.1    Heuman, D.M.2    Vlahcevic, Z.R.3    Gewirtz, D.A.4
  • 102
    • 0032530533 scopus 로고    scopus 로고
    • Taxol resistance mediated by transfection of the liver-specific sister gene of P-glycoprotein
    • S. Childs R.L. Yeh D. Hui V. Ling Taxol resistance mediated by transfection of the liver-specific sister gene of P-glycoprotein Cancer Res 58 1998 4160 4167
    • (1998) Cancer Res , vol.58 , pp. 4160-4167
    • Childs, S.1    Yeh, R.L.2    Hui, D.3    Ling, V.4
  • 103
    • 0028284238 scopus 로고
    • Cholestasis caused by inhibition of the adenosine triphosphate-dependent bile acid transport in rat liver
    • D. Böhme M. Müller I. Leiler G. Jedlitschky D. Keppler Cholestasis caused by inhibition of the adenosine triphosphate-dependent bile acid transport in rat liver Gastroenterology 107 1994 255 265
    • (1994) Gastroenterology , vol.107 , pp. 255-265
    • Böhme, D.1    Müller, M.2    Leiler, I.3    Jedlitschky, G.4    Keppler, D.5
  • 104
    • 0030870794 scopus 로고    scopus 로고
    • Two mechanisms by which ATP depletion potentiates induction of the mitochondrial permeability transition
    • G. Simbula P.A. Glascott Jr. S. Akita J.B. Hoek J.L. Farber Two mechanisms by which ATP depletion potentiates induction of the mitochondrial permeability transition Am J Physiol 273 1997 C479 C488
    • (1997) Am J Physiol , vol.273 , pp. C479-C488
    • Simbula, G.1    Glascott, P.A.2    Akita, S.3    Hoek, J.B.4    Farber, J.L.5
  • 105
  • 106
    • 0021504237 scopus 로고
    • Ca2+ causes active contraction of bile canaliculi: direct evidence from microinjection studies
    • 2+ causes active contraction of bile canaliculi: direct evidence from microinjection studies Proc Natl Acad Sci USA 81 1984 6164 6168
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6164-6168
    • Watanabe, S.1    Phillips, M.J.2
  • 107
    • 0020584554 scopus 로고
    • Effects of cytochalasin D and colchicine on the uptake, translocation, and biliary secretion of horseradish peroxidase and [14C]sodium taurocholate in the rat
    • 14C]sodium taurocholate in the rat Gastroenterology 85 1983 385 394
    • (1983) Gastroenterology , vol.85 , pp. 385-394
    • Kacich, R.L.1    Raymond, R.H.2    Jones, A.L.3
  • 108
    • 0016697537 scopus 로고
    • Phalloidin-induced hyperplasia of actin filaments in rat hepatocytes
    • G. Fabbiani R. Montesano B. Tuchweber M. Salas L. Orci Phalloidin-induced hyperplasia of actin filaments in rat hepatocytes Lab Invest 33 1975 562 569
    • (1975) Lab Invest , vol.33 , pp. 562-569
    • Fabbiani, G.1    Montesano, R.2    Tuchweber, B.3    Salas, M.4    Orci, L.5
  • 109
    • 0026072414 scopus 로고
    • Vasopressin and A23187 stimulate phosphorylation of myosin light chain-1 in isolated rat hepatocytes
    • Y. Yamaguchi E. Dalle Molle W.G. Hardison Vasopressin and A23187 stimulate phosphorylation of myosin light chain-1 in isolated rat hepatocytes Am J Physiol 261 1991 G312 G319
    • (1991) Am J Physiol , vol.261 , pp. G312-G319
    • Yamaguchi, Y.1    Dalle Molle, E.2    Hardison, W.G.3
  • 110
    • 0022568214 scopus 로고
    • Cellular mechanisms of cholestasis
    • D.G. Oelberg R. Lester Cellular mechanisms of cholestasis Annu Rev Med 37 1986 297 317
    • (1986) Annu Rev Med , vol.37 , pp. 297-317
    • Oelberg, D.G.1    Lester, R.2
  • 111
    • 0021198316 scopus 로고
    • The role of calcium in the pathogenesis of gallstones: Ca++ electrode studies of model bile salt solutions and other biologic systems
    • ++ electrode studies of model bile salt solutions and other biologic systems Hepatology 4 1984 228S 243S
    • (1984) Hepatology , vol.4 , pp. 228S-243S
    • Moore, E.W.1
  • 112
    • 0027408588 scopus 로고
    • Ursodeoxycholate mobilizes intracellular Ca2+ and activates phosphorylase α in isolated hepatocytes
    • 2+ and activates phosphorylase α in isolated hepatocytes Am J Physiol 264 1993 G243 G251
    • (1993) Am J Physiol , vol.264 , pp. G243-G251
    • Bouscarel, B.1    Fromm, H.2    Nussbaum, R.3
  • 113
    • 0023948979 scopus 로고
    • Cholestasis and the interactions of sulfated glyco- and taurolithocholate with calcium
    • R. Van der Meer R.J. Vonk F. Kuipers Cholestasis and the interactions of sulfated glyco- and taurolithocholate with calcium Am J Physiol 254 1988 G644 G649
    • (1988) Am J Physiol , vol.254 , pp. G644-G649
    • Van der Meer, R.1    Vonk, R.J.2    Kuipers, F.3
  • 114
    • 0024240343 scopus 로고
    • The calcium ionophore A23187 increases the tight-junctional permeability in rat liver
    • K.S. Kan R. Coleman The calcium ionophore A23187 increases the tight-junctional permeability in rat liver Biochem J 256 1988 1039 1041
    • (1988) Biochem J , vol.256 , pp. 1039-1041
    • Kan, K.S.1    Coleman, R.2
  • 116
    • 0023813484 scopus 로고
    • Hormonal regulation of hepatocyte tight junction permeability
    • P.J. Lowe K. Miyai J.H. Steinbach W.G.M. Hardison Hormonal regulation of hepatocyte tight junction permeability Am J Physiol 255 1988 G454 G461
    • (1988) Am J Physiol , vol.255 , pp. G454-G461
    • Lowe, P.J.1    Miyai, K.2    Steinbach, J.H.3    Hardison, W.G.M.4
  • 117
    • 0018079817 scopus 로고
    • Bile formation in the rat: the role of paracellular shunt pathway
    • T.J. Layden E. Elias J.L. Boyer Bile formation in the rat: the role of paracellular shunt pathway J Clin Invest 62 1978 1375 1385
    • (1978) J Clin Invest , vol.62 , pp. 1375-1385
    • Layden, T.J.1    Elias, E.2    Boyer, J.L.3
  • 118
    • 0030296967 scopus 로고    scopus 로고
    • Vasopressin reduces taurochenodeoxycholate-induced hepato-toxicity by lowering the hepatocyte taurochenodeoxycholate content
    • T. Nakazawa M. Hoshino T. Hayakawa A. Tanaka T. Ohiwa Vasopressin reduces taurochenodeoxycholate-induced hepato-toxicity by lowering the hepatocyte taurochenodeoxycholate content J Hepatol 25 1996 739 747
    • (1996) J Hepatol , vol.25 , pp. 739-747
    • Nakazawa, T.1    Hoshino, M.2    Hayakawa, T.3    Tanaka, A.4    Ohiwa, T.5
  • 119
    • 0028941914 scopus 로고
    • A role for protein kinase C-mediated phosphorylation in eliciting glucagon desensitization in rat hepatocytes
    • A. Savage L. Zeng M.D. Houslay A role for protein kinase C-mediated phosphorylation in eliciting glucagon desensitization in rat hepatocytes Biochem J 307 1995 281 285
    • (1995) Biochem J , vol.307 , pp. 281-285
    • Savage, A.1    Zeng, L.2    Houslay, M.D.3
  • 120
    • 0028234285 scopus 로고
    • Analysis of vasoactive intestinal peptide receptors and the G protein regulation of adenylyl cyclase in seminal vesicle membranes from streptozoto-cindiabetic rats
    • M.S. Rodriguez Pena L.G. Guijarro M.G. Juarranz N. Rodriguez Henche A.M. Bajo F. Aguado J.C. Prieto Analysis of vasoactive intestinal peptide receptors and the G protein regulation of adenylyl cyclase in seminal vesicle membranes from streptozoto-cindiabetic rats Cell Signal 6 1994 147 156
    • (1994) Cell Signal , vol.6 , pp. 147-156
    • Rodriguez Pena, M.S.1    Guijarro, L.G.2    Juarranz, M.G.3    Rodriguez Henche, N.4    Bajo, A.M.5    Aguado, F.6    Prieto, J.C.7
  • 121
    • 0028865815 scopus 로고
    • Differential coupling of glucagon and beta-adrenergic receptors with the small and large forms of the stimulatory G protein
    • T. Yagami Differential coupling of glucagon and beta-adrenergic receptors with the small and large forms of the stimulatory G protein Mol Pharmacol 48 1995 849 854
    • (1995) Mol Pharmacol , vol.48 , pp. 849-854
    • Yagami, T.1
  • 122
    • 0024195969 scopus 로고
    • The role of cyclic AMP in rapid and long-term regulation of gluconeogenesis and glycolysis
    • S.J. Pilkis T.H. Claus M.R. el Maghrabi The role of cyclic AMP in rapid and long-term regulation of gluconeogenesis and glycolysis Adv Second Messenger Phosphoprotein Res 22 1988 175 191
    • (1988) Adv Second Messenger Phosphoprotein Res , vol.22 , pp. 175-191
    • Pilkis, S.J.1    Claus, T.H.2    el Maghrabi, M.R.3
  • 123
    • 0028108414 scopus 로고
    • Bile acid efflux mediated by the rat liver canalicular bile acid transport/ecto-ATPase protein requires serine 503 phosphorylation and is regulated by tyro-sine 488 phosphorylation
    • C.J. Sippel R.J. Fallon D.H. Perlmutter Bile acid efflux mediated by the rat liver canalicular bile acid transport/ecto-ATPase protein requires serine 503 phosphorylation and is regulated by tyro-sine 488 phosphorylation J Biol Chem 269 1994 19539 19545
    • (1994) J Biol Chem , vol.269 , pp. 19539-19545
    • Sippel, C.J.1    Fallon, R.J.2    Perlmutter, D.H.3
  • 125
    • 0016604436 scopus 로고
    • Characteristics common to choleretic increments of bile induced by theophyline, glucagon and SQ-20009 in the dog
    • J.L. Barnhart B. Combes Characteristics common to choleretic increments of bile induced by theophyline, glucagon and SQ-20009 in the dog Proc Soc Exp Biol Med 150 1975 591 596
    • (1975) Proc Soc Exp Biol Med , vol.150 , pp. 591-596
    • Barnhart, J.L.1    Combes, B.2
  • 126
    • 0026787649 scopus 로고
    • Secretin stimulates bile ductular secretory activity through the cAMP system
    • R. Lenzen G. Alpini N. Tavaloni Secretin stimulates bile ductular secretory activity through the cAMP system Am J Physiol 97 1992 G527 G532
    • (1992) Am J Physiol , vol.97 , pp. G527-G532
    • Lenzen, R.1    Alpini, G.2    Tavaloni, N.3
  • 127
    • 0028811653 scopus 로고
    • Protein kinase C: structure, function, and regulation
    • A.C. Newton Protein kinase C: structure, function, and regulation J Biol Chem 270 1995 28495 28498
    • (1995) J Biol Chem , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 128
    • 33745785060 scopus 로고
    • The structure expression, and properties of additional members of the protein kinase C family
    • Y. Ohno T. Fuji T. Ogita U. Kikkawa K. Igarashi Y. Nishizuka The structure expression, and properties of additional members of the protein kinase C family J Biol Chem 266 1991 168 173
    • (1991) J Biol Chem , vol.266 , pp. 168-173
    • Ohno, Y.1    Fuji, T.2    Ogita, T.3    Kikkawa, U.4    Igarashi, K.5    Nishizuka, Y.6
  • 129
    • 0028954737 scopus 로고
    • Ursodeoxycholic acid inhibits glucagon-induced cAMP formation in hamster hepatocytes: a role for PKC
    • B. Bouscarel T.W. Gettys H. Fromm H. Dubner Ursodeoxycholic acid inhibits glucagon-induced cAMP formation in hamster hepatocytes: a role for PKC Am J Physiol 268 1995 G300 G310
    • (1995) Am J Physiol , vol.268 , pp. G300-G310
    • Bouscarel, B.1    Gettys, T.W.2    Fromm, H.3    Dubner, H.4
  • 130
    • 0025769221 scopus 로고
    • Differences in phorbol ester induced decrease of the activity of protein kinse C isozymes in rat hepatocytes
    • M. Robles Flores R. Alcantara-Hernandez J.A. Garcia Sainz Differences in phorbol ester induced decrease of the activity of protein kinse C isozymes in rat hepatocytes Biochim Biophys Acta 1094 1991 77 84
    • (1991) Biochim Biophys Acta , vol.1094 , pp. 77-84
    • Robles Flores, M.1    Alcantara-Hernandez, R.2    Garcia Sainz, J.A.3
  • 132
    • 0029792502 scopus 로고    scopus 로고
    • Hepatocellular protein kinase C activation by bile acids: implications for regulation of cholesterol 7a-hydroxylase
    • R.T. Stravitz Y.-P. Rao Z.R. Vlahcevic E.C. Gurley W.D. Jarvis P.B. Hylemon Y.P. Rao Hepatocellular protein kinase C activation by bile acids: implications for regulation of cholesterol 7a-hydroxylase Am J Physiol 271 1996 G293 G303
    • (1996) Am J Physiol , vol.271 , pp. G293-G303
    • Stravitz, R.T.1    Rao, Y.-P.2    Vlahcevic, Z.R.3    Gurley, E.C.4    Jarvis, W.D.5    Hylemon, P.B.6    Rao, Y.P.7
  • 133
    • 0020326790 scopus 로고
    • Direct activation of calcium-activated phospholipid-dependent protein kinase by tumor-promoting phorbol esters
    • M. Castagna Y. Takai K. Kaibuchi K. Sano U. Kikkawa Y. Nishizuka Direct activation of calcium-activated phospholipid-dependent protein kinase by tumor-promoting phorbol esters J Biol Chem 257 1982 7848 7851
    • (1982) J Biol Chem , vol.257 , pp. 7848-7851
    • Castagna, M.1    Takai, Y.2    Kaibuchi, K.3    Sano, K.4    Kikkawa, U.5    Nishizuka, Y.6
  • 134
    • 0024541436 scopus 로고
    • Functions of sphingolipids and sphingo-lipid breakdown products in cellular regulation
    • Y.A. Hannum R.M. Bell Functions of sphingolipids and sphingo-lipid breakdown products in cellular regulation Science 243 1988 500 507
    • (1988) Science , vol.243 , pp. 500-507
    • Hannum, Y.A.1    Bell, R.M.2
  • 135
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: a theme in signal transduction
    • D. Mochly Rosen Localization of protein kinases by anchoring proteins: a theme in signal transduction Science 268 1995 247 251
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly Rosen, D.1
  • 136
    • 0024375340 scopus 로고
    • Protein kinase C agonists inhibit bile secretion independently of effects on the microcirculation in the isolated perfused rat liver
    • J.G. Corasanti N.D. Smith E.R. Gordon J.L. Boyer Protein kinase C agonists inhibit bile secretion independently of effects on the microcirculation in the isolated perfused rat liver Hepatology 10 1989 8 13
    • (1989) Hepatology , vol.10 , pp. 8-13
    • Corasanti, J.G.1    Smith, N.D.2    Gordon, E.R.3    Boyer, J.L.4
  • 137
    • 0021270226 scopus 로고
    • The effect of glucagon-induced adenosine 3',5'-monophosphate concentrations on bile acid synthesis in isolated rat liver cells
    • K.M. Botham K.E. Suckling G.S. Boyd The effect of glucagon-induced adenosine 3',5'-monophosphate concentrations on bile acid synthesis in isolated rat liver cells FEBS Lett 168 1984 317 320
    • (1984) FEBS Lett , vol.168 , pp. 317-320
    • Botham, K.M.1    Suckling, K.E.2    Boyd, G.S.3
  • 138
    • 0026523504 scopus 로고
    • Cyclic AMP and the regulation of cholesterol metabolism
    • K.M. Botham Cyclic AMP and the regulation of cholesterol metabolism Biochem Soc Trans 20 1992 454 459
    • (1992) Biochem Soc Trans , vol.20 , pp. 454-459
    • Botham, K.M.1
  • 139
    • 0023875807 scopus 로고
    • Role of glucagon in cholecystokinin-stimulated bile flow in dogs
    • 139 D.L. Kaminski Y. Deshpande M.C. Beinfeld Role of glucagon in cholecystokinin-stimulated bile flow in dogs Am J Physiol 254 1988 G864 G869
    • (1988) Am J Physiol , vol.254 , pp. G864-G869
    • Kaminski, D.L.1    Deshpande, Y.2    Beinfeld, M.C.3
  • 140
    • 0023875807 scopus 로고
    • Role of glucagon in cholecystokinin-stimulated bile flow in dogs
    • D.L. Kaminski Y. Deshpande M.C. Beinfeld Role of glucagon in cholecystokinin-stimulated bile flow in dogs Am J Physiol 254 1988 G864 G869
    • (1988) Am J Physiol , vol.254 , pp. G864-G869
    • Kaminski, D.L.1    Deshpande, Y.2    Beinfeld, M.C.3
  • 141
    • 0025077050 scopus 로고
    • DBcAMP stimulates vesicule transport and HRP excretion in isolated perfused rat liver
    • T. Hayakawa R. Bruck O.C. Ng J.L. Boyer DBcAMP stimulates vesicule transport and HRP excretion in isolated perfused rat liver Am J Physiol 259 1990 G727 G735
    • (1990) Am J Physiol , vol.259 , pp. G727-G735
    • Hayakawa, T.1    Bruck, R.2    Ng, O.C.3    Boyer, J.L.4
  • 142
    • 0025167499 scopus 로고
    • Mechanism of glucagon-induced choleresis in guinea pigs
    • R. Lenzen V.J. Hruby N. Tavaloni Mechanism of glucagon-induced choleresis in guinea pigs Am J Physiol 259 1990 G736 G744
    • (1990) Am J Physiol , vol.259 , pp. G736-G744
    • Lenzen, R.1    Hruby, V.J.2    Tavaloni, N.3
  • 144
    • 0019472053 scopus 로고
    • The effect of glucagon, dibutyrylic cyclic AMP and insulin on bile production in the intact rat and the perfused rat liver
    • O.O. Thomsen J.A. Larsen The effect of glucagon, dibutyrylic cyclic AMP and insulin on bile production in the intact rat and the perfused rat liver Acta Physiol Scand 111 1981 23 30
    • (1981) Acta Physiol Scand , vol.111 , pp. 23-30
    • Thomsen, O.O.1    Larsen, J.A.2
  • 145
    • 0022976869 scopus 로고
    • Studies on the hepatic calcium-mobilizing activity of aluminum fluoride and glucagon. Modulation by cAMP and phorbol myristate acetate
    • P.F. Blackmore J.H. Exton Studies on the hepatic calcium-mobilizing activity of aluminum fluoride and glucagon. Modulation by cAMP and phorbol myristate acetate J Biol Chem 261 1986 11056 11063
    • (1986) J Biol Chem , vol.261 , pp. 11056-11063
    • Blackmore, P.F.1    Exton, J.H.2
  • 146
    • 0027363499 scopus 로고
    • Calcium: its modulation in liver by cross-talk between the actions of glucagon and calcium-mobilizing agonists
    • F.L. Bygrave A. Benedetti Calcium: its modulation in liver by cross-talk between the actions of glucagon and calcium-mobilizing agonists Biochem J 296 1993 7 14
    • (1993) Biochem J , vol.296 , pp. 7-14
    • Bygrave, F.L.1    Benedetti, A.2
  • 148
    • 0027288899 scopus 로고
    • Evidence that stimulation of plasma-membrane Ca2+ inflow is an early action of glucagon and dibutyryl cyclic AMP in rat hepatocytes
    • 2+ inflow is an early action of glucagon and dibutyryl cyclic AMP in rat hepatocytes Bio-chem J 292 1993 19 22
    • (1993) Bio-chem J , vol.292 , pp. 19-22
    • Bygrave, F.L.1    Gamberucci, A.2    Fulceri, R.3    Benedetti, A.4
  • 149
    • 0022136024 scopus 로고
    • Effect of glucagon on hepatic taurocholate uptake: relationship to membrane potential
    • J.W. Edmondson B.A. Miller L. Lumeng Effect of glucagon on hepatic taurocholate uptake: relationship to membrane potential Am J Physiol 249 1985 G427 G433
    • (1985) Am J Physiol , vol.249 , pp. G427-G433
    • Edmondson, J.W.1    Miller, B.A.2    Lumeng, L.3
  • 150
    • 0018860802 scopus 로고
    • Antagonistic effect of insulin on glucagon-evoked hyperpolarization. A correlation between changes in membrane potential and gluconeogenesis
    • N. Friedmann G. Dambach Antagonistic effect of insulin on glucagon-evoked hyperpolarization. A correlation between changes in membrane potential and gluconeogenesis Biochim Biophys Acta 596 1980 180 185
    • (1980) Biochim Biophys Acta , vol.596 , pp. 180-185
    • Friedmann, N.1    Dambach, G.2
  • 152
    • 0018910560 scopus 로고
    • Volume- and temperature-dependent permeabilities in isolated rat liver cells
    • B. Berthon M. Claret J.L. Mazet J. Poggioli Volume- and temperature-dependent permeabilities in isolated rat liver cells J Physiol (Lond) 305 1980 267 277
    • (1980) J Physiol (Lond) , vol.305 , pp. 267-277
    • Berthon, B.1    Claret, M.2    Mazet, J.L.3    Poggioli, J.4
  • 153
    • 85119810478 scopus 로고    scopus 로고
    • Role of K+ flux in the regulation of glucagon-induced glucose metabolism in perfused hamster liver (abstr)
    • + flux in the regulation of glucagon-induced glucose metabolism in perfused hamster liver (abstr) Hepatology 28 1998 621A
    • (1998) Hepatology , vol.28 , pp. 621A
    • Adighibe, O.1    Bouscarel, B.2
  • 156
    • 0030841172 scopus 로고    scopus 로고
    • Effect of cholestasis on regulation of cAMP synthesis by glucagon and bile acids in isolated hepatocytes
    • Y. Matsuzaki B. Bouscarel M. Le S. Ceryak T.W. Gettys J. Shoda H. Fromm Effect of cholestasis on regulation of cAMP synthesis by glucagon and bile acids in isolated hepatocytes Am J Physiol 273 1997 G164 G173
    • (1997) Am J Physiol , vol.273 , pp. G164-G173
    • Matsuzaki, Y.1    Bouscarel, B.2    Le, M.3    Ceryak, S.4    Gettys, T.W.5    Shoda, J.6    Fromm, H.7
  • 159
    • 0031798966 scopus 로고    scopus 로고
    • Changes in G protein expression account for impaired modulation of hepatic cAMP formation after bile duct-ligation
    • B. Bouscarel Y. Matsuzaki M. Le T.W. Gettys H. Fromm Changes in G protein expression account for impaired modulation of hepatic cAMP formation after bile duct-ligation Am J Physiol 274 1998 G1151 G1159
    • (1998) Am J Physiol , vol.274 , pp. G1151-G1159
    • Bouscarel, B.1    Matsuzaki, Y.2    Le, M.3    Gettys, T.W.4    Fromm, H.5
  • 160
  • 161
    • 0030870025 scopus 로고    scopus 로고
    • Identification of a bile acid response element in the cholesterol 7 alpha-hydroxylase gene CYP7A
    • D. Stroup M. Crestani J.Y. Chiang Identification of a bile acid response element in the cholesterol 7 alpha-hydroxylase gene CYP7A Am J Physiol 273 1997 G508 G517
    • (1997) Am J Physiol , vol.273 , pp. G508-G517
    • Stroup, D.1    Crestani, M.2    Chiang, J.Y.3
  • 163
    • 17344370605 scopus 로고    scopus 로고
    • Cyclic adenosine monophosphate-mediated protection against bile acid-induced apoptosis in cultured rat hepatocytes
    • C.R. Webster M.S. Anwer Cyclic adenosine monophosphate-mediated protection against bile acid-induced apoptosis in cultured rat hepatocytes Hepatology 27 1998 1324 1331
    • (1998) Hepatology , vol.27 , pp. 1324-1331
    • Webster, C.R.1    Anwer, M.S.2
  • 164
    • 0025810290 scopus 로고
    • The mechanism for synergism between phospholipase C and adenylyl cyclase linked hormones in liver
    • GM Burgess GstJ Bird JF Obie JW. Putney The mechanism for synergism between phospholipase C and adenylyl cyclase linked hormones in liver J Biol Chem 260 1991 4772 4781
    • (1991) J Biol Chem , vol.260 , pp. 4772-4781
    • Burgess, GM1    Bird, GstJ2    Obie, JF3    Putney, JW.4
  • 165
    • 0028332980 scopus 로고
    • The synergistic action (cross-talk) of glucagon and vasopressin induces early bile flow and plasma-membrane calcium fluxes in the perfused rat liver
    • A. Karjalainen F.L. Bygrave The synergistic action (cross-talk) of glucagon and vasopressin induces early bile flow and plasma-membrane calcium fluxes in the perfused rat liver Biochem J 301 1994 187 192
    • (1994) Biochem J , vol.301 , pp. 187-192
    • Karjalainen, A.1    Bygrave, F.L.2
  • 166
    • 0026772018 scopus 로고
    • Hormonal regulation of paracellular permeability in isolated rat hepatocyte couplets
    • M.H. Nathanson A. Gautam O.C. Ng R. Bruck J.L. Boyer Hormonal regulation of paracellular permeability in isolated rat hepatocyte couplets Am J Physiol 262 1992 G1079 G1086
    • (1992) Am J Physiol , vol.262 , pp. G1079-G1086
    • Nathanson, M.H.1    Gautam, A.2    Ng, O.C.3    Bruck, R.4    Boyer, J.L.5
  • 167
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Y. Nishizuka Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C Science 258 1992 607 614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 168
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • J.M. Anderson C.M. Van Itallie Tight junctions and the molecular basis for regulation of paracellular permeability Am J Physiol 269 1995 G467 G475
    • (1995) Am J Physiol , vol.269 , pp. G467-G475
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 169
    • 0011870725 scopus 로고
    • The protein kinase C agonist, 12,13 phorbol dibutyrate counteracts cAMP-stimulated horseradish peroxidase excretion in the isolated perfused rat liver (abstr)
    • T. Hayakawa J.G. Corasanti K.A. Phillips J.L. Boyer The protein kinase C agonist, 12,13 phorbol dibutyrate counteracts cAMP-stimulated horseradish peroxidase excretion in the isolated perfused rat liver (abstr) Hepatology 10 1989 598
    • (1989) Hepatology , vol.10 , pp. 598
    • Hayakawa, T.1    Corasanti, J.G.2    Phillips, K.A.3    Boyer, J.L.4
  • 170
    • 0021278290 scopus 로고
    • The phorbol ester TPA inhibits glucagon-stimulated adenylate cyclase activity
    • C.M. Heyworth A.D. Whetton A.R. Kinsella M.D. Houslay The phorbol ester TPA inhibits glucagon-stimulated adenylate cyclase activity FEBS Lett 170 1984 38 42
    • (1984) FEBS Lett , vol.170 , pp. 38-42
    • Heyworth, C.M.1    Whetton, A.D.2    Kinsella, A.R.3    Houslay, M.D.4
  • 172
    • 0023938260 scopus 로고
    • Bile acids increase cellular free calcium in cultured kidney cells (LLC-PK)
    • M.H. Montrose R. Lester P. Zimniak M.S. Anwer H. Murer Bile acids increase cellular free calcium in cultured kidney cells (LLC-PK) Pflugers Arch 412 1988 164 171
    • (1988) Pflugers Arch , vol.412 , pp. 164-171
    • Montrose, M.H.1    Lester, R.2    Zimniak, P.3    Anwer, M.S.4    Murer, H.5
  • 173
    • 0028354141 scopus 로고
    • Premicellar taurocholate enhances calcium uptake from all regions of rat small intestine
    • A.J. Sanyal J.I. Hirsch E.W. Moore Premicellar taurocholate enhances calcium uptake from all regions of rat small intestine Gastroenterology 106 1994 866 874
    • (1994) Gastroenterology , vol.106 , pp. 866-874
    • Sanyal, A.J.1    Hirsch, J.I.2    Moore, E.W.3
  • 176
    • 0024324754 scopus 로고
    • Effect of bile acids on calcium efflux from isolated rat hepatocytes and perfused rat livers
    • M.S. Anwer J.M. Little D.G. Oelberg P. Zimniak R. Lester Effect of bile acids on calcium efflux from isolated rat hepatocytes and perfused rat livers Proc Soc Exp Biol Med 191 1989 147 152
    • (1989) Proc Soc Exp Biol Med , vol.191 , pp. 147-152
    • Anwer, M.S.1    Little, J.M.2    Oelberg, D.G.3    Zimniak, P.4    Lester, R.5
  • 177
  • 181
    • 0027398769 scopus 로고
    • Effect of bile acids on intracellular calcium in isolated rat hepatocyte couplets
    • N. Thibault F. Ballet Effect of bile acids on intracellular calcium in isolated rat hepatocyte couplets Biochem Pharmacol 45 1993 289 293
    • (1993) Biochem Pharmacol , vol.45 , pp. 289-293
    • Thibault, N.1    Ballet, F.2
  • 182
    • 0023866562 scopus 로고
    • Release of calcium from the endoplasmic reticulum by bile acids in rat liver cells
    • L. Combettes M. Dumont B. Berthon S. Erlinger M. Claret Release of calcium from the endoplasmic reticulum by bile acids in rat liver cells J Biol Chem 263 1988 2299 2303
    • (1988) J Biol Chem , vol.263 , pp. 2299-2303
    • Combettes, L.1    Dumont, M.2    Berthon, B.3    Erlinger, S.4    Claret, M.5
  • 183
    • 0025960077 scopus 로고
    • Evidence for bile acid evoked oscillations of Ca2+ dependent K+ permeability unrelated to a D-myo-inositol 1,4,5-trisphosphate effect in isolated guinea pig liver cells
    • + permeability unrelated to a D-myo-inositol 1,4,5-trisphosphate effect in isolated guinea pig liver cells J Biol Chem 266 1991 268 273
    • (1991) J Biol Chem , vol.266 , pp. 268-273
    • Capiod, T.1    Combettes, L.2    Noel, J.3    Claret, M.4
  • 184
    • 0025350112 scopus 로고
    • Calcium oscillations
    • M.J. Berridge Calcium oscillations J Biol Chem 265 1990 9583 9586
    • (1990) J Biol Chem , vol.265 , pp. 9583-9586
    • Berridge, M.J.1
  • 186
    • 0026482982 scopus 로고
    • Oscillations of cytosolic free calcium concentration in the presence of intracellular antibodies to phosphatidylinositol 4,5-bisphosphate in voltage-clamped guinea-pig hepatocytes
    • J. Noel K. Fukami A.M. Hill T. Capiod Oscillations of cytosolic free calcium concentration in the presence of intracellular antibodies to phosphatidylinositol 4,5-bisphosphate in voltage-clamped guinea-pig hepatocytes Biochem J 288 1992 357 360
    • (1992) Biochem J , vol.288 , pp. 357-360
    • Noel, J.1    Fukami, K.2    Hill, A.M.3    Capiod, T.4
  • 187
    • 0025195254 scopus 로고
    • Release of Ca2+ from the endoplasmic reticulum is not the mechanism for bile acid-induced cholestasis and hepatotoxicity in the intact rat liver
    • 2+ from the endoplasmic reticulum is not the mechanism for bile acid-induced cholestasis and hepatotoxicity in the intact rat liver J Clin Invest 85 1990 1255 1259
    • (1990) J Clin Invest , vol.85 , pp. 1255-1259
    • Farrell, G.C.1    Duddy, S.K.2    Kass, G.E.3    Llopis, J.4    Gahm, A.5    Orrenius, S.6
  • 188
    • 0025167073 scopus 로고
    • Calcium free reperfusion prevents mitochondrial calcium accumulation but exacerbates injury
    • P.W. Cho E.A. Miescher M.G. Clemens Calcium free reperfusion prevents mitochondrial calcium accumulation but exacerbates injury Circ Shock 32 1990 43 53
    • (1990) Circ Shock , vol.32 , pp. 43-53
    • Cho, P.W.1    Miescher, E.A.2    Clemens, M.G.3
  • 189
    • 0026457313 scopus 로고
    • Taurolithocholate-induced Ca2+ release is inhibited by phorbol esters in isolated hepatocytes
    • 2+ release is inhibited by phorbol esters in isolated hepatocytes Biochem J 287 1992 891 896
    • (1992) Biochem J , vol.287 , pp. 891-896
    • Combettes, L.1    Berthon, B.2    Claret, M.3
  • 190
    • 0023850724 scopus 로고
    • Effect of the bile acid taurolithocholate on cell calcium in saponin-treated rat hepatocytes
    • L. Combettes M. Dumont B. Berthon S. Erlinger M. Claret Effect of the bile acid taurolithocholate on cell calcium in saponin-treated rat hepatocytes FEBS Lett 227 1988 161 166
    • (1988) FEBS Lett , vol.227 , pp. 161-166
    • Combettes, L.1    Dumont, M.2    Berthon, B.3    Erlinger, S.4    Claret, M.5
  • 191
    • 0021993764 scopus 로고
    • Inhibition of hepatic α1-adrenergic effects and binding by phorbol myristate acetate
    • C.J. Lynch R. Charest S.B. Bocckino J.H. Exton P.F. Blackmore Inhibition of hepatic α1-adrenergic effects and binding by phorbol myristate acetate J Biol Chem 260 1985 2844 2851
    • (1985) J Biol Chem , vol.260 , pp. 2844-2851
    • Lynch, C.J.1    Charest, R.2    Bocckino, S.B.3    Exton, J.H.4    Blackmore, P.F.5
  • 192
    • 0025719724 scopus 로고
    • Bile acid stimulation of cyclic AMP and ion transport in developing rabbit colon
    • G.D. Potter J.H. Sellin S.M. Burlingame Bile acid stimulation of cyclic AMP and ion transport in developing rabbit colon J Pediatr Gastroenterol Nutr 13 1991 335 341
    • (1991) J Pediatr Gastroenterol Nutr , vol.13 , pp. 335-341
    • Potter, G.D.1    Sellin, J.H.2    Burlingame, S.M.3
  • 194
    • 0028888589 scopus 로고
    • Alteration of cAMP-mediated hormonal responsiveness by bile acids in cells of nonhepatic origin
    • B. Bouscarel S. Ceryak T.W. Gettys H. Fromm F. Noonan Alteration of cAMP-mediated hormonal responsiveness by bile acids in cells of nonhepatic origin Am J Physiol 268 1995 G908 G916
    • (1995) Am J Physiol , vol.268 , pp. G908-G916
    • Bouscarel, B.1    Ceryak, S.2    Gettys, T.W.3    Fromm, H.4    Noonan, F.5
  • 195
    • 0029999555 scopus 로고    scopus 로고
    • Effects of bile acids on iodide uptake and deoxyribonucleic acid synthesis in porcine thyroid cells in primary culture
    • R. Kanri Y. Takiyama I. Makino Effects of bile acids on iodide uptake and deoxyribonucleic acid synthesis in porcine thyroid cells in primary culture Thyroid 6 1996 467 474
    • (1996) Thyroid , vol.6 , pp. 467-474
    • Kanri, R.1    Takiyama, Y.2    Makino, I.3
  • 196
    • 0029058516 scopus 로고
    • Distinct signalling mediates chloride secretion induced by tumor promoter bile salts and phorbol esters in human colonic cells
    • X.P. Huang M. Heyman S.K. Nath M. Castagna J.F. Desjeux Distinct signalling mediates chloride secretion induced by tumor promoter bile salts and phorbol esters in human colonic cells Int J Oncol 6 1995 1159 1163
    • (1995) Int J Oncol , vol.6 , pp. 1159-1163
    • Huang, X.P.1    Heyman, M.2    Nath, S.K.3    Castagna, M.4    Desjeux, J.F.5
  • 197
    • 24844453755 scopus 로고    scopus 로고
    • Chronic effect of bile acids on PGE1-induced cyclic AMP (cAMP) production in human fibro-blasts (abstr)
    • 1-induced cyclic AMP (cAMP) production in human fibro-blasts (abstr) Gastroenterology 112 1997 A1238
    • (1997) Gastroenterology , vol.112 , pp. A1238
    • Ceryak, S.1    Bouscarel, B.2    Fromm, H.3
  • 198
    • 0022531009 scopus 로고
    • Cytosolic bile acid binding protein in rat liver: radioimmunoassay, molecular forms, developmental characteristics and organ distribution
    • A. Stolz Y. Sugiyama J. Kuhlenkamp B. Osadchey T. Yamada W. Belknap W. Balistreri N. Kaplowitz Cytosolic bile acid binding protein in rat liver: radioimmunoassay, molecular forms, developmental characteristics and organ distribution Hepatology 6 1986 433 439
    • (1986) Hepatology , vol.6 , pp. 433-439
    • Stolz, A.1    Sugiyama, Y.2    Kuhlenkamp, J.3    Osadchey, B.4    Yamada, T.5    Belknap, W.6    Balistreri, W.7    Kaplowitz, N.8
  • 200
    • 0023150913 scopus 로고
    • Role of activation of protein kinase C in the stimulation of colonic epithelial proliferation and reactive oxygen formation by bile acids
    • P.A. Craven J. Pfanstiel F.R. Derubertis Role of activation of protein kinase C in the stimulation of colonic epithelial proliferation and reactive oxygen formation by bile acids J Clin Invest 79 1987 532 541
    • (1987) J Clin Invest , vol.79 , pp. 532-541
    • Craven, P.A.1    Pfanstiel, J.2    Derubertis, F.R.3
  • 201
    • 0023294884 scopus 로고
    • The regulation of protein kinase C by chenodeoxycholate, deoxycholate and several structurally related bile acids
    • C.J. Fitzer C.A. O'Brian J.G. Guillem I.B. Weinstein The regulation of protein kinase C by chenodeoxycholate, deoxycholate and several structurally related bile acids Carcinogenesis 8 1987 217 220
    • (1987) Carcinogenesis , vol.8 , pp. 217-220
    • Fitzer, C.J.1    O'Brian, C.A.2    Guillem, J.G.3    Weinstein, I.B.4
  • 202
    • 0026644807 scopus 로고
    • Bile acids, non-phorbol-ester-type tumor promoters, stimulate the phosphorylation of protein kinase C substrates in human platelets and colon cell line HT29
    • X.P. Huang X.T. Fan J.F. Desjeux M. Castagna Bile acids, non-phorbol-ester-type tumor promoters, stimulate the phosphorylation of protein kinase C substrates in human platelets and colon cell line HT29 Int J Cancer 52 1992 444 450
    • (1992) Int J Cancer , vol.52 , pp. 444-450
    • Huang, X.P.1    Fan, X.T.2    Desjeux, J.F.3    Castagna, M.4
  • 203
    • 0031459956 scopus 로고    scopus 로고
    • Activation of protein kinase C α and δ by bile acids: correlation with bile acid structure and diacylglycerol formation
    • Y.-P. Rao R.T. Stravitz Z.R. Vlahcevic E.C. Gurley J.J. Sando P.B. Hylemon Y.P. Rao Activation of protein kinase C α and δ by bile acids: correlation with bile acid structure and diacylglycerol formation J Lipid Res 38 1997 2446 2454
    • (1997) J Lipid Res , vol.38 , pp. 2446-2454
    • Rao, Y.-P.1    Stravitz, R.T.2    Vlahcevic, Z.R.3    Gurley, E.C.4    Sando, J.J.5    Hylemon, P.B.6    Rao, Y.P.7
  • 204
    • 0023770705 scopus 로고
    • The bile acid analog fusidic acid can replace phosphatidylserine in the activation of protein kinase C by 12-O-tetradecanoylphorbol-13-acetate in vitro
    • N.E. Ward C.A. O'Brian The bile acid analog fusidic acid can replace phosphatidylserine in the activation of protein kinase C by 12- O -tetradecanoylphorbol-13-acetate in vitro Carcinogenesis 9 1988 1451 1454
    • (1988) Carcinogenesis , vol.9 , pp. 1451-1454
    • Ward, N.E.1    O'Brian, C.A.2
  • 205
    • 0026545286 scopus 로고
    • Glucagon, vasopressin, and angiotensin II all elicit a rapid, transient increase in hepatocellular protein kinase C activity
    • E.Y. Tang M.D. Houslay Glucagon, vasopressin, and angiotensin II all elicit a rapid, transient increase in hepatocellular protein kinase C activity Biochem J 283 1992 341 346
    • (1992) Biochem J , vol.283 , pp. 341-346
    • Tang, E.Y.1    Houslay, M.D.2
  • 206
    • 85119799321 scopus 로고    scopus 로고
    • Regulation of PKC-α and PKC-β2 by phorbol ester and bile acids in cultured human fibroblasts (abstr)
    • S. Ceryak M. Le G.M. Toso H. Fromm B. Bouscarel Regulation of PKC-α and PKC-β2 by phorbol ester and bile acids in cultured human fibroblasts (abstr) Gastroenterology 114 1998 A1220
    • (1998) Gastroenterology , vol.114 , pp. A1220
    • Ceryak, S.1    Le, M.2    Toso, G.M.3    Fromm, H.4    Bouscarel, B.5
  • 207
    • 85119818961 scopus 로고    scopus 로고
    • Comparative expression and regulation of PKC-α and PKC-β2 by phorbol ester in hepatocytes isolated from bile duct ligated and sham-operated hamsters (abstr)
    • M. Le B. Bouscarel Comparative expression and regulation of PKC-α and PKC-β2 by phorbol ester in hepatocytes isolated from bile duct ligated and sham-operated hamsters (abstr) Gastroenterology 114 1998 A1284
    • (1998) Gastroenterology , vol.114 , pp. A1284
    • Le, M.1    Bouscarel, B.2
  • 208
    • 0028314237 scopus 로고
    • Partial purification of protein kinase C isoenzymes from rat liver
    • G.P. Perletti Partial purification of protein kinase C isoenzymes from rat liver J Biochem Biophys Methods 28 1994 195 204
    • (1994) J Biochem Biophys Methods , vol.28 , pp. 195-204
    • Perletti, G.P.1
  • 209
    • 2542508165 scopus 로고    scopus 로고
    • Five isoenzymes of protein kinase C are expressed in normal and STZ-diabetic rat hepatocytes: effect of phorbol 12-myristate 13- acetate
    • F. Croquet A. Brehier S. Gil J. Davy J. Feger Five isoenzymes of protein kinase C are expressed in normal and STZ-diabetic rat hepatocytes: effect of phorbol 12-myristate 13- acetate Bio-chim Biophys Acta 1315 1996 163 168
    • (1996) Bio-chim Biophys Acta , vol.1315 , pp. 163-168
    • Croquet, F.1    Brehier, A.2    Gil, S.3    Davy, J.4    Feger, J.5
  • 213
    • 0029028553 scopus 로고
    • Over-expression of protein kinase C delta is associated with a delay in preneoplastic lesion development in diethylnitrosamine-induced rat hepatocarcinogenesis
    • C.A. La Porta R. Comolli Over-expression of protein kinase C delta is associated with a delay in preneoplastic lesion development in diethylnitrosamine-induced rat hepatocarcinogenesis Carcinogenesis 16 1995 1233 1238
    • (1995) Carcinogenesis , vol.16 , pp. 1233-1238
    • La Porta, C.A.1    Comolli, R.2
  • 214
    • 0030906632 scopus 로고    scopus 로고
    • Bile salt-induced apoptosis of hepatocytes involves activation of protein kinase C
    • B.A. Jones Y.-P. Rao R.T. Stravitz G.J. Gores Y.P. Rao Bile salt-induced apoptosis of hepatocytes involves activation of protein kinase C Am J Physiol 272 1997 G1109 G1115
    • (1997) Am J Physiol , vol.272 , pp. G1109-G1115
    • Jones, B.A.1    Rao, Y.-P.2    Stravitz, R.T.3    Gores, G.J.4    Rao, Y.P.5
  • 215
    • 0029854499 scopus 로고    scopus 로고
    • Protein kinase C bound to the Golgi apparatus supports the formation of constitutive transport vesicles
    • P. Westermann M. Knoblich O. Maier C. Lindschau H. Haller Protein kinase C bound to the Golgi apparatus supports the formation of constitutive transport vesicles Biochem J 320 1996 651 658
    • (1996) Biochem J , vol.320 , pp. 651-658
    • Westermann, P.1    Knoblich, M.2    Maier, O.3    Lindschau, C.4    Haller, H.5
  • 216
    • 0030829597 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases mediate the stimulation of bile acid secretion by tauroursodeoxycholate in rat liver
    • F. Schliess A.K. Kurz S. vom Dahl D. Haussinger Mitogen-activated protein kinases mediate the stimulation of bile acid secretion by tauroursodeoxycholate in rat liver Gastroenterology 113 1997 1306 1314
    • (1997) Gastroenterology , vol.113 , pp. 1306-1314
    • Schliess, F.1    Kurz, A.K.2    vom Dahl, S.3    Haussinger, D.4
  • 217
    • 0030031467 scopus 로고    scopus 로고
    • Regulation of taurocholate excretion by a hyposmolarity-activated signal transduction pathway in rat liver
    • B. Noé F. Schliess M. Wettstein S. Heinrich D. Häussinger Regulation of taurocholate excretion by a hyposmolarity-activated signal transduction pathway in rat liver Gastroenterology 110 1996 858 865
    • (1996) Gastroenterology , vol.110 , pp. 858-865
    • Noé, B.1    Schliess, F.2    Wettstein, M.3    Heinrich, S.4    Häussinger, D.5


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