메뉴 건너뛰기




Volumn 16, Issue 2, 1996, Pages 201-210

Hepatocellular transport: Role of ATP-binding cassette proteins

Author keywords

adenosine nucleotides; bile secretion; multidrug resistance; organic anions

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE;

EID: 0029970141     PISSN: 02728087     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-1007232     Document Type: Review
Times cited : (24)

References (112)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins CF: ABC transporters: From microorganisms to man. Annu Rev Cell Biol 8:67-113, 1992.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0027132575 scopus 로고
    • ABC transporters: Bacterial exporters
    • Path MJ, Kolter R: ABC transporters: Bacterial exporters. Microbiol Rev 57:995-1017, 1993
    • (1993) Microbiol Rev , vol.57 , pp. 995-1017
    • Path, M.J.1    Kolter, R.2
  • 3
    • 0028906612 scopus 로고
    • The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity
    • Carson MR, Travis SM, Welsh MJ: The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity. J Biol Chem 270:1711-7, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 1711-1717
    • Carson, M.R.1    Travis, S.M.2    Welsh, M.J.3
  • 4
    • 0027519153 scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator Cl-channel by specific protein kinases and protein phosphatases
    • Berger HA, Travis SM, Welsh MJ: Regulation of the cystic fibrosis transmembrane conductance regulator Cl-channel by specific protein kinases and protein phosphatases. J Biol Chem 268:2037-47, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 2037-2047
    • Berger, H.A.1    Travis, S.M.2    Welsh, M.J.3
  • 5
    • 0027311276 scopus 로고
    • Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • Chang XB, Tabcharani JA, Hou YX, et al: Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. J Biol Chem 268:11304-11, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 11304-11311
    • Chang, X.B.1    Tabcharani, J.A.2    Hou, Y.X.3
  • 7
    • 0028245513 scopus 로고
    • Cloning of two novel ABC transporters mapping on human chromosome 9
    • Luciani MF, Denizot F, Savary S, et al: Cloning of two novel ABC transporters mapping on human chromosome 9. Genomics 21.150-9, 1994.
    • (1994) Genomics , vol.21 , pp. 150-159
    • Luciani, M.F.1    Denizot, F.2    Savary, S.3
  • 8
    • 0026749475 scopus 로고
    • DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing
    • Beck S, Kelly A, Radley E, et al: DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing. J Mol Biol 228:433-41, 1992.
    • (1992) J Mol Biol , vol.228 , pp. 433-441
    • Beck, S.1    Kelly, A.2    Radley, E.3
  • 9
    • 0026703416 scopus 로고
    • Location of MHC-encoded transporters in the endoplasmic reticulum and cis-Golgi
    • Kleijmeer MJ, Kelly A, Geuze HJ, et al: Location of MHC-encoded transporters in the endoplasmic reticulum and cis-Golgi. Nature 357:342-4, 1992.
    • (1992) Nature , vol.357 , pp. 342-344
    • Kleijmeer, M.J.1    Kelly, A.2    Geuze, H.J.3
  • 10
    • 0026593016 scopus 로고
    • Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex
    • Kelly A, Powis SH, Kerr LA, et al: Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex. Nature 355:641-4, 1992.
    • (1992) Nature , vol.355 , pp. 641-644
    • Kelly, A.1    Powis, S.H.2    Kerr, L.A.3
  • 11
    • 0025255475 scopus 로고
    • The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily
    • Kamijo K, Taketani S, Yokota S, et al: The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily. J Biol Chem 265:4534-40, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 4534-4540
    • Kamijo, K.1    Taketani, S.2    Yokota, S.3
  • 12
    • 0027391633 scopus 로고
    • Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody
    • Georges E, Tsuruo T, Ling V: Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody. J Biol Chem 268.1792-8, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 1792-1798
    • Georges, E.1    Tsuruo, T.2    Ling, V.3
  • 13
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • Skach WR, Calayag MC, Lingappa VR: Evidence for an alternate model of human P-glycoprotein structure and biogenesis. J Biol Chem 268 6903-8, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 6903-6908
    • Skach, W.R.1    Calayag, M.C.2    Lingappa, V.R.3
  • 14
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach WR, Lingappa VR: Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J Biol Chem 268:23552-61, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 23552-23561
    • Skach, W.R.1    Lingappa, V.R.2
  • 15
    • 0026536805 scopus 로고
    • Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein
    • Valverde MA, Diaz M, Sepulveda FV, et al: Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein. Nature 355:830-3, 1992.
    • (1992) Nature , vol.355 , pp. 830-833
    • Valverde, M.A.1    Diaz, M.2    Sepulveda, F.V.3
  • 16
    • 0027475309 scopus 로고
    • The multidrug resistance (mdr1) gene product functions as an ATP channel
    • Abraham EH, Prat AC, Gerweck L, et al: The multidrug resistance (mdr1) gene product functions as an ATP channel. Proc Natl Acad Sci USA 90.312-6, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 312-316
    • Abraham, E.H.1    Prat, A.C.2    Gerweck, L.3
  • 17
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman MM, Pastan I: Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu Rev Biochem 62:385-427, 1993.
    • (1993) Annu Rev Biochem , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 18
    • 0026640274 scopus 로고
    • Mdr2 encodes P-glycoprotein expressed in the bile canalicular membrane as determined by isoform-specific antibodies
    • Buschman E, Arceci RJ, Croop JM, et al: mdr2 encodes P-glycoprotein expressed in the bile canalicular membrane as determined by isoform-specific antibodies. J Biol Chem 267:18093-9, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 18093-18099
    • Buschman, E.1    Arceci, R.J.2    Croop, J.M.3
  • 19
    • 0028951101 scopus 로고
    • Analysis of a novel cDNA encoding a C219-reactive peptide isolated from methotrexate-selected multidrug-resistant human leukemic cells
    • Norris MD, Gilbert J, Madafiglio J, Haber M: Analysis of a novel cDNA encoding a C219-reactive peptide isolated from methotrexate-selected multidrug-resistant human leukemic cells. Gene 156:313-4, 1995.
    • (1995) Gene , vol.156 , pp. 313-314
    • Norris, M.D.1    Gilbert, J.2    Madafiglio, J.3    Haber, M.4
  • 20
    • 0028104421 scopus 로고
    • A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates
    • Ahmed M, Borsch CM, Taylor SS, et al: A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates. J Biol Chem 269:28506-13, 1994
    • (1994) J Biol Chem , vol.269 , pp. 28506-28513
    • Ahmed, M.1    Borsch, C.M.2    Taylor, S.S.3
  • 21
    • 0026755547 scopus 로고
    • Reduced mRNA levels for the multidrug-resistance genes in cAMP-dependent protein kinase mutant cell lines
    • Chin KV, Chauhan SS, Abraham I, et al: Reduced mRNA levels for the multidrug-resistance genes in cAMP-dependent protein kinase mutant cell lines. J Cell Physiol 152:87-94, 1992.
    • (1992) J Cell Physiol , vol.152 , pp. 87-94
    • Chin, K.V.1    Chauhan, S.S.2    Abraham, I.3
  • 22
    • 0023413829 scopus 로고
    • Cyclic AMP-depen-dent protein kinase regulates sensitivity of cells to multiple drugs
    • Abraham I, Hunter RJ, Sampson KE, et al: Cyclic AMP-depen-dent protein kinase regulates sensitivity of cells to multiple drugs. Mol Cell Biol 7:3098-106, 1987.
    • (1987) Mol Cell Biol , vol.7 , pp. 3098-3106
    • Abraham, I.1    Hunter, R.J.2    Sampson, K.E.3
  • 23
    • 0026598039 scopus 로고
    • Heat-shock responsive elements in the induction of the multidrug resistance gene (MDR1)
    • Kioka N, Yamano Y, Komano T, Ueda K: Heat-shock responsive elements in the induction of the multidrug resistance gene (MDR1) FEES Lett 301:37-40, 1992.
    • (1992) FEES Lett , vol.301 , pp. 37-40
    • Kioka, N.1    Yamano, Y.2    Komano, T.3    Ueda, K.4
  • 24
    • 0023179571 scopus 로고
    • Expression of the multidrug-resistam gene in hepatocarcinogenesis and regenerating rat liver
    • Thorgeirsson SS, Huber BE, Sorrell S, et al: Expression of the multidrug-resistam gene in hepatocarcinogenesis and regenerating rat liver. Science 236:1120-2, 1987.
    • (1987) Science , vol.236 , pp. 1120-1122
    • Thorgeirsson, S.S.1    Huber, B.E.2    Sorrell, S.3
  • 25
    • 0013659750 scopus 로고
    • Carcinogen-induced mdr overexpression is associated with xenobiotic resistance in rat preneoplastic liver nodules and hepatocellular carcinomas
    • Fairchild CR, Ivy SP, Rushmore T, et al: Carcinogen-induced mdr overexpression is associated with xenobiotic resistance in rat preneoplastic liver nodules and hepatocellular carcinomas. Proc Natl Acad Sci USA 84:7701-5, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7701-7705
    • Fairchild, C.R.1    Ivy, S.P.2    Rushmore, T.3
  • 26
    • 0025386379 scopus 로고
    • Regulation of the multidrug resistance gene in regenerating rat liver
    • Marino PA, Gottesman MM, Pastan I: Regulation of the multidrug resistance gene in regenerating rat liver. Cell Growth Differ 1:57-62, 1990.
    • (1990) Cell Growth Differ , vol.1 , pp. 57-62
    • Marino, P.A.1    Gottesman, M.M.2    Pastan, I.3
  • 27
    • 0027362087 scopus 로고
    • Identification of the major phosphorylation domain of murine mdr1b P-glycoprotein. Analysis of the protein kinase A and protein kinase C phosphorylation sites
    • Orr GA, Han EK, Browne PC, et al: Identification of the major phosphorylation domain of murine mdr1b P-glycoprotein. Analysis of the protein kinase A and protein kinase C phosphorylation sites. J Biol Chem 268:25054-62, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 25054-25062
    • Orr, G.A.1    Han, E.K.2    Browne, P.C.3
  • 28
    • 0026775053 scopus 로고
    • Separation of drug transport and chloride channel functions of the human multidrug resistance P-glycoprotein
    • Gill DR, Hyde SC, Higgins CF, et al: Separation of drug transport and chloride channel functions of the human multidrug resistance P-glycoprotein. Cell 71:23-32, 1992.
    • (1992) Cell , vol.71 , pp. 23-32
    • Gill, D.R.1    Hyde, S.C.2    Higgins, C.F.3
  • 29
    • 0019953668 scopus 로고
    • Regulation of bile salt transport in rat liver. Evidence that increased maximum bile salt secretory capacity is due to increased cholic acid receptors
    • Simon FR, Sutherland EM. Gonzalez M: Regulation of bile salt transport in rat liver. Evidence that increased maximum bile salt secretory capacity is due to increased cholic acid receptors. J Clin Invest 70:401-11, 1982.
    • (1982) J Clin Invest , vol.70 , pp. 401-411
    • Simon, F.R.1    Sutherland, E.M.2    Gonzalez, M.3
  • 30
    • 0023213727 scopus 로고
    • Regulation of transmembrane electrical potential gradient in rat hepatocytes in situ
    • Fitz JG, Scharschmidt BF: Regulation of transmembrane electrical potential gradient in rat hepatocytes in situ. Am J Physiol 252:G56-64, 1987.
    • (1987) Am J Physiol , vol.252
    • Fitz, J.G.1    Scharschmidt, B.F.2
  • 31
    • 0023920968 scopus 로고
    • Stimulation of taurocholate and glycocholate efflux from the rat hepatocyte by argmine vasopressin
    • Kuhn WF, Gewirtz DA: Stimulation of taurocholate and glycocholate efflux from the rat hepatocyte by argmine vasopressin. Am J Physiol 254:G732-40, 1988.
    • (1988) Am J Physiol , vol.254
    • Kuhn, W.F.1    Gewirtz, D.A.2
  • 32
    • 0026599145 scopus 로고
    • J774 macrophages secrete antibiotics via organic anion transporters
    • Cao CX, Silverstein SC, Neu HC, Steinberg TH: J774 macrophages secrete antibiotics via organic anion transporters. J Infect Dis 165:322-8, 1992.
    • (1992) J Infect Dis , vol.165 , pp. 322-328
    • Cao, C.X.1    Silverstein, S.C.2    Neu, H.C.3    Steinberg, T.H.4
  • 33
    • 0027474486 scopus 로고
    • Characterization of endogenous carner-mediated taurocholate efflux from Xenopus laevis oocytes
    • Shneider BL, Moyer MS: Characterization of endogenous carner-mediated taurocholate efflux from Xenopus laevis oocytes. J Biol Chem 268:6985-8, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 6985-6988
    • Shneider, B.L.1    Moyer, M.S.2
  • 34
    • 0027210070 scopus 로고
    • ATP-dependent glutathione S-conjugate export pump in the vacuolar membrane of plants
    • Martinoia E, Grill E, Tommasini R, et al: ATP-dependent glutathione S-conjugate export pump in the vacuolar membrane of plants. Nature 364:247-9, 1993.
    • (1993) Nature , vol.364 , pp. 247-249
    • Martinoia, E.1    Grill, E.2    Tommasini, R.3
  • 35
    • 0027225833 scopus 로고
    • Direct energization of bile acid transport into plant vacuoles
    • Hortensteiner S, Vogt E, Hagenbuch B, et al: Direct energization of bile acid transport into plant vacuoles. J Biol Chem 268:18446-9, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 18446-18449
    • Hortensteiner, S.1    Vogt, E.2    Hagenbuch, B.3
  • 36
    • 0028074888 scopus 로고
    • ATP-dependent transport of organic anions in secretory vesicles of Saccharomyces cerevisiae
    • St-Pierre MV, Ruetz S, Epstein LF, et al: ATP-dependent transport of organic anions in secretory vesicles of Saccharomyces cerevisiae Proc Natl Acad Sci USA 91:9476-9, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9476-9479
    • St-Pierre, M.V.1    Ruetz, S.2    Epstein, L.F.3
  • 37
    • 0025281139 scopus 로고
    • Carrier-mediated transport in the hepatic distribution and elimination of drugs, with special reference to the category of organic cations
    • Meijer DK, Mol WE, Muller M, Kurz G: Carrier-mediated transport in the hepatic distribution and elimination of drugs, with special reference to the category of organic cations. J Pharmacokinet Biopharm 18:35-70, 1990.
    • (1990) J Pharmacokinet Biopharm , vol.18 , pp. 35-70
    • Meijer, D.K.1    Mol, W.E.2    Muller, M.3    Kurz, G.4
  • 39
    • 0028342805 scopus 로고
    • Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: Evidence against direct drug extrusion from the plasma membrane
    • Altenberg GA, Vanoye CG, Horton JK, Reuss L: Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: Evidence against direct drug extrusion from the plasma membrane. Proc Natl Acad Sci USA 91:4654-7, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4654-4657
    • Altenberg, G.A.1    Vanoye, C.G.2    Horton, J.K.3    Reuss, L.4
  • 40
    • 0028229150 scopus 로고
    • Disruption of the mouse mdrla P-glycoprotem gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs
    • Schinkel AH, Smit JJ, van Tellingen O, et al: Disruption of the mouse mdrla P-glycoprotem gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs. Cell 77491-502, 1994.
    • (1994) Cell , vol.77 , pp. 491-502
    • Schinkel, A.H.1    Smit, J.J.2    Van Tellingen, O.3
  • 41
    • 0026442692 scopus 로고
    • Organic cation transport by rat liver plasma membrane vesicles: Studies with tetraethylammonium
    • Moseley RH, Jarose SM, Permoad P: Organic cation transport by rat liver plasma membrane vesicles: Studies with tetraethylammonium. Am J Physiol 263:G775-85, 1992.
    • (1992) Am J Physiol , vol.263
    • Moseley, R.H.1    Jarose, S.M.2    Permoad, P.3
  • 42
    • 8944249766 scopus 로고
    • A 1.8-3 kD mRNA encodes for a hepatic organic cation transport protein (Abstract)
    • Xie MH, Cochran M, Lidofsky SD, Scharschmidt BF: A 1.8-3 kD mRNA encodes for a hepatic organic cation transport protein (Abstract) Hepatology 16:147A, 1992.
    • (1992) Hepatology , vol.16
    • Xie, M.H.1    Cochran, M.2    Lidofsky, S.D.3    Scharschmidt, B.F.4
  • 43
    • 4243970805 scopus 로고
    • Mechanisms for the hepatic uptake and biliary excretion of cationic drugs
    • Moseley RH, Smit H, van Solkema BGH, et al: Mechanisms for the hepatic uptake and biliary excretion of cationic drugs (Abstract). Hepatology 20:261, 1994.
    • (1994) Hepatology , vol.20 , pp. 261
    • Moseley, R.H.1    Smit, H.2    Van Solkema, B.G.H.3
  • 44
    • 0024371025 scopus 로고
    • The function of Gp170, the multidrug resistance gene product, in rat liver canalicular membrane vesicles
    • Kamimoto Y, Gatmaitan Z, Hsu J, Arias IM: The function of Gp170, the multidrug resistance gene product, in rat liver canalicular membrane vesicles. J Biol Chem 264:11693-8, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 11693-11698
    • Kamimoto, Y.1    Gatmaitan, Z.2    Hsu, J.3    Arias, I.M.4
  • 45
    • 0027522810 scopus 로고
    • The biology of the bile canaliculus, 1993
    • Arias IM, Che M, Gatmaitan Z, et al: The biology of the bile canaliculus, 1993. Hepatology 17:318-29, 1993.
    • (1993) Hepatology , vol.17 , pp. 318-329
    • Arias, I.M.1    Che, M.2    Gatmaitan, Z.3
  • 46
    • 0028220381 scopus 로고
    • ATP-dependent transport of amphiphilic cations across the hepatocyte canalicular membrane mediated by mdr1 P-glycoprotein
    • Muller M, Mayer R, Hero U, Keppler D: ATP-dependent transport of amphiphilic cations across the hepatocyte canalicular membrane mediated by mdr1 P-glycoprotein. FEBS Lett 343:168-72, 1994.
    • (1994) FEBS Lett , vol.343 , pp. 168-172
    • Muller, M.1    Mayer, R.2    Hero, U.3    Keppler, D.4
  • 47
    • 0022970788 scopus 로고
    • Missing Cl conductance in cystic fibrosis
    • Quinton PM: Missing Cl conductance in cystic fibrosis. Am J Physiol 251:C649-52, 1986.
    • (1986) Am J Physiol , vol.251
    • Quinton, P.M.1
  • 48
    • 0025349031 scopus 로고
    • Cystic fibrosis: A disease in electrolyte transport
    • Quinton PM: Cystic fibrosis: A disease in electrolyte transport. FASEB J 4:2709-17, 1990.
    • (1990) FASEB J , vol.4 , pp. 2709-2717
    • Quinton, P.M.1
  • 49
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan JR, Rommens JM, Kerem B-S, et al: Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA. Science 245:1066-72, 1989.
    • (1989) Science , vol.245 , pp. 1066-1072
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.-S.3
  • 50
    • 0029127039 scopus 로고
    • Regulation of ion channels by ABC transporters that secrete ATP
    • Al-Awqati Q: Regulation of ion channels by ABC transporters that secrete ATP. Science 269:805-6, 1995.
    • (1995) Science , vol.269 , pp. 805-806
    • Al-Awqati, Q.1
  • 51
    • 0027191065 scopus 로고
    • CFTR and outward rectifying chloride channels are distinct proteins with a regulatory relationship
    • Gabriel SE, Clarke LL, Boucher RC, Stutts MJ: CFTR and outward rectifying chloride channels are distinct proteins with a regulatory relationship. Nature 363:263-8, 1993.
    • (1993) Nature , vol.363 , pp. 263-268
    • Gabriel, S.E.1    Clarke, L.L.2    Boucher, R.C.3    Stutts, M.J.4
  • 52
    • 0027937589 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator is a dual ATP and chloride channel
    • Reisin IL, Prat AG, Abraham EH, et al: The cystic fibrosis transmembrane conductance regulator is a dual ATP and chloride channel. J Biol Chem 269:20584-91, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 20584-20591
    • Reisin, I.L.1    Prat, A.G.2    Abraham, E.H.3
  • 53
    • 0025868103 scopus 로고
    • Demonstration that CFTR is a chloride channel by alteration of its anion selectivity
    • Anderson MP, Gregory RJ, Thompson S, et al: Demonstration that CFTR is a chloride channel by alteration of its anion selectivity. Science 253:202-5, 1991.
    • (1991) Science , vol.253 , pp. 202-205
    • Anderson, M.P.1    Gregory, R.J.2    Thompson, S.3
  • 54
    • 0027134853 scopus 로고
    • Localization of the cystic fibrosis transmembrane conductance regulator in human bile duct epithelial cells
    • Cohn JA, Strong TV, Picciotto MR, et al: Localization of the cystic fibrosis transmembrane conductance regulator in human bile duct epithelial cells. Gastroenterology 105:1857-64, 1993.
    • (1993) Gastroenterology , vol.105 , pp. 1857-1864
    • Cohn, J.A.1    Strong, T.V.2    Picciotto, M.R.3
  • 55
    • 0027523995 scopus 로고
    • Regulation of membrane chloride currents in rat bile duct epithelial cells
    • Fitz JG, Basavappa S, McGill J, et al: Regulation of membrane chloride currents in rat bile duct epithelial cells. J Clin Invest 91:319-28, 1993.
    • (1993) J Clin Invest , vol.91 , pp. 319-328
    • Fitz, J.G.1    Basavappa, S.2    McGill, J.3
  • 57
    • 0027526366 scopus 로고
    • CAMP-regulated whole cell chloride currents in pancreatic duct cells
    • Gray MA, Plant S, Argent BE: cAMP-regulated whole cell chloride currents in pancreatic duct cells. Am J Physiol 264:C591-602, 1993.
    • (1993) Am J Physiol , vol.264
    • Gray, M.A.1    Plant, S.2    Argent, B.E.3
  • 58
    • 0025834174 scopus 로고
    • Localization of the cystic fibrosis transmembrane conductance regulator in pancreas
    • Marino CR, Matovcik LM, Gorelick FS, Cohn JA: Localization of the cystic fibrosis transmembrane conductance regulator in pancreas. J Clin Invest 88:712-6, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 712-716
    • Marino, C.R.1    Matovcik, L.M.2    Gorelick, F.S.3    Cohn, J.A.4
  • 59
    • 0028157831 scopus 로고
    • Localization of cystic fibrosis transmembrane conductance regulator mRNA in the human gastrointestinal tract by in situ hybridization
    • Strong TV, Boehm K, Collins FS: Localization of cystic fibrosis transmembrane conductance regulator mRNA in the human gastrointestinal tract by in situ hybridization. J Clin Invest 93:347-54, 1994.
    • (1994) J Clin Invest , vol.93 , pp. 347-354
    • Strong, T.V.1    Boehm, K.2    Collins, F.S.3
  • 60
    • 8944222107 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator gene is expressed in human gallbladder epithelial cells
    • Dray-Charier N, Paul A, Veissiere D, et al: The cystic fibrosis transmembrane conductance regulator gene is expressed in human gallbladder epithelial cells (Abstract). Hepatology 20:259A, 1994.
    • (1994) Hepatology , vol.20
    • Dray-Charier, N.1    Paul, A.2    Veissiere, D.3
  • 61
    • 0027223866 scopus 로고
    • cAMP-activated apical membrane chloride channels in Necturus gallbladder epithelium. Conductance, selectivity, and block
    • Copello J, Heming TA, Segal Y, Reuss L. cAMP-activated apical membrane chloride channels in Necturus gallbladder epithelium. Conductance, selectivity, and block. J Gen Physiol 102:177-99, 1993.
    • (1993) J Gen Physiol , vol.102 , pp. 177-199
    • Copello, J.1    Heming, T.A.2    Segal, Y.3    Reuss, L.4
  • 62
    • 0028057167 scopus 로고
    • Muscarinic stimulation of gallbladder epithelium. III. Antagonism of cAMP-mediated effects
    • Altenberg GA, Subramanyam M, Reuss L: Muscarinic stimulation of gallbladder epithelium. III. Antagonism of cAMP-mediated effects. Am J Physiol 267:C1196-1202, 1994.
    • (1994) Am J Physiol , vol.267
    • Altenberg, G.A.1    Subramanyam, M.2    Reuss, L.3
  • 63
    • 0028982894 scopus 로고
    • CFTR as a cAMP-dependent regulator of sodium channels
    • Stutts MJ, Canessa CM, Olsen JC, et al: CFTR as a cAMP-dependent regulator of sodium channels. Science 269 847-50, 1995.
    • (1995) Science , vol.269 , pp. 847-850
    • Stutts, M.J.1    Canessa, C.M.2    Olsen, J.C.3
  • 64
    • 0025874599 scopus 로고
    • Activation by extracellular nucleotides of chloride secretion in the airway epithelia of patients with cystic fibrosis
    • Knowles MR, Clarke LL, Boucher RC: Activation by extracellular nucleotides of chloride secretion in the airway epithelia of patients with cystic fibrosis. N Engl J Med 325:533-8, 1991.
    • (1991) N Engl J Med , vol.325 , pp. 533-538
    • Knowles, M.R.1    Clarke, L.L.2    Boucher, R.C.3
  • 65
    • 0027457145 scopus 로고
    • ATP-dependent transport systems for organic anions
    • Zimniak P, Awasthi YC: ATP-dependent transport systems for organic anions. Hepatology 17:330-9, 1993.
    • (1993) Hepatology , vol.17 , pp. 330-339
    • Zimniak, P.1    Awasthi, Y.C.2
  • 66
    • 0027361042 scopus 로고
    • Dubin-Johnson and Rotor syndromes: Molecular basis and pathogenesis
    • Zimniak P: Dubin-Johnson and Rotor syndromes: Molecular basis and pathogenesis. Semin Liver Dis 13:248-60, 1993.
    • (1993) Semin Liver Dis , vol.13 , pp. 248-260
    • Zimniak, P.1
  • 67
    • 0027095653 scopus 로고
    • Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line
    • Cole SP, Bhardwaj G, Gerlach JH, et al: Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line. Science 258:1650-4, 1992.
    • (1992) Science , vol.258 , pp. 1650-1654
    • Cole, S.P.1    Bhardwaj, G.2    Gerlach, J.H.3
  • 68
    • 0028578004 scopus 로고
    • Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport
    • Muller M, Meijer C, Zaman GJ, et al: Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport. Proc Natl Acad Sci USA 91:13033-7, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 13033-13037
    • Muller, M.1    Meijer, C.2    Zaman, G.J.3
  • 69
    • 8944227971 scopus 로고
    • Expression and localization of the MRP-encoded conjugate export pump in human and rat liver
    • in press
    • Mayer R, Kartenbeck J, Buchler M, et al: Expression and localization of the MRP-encoded conjugate export pump in human and rat liver (Abstract). Hepatology 1995 (in press).
    • (1995) Hepatology
    • Mayer, R.1    Kartenbeck, J.2    Buchler, M.3
  • 70
    • 0029981430 scopus 로고    scopus 로고
    • Congenital jaundice in rats with a raultidrug resistance-associated protein gene
    • Paulusma CC, Bosma PJ, Zaman GJR, et al: Congenital jaundice in rats with a raultidrug resistance-associated protein gene. Science 271:1126-8, 1996.
    • (1996) Science , vol.271 , pp. 1126-1128
    • Paulusma, C.C.1    Bosma, P.J.2    Zaman, G.J.R.3
  • 71
    • 8944256857 scopus 로고
    • Physiological utility of biliary secretion and excretion
    • Keppler D, Jungermann K (eds): Dordrecht, Kluwer Academic Publishers
    • Hofmann AF: Physiological utility of biliary secretion and excretion. In: Keppler D, Jungermann K (eds): Transport in the liver. Dordrecht, Kluwer Academic Publishers, 1994, pp 17-31.
    • (1994) Transport in the Liver , pp. 17-31
    • Hofmann, A.F.1
  • 72
    • 8944234842 scopus 로고
    • Intracellular vesicles and the transport of organic anions
    • Keppler D, Jungermann K (eds): Dordrecht, Kluwer Academic Publishers
    • Oude-Elferink RP, Roelofsen H, Bakker C, et al: Intracellular vesicles and the transport of organic anions. In: Keppler D, Jungermann K (eds): Transport in the liver. Dordrecht, Kluwer Academic Publishers, 1994, pp 117-26.
    • (1994) Transport in the Liver , pp. 117-126
    • Oude-Elferink, R.P.1    Roelofsen, H.2    Bakker, C.3
  • 74
    • 0027363563 scopus 로고
    • Homozygous disruption of the munne mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease
    • Smit JJ, Schinkel AH, Oude Elferink RP, et al: Homozygous disruption of the munne mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease. Cell 75:451-62, 1993.
    • (1993) Cell , vol.75 , pp. 451-462
    • Smit, J.J.1    Schinkel, A.H.2    Oude Elferink, R.P.3
  • 75
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • Ruetz S, Gros P: Phosphatidylcholine translocase: A physiological role for the mdr2 gene. Cell 77:1071-81, 1994.
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 76
    • 0027466820 scopus 로고
    • Evidence for the presence of a phosphatidylcholine translocator in isolated rat liver canalicular plasma membrane vesicles
    • Berr F, Meier PJ, Stieger B: Evidence for the presence of a phosphatidylcholine translocator in isolated rat liver canalicular plasma membrane vesicles. J Biol Chem 268:3976-9, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 3976-3979
    • Berr, F.1    Meier, P.J.2    Stieger, B.3
  • 77
    • 1842271229 scopus 로고
    • Hepatocytes express an array of novel ATP binding cassette (ABC) proteins with apparently diverse functions
    • Lomri N, Cavalieri RR, Rahmaoui C, Scharschmidt BF: Hepatocytes express an array of novel ATP binding cassette (ABC) proteins with apparently diverse functions (Abstract). Hepatology 22:312, 1995.
    • (1995) Hepatology , vol.22 , pp. 312
    • Lomri, N.1    Cavalieri, R.R.2    Rahmaoui, C.3    Scharschmidt, B.F.4
  • 78
    • 0026072857 scopus 로고
    • Mechanisms and regulation of bile secretion
    • Nathanson MH, Boyer JL: Mechanisms and regulation of bile secretion. Hepatology 14:551-66, 1991.
    • (1991) Hepatology , vol.14 , pp. 551-566
    • Nathanson, M.H.1    Boyer, J.L.2
  • 79
    • 0028303784 scopus 로고
    • Evidence for defective primary bile acid secretion in children with progressive familial intrahepatic cholestasis (Byler disease)
    • Jacquemin E, Dumont M, Bernard O, et al: Evidence for defective primary bile acid secretion in children with progressive familial intrahepatic cholestasis (Byler disease). Eur J Pediatr 153:424-8, 1994.
    • (1994) Eur J Pediatr , vol.153 , pp. 424-428
    • Jacquemin, E.1    Dumont, M.2    Bernard, O.3
  • 80
    • 0027225501 scopus 로고
    • Ethinylestradiol treatment induces multiple canalicular membrane transport alterations in rat liver
    • Bossard R, Stieger B, O'Neill B, et al: Ethinylestradiol treatment induces multiple canalicular membrane transport alterations in rat liver. J Clin Invest 91:2714-20, 1993.
    • (1993) J Clin Invest , vol.91 , pp. 2714-2720
    • Bossard, R.1    Stieger, B.2    O'Neill, B.3
  • 81
    • 0027254929 scopus 로고
    • Cyclosporin, the biology of the bile canaliculus, and cholestasis
    • Arias IM: Cyclosporin, the biology of the bile canaliculus, and cholestasis. Gastroenterology 104:1558-60, 1993.
    • (1993) Gastroenterology , vol.104 , pp. 1558-1560
    • Arias, I.M.1
  • 82
    • 0024387006 scopus 로고
    • Localization of the ecto-ATPase (ecto-nucleotidase) in the rat hepatocyte plasma membrane. Implications for the functions of the ecto-ATPase
    • Lin SH: Localization of the ecto-ATPase (ecto-nucleotidase) in the rat hepatocyte plasma membrane. Implications for the functions of the ecto-ATPase. J Biol Chem 264:14403-7, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 14403-14407
    • Lin, S.H.1
  • 83
    • 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
    • Lin SH, Guidotti G: 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 264:14408-14, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 14408-14414
    • Lin, S.H.1    Guidotti, G.2
  • 84
    • 0027390262 scopus 로고
    • The rat liver ecto-ATPase is also a canalicular bile acid transport protein
    • Sippel CJ, Suchy FJ, Ananthanarayanan M, Perlmutter DH: The rat liver ecto-ATPase is also a canalicular bile acid transport protein. J Biol Chem 268:2083-91, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 2083-2091
    • Sippel, C.J.1    Suchy, F.J.2    Ananthanarayanan, M.3    Perlmutter, D.H.4
  • 85
    • 0011279784 scopus 로고
    • Canalicular ectoATPase and ATP-dependent transport
    • Keppler D, Jungermann K (eds): Dordrecht, Kluwer Academic Publishers
    • Arias IM, Ortiz D, Leveille-Webster C, et al: Canalicular ectoATPase and ATP-dependent transport. In: Keppler D, Jungermann K (eds): Transport in the liver. Dordrecht, Kluwer Academic Publishers, 1994, pp 149-55.
    • (1994) Transport in the Liver , pp. 149-155
    • Arias, I.M.1    Ortiz, D.2    Leveille-Webster, C.3
  • 86
    • 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 tyrosme 488 phosphorylation
    • Sippel CJ, Fallon RJ, Perlmutter DH: Bile acid efflux mediated by the rat liver canalicular bile acid transport/ecto-ATPase protein requires serine 503 phosphorylation and is regulated by tyrosme 488 phosphorylation J Biol Chem 269:19539-45, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 19539-19545
    • Sippel, C.J.1    Fallon, R.J.2    Perlmutter, D.H.3
  • 87
    • 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
    • Sippel CJ, McCollum MJ, Perlmutter DH: 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 269:2820-6, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 2820-2826
    • Sippel, C.J.1    McCollum, M.J.2    Perlmutter, D.H.3
  • 88
    • 0027984777 scopus 로고
    • Hepatocellular transport of bile acids. Evidence for distinct subcellular localizations of electrogenic and ATP-dependent taurocholate transport in rat hepatocytes
    • Kast C, Stieger B, Winterhalter KH, Meier PJ: Hepatocellular transport of bile acids. Evidence for distinct subcellular localizations of electrogenic and ATP-dependent taurocholate transport in rat hepatocytes. J Biol Chem 269:5179-86, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 5179-5186
    • Kast, C.1    Stieger, B.2    Winterhalter, K.H.3    Meier, P.J.4
  • 89
    • 0029064477 scopus 로고
    • Enhanced secretion of glycocholic acid in a specially adapted cell line is associated with over-expression of apparently novel ATP-binding cassette proteins
    • Brown RS, Lomri N, De Voss J, et al: Enhanced secretion of glycocholic acid in a specially adapted cell line is associated with over-expression of apparently novel ATP-binding cassette proteins. Proc Natl Acad Sci USA 92:5421-5, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5421-5425
    • Brown, R.S.1    Lomri, N.2    De Voss, J.3
  • 90
    • 0025141784 scopus 로고
    • Detection of P-glycoprotein isoforms by gene-specific monoclonal antibodies
    • Georges E, Bradley G, Gariepy J, Ling V: Detection of P-glycoprotein isoforms by gene-specific monoclonal antibodies. Proc Natl Acad Sci USA 87:152-6, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 152-156
    • Georges, E.1    Bradley, G.2    Gariepy, J.3    Ling, V.4
  • 91
    • 0026487058 scopus 로고
    • Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone
    • Ueda K, Okamura N, Hirai M, et al: Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone. J Biol Chem 267:24248-52, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24248-24252
    • Ueda, K.1    Okamura, N.2    Hirai, M.3
  • 92
    • 0025131387 scopus 로고
    • Progesterone photoaffinity labels P-glycoprotein in multidrug-resistant human leukemic lymphoblasts
    • Qian XD, Beck WT: Progesterone photoaffinity labels P-glycoprotein in multidrug-resistant human leukemic lymphoblasts. J Biol Chem 265:18753-6, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 18753-18756
    • Qian, X.D.1    Beck, W.T.2
  • 93
    • 0026772932 scopus 로고
    • Characterization of multidrug-resistant pituitary tumor cells
    • Nelson EJ, Hinkle PM: Characterization of multidrug-resistant pituitary tumor cells. Endocrinology 130:3246-56, 1992.
    • (1992) Endocrinology , vol.130 , pp. 3246-3256
    • Nelson, E.J.1    Hinkle, P.M.2
  • 94
    • 0029013333 scopus 로고
    • LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones
    • Kralli A, Bohen SP, Yamamoto KR: LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones. Proc Natl Acad Sci USA 92:4701-5, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4701-4705
    • Kralli, A.1    Bohen, S.P.2    Yamamoto, K.R.3
  • 95
    • 85035165692 scopus 로고
    • Hepatocellular thyroid hormone efflux is a novel mechanism for regulation of thyroid hormone action
    • Ribeiro RCJ, Cavalieri RR, Lomri N, et al: Hepatocellular thyroid hormone efflux is a novel mechanism for regulation of thyroid hormone action (Abstract). Hepatology 22.288A, 1995.
    • (1995) Hepatology , vol.22
    • Ribeiro, R.C.J.1    Cavalieri, R.R.2    Lomri, N.3
  • 96
    • 0022393946 scopus 로고
    • Characterization of responses of isolated rat hepatocytes to ATP and ADP
    • Charest R, Blackmore PF, Exton JH. Characterization of responses of isolated rat hepatocytes to ATP and ADP. J Biol Chem 260:15789-94, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 15789-15794
    • Charest, R.1    Blackmore, P.F.2    Exton, J.H.3
  • 97
    • 0023654280 scopus 로고
    • Phosphatidylcholine breakdown in rat liver plasma membranes. Roles of guanine nucleotides and P2-punnergic agonists
    • Irving HR, Exton JH: Phosphatidylcholine breakdown in rat liver plasma membranes. Roles of guanine nucleotides and P2-punnergic agonists. J Biol Chem 262:3440-3, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 3440-3443
    • Irving, H.R.1    Exton, J.H.2
  • 98
    • 0028361686 scopus 로고
    • Adenosine triphosphate activates ion permeabilities in biliary epithelial cells
    • McGill JM, Basavappa S, Mangel AW, et al: Adenosine triphosphate activates ion permeabilities in biliary epithelial cells. Gastroenterology 107:236-3, 1994.
    • (1994) Gastroenterology , vol.107 , pp. 236-243
    • McGill, J.M.1    Basavappa, S.2    Mangel, A.W.3
  • 99
    • 0028988870 scopus 로고
    • 2u identification and function in human intrahepatic biliary epithelial cell lines
    • 2u identification and function in human intrahepatic biliary epithelial cell lines. Call Cal 17:375-83, 1995.
    • (1995) Call Cal , vol.17 , pp. 375-383
    • Wolkiff, L.E.1    Perron, R.D.2    Grubman, S.A.3
  • 100
    • 0024248216 scopus 로고
    • Stimulation of throm-boxane release by extracellular UTP and ATP from perfused liver
    • Haussinger D, Busshardt E, Stehle T, et al: Stimulation of throm-boxane release by extracellular UTP and ATP from perfused liver. Eur J Biochem 178:249-56, 1988.
    • (1988) Eur J Biochem , vol.178 , pp. 249-256
    • Haussinger, D.1    Busshardt, E.2    Stehle, T.3
  • 101
    • 0028279340 scopus 로고
    • Nucleotide receptors activate cation, potassium, and chloride currents in a liver cell line
    • Fitz JG, Sostman AH: Nucleotide receptors activate cation, potassium, and chloride currents in a liver cell line. Am J Physiol 266:G544-53, 1994.
    • (1994) Am J Physiol , vol.266
    • Fitz, J.G.1    Sostman, A.H.2
  • 102
    • 0027975497 scopus 로고
    • Regulation of cation channels in liver cells by intracellular calcium and protein kinase C
    • Fitz JG, Sostman AH, Middleton JP: Regulation of cation channels in liver cells by intracellular calcium and protein kinase C Am J Physiol 266:G677-84, 1994.
    • (1994) Am J Physiol , vol.266
    • Fitz, J.G.1    Sostman, A.H.2    Middleton, J.P.3
  • 103
  • 104
    • 0028980536 scopus 로고
    • CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP
    • Schweibert EM, Egan ME, Hwang T-H, et al: CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP. Cell 81:1063-73, 1995.
    • (1995) Cell , vol.81 , pp. 1063-1073
    • Schweibert, E.M.1    Egan, M.E.2    Hwang, T.-H.3
  • 105
    • 0028029015 scopus 로고
    • Multiple modes of regulation of airway epithelial chloride secretion by extracellular ATP
    • Stutts MJ, Fitz JG, Paradiso AM, Boucher RC: Multiple modes of regulation of airway epithelial chloride secretion by extracellular ATP. Am J Physiol 267:C1442-51, 1994.
    • (1994) Am J Physiol , vol.267
    • Stutts, M.J.1    Fitz, J.G.2    Paradiso, A.M.3    Boucher, R.C.4
  • 106
    • 0025906695 scopus 로고
    • Variable deletion of exon 9 coding sequences in cystic fibrosis transmembrane conductance regulator gene mRNA transcripts in normal bronchial epithelium
    • Chu CS, Trapnell BC, Murtagh JJ Jr, et al: Variable deletion of exon 9 coding sequences in cystic fibrosis transmembrane conductance regulator gene mRNA transcripts in normal bronchial epithelium. EMBO J 10:1355-63, 1991.
    • (1991) EMBO J , vol.10 , pp. 1355-1363
    • Chu, C.S.1    Trapnell, B.C.2    Murtagh Jr., J.J.3
  • 108
    • 0025815742 scopus 로고
    • Electrophysiological effects of extracellular ATP on Necturus gallbladder epithelium
    • Cotton CU, Reuss L: Electrophysiological effects of extracellular ATP on Necturus gallbladder epithelium. J Gen Physiol 97:949-71, 1991.
    • (1991) J Gen Physiol , vol.97 , pp. 949-971
    • Cotton, C.U.1    Reuss, L.2
  • 110
    • 0027287975 scopus 로고
    • GTP-binding proteins regulate high conductance anion channels in rat bile duct epithelial cells
    • McGill JM, Gettys TW, Basavappa S, Fitz JG: GTP-binding proteins regulate high conductance anion channels in rat bile duct epithelial cells. J Membr Biol 133:253-61, 1993.
    • (1993) J Membr Biol , vol.133 , pp. 253-261
    • McGill, J.M.1    Gettys, T.W.2    Basavappa, S.3    Fitz, J.G.4
  • 111
    • 8944249765 scopus 로고
    • Calcium-activated chloride channels in a human biliary cell line: A potential site for regulation of ductular secretion
    • Schlanker T, Roman RM, Fitz JG: Calcium-activated chloride channels in a human biliary cell line: A potential site for regulation of ductular secretion (Abstract). Gastroenterology 108:A1165, 1995.
    • (1995) Gastroenterology , vol.108
    • Schlanker, T.1    Roman, R.M.2    Fitz, J.G.3
  • 112
    • 0029025787 scopus 로고
    • Primary structure and functional expression of a cDNA encoding the bile canalicular, purine-specific Na(+)-nucleoside cotransporter
    • Che M, Ortiz DF, Arias IM: Primary structure and functional expression of a cDNA encoding the bile canalicular, purine-specific Na(+)-nucleoside cotransporter. J Biol Chem 270:13596-9, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 13596-13599
    • Che, M.1    Ortiz, D.F.2    Arias, I.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.