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Volumn 2, Issue , 2012, Pages 1485-1506

Mechanisms of Hepatocyte Organic Anion Transport

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EID: 84882501423     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382026-6.00054-3     Document Type: Chapter
Times cited : (4)

References (313)
  • 1
    • 0020375501 scopus 로고
    • Effect of nafenopin on the uptake of bilirubin and sulfobromophthalein by isolated perfused rat liver
    • Gartner U, Stockert RJ, Levine WG, Wolkoff AW Effect of nafenopin on the uptake of bilirubin and sulfobromophthalein by isolated perfused rat liver. Gastroenterology 1982, 83:1163-1169.
    • (1982) Gastroenterology , vol.83 , pp. 1163-1169
    • Gartner, U.1    Stockert, R.J.2    Levine, W.G.3    Wolkoff, A.W.4
  • 2
    • 0020610272 scopus 로고
    • Hepatic bilirubin uptake in the isolated perfused rat liver is not facilitated by albumin binding
    • Stollman YR, Gartner U, Theilmann L, Ohmi N, Wolkoff AW Hepatic bilirubin uptake in the isolated perfused rat liver is not facilitated by albumin binding. J Clin Invest 1983, 72:718-723.
    • (1983) J Clin Invest , vol.72 , pp. 718-723
    • Stollman, Y.R.1    Gartner, U.2    Theilmann, L.3    Ohmi, N.4    Wolkoff, A.W.5
  • 3
    • 0030842164 scopus 로고    scopus 로고
    • Effect of fasting on the uptake of bilirubin and sulfobromophthalein by the isolated perfused rat liver
    • Gartner U, Goeser T, Wolkoff AW Effect of fasting on the uptake of bilirubin and sulfobromophthalein by the isolated perfused rat liver. Gastroenterology 1997, 113:1707-1713.
    • (1997) Gastroenterology , vol.113 , pp. 1707-1713
    • Gartner, U.1    Goeser, T.2    Wolkoff, A.W.3
  • 4
    • 0023222122 scopus 로고
    • The role of an albumin receptor in hepatic organic anion uptake: the controversy continues
    • Wolkoff AW The role of an albumin receptor in hepatic organic anion uptake: the controversy continues. Hepatology 1987, 7:777-779.
    • (1987) Hepatology , vol.7 , pp. 777-779
    • Wolkoff, A.W.1
  • 6
    • 0025780035 scopus 로고
    • Role of chloride and intracellular pH on the activity of the rat hepatocyte organic anion transporter
    • Min AD, Johansen KJ, Campbell CG, Wolkoff AW Role of chloride and intracellular pH on the activity of the rat hepatocyte organic anion transporter. J Clin Invest 1991, 87:1496-1502.
    • (1991) J Clin Invest , vol.87 , pp. 1496-1502
    • Min, A.D.1    Johansen, K.J.2    Campbell, C.G.3    Wolkoff, A.W.4
  • 7
    • 0021905486 scopus 로고
    • The role of albumin in the hepatic transport of bilirubin: studies in mutant analbuminemic rats
    • Inoue M, Hirata E, Morino Y, Nagase S, Chowdhury JR, Chowdhury NR, et al. The role of albumin in the hepatic transport of bilirubin: studies in mutant analbuminemic rats. J Biochem 1985, 97:737-743.
    • (1985) J Biochem , vol.97 , pp. 737-743
    • Inoue, M.1    Hirata, E.2    Morino, Y.3    Nagase, S.4    Chowdhury, J.R.5    Chowdhury, N.R.6
  • 8
    • 0017228269 scopus 로고
    • Uptake of bromosulfophthalein by isolated liver cells
    • Schwenk M, Burr R, Schwarz L, Pfaff E Uptake of bromosulfophthalein by isolated liver cells. Eur J Biochem 1976, 64:189-197.
    • (1976) Eur J Biochem , vol.64 , pp. 189-197
    • Schwenk, M.1    Burr, R.2    Schwarz, L.3    Pfaff, E.4
  • 10
    • 0018939043 scopus 로고
    • Uptake of sulfobromophthalein-glutathione conjugate by isolated hepatocytes
    • Schwarz LR, Gotz R, Klaassen CD Uptake of sulfobromophthalein-glutathione conjugate by isolated hepatocytes. Am J Physiol 1980, 239:C118-C123.
    • (1980) Am J Physiol , vol.239
    • Schwarz, L.R.1    Gotz, R.2    Klaassen, C.D.3
  • 11
    • 0038081033 scopus 로고    scopus 로고
    • The human organic anion transport protein SLC21A6 is not sufficient for bilirubin transport
    • Wang P, Kim RB, Chowdhury JR, Wolkoff AW The human organic anion transport protein SLC21A6 is not sufficient for bilirubin transport. J Biol Chem 2003, 278:20695-20699.
    • (2003) J Biol Chem , vol.278 , pp. 20695-20699
    • Wang, P.1    Kim, R.B.2    Chowdhury, J.R.3    Wolkoff, A.W.4
  • 12
    • 0026331012 scopus 로고
    • Organic anion transport in HepG2 cells: absence of the high-affinity, chloride-dependent transporter
    • Min AD, Goeser T, Liu R, Campbell CG, Novikoff PM, Wolkoff AW Organic anion transport in HepG2 cells: absence of the high-affinity, chloride-dependent transporter. Hepatology 1991, 14:1217-1223.
    • (1991) Hepatology , vol.14 , pp. 1217-1223
    • Min, A.D.1    Goeser, T.2    Liu, R.3    Campbell, C.G.4    Novikoff, P.M.5    Wolkoff, A.W.6
  • 13
    • 0029889501 scopus 로고    scopus 로고
    • Hepatocellular sinusoidal membrane organic anion transport and transporters
    • Wolkoff AW Hepatocellular sinusoidal membrane organic anion transport and transporters. Semin Liver Dis 1996, 16:121-127.
    • (1996) Semin Liver Dis , vol.16 , pp. 121-127
    • Wolkoff, A.W.1
  • 14
    • 0026331027 scopus 로고
    • Expression of the hepatocellular chloride-dependent sulfobromophthalein uptake system in Xenopus laevis oocytes
    • Jacquemin E, Hagenbuch B, Stieger B, Wolkoff AW, Meier PJ Expression of the hepatocellular chloride-dependent sulfobromophthalein uptake system in Xenopus laevis oocytes. J Clin Invest 1991, 88:2146-2149.
    • (1991) J Clin Invest , vol.88 , pp. 2146-2149
    • Jacquemin, E.1    Hagenbuch, B.2    Stieger, B.3    Wolkoff, A.W.4    Meier, P.J.5
  • 15
    • 0019793645 scopus 로고
    • Modulation of the transport of bilirubin and asialoorosomucoid during liver regeneration
    • Gartner U, Stockert RJ, Morell AG, Wolkoff AW Modulation of the transport of bilirubin and asialoorosomucoid during liver regeneration. Hepatology 1981, 1:99-106.
    • (1981) Hepatology , vol.1 , pp. 99-106
    • Gartner, U.1    Stockert, R.J.2    Morell, A.G.3    Wolkoff, A.W.4
  • 17
    • 0033968255 scopus 로고    scopus 로고
    • Down-regulation by extracellular ATP of rat hepatocyte organic anion transport is mediated by serine phosphorylation of oatp1
    • Glavy JS, Wu SM, Wang PJ, Orr GA, Wolkoff AW Down-regulation by extracellular ATP of rat hepatocyte organic anion transport is mediated by serine phosphorylation of oatp1. J Biol Chem 2000, 275:1479-1484.
    • (2000) J Biol Chem , vol.275 , pp. 1479-1484
    • Glavy, J.S.1    Wu, S.M.2    Wang, P.J.3    Orr, G.A.4    Wolkoff, A.W.5
  • 18
    • 0018566691 scopus 로고
    • Isolation of an organic anion binding protein from rat liver plasma membrane fractions by affinity chromatography
    • Reichen J, Berk PD Isolation of an organic anion binding protein from rat liver plasma membrane fractions by affinity chromatography. Biochem Biophys Res Commun 1979, 91:484-489.
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 484-489
    • Reichen, J.1    Berk, P.D.2
  • 19
    • 49049148030 scopus 로고
    • Binding of unconjugated and conjugated sulfobromophthalein to rat liver plasma membrane fractions in vitro
    • Reichen J, Blitzer BL, Berk PD Binding of unconjugated and conjugated sulfobromophthalein to rat liver plasma membrane fractions in vitro. Biochim Biophys Acta 1981, 640:298-312.
    • (1981) Biochim Biophys Acta , vol.640 , pp. 298-312
    • Reichen, J.1    Blitzer, B.L.2    Berk, P.D.3
  • 20
    • 0020636502 scopus 로고
    • Physicochemical and immunohistological studies of a sulfobromophthalein-and bilirubin-binding protein from rat liver plasma membranes
    • Stremmel W, Gerber MA, Glezerov V, Thung SN, Kochwa S, Berk PD Physicochemical and immunohistological studies of a sulfobromophthalein-and bilirubin-binding protein from rat liver plasma membranes. J Clin Invest 1983, 71:1796-1805.
    • (1983) J Clin Invest , vol.71 , pp. 1796-1805
    • Stremmel, W.1    Gerber, M.A.2    Glezerov, V.3    Thung, S.N.4    Kochwa, S.5    Berk, P.D.6
  • 21
    • 0020489214 scopus 로고
    • Further studies on bilitranslocase, a plasma membrane protein involved in hepatic organic anion uptake
    • Lunazzi G, Tiribelli C, Gazzin B, Sottocasa G Further studies on bilitranslocase, a plasma membrane protein involved in hepatic organic anion uptake. Biochim Biophys Acta 1982, 685:117-122.
    • (1982) Biochim Biophys Acta , vol.685 , pp. 117-122
    • Lunazzi, G.1    Tiribelli, C.2    Gazzin, B.3    Sottocasa, G.4
  • 22
    • 0025056595 scopus 로고
    • Cellular uptake of conjugate bilirubin and sulfobromophthalein (BSP) by the human hepatoma cell line Hep G2 is mediated by a membrane BSP/bilirubin binding protein
    • Stremmel W, Diede HE Cellular uptake of conjugate bilirubin and sulfobromophthalein (BSP) by the human hepatoma cell line Hep G2 is mediated by a membrane BSP/bilirubin binding protein. J Hepatol 1990, 10:99-104.
    • (1990) J Hepatol , vol.10 , pp. 99-104
    • Stremmel, W.1    Diede, H.E.2
  • 23
    • 0025152017 scopus 로고
    • Biochemical and molecular aspects of the hepatic uptake of organic anions
    • Tiribelli C, Lunazzi GC, Sottocasa GL Biochemical and molecular aspects of the hepatic uptake of organic anions. Biochim Biophys Acta 1990, 1031:261-275.
    • (1990) Biochim Biophys Acta , vol.1031 , pp. 261-275
    • Tiribelli, C.1    Lunazzi, G.C.2    Sottocasa, G.L.3
  • 26
    • 0024580791 scopus 로고
    • Bilitranslocase is the protein responsible for the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver: immunochemical evidence using mono-and poly-clonal antibodies
    • Miccio M, Baldini G, Basso V, Grazzin B, Lunazzi GC, Tiribelli C, et al. Bilitranslocase is the protein responsible for the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver: immunochemical evidence using mono-and poly-clonal antibodies. Biochim Biophys Acta 1989, 981:115-120.
    • (1989) Biochim Biophys Acta , vol.981 , pp. 115-120
    • Miccio, M.1    Baldini, G.2    Basso, V.3    Grazzin, B.4    Lunazzi, G.C.5    Tiribelli, C.6
  • 27
    • 0038018460 scopus 로고    scopus 로고
    • The stomach as a site for anthocyanins absorption from food
    • Passamonti S, Vrhovsek U, Vanzo A, Mattivi F The stomach as a site for anthocyanins absorption from food. FEBS Lett 2003, 544:210-213.
    • (2003) FEBS Lett , vol.544 , pp. 210-213
    • Passamonti, S.1    Vrhovsek, U.2    Vanzo, A.3    Mattivi, F.4
  • 28
    • 0026633806 scopus 로고
    • Transport of sulfobromophthalein and taurocholate in the HepG2 cell line in relation to the expression of membrane carrier proteins
    • Marchegiano P, Carubbi F, Tiribelli C, Amarri S, Stebel M, Lunazzi GC, et al. Transport of sulfobromophthalein and taurocholate in the HepG2 cell line in relation to the expression of membrane carrier proteins. Biochem Biophys Res Commun 1992, 183:1203-1208.
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 1203-1208
    • Marchegiano, P.1    Carubbi, F.2    Tiribelli, C.3    Amarri, S.4    Stebel, M.5    Lunazzi, G.C.6
  • 29
    • 72049124853 scopus 로고    scopus 로고
    • Expression of bilitranslocase in the vascular endothelium and its function as a flavonoid transporter
    • Maestro A, Terdoslavich M, Vanzo A, Kuku A, Tramer F, Nicolin V, et al. Expression of bilitranslocase in the vascular endothelium and its function as a flavonoid transporter. Cardiovasc Res 2010, 85:175-183.
    • (2010) Cardiovasc Res , vol.85 , pp. 175-183
    • Maestro, A.1    Terdoslavich, M.2    Vanzo, A.3    Kuku, A.4    Tramer, F.5    Nicolin, V.6
  • 30
    • 0032577917 scopus 로고    scopus 로고
    • The bilirubin-binding motif of bilitranslocase and its relation to conserved motifs in ancient biliproteins
    • Battiston L, Passamonti S, Macagno A, Sottocasa GL The bilirubin-binding motif of bilitranslocase and its relation to conserved motifs in ancient biliproteins. Biochem Biophys Res Commun 1998, 247:687-692.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 687-692
    • Battiston, L.1    Passamonti, S.2    Macagno, A.3    Sottocasa, G.L.4
  • 31
    • 0032802760 scopus 로고    scopus 로고
    • Specific sequence-directed anti-bilitranslocase antibodies as a tool to detect potentially bilirubin-binding proteins in different tissues of the rat
    • Battiston L, Macagno A, Passamonti S, Micali F, Sottocasa GL Specific sequence-directed anti-bilitranslocase antibodies as a tool to detect potentially bilirubin-binding proteins in different tissues of the rat. FEBS Lett 1999, 453:351-355.
    • (1999) FEBS Lett , vol.453 , pp. 351-355
    • Battiston, L.1    Macagno, A.2    Passamonti, S.3    Micali, F.4    Sottocasa, G.L.5
  • 32
    • 0018968775 scopus 로고
    • Identification, purification, and partial characterization of an organic anion binding protein from rat liver cell plasma membrane
    • Wolkoff AW, Chung CT Identification, purification, and partial characterization of an organic anion binding protein from rat liver cell plasma membrane. J Clin Invest 1980, 65:1152-1161.
    • (1980) J Clin Invest , vol.65 , pp. 1152-1161
    • Wolkoff, A.W.1    Chung, C.T.2
  • 33
    • 0025284730 scopus 로고
    • The rat hepatocyte plasma membrane organic anion binding protein is immunologically related to the mitochondrial F1 adenosine triphosphatase beta-subunit
    • Goeser T, Nakata R, Braly LF, Sosiak A, Campbell CG, Dermietzel R, et al. The rat hepatocyte plasma membrane organic anion binding protein is immunologically related to the mitochondrial F1 adenosine triphosphatase beta-subunit. J Clin Invest 1990, 86:220-227.
    • (1990) J Clin Invest , vol.86 , pp. 220-227
    • Goeser, T.1    Nakata, R.2    Braly, L.F.3    Sosiak, A.4    Campbell, C.G.5    Dermietzel, R.6
  • 35
    • 1242272736 scopus 로고    scopus 로고
    • Organic anion transporting polypeptides of the OATP/SLC21 family: phylogenetic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties
    • Hagenbuch B, Meier PJ Organic anion transporting polypeptides of the OATP/SLC21 family: phylogenetic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties. Pflugers Arch 2004, 447:653-665.
    • (2004) Pflugers Arch , vol.447 , pp. 653-665
    • Hagenbuch, B.1    Meier, P.J.2
  • 37
    • 0037427972 scopus 로고    scopus 로고
    • The superfamily of organic anion transporting polypeptides
    • Hagenbuch B, Meier PJ The superfamily of organic anion transporting polypeptides. Biochim Biophys Acta 2003, 1609:1-18.
    • (2003) Biochim Biophys Acta , vol.1609 , pp. 1-18
    • Hagenbuch, B.1    Meier, P.J.2
  • 38
    • 77949398878 scopus 로고    scopus 로고
    • Xenobiotic, bile acid, and cholesterol transporters: function and regulation
    • Klaassen CD, Aleksunes LM Xenobiotic, bile acid, and cholesterol transporters: function and regulation. Pharmacol Rev 2010, 62:1-96.
    • (2010) Pharmacol Rev , vol.62 , pp. 1-96
    • Klaassen, C.D.1    Aleksunes, L.M.2
  • 39
    • 0028807537 scopus 로고
    • Stable inducible expression of a functional rat liver organic anion transport protein in HeLa Cells
    • Shi X, Bai S, Ford AC, Burk RD, Jacquemin E, Hagenbuch B, et al. Stable inducible expression of a functional rat liver organic anion transport protein in HeLa Cells. J Biol Chem 1995, 270:25591-25595.
    • (1995) J Biol Chem , vol.270 , pp. 25591-25595
    • Shi, X.1    Bai, S.2    Ford, A.C.3    Burk, R.D.4    Jacquemin, E.5    Hagenbuch, B.6
  • 41
    • 15844387507 scopus 로고    scopus 로고
    • The peptide-based thrombin inhibitor CRC 220 is a new substrate of the basolateral rat liver organic anion-transporting polypeptide
    • Eckhardt U, Horz JA, Petzinger E, Stuber W, Reers M, Dickneite G, et al. The peptide-based thrombin inhibitor CRC 220 is a new substrate of the basolateral rat liver organic anion-transporting polypeptide. Hepatology 1998, 24:380-384.
    • (1998) Hepatology , vol.24 , pp. 380-384
    • Eckhardt, U.1    Horz, J.A.2    Petzinger, E.3    Stuber, W.4    Reers, M.5    Dickneite, G.6
  • 42
    • 17344364101 scopus 로고    scopus 로고
    • The modified dipeptide, enalapril, an angiotensin-converting enzyme inhibitor, is transported by the rat liver organic anion transport protein
    • Pang KS, Wang PJ, Chung AY, Wolkoff AW The modified dipeptide, enalapril, an angiotensin-converting enzyme inhibitor, is transported by the rat liver organic anion transport protein. Hepatology 1998, 28:1341-1346.
    • (1998) Hepatology , vol.28 , pp. 1341-1346
    • Pang, K.S.1    Wang, P.J.2    Chung, A.Y.3    Wolkoff, A.W.4
  • 43
    • 0029876335 scopus 로고    scopus 로고
    • Estradiol 17b-D-glucuronide is a high-affinity substrate for oatp organic anion transporter
    • Kanai N, Lu R, Bao Y, Wolkoff AW, Vore M, Schuster VL Estradiol 17b-D-glucuronide is a high-affinity substrate for oatp organic anion transporter. Am J Physiol 1996, 270:F326-F331.
    • (1996) Am J Physiol , vol.270
    • Kanai, N.1    Lu, R.2    Bao, Y.3    Wolkoff, A.W.4    Vore, M.5    Schuster, V.L.6
  • 44
    • 0030098277 scopus 로고    scopus 로고
    • Polyspecific drug and steroid clearance by an organic anion transporter of mammalian liver
    • Bossuyt X, Muller M, Hagenbuch B, Meier PJ Polyspecific drug and steroid clearance by an organic anion transporter of mammalian liver. J Pharm Exper Ther 1996, 276:891-896.
    • (1996) J Pharm Exper Ther , vol.276 , pp. 891-896
    • Bossuyt, X.1    Muller, M.2    Hagenbuch, B.3    Meier, P.J.4
  • 45
    • 22944440991 scopus 로고    scopus 로고
    • Comparative pharmacophore modeling of organic anion transporting polypeptides: a meta-analysis of rat Oatp1a1 and human OATP1B1
    • Chang C, Pang KS, Swaan PW, Ekins S Comparative pharmacophore modeling of organic anion transporting polypeptides: a meta-analysis of rat Oatp1a1 and human OATP1B1. J Pharmacol Exp Ther 2005, 314:533-541.
    • (2005) J Pharmacol Exp Ther , vol.314 , pp. 533-541
    • Chang, C.1    Pang, K.S.2    Swaan, P.W.3    Ekins, S.4
  • 46
    • 42049090778 scopus 로고    scopus 로고
    • Topological assessment of oatp1a1: a 12 transmembrane domain integral membrane protein with three N-linked carbohydrate chains
    • Wang P, Hata S, Xiao Y, Murray JW, Wolkoff AW Topological assessment of oatp1a1: a 12 transmembrane domain integral membrane protein with three N-linked carbohydrate chains. Am J Physiol Gastrointest Liver Physiol 2008.
    • (2008) Am J Physiol Gastrointest Liver Physiol
    • Wang, P.1    Hata, S.2    Xiao, Y.3    Murray, J.W.4    Wolkoff, A.W.5
  • 48
    • 0031717725 scopus 로고    scopus 로고
    • Dichotomous development of the organic anion transport protein in liver and choroid plexus
    • Angeletti RH, Bergwerk AJ, Novikoff PM, Wolkoff AW Dichotomous development of the organic anion transport protein in liver and choroid plexus. Am J Physiol 1998, 275:C882-C887.
    • (1998) Am J Physiol , vol.275
    • Angeletti, R.H.1    Bergwerk, A.J.2    Novikoff, P.M.3    Wolkoff, A.W.4
  • 49
    • 16044374493 scopus 로고    scopus 로고
    • Immunologic distribution of an organic anion transport protein in rat liver and kidney
    • Bergwerk AJ, Shi X, Ford AC, Kanai N, Jacquemin E, Burk RD, et al. Immunologic distribution of an organic anion transport protein in rat liver and kidney. Am J Physiol 1996, 271:G231-G238.
    • (1996) Am J Physiol , vol.271
    • Bergwerk, A.J.1    Shi, X.2    Ford, A.C.3    Kanai, N.4    Jacquemin, E.5    Burk, R.D.6
  • 50
    • 69449099763 scopus 로고    scopus 로고
    • Organic anion transporting polypeptide (Oatp) 1a1-mediated perfluorooctanoate transport and evidence for a renal reabsorption mechanism of Oatp1a1 in renal elimination of perfluorocarboxylates in rats
    • Yang CH, Glover KP, Han X Organic anion transporting polypeptide (Oatp) 1a1-mediated perfluorooctanoate transport and evidence for a renal reabsorption mechanism of Oatp1a1 in renal elimination of perfluorocarboxylates in rats. Toxicol Lett 2009, 190:163-171.
    • (2009) Toxicol Lett , vol.190 , pp. 163-171
    • Yang, C.H.1    Glover, K.P.2    Han, X.3
  • 51
    • 22344452137 scopus 로고    scopus 로고
    • Tissue distribution and ontogeny of mouse organic anion transporting polypeptides (Oatps)
    • Cheng X, Maher J, Chen C, Klaassen CD Tissue distribution and ontogeny of mouse organic anion transporting polypeptides (Oatps). Drug Metab Dispos 2005, 33:1062-1073.
    • (2005) Drug Metab Dispos , vol.33 , pp. 1062-1073
    • Cheng, X.1    Maher, J.2    Chen, C.3    Klaassen, C.D.4
  • 52
    • 47949104688 scopus 로고    scopus 로고
    • Targeted disruption of murine organic anion-transporting polypeptide 1b2 (oatp1b2/Slco1b2) significantly alters disposition of prototypical drug substrates pravastatin and rifampin
    • Zaher H, zu Schwabedissen HE, Tirona RG, Cox ML, Obert LA, Agrawal N, et al. Targeted disruption of murine organic anion-transporting polypeptide 1b2 (oatp1b2/Slco1b2) significantly alters disposition of prototypical drug substrates pravastatin and rifampin. Mol Pharmacol 2008, 74:320-329.
    • (2008) Mol Pharmacol , vol.74 , pp. 320-329
    • Zaher, H.1    zu Schwabedissen, H.E.2    Tirona, R.G.3    Cox, M.L.4    Obert, L.A.5    Agrawal, N.6
  • 53
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988, 16:10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 54
    • 24044445813 scopus 로고    scopus 로고
    • Interaction with PDZK1 is required for expression of organic anion transporting protein 1A1 (OATP1A1) on the hepatocyte surface
    • Wang P, Wang JJ, Xiao Y, Murray JW, Novikoff PM, Angeletti RH, et al. Interaction with PDZK1 is required for expression of organic anion transporting protein 1A1 (OATP1A1) on the hepatocyte surface. J Biol Chem 2005, 280:30143-30149.
    • (2005) J Biol Chem , vol.280 , pp. 30143-30149
    • Wang, P.1    Wang, J.J.2    Xiao, Y.3    Murray, J.W.4    Novikoff, P.M.5    Angeletti, R.H.6
  • 55
    • 25644441718 scopus 로고    scopus 로고
    • Vascular binding, blood flow, transporter, and enzyme interactions on the processing of digoxin in rat liver
    • Liu L, Mak E, Tirona RG, Tan E, Novikoff PM, Wang P, et al. Vascular binding, blood flow, transporter, and enzyme interactions on the processing of digoxin in rat liver. J Pharmacol Exp Ther 2005, 315:433-448.
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 433-448
    • Liu, L.1    Mak, E.2    Tirona, R.G.3    Tan, E.4    Novikoff, P.M.5    Wang, P.6
  • 57
    • 0028108370 scopus 로고
    • Functional characterization of the basolateral rat liver organic anion transporting polypeptide
    • Kullak-Ublick G-A, Hagenbuch B, Stieger B, Wolkoff AW, Meier PJ Functional characterization of the basolateral rat liver organic anion transporting polypeptide. Hepatology 1994, 20:411-416.
    • (1994) Hepatology , vol.20 , pp. 411-416
    • Kullak-Ublick, G.-A.1    Hagenbuch, B.2    Stieger, B.3    Wolkoff, A.W.4    Meier, P.J.5
  • 58
    • 0030437929 scopus 로고    scopus 로고
    • Uptake of the mycotoxin ochratoxin A in liver cells occurs via the cloned organic anion transporting polypeptide
    • Kontaxi M, Eckhardt U, Hagenbuch B, Stieger B, Meier PJ, Petzinger E Uptake of the mycotoxin ochratoxin A in liver cells occurs via the cloned organic anion transporting polypeptide. J Pharm Exper Ther 1996, 279:1507-1513.
    • (1996) J Pharm Exper Ther , vol.279 , pp. 1507-1513
    • Kontaxi, M.1    Eckhardt, U.2    Hagenbuch, B.3    Stieger, B.4    Meier, P.J.5    Petzinger, E.6
  • 60
    • 0029876334 scopus 로고    scopus 로고
    • Transient expression of oatp organic anion transporter in mammalian cells: identification of candidate substrates
    • Kanai N, Lu R, Bao Y, Wolkoff AW, Schuster VL Transient expression of oatp organic anion transporter in mammalian cells: identification of candidate substrates. Am J Physiol 1996, 270:F319-F325.
    • (1996) Am J Physiol , vol.270
    • Kanai, N.1    Lu, R.2    Bao, Y.3    Wolkoff, A.W.4    Schuster, V.L.5
  • 61
    • 50049110841 scopus 로고    scopus 로고
    • Utility of a novel Oatp1b2 knockout mouse model for evaluating the role of Oatp1b2 in the hepatic uptake of model compounds
    • Chen C, Stock JL, Liu X, Shi J, Van Deusen JW, Dimattia DA, et al. Utility of a novel Oatp1b2 knockout mouse model for evaluating the role of Oatp1b2 in the hepatic uptake of model compounds. Drug Metab Dispos 2008, 36:1840-1845.
    • (2008) Drug Metab Dispos , vol.36 , pp. 1840-1845
    • Chen, C.1    Stock, J.L.2    Liu, X.3    Shi, J.4    Van Deusen, J.W.5    Dimattia, D.A.6
  • 62
    • 42149136754 scopus 로고    scopus 로고
    • Characterization of organic anion transporting polypeptide 1b2-null mice: essential role in hepatic uptake/toxicity of phalloidin and microcystin-LR
    • Lu H, Choudhuri S, Ogura K, Csanaky IL, Lei X, Cheng X, et al. Characterization of organic anion transporting polypeptide 1b2-null mice: essential role in hepatic uptake/toxicity of phalloidin and microcystin-LR. Toxicol Sci 2008, 103:35-45.
    • (2008) Toxicol Sci , vol.103 , pp. 35-45
    • Lu, H.1    Choudhuri, S.2    Ogura, K.3    Csanaky, I.L.4    Lei, X.5    Cheng, X.6
  • 64
    • 34447335619 scopus 로고    scopus 로고
    • Effect of drug transporter genotypes on pravastatin disposition in European-and African-American participants
    • Ho RH, Choi L, Lee W, Mayo G, Schwarz UI, Tirona RG, et al. Effect of drug transporter genotypes on pravastatin disposition in European-and African-American participants. Pharmacogenet Genomics 2007, 17:647-656.
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 647-656
    • Ho, R.H.1    Choi, L.2    Lee, W.3    Mayo, G.4    Schwarz, U.I.5    Tirona, R.G.6
  • 65
    • 38549159477 scopus 로고    scopus 로고
    • Influence of OATP1B1 genotype on the pharmacokinetics of rosuvastatin in Koreans
    • Choi JH, Lee MG, Cho JY, Lee JE, Kim KH, Park K Influence of OATP1B1 genotype on the pharmacokinetics of rosuvastatin in Koreans. Clin Pharmacol Ther 2008, 83:251-257.
    • (2008) Clin Pharmacol Ther , vol.83 , pp. 251-257
    • Choi, J.H.1    Lee, M.G.2    Cho, J.Y.3    Lee, J.E.4    Kim, K.H.5    Park, K.6
  • 66
    • 35448946484 scopus 로고    scopus 로고
    • SLCO1B1 (OATP1B1, an uptake transporter) and ABCG2 (BCRP, an efflux transporter) variant alleles and pharmacokinetics of pitavastatin in healthy volunteers
    • Ieiri I, Suwannakul S, Maeda K, Uchimaru H, Hashimoto K, Kimura M, et al. SLCO1B1 (OATP1B1, an uptake transporter) and ABCG2 (BCRP, an efflux transporter) variant alleles and pharmacokinetics of pitavastatin in healthy volunteers. Clin Pharmacol Ther 2007, 82:541-547.
    • (2007) Clin Pharmacol Ther , vol.82 , pp. 541-547
    • Ieiri, I.1    Suwannakul, S.2    Maeda, K.3    Uchimaru, H.4    Hashimoto, K.5    Kimura, M.6
  • 67
    • 34548009561 scopus 로고    scopus 로고
    • SLCO1B1 521T→C functional genetic polymorphism and lipid-lowering efficacy of multiple-dose pravastatin in Chinese coronary heart disease patients
    • Zhang W, Chen BL, Ozdemir V, He YJ, Zhou G, Peng DD, et al. SLCO1B1 521T→C functional genetic polymorphism and lipid-lowering efficacy of multiple-dose pravastatin in Chinese coronary heart disease patients. Br J Clin Pharmacol 2007, 64:346-352.
    • (2007) Br J Clin Pharmacol , vol.64 , pp. 346-352
    • Zhang, W.1    Chen, B.L.2    Ozdemir, V.3    He, Y.J.4    Zhou, G.5    Peng, D.D.6
  • 68
    • 33846034416 scopus 로고    scopus 로고
    • Influence of drug transporter polymorphisms on pravastatin pharmacokinetics in humans
    • Kivisto KT, Niemi M Influence of drug transporter polymorphisms on pravastatin pharmacokinetics in humans. Pharm Res 2007, 24:239-247.
    • (2007) Pharm Res , vol.24 , pp. 239-247
    • Kivisto, K.T.1    Niemi, M.2
  • 69
    • 77955300958 scopus 로고    scopus 로고
    • Organic anion transporting polypeptide 1a/1b-knockout mice provide insights into hepatic handling of bilirubin, bile acids, and drugs
    • van de SE, Wagenaar E, van der Kruijssen CM, Burggraaff JE, de Waart DR, Elferink RP, et al. Organic anion transporting polypeptide 1a/1b-knockout mice provide insights into hepatic handling of bilirubin, bile acids, and drugs. J Clin Invest 2010, 120:2942-2952.
    • (2010) J Clin Invest , vol.120 , pp. 2942-2952
    • van de, S.E.1    Wagenaar, E.2    van der Kruijssen, C.M.3    Burggraaff, J.E.4    de Waart, D.R.5    Elferink, R.P.6
  • 70
    • 0034767938 scopus 로고    scopus 로고
    • Protein kinase C suppresses rat organic anion transporting polypeptide 1-and 2-mediated uptake
    • Guo GL, Klaassen CD Protein kinase C suppresses rat organic anion transporting polypeptide 1-and 2-mediated uptake. J Pharmacol Exp Ther 2001, 299:551-557.
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 551-557
    • Guo, G.L.1    Klaassen, C.D.2
  • 71
    • 33644857689 scopus 로고    scopus 로고
    • Rat organic anion transporting protein 1A1 (Oatp1a1): purification and phosphopeptide assignment
    • Xiao Y, Nieves E, Angeletti RH, Orr GA, Wolkoff AW Rat organic anion transporting protein 1A1 (Oatp1a1): purification and phosphopeptide assignment. Biochem 2006, 45:3357-3369.
    • (2006) Biochem , vol.45 , pp. 3357-3369
    • Xiao, Y.1    Nieves, E.2    Angeletti, R.H.3    Orr, G.A.4    Wolkoff, A.W.5
  • 72
    • 4444266366 scopus 로고    scopus 로고
    • Differential expression of bile salt and organic anion transporters in developing rat liver
    • Gao B, St.Pierre MV, Stieger B, Meier PJ Differential expression of bile salt and organic anion transporters in developing rat liver. J Hepatol 2004, 41:201-208.
    • (2004) J Hepatol , vol.41 , pp. 201-208
    • Gao, B.1    St.Pierre, M.V.2    Stieger, B.3    Meier, P.J.4
  • 73
    • 1342304081 scopus 로고    scopus 로고
    • +-taurocholate cotransporting polypeptide (SLC10A1) reveals a domain critical for bile acid substrate recognition
    • +-taurocholate cotransporting polypeptide (SLC10A1) reveals a domain critical for bile acid substrate recognition. J Biol Chem 2004, 279:7213-7222.
    • (2004) J Biol Chem , vol.279 , pp. 7213-7222
    • Ho, R.H.1    Leake, B.F.2    Roberts, R.L.3    Lee, W.4    Kim, R.B.5
  • 74
    • 33749290063 scopus 로고    scopus 로고
    • Ethinyl estradiol cholestasis involves alterations in expression of liver sinusoidal transporters
    • Simon FR, Fortune J, Iwahashi M, Gartung C, Wolkoff AW, Sutherland E Ethinyl estradiol cholestasis involves alterations in expression of liver sinusoidal transporters. Am J Physiol 1996, 271:G1043-G1052.
    • (1996) Am J Physiol , vol.271
    • Simon, F.R.1    Fortune, J.2    Iwahashi, M.3    Gartung, C.4    Wolkoff, A.W.5    Sutherland, E.6
  • 76
    • 0032810191 scopus 로고    scopus 로고
    • Effects of LPS on transport of indocyanine green and alanine uptake in perfused rat liver
    • Lund M, Kang L, Tygstrup N, Wolkoff AW, Ott P Effects of LPS on transport of indocyanine green and alanine uptake in perfused rat liver. Am J Physiol 1999, 277:G91-G100.
    • (1999) Am J Physiol , vol.277
    • Lund, M.1    Kang, L.2    Tygstrup, N.3    Wolkoff, A.W.4    Ott, P.5
  • 77
    • 0032998834 scopus 로고    scopus 로고
    • Molecular regulation of hepatocellular transport systems in cholestasis
    • Trauner M, Meier PJ, Boyer JL Molecular regulation of hepatocellular transport systems in cholestasis. J Hepatol 1999, 31:165-178.
    • (1999) J Hepatol , vol.31 , pp. 165-178
    • Trauner, M.1    Meier, P.J.2    Boyer, J.L.3
  • 79
    • 0032936162 scopus 로고    scopus 로고
    • Characterization of the mechanisms involved in the gender differences in hepatic taurocholate uptake
    • Simon FR, Fortune J, Iwahashi M, Bowman S, Wolkoff A, Sutherland E Characterization of the mechanisms involved in the gender differences in hepatic taurocholate uptake. Am J Physiol 1999, 276:G556-G565.
    • (1999) Am J Physiol , vol.276
    • Simon, F.R.1    Fortune, J.2    Iwahashi, M.3    Bowman, S.4    Wolkoff, A.5    Sutherland, E.6
  • 80
    • 0036721559 scopus 로고    scopus 로고
    • Expression of rat hepatic multidrug resistance-associated proteins and organic anion transporters in pregnancy
    • Cao J, Stieger B, Meier PJ, Vore M Expression of rat hepatic multidrug resistance-associated proteins and organic anion transporters in pregnancy. Am J Physiol Gastrointest Liver Physiol 2002, 283:G757-G766.
    • (2002) Am J Physiol Gastrointest Liver Physiol , vol.283
    • Cao, J.1    Stieger, B.2    Meier, P.J.3    Vore, M.4
  • 81
    • 0035192777 scopus 로고    scopus 로고
    • Differential regulation of hepatic bile salt and organic anion transporters in pregnant and postpartum rats and the role of prolactin
    • Cao J, Huang L, Liu Y, Hoffman T, Stieger B, Meier PJ, et al. Differential regulation of hepatic bile salt and organic anion transporters in pregnant and postpartum rats and the role of prolactin. Hepatology 2001, 33:140-147.
    • (2001) Hepatology , vol.33 , pp. 140-147
    • Cao, J.1    Huang, L.2    Liu, Y.3    Hoffman, T.4    Stieger, B.5    Meier, P.J.6
  • 82
    • 84920357266 scopus 로고    scopus 로고
    • Differential expression of basolateral and canalicular organic anion transporters during regeneration of rat liver
    • Gerloff T, Geier A, Stieger B, Hagenbuch B, Meier PJ, Matern S, et al. Differential expression of basolateral and canalicular organic anion transporters during regeneration of rat liver. Gastroenterology 1999, 117:1408-1415.
    • (1999) Gastroenterology , vol.117 , pp. 1408-1415
    • Gerloff, T.1    Geier, A.2    Stieger, B.3    Hagenbuch, B.4    Meier, P.J.5    Matern, S.6
  • 83
    • 0034664729 scopus 로고    scopus 로고
    • Targeted disruption of the nuclear receptor FXR/BAR impairs bile acid and lipid homeostasis
    • Sinal CJ, Tohkin M, Miyata M, Ward JM, Lambert G, Gonzalez FJ Targeted disruption of the nuclear receptor FXR/BAR impairs bile acid and lipid homeostasis. Cell 2000, 102:731-744.
    • (2000) Cell , vol.102 , pp. 731-744
    • Sinal, C.J.1    Tohkin, M.2    Miyata, M.3    Ward, J.M.4    Lambert, G.5    Gonzalez, F.J.6
  • 84
    • 0037379362 scopus 로고    scopus 로고
    • Bile salt transporters: molecular characterization, function, and regulation
    • Trauner M, Boyer JL Bile salt transporters: molecular characterization, function, and regulation. Physiol Rev 2003, 83:633-671.
    • (2003) Physiol Rev , vol.83 , pp. 633-671
    • Trauner, M.1    Boyer, J.L.2
  • 85
    • 0035072875 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor-1alpha is an essential regulator of bile acid and plasma cholesterol metabolism
    • Shih DQ, Bussen M, Sehayek E, Ananthanarayanan M, Shneider BL, Suchy FJ, et al. Hepatocyte nuclear factor-1alpha is an essential regulator of bile acid and plasma cholesterol metabolism. Nat Genet 2001, 27:375-382.
    • (2001) Nat Genet , vol.27 , pp. 375-382
    • Shih, D.Q.1    Bussen, M.2    Sehayek, E.3    Ananthanarayanan, M.4    Shneider, B.L.5    Suchy, F.J.6
  • 86
    • 0035141324 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis
    • Hayhurst GP, Lee YH, Lambert G, Ward JM, Gonzalez FJ Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis. Mol Cell Biol 2001, 21:1393-1403.
    • (2001) Mol Cell Biol , vol.21 , pp. 1393-1403
    • Hayhurst, G.P.1    Lee, Y.H.2    Lambert, G.3    Ward, J.M.4    Gonzalez, F.J.5
  • 87
    • 0346100571 scopus 로고    scopus 로고
    • Enterohepatic bile salt transporters in normal physiology and liver disease
    • Kullak-Ublick GA, Stieger B, Meier PJ Enterohepatic bile salt transporters in normal physiology and liver disease. Gastroenterology 2004, 126:322-342.
    • (2004) Gastroenterology , vol.126 , pp. 322-342
    • Kullak-Ublick, G.A.1    Stieger, B.2    Meier, P.J.3
  • 89
    • 0036205380 scopus 로고    scopus 로고
    • Induction of rat organic anion transporting polypeptide 2 by pregnenolone-16alpha-carbonitrile is via interaction with pregnane X receptor
    • Guo GL, Staudinger J, Ogura K, Klaassen CD Induction of rat organic anion transporting polypeptide 2 by pregnenolone-16alpha-carbonitrile is via interaction with pregnane X receptor. Mol Pharmacol 2002, 61:832-839.
    • (2002) Mol Pharmacol , vol.61 , pp. 832-839
    • Guo, G.L.1    Staudinger, J.2    Ogura, K.3    Klaassen, C.D.4
  • 90
    • 0035813209 scopus 로고    scopus 로고
    • Characterization of the human OATP-C (SLC21A6) gene promoter and regulation of liver-specific OATP genes by hepatocyte nuclear factor 1 alpha
    • Jung D, Hagenbuch B, Gresh L, Pontoglio M, Meier PJ, Kullak-Ublick GA Characterization of the human OATP-C (SLC21A6) gene promoter and regulation of liver-specific OATP genes by hepatocyte nuclear factor 1 alpha. J Biol Chem 2001, 276:37206-37214.
    • (2001) J Biol Chem , vol.276 , pp. 37206-37214
    • Jung, D.1    Hagenbuch, B.2    Gresh, L.3    Pontoglio, M.4    Meier, P.J.5    Kullak-Ublick, G.A.6
  • 91
    • 0034982907 scopus 로고    scopus 로고
    • Differential effects of microsomal enzyme-inducing chemicals on the hepatic expression of rat organic anion transporters, OATP1 and OATP2
    • Rausch-Derra LC, Hartley DP, Meier PJ, Klaassen CD Differential effects of microsomal enzyme-inducing chemicals on the hepatic expression of rat organic anion transporters, OATP1 and OATP2. Hepatology 2001, 33:1469-1478.
    • (2001) Hepatology , vol.33 , pp. 1469-1478
    • Rausch-Derra, L.C.1    Hartley, D.P.2    Meier, P.J.3    Klaassen, C.D.4
  • 92
    • 0034958172 scopus 로고    scopus 로고
    • Effect of phenobarbital on the expression of bile salt and organic anion transporters of rat liver
    • Hagenbuch N, Reichel C, Stieger B, Cattori V, Fattinger KE, Landmann L, et al. Effect of phenobarbital on the expression of bile salt and organic anion transporters of rat liver. J Hepatol 2001, 34:881-887.
    • (2001) J Hepatol , vol.34 , pp. 881-887
    • Hagenbuch, N.1    Reichel, C.2    Stieger, B.3    Cattori, V.4    Fattinger, K.E.5    Landmann, L.6
  • 93
    • 0037216648 scopus 로고    scopus 로고
    • Human organic anion transporting polypeptide-C (SLC21A6) is a major determinant of rifampin-mediated pregnane X receptor activation
    • Tirona RG, Leake BF, Wolkoff AW, Kim RB Human organic anion transporting polypeptide-C (SLC21A6) is a major determinant of rifampin-mediated pregnane X receptor activation. J Pharmacol Exp Ther 2003, 304:223-228.
    • (2003) J Pharmacol Exp Ther , vol.304 , pp. 223-228
    • Tirona, R.G.1    Leake, B.F.2    Wolkoff, A.W.3    Kim, R.B.4
  • 95
    • 48749112588 scopus 로고    scopus 로고
    • Xenobiotic transporters of the human organic anion transporting polypeptides (OATP) family
    • Hagenbuch B, Gui C Xenobiotic transporters of the human organic anion transporting polypeptides (OATP) family. Xenobiotica 2008, 38:778-801.
    • (2008) Xenobiotica , vol.38 , pp. 778-801
    • Hagenbuch, B.1    Gui, C.2
  • 99
    • 0017227331 scopus 로고
    • Effect of graded bilirubin loads on bilirubin transport by perfused rat liver
    • Bloomer JR, Zaccaria J Effect of graded bilirubin loads on bilirubin transport by perfused rat liver. Am J Physiol 1976, 230:736-742.
    • (1976) Am J Physiol , vol.230 , pp. 736-742
    • Bloomer, J.R.1    Zaccaria, J.2
  • 100
    • 0037907742 scopus 로고    scopus 로고
    • Role of organic anion-transporting polypeptides, OATP-A, OATP-C and OATP-8, in the human placenta-maternal liver tandem excretory pathway for foetal bilirubin
    • Briz O, Serrano MA, Macias RI, Gonzalez-Gallego J, Marin JJ Role of organic anion-transporting polypeptides, OATP-A, OATP-C and OATP-8, in the human placenta-maternal liver tandem excretory pathway for foetal bilirubin. Biochem J 2003, 371:897-905.
    • (2003) Biochem J , vol.371 , pp. 897-905
    • Briz, O.1    Serrano, M.A.2    Macias, R.I.3    Gonzalez-Gallego, J.4    Marin, J.J.5
  • 101
    • 0035971239 scopus 로고    scopus 로고
    • Hepatic uptake of bilirubin and its conjugates by the human organic anion transporter SLC21A6
    • Cui Y, Konig J, Leier I, Buchholz U, Keppler D Hepatic uptake of bilirubin and its conjugates by the human organic anion transporter SLC21A6. J Biol Chem 2001, 276:9626-9630.
    • (2001) J Biol Chem , vol.276 , pp. 9626-9630
    • Cui, Y.1    Konig, J.2    Leier, I.3    Buchholz, U.4    Keppler, D.5
  • 102
    • 0033574696 scopus 로고    scopus 로고
    • Unconjugated bilirubin exhibits spontaneous diffusion through model lipid bilayers and native hepatocyte membranes
    • Zucker SD, Goessling W, Hoppin AG Unconjugated bilirubin exhibits spontaneous diffusion through model lipid bilayers and native hepatocyte membranes. J Biol Chem 1999, 274:10852-10862.
    • (1999) J Biol Chem , vol.274 , pp. 10852-10862
    • Zucker, S.D.1    Goessling, W.2    Hoppin, A.G.3
  • 103
    • 0033951150 scopus 로고    scopus 로고
    • Mechanism of hepatocellular uptake of albumin-bound bilirubin
    • Zucker SD, Goessling W Mechanism of hepatocellular uptake of albumin-bound bilirubin. Biochim Biophys Acta 2000, 1463:197-208.
    • (2000) Biochim Biophys Acta , vol.1463 , pp. 197-208
    • Zucker, S.D.1    Goessling, W.2
  • 104
    • 0020329553 scopus 로고
    • Quantitative aspects of the interaction of bile acids with human serum albumin
    • Roda A, Cappelleri G, Aldini R, Roda E, Barbara L Quantitative aspects of the interaction of bile acids with human serum albumin. J Lipid Res 1982, 23:490-495.
    • (1982) J Lipid Res , vol.23 , pp. 490-495
    • Roda, A.1    Cappelleri, G.2    Aldini, R.3    Roda, E.4    Barbara, L.5
  • 105
    • 0021995611 scopus 로고
    • Bile acid binding in plasma: the importance of lipoproteins
    • Salvioli G, Lugli R, Pradelli JM, Gigliotti G Bile acid binding in plasma: the importance of lipoproteins. FEBS Lett 1985, 187:272-276.
    • (1985) FEBS Lett , vol.187 , pp. 272-276
    • Salvioli, G.1    Lugli, R.2    Pradelli, J.M.3    Gigliotti, G.4
  • 106
    • 0017092068 scopus 로고
    • Uptake of bile acids by perfused rat liver
    • Reichen J, Paumgartner G Uptake of bile acids by perfused rat liver. Am J Physiol 1976, 231:734-742.
    • (1976) Am J Physiol , vol.231 , pp. 734-742
    • Reichen, J.1    Paumgartner, G.2
  • 109
    • 0017169220 scopus 로고
    • Investigations on the sodium dependence of bile acid fluxes in the isolated perfused rat liver
    • Dietmaier A, Gasser R, Graf J, Peterlik M Investigations on the sodium dependence of bile acid fluxes in the isolated perfused rat liver. Biochim Biophys Acta 1976, 443:81-91.
    • (1976) Biochim Biophys Acta , vol.443 , pp. 81-91
    • Dietmaier, A.1    Gasser, R.2    Graf, J.3    Peterlik, M.4
  • 110
    • 0020464777 scopus 로고
    • Taurocholate transport by rat liver sinusoidal membrane vesicles: evidence of sodium cotransport
    • Inoue M, Kinne R, Tran T, Arias IM Taurocholate transport by rat liver sinusoidal membrane vesicles: evidence of sodium cotransport. Hepatology 1982, 2:572-579.
    • (1982) Hepatology , vol.2 , pp. 572-579
    • Inoue, M.1    Kinne, R.2    Tran, T.3    Arias, I.M.4
  • 111
    • 0020027896 scopus 로고
    • Sodium ion-coupled uptake of taurocholate by rat-liver plasma membrane vesicles
    • Ruifrok PG, Meijer DK Sodium ion-coupled uptake of taurocholate by rat-liver plasma membrane vesicles. Liver 1982, 2:28-34.
    • (1982) Liver , vol.2 , pp. 28-34
    • Ruifrok, P.G.1    Meijer, D.K.2
  • 112
    • 0020617090 scopus 로고
    • Direct determination of the driving forces for taurocholate uptake into rat liver plasma membrane vesicles
    • Duffy MC, Blitzer BL, Boyer JL Direct determination of the driving forces for taurocholate uptake into rat liver plasma membrane vesicles. J Clin Invest 1983, 72:1470-1481.
    • (1983) J Clin Invest , vol.72 , pp. 1470-1481
    • Duffy, M.C.1    Blitzer, B.L.2    Boyer, J.L.3
  • 113
    • 0021180138 scopus 로고
    • A new method for the rapid isolation of basolateral plasma membrane vesicles from rat liver. Characterization, validation, and bile acid transport studies
    • Blitzer BL, Donovan CB A new method for the rapid isolation of basolateral plasma membrane vesicles from rat liver. Characterization, validation, and bile acid transport studies. J Biol Chem 1984, 259:9295-9301.
    • (1984) J Biol Chem , vol.259 , pp. 9295-9301
    • Blitzer, B.L.1    Donovan, C.B.2
  • 114
    • 0021250574 scopus 로고
    • Mechanisms of taurocholate transport in canalicular and basolateral rat liver plasma membrane vesicles. Evidence for an electrogenic canalicular organic anion carrier
    • Meier PJ, Meier-Abt A, Barrett C, Boyer JL Mechanisms of taurocholate transport in canalicular and basolateral rat liver plasma membrane vesicles. Evidence for an electrogenic canalicular organic anion carrier. J Biol Chem 1984, 259:10614-10622.
    • (1984) J Biol Chem , vol.259 , pp. 10614-10622
    • Meier, P.J.1    Meier-Abt, A.2    Barrett, C.3    Boyer, J.L.4
  • 115
    • 0021747495 scopus 로고
    • Ionic requirements for taurocholate transport in rat liver plasma membrane vesicles
    • Simion FA, Fleischer B, Fleischer S Ionic requirements for taurocholate transport in rat liver plasma membrane vesicles. J Bioenerg Biomembr 1984, 16:507-515.
    • (1984) J Bioenerg Biomembr , vol.16 , pp. 507-515
    • Simion, F.A.1    Fleischer, B.2    Fleischer, S.3
  • 116
    • 0027405329 scopus 로고
    • Hepatic taurocholate uptake is electrogenic and influenced by transmembrane potential difference
    • Lidofsky SD, Fitz JG, Weisiger RA, Scharschmidt BF Hepatic taurocholate uptake is electrogenic and influenced by transmembrane potential difference. Am J Physiol 1993, 264:G478-G485.
    • (1993) Am J Physiol , vol.264
    • Lidofsky, S.D.1    Fitz, J.G.2    Weisiger, R.A.3    Scharschmidt, B.F.4
  • 117
    • 0020966926 scopus 로고
    • Characterization of the bile acid transport system in normal and transformed hepatocytes. Photoaffinity labeling of the taurocholate carrier protein
    • von Dippe P, Levy D Characterization of the bile acid transport system in normal and transformed hepatocytes. Photoaffinity labeling of the taurocholate carrier protein. J Biol Chem 1983, 258:8896-8901.
    • (1983) J Biol Chem , vol.258 , pp. 8896-8901
    • von Dippe, P.1    Levy, D.2
  • 118
    • 0021219288 scopus 로고
    • Identity of hepatic membrane transport systems for bile salts, phalloidin, and antamanide by photoaffinity labeling
    • Wieland T, Nassal M, Kramer W, Fricker G, Bickel U, Kurz G Identity of hepatic membrane transport systems for bile salts, phalloidin, and antamanide by photoaffinity labeling. Proc Natl Acad Sci USA 1984, 81:5232-5236.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 5232-5236
    • Wieland, T.1    Nassal, M.2    Kramer, W.3    Fricker, G.4    Bickel, U.5    Kurz, G.6
  • 119
    • 0024392379 scopus 로고
    • Determination of the apparent functional molecular mass of the hepatocellular sodium-dependent taurocholate transporter by radiation inactivation
    • Elsner R, Ziegler K Determination of the apparent functional molecular mass of the hepatocellular sodium-dependent taurocholate transporter by radiation inactivation. Biochim Biophys Acta 1989, 983:113-117.
    • (1989) Biochim Biophys Acta , vol.983 , pp. 113-117
    • Elsner, R.1    Ziegler, K.2
  • 120
    • 0026657148 scopus 로고
    • Radiation inactivation of multispecific transport systems for bile acids and xenobiotics in basolateral rat liver plasma membrane vesicles
    • Elsner RH, Ziegler K Radiation inactivation of multispecific transport systems for bile acids and xenobiotics in basolateral rat liver plasma membrane vesicles. J Biol Chem 1992, 267:9788-9793.
    • (1992) J Biol Chem , vol.267 , pp. 9788-9793
    • Elsner, R.H.1    Ziegler, K.2
  • 122
    • 0029615982 scopus 로고
    • Molecular mechanisms of hepatic bile salt transport from sinusoidal blood into bile
    • Meier PJ Molecular mechanisms of hepatic bile salt transport from sinusoidal blood into bile. Am J Physiol 1995, 269:G801-G812.
    • (1995) Am J Physiol , vol.269
    • Meier, P.J.1
  • 123
    • 0033969983 scopus 로고    scopus 로고
    • +/taurocholate cotransporting polypeptide (ntcp): comparative studies on the inhibitory effect of their possible substrates in hepatocytes and cDNA-transfected COS-7 cells
    • +/taurocholate cotransporting polypeptide (ntcp): comparative studies on the inhibitory effect of their possible substrates in hepatocytes and cDNA-transfected COS-7 cells. J Pharm Exper Ther 2000, 292:505-511.
    • (2000) J Pharm Exper Ther , vol.292 , pp. 505-511
    • Kouzuki, H.1    Suzuki, H.2    Stieger, B.3    Meier, P.J.4    Sugiyama, Y.5
  • 124
    • 0030725999 scopus 로고    scopus 로고
    • Substrate specificity of sinusoidal bile acid and organic anion uptake systems in rat and human liver
    • Meier PJ, Eckhardt U, Schroeder A, Hagenbuch B, Stieger B Substrate specificity of sinusoidal bile acid and organic anion uptake systems in rat and human liver. Hepatology 1997, 26:1667-1677.
    • (1997) Hepatology , vol.26 , pp. 1667-1677
    • Meier, P.J.1    Eckhardt, U.2    Schroeder, A.3    Hagenbuch, B.4    Stieger, B.5
  • 126
    • 0033380340 scopus 로고    scopus 로고
    • Substrate specificity of the ileal and the hepatic Na(+)/bile acid cotransporters of the rabbit. II. A reliable 3D QSAR pharmacophore model for the ileal Na( + )/bile acid cotransporter
    • Baringhaus KH, Matter H, Stengelin S, Kramer W Substrate specificity of the ileal and the hepatic Na(+)/bile acid cotransporters of the rabbit. II. A reliable 3D QSAR pharmacophore model for the ileal Na( + )/bile acid cotransporter. J Lipid Res 1999, 40:2158-2168.
    • (1999) J Lipid Res , vol.40 , pp. 2158-2168
    • Baringhaus, K.H.1    Matter, H.2    Stengelin, S.3    Kramer, W.4
  • 127
    • 0032822957 scopus 로고    scopus 로고
    • Substrate specificity of the ileal and the hepatic Na( + )/bile acid cotransporters of the rabbit. I. Transport studies with membrane vesicles and cell lines expressing the cloned transporters
    • Kramer W, Stengelin S, Baringhaus KH, Enhsen A, Heuer H, Becker W, et al. Substrate specificity of the ileal and the hepatic Na( + )/bile acid cotransporters of the rabbit. I. Transport studies with membrane vesicles and cell lines expressing the cloned transporters. J Lipid Res 1999, 40:1604-1617.
    • (1999) J Lipid Res , vol.40 , pp. 1604-1617
    • Kramer, W.1    Stengelin, S.2    Baringhaus, K.H.3    Enhsen, A.4    Heuer, H.5    Becker, W.6
  • 128
    • 0029099818 scopus 로고
    • Differential ontogenic regulation of basolateral and canalicular bile acid transport proteins in rat liver
    • Hardikar W, Ananthanarayanan M, Suchy FJ Differential ontogenic regulation of basolateral and canalicular bile acid transport proteins in rat liver. J Biol Chem 1995, 270:20841-20846.
    • (1995) J Biol Chem , vol.270 , pp. 20841-20846
    • Hardikar, W.1    Ananthanarayanan, M.2    Suchy, F.J.3
  • 131
    • 48749087514 scopus 로고    scopus 로고
    • Bile acid transporters in health and disease
    • Kosters A, Karpen SJ Bile acid transporters in health and disease. Xenobiotica 2008, 38:1043-1071.
    • (2008) Xenobiotica , vol.38 , pp. 1043-1071
    • Kosters, A.1    Karpen, S.J.2
  • 132
    • 0029822980 scopus 로고    scopus 로고
    • Effect of antisense oligonucleotides on the expression of hepatocellular bile acid and organic anion uptake systems in Xenopus laevis oocytes
    • Hagenbuch B, Scharschmidt BF, Meier PJ Effect of antisense oligonucleotides on the expression of hepatocellular bile acid and organic anion uptake systems in Xenopus laevis oocytes. Biochem J 1996, 316:901-904.
    • (1996) Biochem J , vol.316 , pp. 901-904
    • Hagenbuch, B.1    Scharschmidt, B.F.2    Meier, P.J.3
  • 133
    • 0037304264 scopus 로고    scopus 로고
    • Bile acid regulation of hepatic physiology: I. Hepatocyte transport of bile acids
    • Wolkoff AW, Cohen DE Bile acid regulation of hepatic physiology: I. Hepatocyte transport of bile acids. Am J Physiol Gastrointest Liver Physiol 2003, 284:G175-G179.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.284
    • Wolkoff, A.W.1    Cohen, D.E.2
  • 134
    • 0345304768 scopus 로고    scopus 로고
    • Glucose transporter type1 (GLUT-1) deficiency
    • Gordon N, Newton RW Glucose transporter type1 (GLUT-1) deficiency. Brain Dev 2003, 25:477-480.
    • (2003) Brain Dev , vol.25 , pp. 477-480
    • Gordon, N.1    Newton, R.W.2
  • 136
    • 0031006578 scopus 로고    scopus 로고
    • Compound missense mutations in the sodium/D-glucose cotransporter result in trafficking defects
    • Martin MG, Lostao MP, Turk E, Lam J, Kreman M, Wright EM Compound missense mutations in the sodium/D-glucose cotransporter result in trafficking defects. Gastroenterology 1997, 112:1206-1212.
    • (1997) Gastroenterology , vol.112 , pp. 1206-1212
    • Martin, M.G.1    Lostao, M.P.2    Turk, E.3    Lam, J.4    Kreman, M.5    Wright, E.M.6
  • 137
    • 0141818009 scopus 로고    scopus 로고
    • Targeted deletion of the ileal bile acid transporter eliminates enterohepatic cycling of bile acids in mice
    • Dawson PA, Haywood J, Craddock AL, Wilson M, Tietjen M, Kluckman K, et al. Targeted deletion of the ileal bile acid transporter eliminates enterohepatic cycling of bile acids in mice. J Biol Chem 2003, 278:33920-33927.
    • (2003) J Biol Chem , vol.278 , pp. 33920-33927
    • Dawson, P.A.1    Haywood, J.2    Craddock, A.L.3    Wilson, M.4    Tietjen, M.5    Kluckman, K.6
  • 138
    • 0030944084 scopus 로고    scopus 로고
    • Primary bile acid malabsorption caused by mutations in the ileal sodium-dependent bile acid transporter gene (SLC10A2)
    • Oelkers P, Kirby LC, Heubi JE, Dawson PA Primary bile acid malabsorption caused by mutations in the ileal sodium-dependent bile acid transporter gene (SLC10A2). J Clin Invest 1997, 99:1880-1887.
    • (1997) J Clin Invest , vol.99 , pp. 1880-1887
    • Oelkers, P.1    Kirby, L.C.2    Heubi, J.E.3    Dawson, P.A.4
  • 139
    • 0028866988 scopus 로고
    • Identification of a mutation in the ileal sodium-dependent bile acid transporter gene that abolishes transport activity
    • Wong MH, Oelkers P, Dawson PA Identification of a mutation in the ileal sodium-dependent bile acid transporter gene that abolishes transport activity. J Biol Chem 1995, 270:27228-27234.
    • (1995) J Biol Chem , vol.270 , pp. 27228-27234
    • Wong, M.H.1    Oelkers, P.2    Dawson, P.A.3
  • 140
    • 1342305177 scopus 로고    scopus 로고
    • The Q267E mutation in the sodium/iodide symporter (NIS) causes congenital iodide transport defect (ITD) by decreasing the NIS turnover number
    • De LV, Ginter CS, Carrasco N The Q267E mutation in the sodium/iodide symporter (NIS) causes congenital iodide transport defect (ITD) by decreasing the NIS turnover number. J Cell Sci 2004, 117:677-687.
    • (2004) J Cell Sci , vol.117 , pp. 677-687
    • De, L.V.1    Ginter, C.S.2    Carrasco, N.3
  • 142
    • 0033917722 scopus 로고    scopus 로고
    • A novel V59E missense mutation in the sodium iodide symporter gene in a family with iodide transport defect
    • Fujiwara H, Tatsumi K, Tanaka S, Kimura M, Nose O, Amino N A novel V59E missense mutation in the sodium iodide symporter gene in a family with iodide transport defect. Thyroid 2000, 10:471-474.
    • (2000) Thyroid , vol.10 , pp. 471-474
    • Fujiwara, H.1    Tatsumi, K.2    Tanaka, S.3    Kimura, M.4    Nose, O.5    Amino, N.6
  • 143
    • 0032874718 scopus 로고    scopus 로고
    • Biliary fibrosis associated with altered bile composition in a mouse model of erythropoietic protoporphyria
    • Meerman L, Koopen NR, Bloks V, van Goor H, Havinga R, Wolthers BG, et al. Biliary fibrosis associated with altered bile composition in a mouse model of erythropoietic protoporphyria. Gastroenterology 1999, 117:696-705.
    • (1999) Gastroenterology , vol.117 , pp. 696-705
    • Meerman, L.1    Koopen, N.R.2    Bloks, V.3    van Goor, H.4    Havinga, R.5    Wolthers, B.G.6
  • 145
    • 0029998352 scopus 로고    scopus 로고
    • The functional expression of sodium-dependent bile acid transport in Madin-Darby canine kidney cells transfected with the cDNA for microsomal epoxide hydrolase
    • von Dippe P, Amoui M, Stellwagen RH, Levy D The functional expression of sodium-dependent bile acid transport in Madin-Darby canine kidney cells transfected with the cDNA for microsomal epoxide hydrolase. J Biol Chem 1996, 271:18176-18180.
    • (1996) J Biol Chem , vol.271 , pp. 18176-18180
    • von Dippe, P.1    Amoui, M.2    Stellwagen, R.H.3    Levy, D.4
  • 146
    • 0025161557 scopus 로고
    • Reconstitution of the immunopurified 49-kDa sodium-dependent bile acid transport protein derived from hepatocyte sinusoidal plasma membranes
    • von Dippe P, Levy D Reconstitution of the immunopurified 49-kDa sodium-dependent bile acid transport protein derived from hepatocyte sinusoidal plasma membranes. J Biol Chem 1990, 265:14812-14816.
    • (1990) J Biol Chem , vol.265 , pp. 14812-14816
    • von Dippe, P.1    Levy, D.2
  • 147
    • 0033600817 scopus 로고    scopus 로고
    • Membrane topology and cell surface targeting of microsomal epoxide hydrolase. Evidence for multiple topological orientations
    • Zhu Q, von Dippe P, Xing W, Levy D Membrane topology and cell surface targeting of microsomal epoxide hydrolase. Evidence for multiple topological orientations. J Biol Chem 1999, 274:27898-27904.
    • (1999) J Biol Chem , vol.274 , pp. 27898-27904
    • Zhu, Q.1    von Dippe, P.2    Xing, W.3    Levy, D.4
  • 148
    • 0028786094 scopus 로고
    • Relationship between the microsomal epoxide hydrolase and the hepatocellular transport of bile acids and xenobiotics
    • Honscha W, Platte HD, Oesch F, Friedberg T Relationship between the microsomal epoxide hydrolase and the hepatocellular transport of bile acids and xenobiotics. Biochem J 1995, 311:975-979.
    • (1995) Biochem J , vol.311 , pp. 975-979
    • Honscha, W.1    Platte, H.D.2    Oesch, F.3    Friedberg, T.4
  • 149
    • 0033588227 scopus 로고    scopus 로고
    • Targeted disruption of the microsomal epoxide hydrolase gene. Microsomal epoxide hydrolase is required for the carcinogenic activity of 7,12-dimethylbenz[a]anthracene
    • Miyata M, Kudo G, Lee YH, Yang TJ, Gelboin HV, Fernandez-Salguero P, et al. Targeted disruption of the microsomal epoxide hydrolase gene. Microsomal epoxide hydrolase is required for the carcinogenic activity of 7,12-dimethylbenz[a]anthracene. J Biol Chem 1999, 274:23963-23968.
    • (1999) J Biol Chem , vol.274 , pp. 23963-23968
    • Miyata, M.1    Kudo, G.2    Lee, Y.H.3    Yang, T.J.4    Gelboin, H.V.5    Fernandez-Salguero, P.6
  • 150
    • 0037325403 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha (PPARalpha)-mediated regulation of multidrug resistance 2 (Mdr2) expression and function in mice
    • Kok T, Bloks VW, Wolters H, Havinga R, Jansen PL, Staels B, et al. Peroxisome proliferator-activated receptor alpha (PPARalpha)-mediated regulation of multidrug resistance 2 (Mdr2) expression and function in mice. Biochem J 2003, 369:539-547.
    • (2003) Biochem J , vol.369 , pp. 539-547
    • Kok, T.1    Bloks, V.W.2    Wolters, H.3    Havinga, R.4    Jansen, P.L.5    Staels, B.6
  • 151
    • 0037388506 scopus 로고    scopus 로고
    • Protein expression changes in the Sprague Dawley rat liver proteome following administration of peroxisome proliferator activated receptor alpha and gamma ligands
    • White IR, Man WJ, Bryant D, Bugelski P, Camilleri P, Cutler P, et al. Protein expression changes in the Sprague Dawley rat liver proteome following administration of peroxisome proliferator activated receptor alpha and gamma ligands. Proteomics 2003, 3:505-512.
    • (2003) Proteomics , vol.3 , pp. 505-512
    • White, I.R.1    Man, W.J.2    Bryant, D.3    Bugelski, P.4    Camilleri, P.5    Cutler, P.6
  • 153
    • 0026021332 scopus 로고
    • +-dependent taurocholate transporter: influence of side chain length and charge
    • +-dependent taurocholate transporter: influence of side chain length and charge. Hepatology 1991, 13:68-72.
    • (1991) Hepatology , vol.13 , pp. 68-72
    • Hardison, W.G.M.1    Heasley, V.L.2    Shellhamer, D.F.3
  • 154
    • 77953784269 scopus 로고    scopus 로고
    • Transporter studies with the 3-O-sulfate conjugate of 17alpha-ethinylestradiol: assessment of human liver drug transporters
    • Han YH, Busler D, Hong Y, Tian Y, Chen C, Rodrigues AD Transporter studies with the 3-O-sulfate conjugate of 17alpha-ethinylestradiol: assessment of human liver drug transporters. Drug Metab Dispos 2010, 38:1072-1082.
    • (2010) Drug Metab Dispos , vol.38 , pp. 1072-1082
    • Han, Y.H.1    Busler, D.2    Hong, Y.3    Tian, Y.4    Chen, C.5    Rodrigues, A.D.6
  • 155
    • 0023319175 scopus 로고
    • Taurocholate uptake by isolated skate hepatocytes: effect of albumin
    • Smith DJ, Grossbard M, Gordon ER, Boyer JL Taurocholate uptake by isolated skate hepatocytes: effect of albumin. Am J Physiol 1987, 252:G479-G484.
    • (1987) Am J Physiol , vol.252
    • Smith, D.J.1    Grossbard, M.2    Gordon, E.R.3    Boyer, J.L.4
  • 156
    • 0028814040 scopus 로고
    • Expression of sodium-independent organic anion uptake systems of skate liver in Xenopus laevis oocytes
    • Jacquemin E, Hagenbuch B, Wolkoff AW, Meier PJ, Boyer JL Expression of sodium-independent organic anion uptake systems of skate liver in Xenopus laevis oocytes. Am J Physiol 1995, 268:G18-G23.
    • (1995) Am J Physiol , vol.268
    • Jacquemin, E.1    Hagenbuch, B.2    Wolkoff, A.W.3    Meier, P.J.4    Boyer, J.L.5
  • 158
    • 0041344702 scopus 로고    scopus 로고
    • Functional complementation between a novel mammalian polygenic transport complex and an evolutionarily ancient organic solute transporter, OSTalpha-OSTbeta
    • Seward DJ, Koh AS, Boyer JL, Ballatori N Functional complementation between a novel mammalian polygenic transport complex and an evolutionarily ancient organic solute transporter, OSTalpha-OSTbeta. J Biol Chem 2003, 278:27473-27482.
    • (2003) J Biol Chem , vol.278 , pp. 27473-27482
    • Seward, D.J.1    Koh, A.S.2    Boyer, J.L.3    Ballatori, N.4
  • 159
    • 16344396301 scopus 로고    scopus 로고
    • The heteromeric organic solute transporter alpha-beta, Ostalpha -Ostbeta, is an ileal basolateral bile acid transporter
    • Dawson PA, Hubbert M, Haywood J, Craddock AL, Zerangue N, Christian WV, et al. The heteromeric organic solute transporter alpha-beta, Ostalpha -Ostbeta, is an ileal basolateral bile acid transporter. J Biol Chem 2004.
    • (2004) J Biol Chem
    • Dawson, P.A.1    Hubbert, M.2    Haywood, J.3    Craddock, A.L.4    Zerangue, N.5    Christian, W.V.6
  • 160
    • 41649089141 scopus 로고    scopus 로고
    • The organic solute transporter alpha-beta, Ostalpha-Ostbeta, is essential for intestinal bile acid transport and homeostasis
    • Rao A, Haywood J, Craddock AL, Belinsky MG, Kruh GD, Dawson PA The organic solute transporter alpha-beta, Ostalpha-Ostbeta, is essential for intestinal bile acid transport and homeostasis. Proc Natl Acad Sci USA 2008, 105:3891-3896.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3891-3896
    • Rao, A.1    Haywood, J.2    Craddock, A.L.3    Belinsky, M.G.4    Kruh, G.D.5    Dawson, P.A.6
  • 161
    • 77951523553 scopus 로고    scopus 로고
    • Organic solute transporter, OSTalpha-OSTbeta: its role in bile acid transport and cholestasis
    • Soroka CJ, Ballatori N, Boyer JL Organic solute transporter, OSTalpha-OSTbeta: its role in bile acid transport and cholestasis. Semin Liver Dis 2010, 30:178-185.
    • (2010) Semin Liver Dis , vol.30 , pp. 178-185
    • Soroka, C.J.1    Ballatori, N.2    Boyer, J.L.3
  • 162
    • 73449095758 scopus 로고    scopus 로고
    • Mouse organic solute transporter alpha deficiency enhances renal excretion of bile acids and attenuates cholestasis
    • Soroka CJ, Mennone A, Hagey LR, Ballatori N, Boyer JL Mouse organic solute transporter alpha deficiency enhances renal excretion of bile acids and attenuates cholestasis. Hepatology 2010, 51:181-190.
    • (2010) Hepatology , vol.51 , pp. 181-190
    • Soroka, C.J.1    Mennone, A.2    Hagey, L.R.3    Ballatori, N.4    Boyer, J.L.5
  • 163
    • 0021968698 scopus 로고
    • Taurocholate transport by basolateral plasma membrane vesicles isolated from developing rat liver
    • Suchy FJ, Courchene SM, Blitzer BL Taurocholate transport by basolateral plasma membrane vesicles isolated from developing rat liver. Am J Physiol 1985, 248:G648-G654.
    • (1985) Am J Physiol , vol.248
    • Suchy, F.J.1    Courchene, S.M.2    Blitzer, B.L.3
  • 167
    • 1542724881 scopus 로고    scopus 로고
    • Cellular regulation of hepatic bile acid transport in health and cholestasis
    • Anwer MS Cellular regulation of hepatic bile acid transport in health and cholestasis. Hepatology 2004, 39:581-590.
    • (2004) Hepatology , vol.39 , pp. 581-590
    • Anwer, M.S.1
  • 169
    • 0031738338 scopus 로고    scopus 로고
    • Sodium taurocholate cotransporting polypeptide is a serine, threonine phosphoprotein and is dephosphorylated by cyclic adenosine monophosphate
    • Mukhopadhyay S, Ananthanarayanan M, Stieger B, Meier PJ, Suchy FJ, Anwer MS Sodium taurocholate cotransporting polypeptide is a serine, threonine phosphoprotein and is dephosphorylated by cyclic adenosine monophosphate. Hepatology 1998, 28:1629-1636.
    • (1998) Hepatology , vol.28 , pp. 1629-1636
    • Mukhopadhyay, S.1    Ananthanarayanan, M.2    Stieger, B.3    Meier, P.J.4    Suchy, F.J.5    Anwer, M.S.6
  • 171
    • 0032995996 scopus 로고    scopus 로고
    • Short-term regulation of bile acid uptake by microfilament-dependent translocation of rat ntcp to the plasma membrane
    • Dranoff JA, McClure M, Burgstahler AD, Denson LA, Crawford AR, Crawford JM, et al. Short-term regulation of bile acid uptake by microfilament-dependent translocation of rat ntcp to the plasma membrane. Hepatology 1999, 30:223-229.
    • (1999) Hepatology , vol.30 , pp. 223-229
    • Dranoff, J.A.1    McClure, M.2    Burgstahler, A.D.3    Denson, L.A.4    Crawford, A.R.5    Crawford, J.M.6
  • 173
    • 0033369266 scopus 로고    scopus 로고
    • Role of the PI3K/PKB signaling pathway in cAMP-mediated translocation of rat liver ntcp
    • Webster CRL, Anwer MS Role of the PI3K/PKB signaling pathway in cAMP-mediated translocation of rat liver ntcp. Am J Physiol 1999, 277:G1165-G1172.
    • (1999) Am J Physiol , vol.277
    • Webster, C.R.L.1    Anwer, M.S.2
  • 174
    • 14844289742 scopus 로고    scopus 로고
    • Vesicles containing ntcp are part of the recycling endosome pool and are enriched in dynein and myosin IIA
    • Sarkar S, Bananis E, Nath S, Anwer MS, Murray JW, Wolkoff AW Vesicles containing ntcp are part of the recycling endosome pool and are enriched in dynein and myosin IIA. Hepatology 2004, 40:487A.
    • (2004) Hepatology , vol.40
    • Sarkar, S.1    Bananis, E.2    Nath, S.3    Anwer, M.S.4    Murray, J.W.5    Wolkoff, A.W.6
  • 175
    • 2442681520 scopus 로고    scopus 로고
    • Cross-talk between protein kinases Czeta and B in cyclic AMP-mediated sodium taurocholate co-transporting polypeptide translocation in hepatocytes
    • McConkey M, Gillin H, Webster CR, Anwer MS Cross-talk between protein kinases Czeta and B in cyclic AMP-mediated sodium taurocholate co-transporting polypeptide translocation in hepatocytes. J Biol Chem 2004, 279:20882-20888.
    • (2004) J Biol Chem , vol.279 , pp. 20882-20888
    • McConkey, M.1    Gillin, H.2    Webster, C.R.3    Anwer, M.S.4
  • 176
    • 33745757459 scopus 로고    scopus 로고
    • PKCz is required for microtubule-based motility of vesicles containing the ntcp transporter
    • Sarkar S, Bananis E, Nath S, Anwer MS, Wolkoff AW, Murray JW PKCz is required for microtubule-based motility of vesicles containing the ntcp transporter. Traffic 2006, 7:1078-1091.
    • (2006) Traffic , vol.7 , pp. 1078-1091
    • Sarkar, S.1    Bananis, E.2    Nath, S.3    Anwer, M.S.4    Wolkoff, A.W.5    Murray, J.W.6
  • 177
    • 41849085244 scopus 로고    scopus 로고
    • Single vesicle analysis of endocytic fission on microtubules in vitro
    • Murray JW, Sarkar S, Wolkoff AW Single vesicle analysis of endocytic fission on microtubules in vitro. Traffic 2008, 9:833-847.
    • (2008) Traffic , vol.9 , pp. 833-847
    • Murray, J.W.1    Sarkar, S.2    Wolkoff, A.W.3
  • 178
    • 32344446788 scopus 로고    scopus 로고
    • Assay of Rab4-dependent trafficking on microtubules
    • Murray JW, Wolkoff AW Assay of Rab4-dependent trafficking on microtubules. Methods Enzymol 2005, 403:92-107.
    • (2005) Methods Enzymol , vol.403 , pp. 92-107
    • Murray, J.W.1    Wolkoff, A.W.2
  • 180
    • 0021280651 scopus 로고
    • Characterization of uptake of steroid glucuronides into isolated male and female rat hepatocytes
    • Brock WJ, Vore M Characterization of uptake of steroid glucuronides into isolated male and female rat hepatocytes. J Pharmacol Exp Ther 1984, 229:175-181.
    • (1984) J Pharmacol Exp Ther , vol.229 , pp. 175-181
    • Brock, W.J.1    Vore, M.2
  • 183
    • 0021531042 scopus 로고
    • The effect of pregnancy and treatment with 17 beta-estradiol on the transport of organic anions into isolated rat hepatocytes
    • Brock WJ, Vore M The effect of pregnancy and treatment with 17 beta-estradiol on the transport of organic anions into isolated rat hepatocytes. Drug Metab Dispos 1984, 12:713-716.
    • (1984) Drug Metab Dispos , vol.12 , pp. 713-716
    • Brock, W.J.1    Vore, M.2
  • 184
    • 0027515236 scopus 로고
    • +/taurocholate cotransport in isolated hepatocytes from postpartum rats and ovariectomized rats
    • +/taurocholate cotransport in isolated hepatocytes from postpartum rats and ovariectomized rats. J Pharmacol Exp Ther 1993, 267:82-87.
    • (1993) J Pharmacol Exp Ther , vol.267 , pp. 82-87
    • Ganguly, T.1    Hyde, J.F.2    Vore, M.3
  • 187
    • 77951561501 scopus 로고    scopus 로고
    • Nuclear receptor regulation of the adaptive response of bile acid transporters in cholestasis
    • Wagner M, Zollner G, Trauner M Nuclear receptor regulation of the adaptive response of bile acid transporters in cholestasis. Semin Liver Dis 2010, 30:160-177.
    • (2010) Semin Liver Dis , vol.30 , pp. 160-177
    • Wagner, M.1    Zollner, G.2    Trauner, M.3
  • 188
    • 0033980287 scopus 로고    scopus 로고
    • Expression of the bile salt export pump is maintained after chronic cholestasis in the rat
    • Lee JM, Trauner M, Soroka CJ, Stieger B, Meier PJ, Boyer JL Expression of the bile salt export pump is maintained after chronic cholestasis in the rat. Gastroenterology 2000, 118:163-172.
    • (2000) Gastroenterology , vol.118 , pp. 163-172
    • Lee, J.M.1    Trauner, M.2    Soroka, C.J.3    Stieger, B.4    Meier, P.J.5    Boyer, J.L.6
  • 189
    • 0033744558 scopus 로고    scopus 로고
    • Molecular alterations in hepatocyte transport mechanisms in acquired cholestatic liver disorders
    • Lee J, Boyer JL Molecular alterations in hepatocyte transport mechanisms in acquired cholestatic liver disorders. Semin Liver Dis 2000, 20:373-384.
    • (2000) Semin Liver Dis , vol.20 , pp. 373-384
    • Lee, J.1    Boyer, J.L.2
  • 190
    • 0021254056 scopus 로고
    • Hepatic transport of sulfated and nonsulfated bile acids in the rat following relief of bile duct obstruction
    • Cleland DP, Bartholomew TC, Billing BH Hepatic transport of sulfated and nonsulfated bile acids in the rat following relief of bile duct obstruction. Hepatology 1984, 4:477-485.
    • (1984) Hepatology , vol.4 , pp. 477-485
    • Cleland, D.P.1    Bartholomew, T.C.2    Billing, B.H.3
  • 191
    • 0024452479 scopus 로고
    • Extrahepatic obstructive cholestasis reverses the bile salt secretory polarity of rat hepatocytes
    • Fricker G, Landmann L, Meier PJ Extrahepatic obstructive cholestasis reverses the bile salt secretory polarity of rat hepatocytes. J Clin Invest 1989, 84:876-885.
    • (1989) J Clin Invest , vol.84 , pp. 876-885
    • Fricker, G.1    Landmann, L.2    Meier, P.J.3
  • 192
    • 0028943550 scopus 로고
    • Pattern of bile acid regurgitation and metabolism during perfusion of the bile duct obstructed rat liver
    • Baumgartner U, Scholmerich J, Weitzel C, Ihling C, Sellinger M, Lohle E, et al. Pattern of bile acid regurgitation and metabolism during perfusion of the bile duct obstructed rat liver. J Hepatol 1995, 22:208-218.
    • (1995) J Hepatol , vol.22 , pp. 208-218
    • Baumgartner, U.1    Scholmerich, J.2    Weitzel, C.3    Ihling, C.4    Sellinger, M.5    Lohle, E.6
  • 193
    • 34249747403 scopus 로고    scopus 로고
    • Hepatoprotective role of PXR activation and MRP3 in cholic acid-induced cholestasis
    • Teng S, Piquette-Miller M Hepatoprotective role of PXR activation and MRP3 in cholic acid-induced cholestasis. Br J Pharmacol 2007, 151:367-376.
    • (2007) Br J Pharmacol , vol.151 , pp. 367-376
    • Teng, S.1    Piquette-Miller, M.2
  • 194
  • 196
    • 33846706434 scopus 로고    scopus 로고
    • The apical conjugate efflux pump ABCC2 (MRP2)
    • Nies AT, Keppler D The apical conjugate efflux pump ABCC2 (MRP2). Pflugers Arch 2007, 453:643-659.
    • (2007) Pflugers Arch , vol.453 , pp. 643-659
    • Nies, A.T.1    Keppler, D.2
  • 199
    • 0021325788 scopus 로고
    • Biliary transport of glutathione S-conjugate by rat liver canalicular membrane vesicles
    • Inoue M, Akerboom TPM, Sies H, Kinne R, Thao T, Arias IM Biliary transport of glutathione S-conjugate by rat liver canalicular membrane vesicles. J Biol Chem 1984, 259:4998-5002.
    • (1984) J Biol Chem , vol.259 , pp. 4998-5002
    • Inoue, M.1    Akerboom, T.P.M.2    Sies, H.3    Kinne, R.4    Thao, T.5    Arias, I.M.6
  • 200
    • 0025991571 scopus 로고
    • Rat liver canalicular membrane vesicles contain an ATP-dependent bile acid transport system
    • Nishida T, Gatmaitan Z, Che M, Arias IM Rat liver canalicular membrane vesicles contain an ATP-dependent bile acid transport system. Proc Natl Acad Sci USA 1991, 88:6590-6594.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6590-6594
    • Nishida, T.1    Gatmaitan, Z.2    Che, M.3    Arias, I.M.4
  • 201
    • 0026044685 scopus 로고
    • ATP-dependent transport of taurocholate across the hepatocyte canalicular membrane mediated by a 110-kDa glycoprotein binding ATP and bile salt
    • Muller M, Ishikawa T, Berger U, Klunemann C, Lucka L, Schreyer A, et al. ATP-dependent transport of taurocholate across the hepatocyte canalicular membrane mediated by a 110-kDa glycoprotein binding ATP and bile salt. J Biol Chem 1991, 266:18920-18926.
    • (1991) J Biol Chem , vol.266 , pp. 18920-18926
    • Muller, M.1    Ishikawa, T.2    Berger, U.3    Klunemann, C.4    Lucka, L.5    Schreyer, A.6
  • 202
  • 203
    • 0026529394 scopus 로고
    • ATP-dependent bile-salt transport in canalicular rat liver plasma-membrane vesicles
    • Stieger B, O'Neill B, Meier PJ ATP-dependent bile-salt transport in canalicular rat liver plasma-membrane vesicles. Biochem J 1992, 284:67-74.
    • (1992) Biochem J , vol.284 , pp. 67-74
    • Stieger, B.1    O'Neill, B.2    Meier, P.J.3
  • 204
    • 0023735806 scopus 로고
    • Functional reconstitution of the canalicular bile salt transport system of rat liver
    • Ruetz S, Hugentobler G, Meier PJ Functional reconstitution of the canalicular bile salt transport system of rat liver. Proc Natl Acad Sci USA 1988, 85:6147-6151.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6147-6151
    • Ruetz, S.1    Hugentobler, G.2    Meier, P.J.3
  • 205
    • 0027210463 scopus 로고
    • Characterization of the ATP-dependent taurocholate-carrier protein (gp110) of the hepatocyte canalicular membrane
    • Becker A, Lucka L, Kilian C, Kannicht C, Reutter W Characterization of the ATP-dependent taurocholate-carrier protein (gp110) of the hepatocyte canalicular membrane. Eur J Biochem 1993, 214:539-548.
    • (1993) Eur J Biochem , vol.214 , pp. 539-548
    • Becker, A.1    Lucka, L.2    Kilian, C.3    Kannicht, C.4    Reutter, W.5
  • 206
    • 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 1989, 264:14403-14407.
    • (1989) J Biol Chem , vol.264 , pp. 14403-14407
    • Lin, S.H.1
  • 207
    • 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
    • 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. J Biol Chem 1989, 264:14408-14414.
    • (1989) J Biol Chem , vol.264 , pp. 14408-14414
    • Lin, S.H.1    Guidotti, G.2
  • 208
    • 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 1993, 268:2083-2091.
    • (1993) J Biol Chem , vol.268 , pp. 2083-2091
    • Sippel, C.J.1    Suchy, F.J.2    Ananthanarayanan, M.3    Perlmutter, D.H.4
  • 209
    • 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 1994, 269:5179-5186.
    • (1994) J Biol Chem , vol.269 , pp. 5179-5186
    • Kast, C.1    Stieger, B.2    Winterhalter, K.H.3    Meier, P.J.4
  • 210
    • 0030963905 scopus 로고    scopus 로고
    • Evidence for an ATP-dependent bile acid transport protein other than the canalicular liver ecto-ATPase in rats
    • Luther TT, Hammerman P, Rahmaoui CM, Lee PP, Sela-Herman S, Matula GS, et al. Evidence for an ATP-dependent bile acid transport protein other than the canalicular liver ecto-ATPase in rats. Gastroenterology 1997, 113:249-254.
    • (1997) Gastroenterology , vol.113 , pp. 249-254
    • Luther, T.T.1    Hammerman, P.2    Rahmaoui, C.M.3    Lee, P.P.4    Sela-Herman, S.5    Matula, G.S.6
  • 211
    • 0032540277 scopus 로고    scopus 로고
    • The sister of P-glycoprotein represents the canalicular bile salt export pump of mammalian liver
    • Gerloff T, Stieger B, Hagenbuch B, Madon J, Landmann L, Roth J, et al. The sister of P-glycoprotein represents the canalicular bile salt export pump of mammalian liver. J Biol Chem 1998, 273:10046-10050.
    • (1998) J Biol Chem , vol.273 , pp. 10046-10050
    • Gerloff, T.1    Stieger, B.2    Hagenbuch, B.3    Madon, J.4    Landmann, L.5    Roth, J.6
  • 213
    • 77951613087 scopus 로고    scopus 로고
    • The bile salt export pump: clinical and experimental aspects of genetic and acquired cholestatic liver disease
    • Lam P, Soroka CJ, Boyer JL The bile salt export pump: clinical and experimental aspects of genetic and acquired cholestatic liver disease. Semin Liver Dis 2010, 30:125-133.
    • (2010) Semin Liver Dis , vol.30 , pp. 125-133
    • Lam, P.1    Soroka, C.J.2    Boyer, J.L.3
  • 214
    • 0035852720 scopus 로고    scopus 로고
    • Targeted inactivation of sister of P-glycoprotein gene (spgp) in mice results in nonprogressive but persistent intrahepatic cholestasis
    • Wang R, Salem M, Yousef IM, Tuchweber B, Lam P, Childs SJ, et al. Targeted inactivation of sister of P-glycoprotein gene (spgp) in mice results in nonprogressive but persistent intrahepatic cholestasis. Proc Natl Acad Sci USA 2001, 98:2011-2016.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2011-2016
    • Wang, R.1    Salem, M.2    Yousef, I.M.3    Tuchweber, B.4    Lam, P.5    Childs, S.J.6
  • 215
    • 0033984873 scopus 로고    scopus 로고
    • Drug and estrogen-induced cholestasis through inhibition of the hepatocellular bile salt export pump (bsep) of rat liver
    • Stieger B, Fattinger K, Madon J, Kullak-Ublick GA, Meier PJ Drug and estrogen-induced cholestasis through inhibition of the hepatocellular bile salt export pump (bsep) of rat liver. Gastroenterology 2000, 118:422-430.
    • (2000) Gastroenterology , vol.118 , pp. 422-430
    • Stieger, B.1    Fattinger, K.2    Madon, J.3    Kullak-Ublick, G.A.4    Meier, P.J.5
  • 217
    • 22944458539 scopus 로고    scopus 로고
    • Bile salt export pump (BSEP/ABCB11) can transport a nonbile acid substrate, pravastatin
    • Hirano M, Maeda K, Hayashi H, Kusuhara H, Sugiyama Y Bile salt export pump (BSEP/ABCB11) can transport a nonbile acid substrate, pravastatin. J Pharmacol Exp Ther 2005, 314:876-882.
    • (2005) J Pharmacol Exp Ther , vol.314 , pp. 876-882
    • Hirano, M.1    Maeda, K.2    Hayashi, H.3    Kusuhara, H.4    Sugiyama, Y.5
  • 218
  • 219
    • 77951571805 scopus 로고    scopus 로고
    • The spectrum of liver diseases related to ABCB4 gene mutations: pathophysiology and clinical aspects
    • Davit-Spraul A, Gonzales E, Baussan C, Jacquemin E The spectrum of liver diseases related to ABCB4 gene mutations: pathophysiology and clinical aspects. Semin Liver Dis 2010, 30:134-146.
    • (2010) Semin Liver Dis , vol.30 , pp. 134-146
    • Davit-Spraul, A.1    Gonzales, E.2    Baussan, C.3    Jacquemin, E.4
  • 220
    • 77951487115 scopus 로고    scopus 로고
    • ATP8B1 and ABCB11 analysis in 62 children with normal gamma-glutamyl transferase progressive familial intrahepatic cholestasis (PFIC): phenotypic differences between PFIC1 and PFIC2 and natural history
    • Davit-Spraul A, Fabre M, Branchereau S, Baussan C, Gonzales E, Stieger B, et al. ATP8B1 and ABCB11 analysis in 62 children with normal gamma-glutamyl transferase progressive familial intrahepatic cholestasis (PFIC): phenotypic differences between PFIC1 and PFIC2 and natural history. Hepatology 2010, 51:1645-1655.
    • (2010) Hepatology , vol.51 , pp. 1645-1655
    • Davit-Spraul, A.1    Fabre, M.2    Branchereau, S.3    Baussan, C.4    Gonzales, E.5    Stieger, B.6
  • 223
    • 0034798633 scopus 로고    scopus 로고
    • FIC1, the protein affected in two forms of hereditary cholestasis, is localized in the cholangiocyte and the canalicular membrane of the hepatocyte
    • Eppens EF, van Mil SW, de Vree JM, Mok KS, Juijn JA, Oude Elferink RP, et al. FIC1, the protein affected in two forms of hereditary cholestasis, is localized in the cholangiocyte and the canalicular membrane of the hepatocyte. J Hepatol 2001, 35:436-443.
    • (2001) J Hepatol , vol.35 , pp. 436-443
    • Eppens, E.F.1    van Mil, S.W.2    de Vree, J.M.3    Mok, K.S.4    Juijn, J.A.5    Oude Elferink, R.P.6
  • 224
    • 3242812869 scopus 로고    scopus 로고
    • Taurocholate transport by hepatic and intestinal bile acid transporters is independent of FIC1 overexpression in Madin-Darby canine kidney cells
    • Harris MJ, Kagawa T, Dawson PA, Arias IM Taurocholate transport by hepatic and intestinal bile acid transporters is independent of FIC1 overexpression in Madin-Darby canine kidney cells. J Gastroenterol Hepatol 2004, 19:819-825.
    • (2004) J Gastroenterol Hepatol , vol.19 , pp. 819-825
    • Harris, M.J.1    Kagawa, T.2    Dawson, P.A.3    Arias, I.M.4
  • 225
    • 33745906532 scopus 로고    scopus 로고
    • Atp8b1 deficiency in mice reduces resistance of the canalicular membrane to hydrophobic bile salts and impairs bile salt transport
    • Paulusma CC, Groen A, Kunne C, Ho-Mok KS, Spijkerboer AL, Rudi dW, et al. Atp8b1 deficiency in mice reduces resistance of the canalicular membrane to hydrophobic bile salts and impairs bile salt transport. Hepatology 2006, 44:195-204.
    • (2006) Hepatology , vol.44 , pp. 195-204
    • Paulusma, C.C.1    Groen, A.2    Kunne, C.3    Ho-Mok, K.S.4    Spijkerboer, A.L.5    Rudi, D.6
  • 226
    • 60449097716 scopus 로고    scopus 로고
    • ATP8B1 deficiency disrupts the bile canalicular membrane bilayer structure in hepatocytes, but FXR expression and activity are maintained
    • Cai SY, Gautam S, Nguyen T, Soroka CJ, Rahner C, Boyer JL ATP8B1 deficiency disrupts the bile canalicular membrane bilayer structure in hepatocytes, but FXR expression and activity are maintained. Gastroenterology 2009, 136:1060-1069.
    • (2009) Gastroenterology , vol.136 , pp. 1060-1069
    • Cai, S.Y.1    Gautam, S.2    Nguyen, T.3    Soroka, C.J.4    Rahner, C.5    Boyer, J.L.6
  • 228
    • 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 1994, 77:1071-1081.
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 229
    • 34547400136 scopus 로고    scopus 로고
    • Bile salt-dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4
    • Morita SY, Kobayashi A, Takanezawa Y, Kioka N, Handa T, Arai H, et al. Bile salt-dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4. Hepatology 2007, 46:188-199.
    • (2007) Hepatology , vol.46 , pp. 188-199
    • Morita, S.Y.1    Kobayashi, A.2    Takanezawa, Y.3    Kioka, N.4    Handa, T.5    Arai, H.6
  • 230
    • 0035205166 scopus 로고    scopus 로고
    • Role of multidrug resistance 3 deficiency in pediatric and adult liver disease: one gene for three diseases
    • Jacquemin E Role of multidrug resistance 3 deficiency in pediatric and adult liver disease: one gene for three diseases. Semin Liver Dis 2001, 21:551-562.
    • (2001) Semin Liver Dis , vol.21 , pp. 551-562
    • Jacquemin, E.1
  • 231
    • 0027363563 scopus 로고
    • Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease
    • Smit JJ, Schinkel AH, Oude Elferink RP, Groen AK, Wagenaar E, van Deemter L, et al. Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease. Cell 1993, 75:451-462.
    • (1993) Cell , vol.75 , pp. 451-462
    • Smit, J.J.1    Schinkel, A.H.2    Oude Elferink, R.P.3    Groen, A.K.4    Wagenaar, E.5    van Deemter, L.6
  • 232
    • 80054725518 scopus 로고    scopus 로고
    • The hyperbilirubinemias
    • McGraw Hill, New York, A.S. Fauci, E. Braunwald, D.L. Kasper, S.L. Hauser, D.L. Longo, J.L. Jameson, J. Loscalzo (Eds.)
    • Wolkoff AW The hyperbilirubinemias. Harrison's Principles of Internal Medicine 2010, 1927-1931. McGraw Hill, New York. 17th ed. A.S. Fauci, E. Braunwald, D.L. Kasper, S.L. Hauser, D.L. Longo, J.L. Jameson, J. Loscalzo (Eds.).
    • (2010) Harrison's Principles of Internal Medicine , pp. 1927-1931
    • Wolkoff, A.W.1
  • 233
    • 0026490803 scopus 로고
    • Two distinct mechanisms for bilirubin glucuronide transport by rat bile canalicular membrane vesicles. Demonstration of defective ATP-dependent transport in rats (TR-) with inherited conjugated hyperbilirubinemia
    • Nishida T, Gatmaitan Z, Roy-Chowdhry J, Arias IM Two distinct mechanisms for bilirubin glucuronide transport by rat bile canalicular membrane vesicles. Demonstration of defective ATP-dependent transport in rats (TR-) with inherited conjugated hyperbilirubinemia. J Clin Invest 1992, 90:2130-2135.
    • (1992) J Clin Invest , vol.90 , pp. 2130-2135
    • Nishida, T.1    Gatmaitan, Z.2    Roy-Chowdhry, J.3    Arias, I.M.4
  • 234
    • 0025336413 scopus 로고
    • Defective ATP-dependent bile canalicular transport of organic anions in mutant (TR-) rats with conjugated hyperbilirubinemia
    • Kitamura T, Jansen P, Hardenbrook C, Kamimoto Y, Gatmaitan Z, Arias IM Defective ATP-dependent bile canalicular transport of organic anions in mutant (TR-) rats with conjugated hyperbilirubinemia. Proc Natl Acad Sci USA 1990, 87:3557-3561.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3557-3561
    • Kitamura, T.1    Jansen, P.2    Hardenbrook, C.3    Kamimoto, Y.4    Gatmaitan, Z.5    Arias, I.M.6
  • 235
    • 0026516095 scopus 로고
    • ATP-dependent organic anion transport system in normal and TR-rat liver canalicular membranes
    • Nishida T, Hardenbrook C, Gatmaitan Z, Arias IM ATP-dependent organic anion transport system in normal and TR-rat liver canalicular membranes. Am J Physiol 1992, 262:G629-G635.
    • (1992) Am J Physiol , vol.262
    • Nishida, T.1    Hardenbrook, C.2    Gatmaitan, Z.3    Arias, I.M.4
  • 236
    • 0021804301 scopus 로고
    • Hereditary chronic conjugated hyperbilirubinemia in mutant rats caused by defective hepatic anion transport
    • Jansen PL, Peters WH, Lamers WH Hereditary chronic conjugated hyperbilirubinemia in mutant rats caused by defective hepatic anion transport. Hepatology 1985, 5:573-579.
    • (1985) Hepatology , vol.5 , pp. 573-579
    • Jansen, P.L.1    Peters, W.H.2    Lamers, W.H.3
  • 237
    • 0015928906 scopus 로고
    • Inheritance of the Dubin-Johnson syndrome
    • Wolkoff AW, Cohen LE, Arias IM Inheritance of the Dubin-Johnson syndrome. N Engl J Med 1973, 288:113-117.
    • (1973) N Engl J Med , vol.288 , pp. 113-117
    • Wolkoff, A.W.1    Cohen, L.E.2    Arias, I.M.3
  • 238
    • 0029133131 scopus 로고
    • Expression of the MRP gene-encoded conjugate export pump in liver and its selective absence from the canalicular membrane in transport-deficient mutant hepatocytes
    • Mayer R, Kartenbeck J, Buchler M, Jedlitschky G, Leier I, Keppler D Expression of the MRP gene-encoded conjugate export pump in liver and its selective absence from the canalicular membrane in transport-deficient mutant hepatocytes. J Cell Biol 1995, 131:137-150.
    • (1995) J Cell Biol , vol.131 , pp. 137-150
    • Mayer, R.1    Kartenbeck, J.2    Buchler, M.3    Jedlitschky, G.4    Leier, I.5    Keppler, D.6
  • 239
    • 0029986408 scopus 로고    scopus 로고
    • Absence of the canalicular isoform of the MRP gene-encoded conjugate export pump from the hepatocytes in Dubin-Johnson syndrome
    • Kartenbeck J, Leuschner U, Mayer R, Keppler D Absence of the canalicular isoform of the MRP gene-encoded conjugate export pump from the hepatocytes in Dubin-Johnson syndrome. Hepatology 1996, 23:1061-1066.
    • (1996) Hepatology , vol.23 , pp. 1061-1066
    • Kartenbeck, J.1    Leuschner, U.2    Mayer, R.3    Keppler, D.4
  • 241
    • 0031160517 scopus 로고    scopus 로고
    • Hepatic canalicular membrane 5: expression and localization of the conjugate export pump encoded by the MRP2 (cMRP/cMOAT) gene in liver
    • Keppler D, Konig J Hepatic canalicular membrane 5: expression and localization of the conjugate export pump encoded by the MRP2 (cMRP/cMOAT) gene in liver. FASEB J 1997, 11:509-516.
    • (1997) FASEB J , vol.11 , pp. 509-516
    • Keppler, D.1    Konig, J.2
  • 243
    • 0036648878 scopus 로고    scopus 로고
    • Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes
    • Kikuchi S, Hata M, Fukumoto K, Yamane Y, Matsui T, Tamura A, et al. Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Nat Genet 2002, 31:320-325.
    • (2002) Nat Genet , vol.31 , pp. 320-325
    • Kikuchi, S.1    Hata, M.2    Fukumoto, K.3    Yamane, Y.4    Matsui, T.5    Tamura, A.6
  • 244
    • 85047697477 scopus 로고    scopus 로고
    • Structural requirements for the apical sorting of human multidrug resistance protein 2 (ABCC2)
    • Nies AT, Konig J, Cui Y, Brom M, Spring H, Keppler D Structural requirements for the apical sorting of human multidrug resistance protein 2 (ABCC2). Eur J Biochem 2002, 269:1866-1876.
    • (2002) Eur J Biochem , vol.269 , pp. 1866-1876
    • Nies, A.T.1    Konig, J.2    Cui, Y.3    Brom, M.4    Spring, H.5    Keppler, D.6
  • 245
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: structural modules for protein complex assembly
    • Hung AY, Sheng M PDZ domains: structural modules for protein complex assembly. J Biol Chem 2002, 277:5699-5702.
    • (2002) J Biol Chem , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 246
    • 0035831094 scopus 로고    scopus 로고
    • Characterization of bile acid transport mediated by multidrug resistance associated protein 2 and bile salt export pump
    • Akita H, Suzuki H, Ito K, Kinoshita S, Sato N, Takikawa H, et al. Characterization of bile acid transport mediated by multidrug resistance associated protein 2 and bile salt export pump. Biochim Biophys Acta 2001, 1511:7-16.
    • (2001) Biochim Biophys Acta , vol.1511 , pp. 7-16
    • Akita, H.1    Suzuki, H.2    Ito, K.3    Kinoshita, S.4    Sato, N.5    Takikawa, H.6
  • 247
    • 0034723163 scopus 로고    scopus 로고
    • ATP-dependent transport of bile salts by rat multidrug resistance-associated protein 3 (Mrp3)
    • Hirohashi T, Suzuki H, Takikawa H, Sugiyama Y ATP-dependent transport of bile salts by rat multidrug resistance-associated protein 3 (Mrp3). J Biol Chem 2000, 275:2905-2910.
    • (2000) J Biol Chem , vol.275 , pp. 2905-2910
    • Hirohashi, T.1    Suzuki, H.2    Takikawa, H.3    Sugiyama, Y.4
  • 248
    • 0031866357 scopus 로고    scopus 로고
    • Hepatic expression of multidrug resistance-associated protein-like proteins maintained in eisai hyperbilirubinemic rats
    • Hirohashi T, Suzuki H, Ito K, Ogawa K, Kume K, Shimizu T, et al. Hepatic expression of multidrug resistance-associated protein-like proteins maintained in eisai hyperbilirubinemic rats. Mol Pharmacol 1998, 53:1068-1075.
    • (1998) Mol Pharmacol , vol.53 , pp. 1068-1075
    • Hirohashi, T.1    Suzuki, H.2    Ito, K.3    Ogawa, K.4    Kume, K.5    Shimizu, T.6
  • 249
    • 0034802573 scopus 로고    scopus 로고
    • Sinusoidal efflux of taurocholate is enhanced in Mrp2-deficient rat liver
    • Akita H, Suzuki H, Sugiyama Y Sinusoidal efflux of taurocholate is enhanced in Mrp2-deficient rat liver. Pharm Res 2001, 18:1119-1125.
    • (2001) Pharm Res , vol.18 , pp. 1119-1125
    • Akita, H.1    Suzuki, H.2    Sugiyama, Y.3
  • 250
    • 0032926354 scopus 로고    scopus 로고
    • Characterization of the human multidrug resistance protein isoform MRP3 localized to the basolateral hepatocyte membrane
    • Konig J, Rost D, Cui Y, Keppler D Characterization of the human multidrug resistance protein isoform MRP3 localized to the basolateral hepatocyte membrane. Hepatology 1999, 29:1156-1163.
    • (1999) Hepatology , vol.29 , pp. 1156-1163
    • Konig, J.1    Rost, D.2    Cui, Y.3    Keppler, D.4
  • 251
    • 0035080391 scopus 로고    scopus 로고
    • Cellular localization and up-regulation of multidrug resistance-associated protein 3 in hepatocytes and cholangiocytes during obstructive cholestasis in rat liver
    • Soroka CJ, Lee JM, Azzaroli F, Boyer JL Cellular localization and up-regulation of multidrug resistance-associated protein 3 in hepatocytes and cholangiocytes during obstructive cholestasis in rat liver. Hepatology 2001, 33:783-791.
    • (2001) Hepatology , vol.33 , pp. 783-791
    • Soroka, C.J.1    Lee, J.M.2    Azzaroli, F.3    Boyer, J.L.4
  • 252
    • 0034928631 scopus 로고    scopus 로고
    • Up-regulation of basolateral multidrug resistance protein 3 (Mrp3) in cholestatic rat liver
    • Donner MG, Keppler D Up-regulation of basolateral multidrug resistance protein 3 (Mrp3) in cholestatic rat liver. Hepatology 2001, 34:351-359.
    • (2001) Hepatology , vol.34 , pp. 351-359
    • Donner, M.G.1    Keppler, D.2
  • 254
    • 2542471454 scopus 로고    scopus 로고
    • Enhanced expression of basolateral multidrug resistance protein isoforms Mrp3 and Mrp5 in rat liver by LPS
    • Donner MG, Warskulat U, Saha N, Haussinger D Enhanced expression of basolateral multidrug resistance protein isoforms Mrp3 and Mrp5 in rat liver by LPS. Biol Chem 2004, 385:331-339.
    • (2004) Biol Chem , vol.385 , pp. 331-339
    • Donner, M.G.1    Warskulat, U.2    Saha, N.3    Haussinger, D.4
  • 255
    • 1642316825 scopus 로고    scopus 로고
    • Multidrug resistance-associated protein 4 is up-regulated in liver but down-regulated in kidney in obstructive cholestasis in the rat
    • Denk GU, Soroka CJ, Takeyama Y, Chen WS, Schuetz JD, Boyer JL Multidrug resistance-associated protein 4 is up-regulated in liver but down-regulated in kidney in obstructive cholestasis in the rat. J Hepatol 2004, 40:585-591.
    • (2004) J Hepatol , vol.40 , pp. 585-591
    • Denk, G.U.1    Soroka, C.J.2    Takeyama, Y.3    Chen, W.S.4    Schuetz, J.D.5    Boyer, J.L.6
  • 257
    • 0037214404 scopus 로고    scopus 로고
    • Molecular characterization of a multidrug resistance-associated protein, Mrp2, from the little skate
    • Cai SY, Soroka CJ, Ballatori N, Boyer JL Molecular characterization of a multidrug resistance-associated protein, Mrp2, from the little skate. Am J Physiol Regul Integr Comp Physiol 2003, 284:R125-R130.
    • (2003) Am J Physiol Regul Integr Comp Physiol , vol.284
    • Cai, S.Y.1    Soroka, C.J.2    Ballatori, N.3    Boyer, J.L.4
  • 259
    • 0034880339 scopus 로고    scopus 로고
    • Bile salt export pump is highly conserved during vertebrate evolution and its expression is inhibited by PFIC type II mutations
    • Cai SY, Wang L, Ballatori N, Boyer JL Bile salt export pump is highly conserved during vertebrate evolution and its expression is inhibited by PFIC type II mutations. Am J Physiol Gastrointest Liver Physiol 2001, 281:G316-G322.
    • (2001) Am J Physiol Gastrointest Liver Physiol , vol.281
    • Cai, S.Y.1    Wang, L.2    Ballatori, N.3    Boyer, J.L.4
  • 260
    • 0033036103 scopus 로고    scopus 로고
    • Regulation of hepatic transport systems involved in bile secretion during liver regeneration in rats
    • Vos TA, Ros JE, Havinga R, Moshage H, Kuipers F, Jansen PLM, et al. Regulation of hepatic transport systems involved in bile secretion during liver regeneration in rats. Hepatology 1999, 29:1833-1839.
    • (1999) Hepatology , vol.29 , pp. 1833-1839
    • Vos, T.A.1    Ros, J.E.2    Havinga, R.3    Moshage, H.4    Kuipers, F.5    Jansen, P.L.M.6
  • 261
    • 0037313267 scopus 로고    scopus 로고
    • Differential developmental regulation of rat liver canalicular membrane transporters Bsep and Mrp2
    • Tomer G, Ananthanarayanan M, Weymann A, Balasubramanian N, Suchy FJ Differential developmental regulation of rat liver canalicular membrane transporters Bsep and Mrp2. Pediatr Res 2003, 53:288-294.
    • (2003) Pediatr Res , vol.53 , pp. 288-294
    • Tomer, G.1    Ananthanarayanan, M.2    Weymann, A.3    Balasubramanian, N.4    Suchy, F.J.5
  • 264
    • 0029834808 scopus 로고    scopus 로고
    • Development of organic anion transport in the liver
    • Barth A, Fleck C, Klinger W Development of organic anion transport in the liver. Exp Toxic Pathol 1996, 48:421-432.
    • (1996) Exp Toxic Pathol , vol.48 , pp. 421-432
    • Barth, A.1    Fleck, C.2    Klinger, W.3
  • 265
    • 0015856707 scopus 로고
    • Perinatal development of indocyanine green biliary excretion in guinea pigs
    • Hwang SW, Dixon RL Perinatal development of indocyanine green biliary excretion in guinea pigs. Am J Physiol 1973, 225:1454-1459.
    • (1973) Am J Physiol , vol.225 , pp. 1454-1459
    • Hwang, S.W.1    Dixon, R.L.2
  • 266
    • 0031875684 scopus 로고    scopus 로고
    • Hepatobiliary transport: molecular mechanisms of development and cholestasis
    • Arrese M, Ananthananarayanan M, Suchy FJ Hepatobiliary transport: molecular mechanisms of development and cholestasis. Pediatr Res 1998, 44:141-147.
    • (1998) Pediatr Res , vol.44 , pp. 141-147
    • Arrese, M.1    Ananthananarayanan, M.2    Suchy, F.J.3
  • 267
    • 23444456468 scopus 로고    scopus 로고
    • Developmental expression of canalicular transporter genes in human liver
    • Chen HL, Chen HL, Liu YJ, Feng CH, Wu CY, Shyu MK, et al. Developmental expression of canalicular transporter genes in human liver. J Hepatol 2005, 43:472-477.
    • (2005) J Hepatol , vol.43 , pp. 472-477
    • Chen, H.L.1    Chen, H.L.2    Liu, Y.J.3    Feng, C.H.4    Wu, C.Y.5    Shyu, M.K.6
  • 269
    • 0021163325 scopus 로고
    • Conjugation and maximal biliary excretion of bilirubin in the rat during pregnancy and lactation and during estroprogestogen treatment
    • Muraca M, Leyten R, Fevery J Conjugation and maximal biliary excretion of bilirubin in the rat during pregnancy and lactation and during estroprogestogen treatment. Hepatology 1984, 4:633-638.
    • (1984) Hepatology , vol.4 , pp. 633-638
    • Muraca, M.1    Leyten, R.2    Fevery, J.3
  • 270
    • 0022337322 scopus 로고
    • Effects of taurocholate infusion on biliary excretion in isolated perfused rat livers. Decreased biliary excretion of dibromosulfophthalein in pregnancy
    • Durham S, Mack R, Vore M Effects of taurocholate infusion on biliary excretion in isolated perfused rat livers. Decreased biliary excretion of dibromosulfophthalein in pregnancy. Drug Metab Dispos 1985, 13:695-699.
    • (1985) Drug Metab Dispos , vol.13 , pp. 695-699
    • Durham, S.1    Mack, R.2    Vore, M.3
  • 271
    • 0032558588 scopus 로고    scopus 로고
    • Molecular pathogenesis of cholestasis
    • Trauner M, Meier PJ, Boyer JL Molecular pathogenesis of cholestasis. N Engl J Med 1998, 339:1217-1227.
    • (1998) N Engl J Med , vol.339 , pp. 1217-1227
    • Trauner, M.1    Meier, P.J.2    Boyer, J.L.3
  • 272
    • 0029737476 scopus 로고    scopus 로고
    • Effect of endotoxin on bile acid transport in rat liver: a potential model for sepsis-associated cholestasis
    • Moseley RH, Wang W, Takeda H, Lown K, Shick L, Ananthanarayanan M, et al. Effect of endotoxin on bile acid transport in rat liver: a potential model for sepsis-associated cholestasis. Am J Physiol 1996, 271:G137-G146.
    • (1996) Am J Physiol , vol.271
    • Moseley, R.H.1    Wang, W.2    Takeda, H.3    Lown, K.4    Shick, L.5    Ananthanarayanan, M.6
  • 273
    • 0031013566 scopus 로고    scopus 로고
    • Hepatocyte transport of bile acids and organic anions in endotoxemic rats: impaired uptake and secretion
    • Bolder U, Ton-Nu HT, Schteingart CD, Frick E, Hofmann AF Hepatocyte transport of bile acids and organic anions in endotoxemic rats: impaired uptake and secretion. Gastroenterology 1997, 112:214-225.
    • (1997) Gastroenterology , vol.112 , pp. 214-225
    • Bolder, U.1    Ton-Nu, H.T.2    Schteingart, C.D.3    Frick, E.4    Hofmann, A.F.5
  • 275
    • 0031738416 scopus 로고    scopus 로고
    • Up-regulation of the multidrug resistance genes, Mrp1 and Mdr1b, and down-regulation of the organic anion transporter, Mrp2, and the bile salt transporter, Spgp, in endotoxemic rat liver
    • Vos TA, Hooiveld GJ, Koning H, Childs S, Meijer DK, Moshage H, et al. Up-regulation of the multidrug resistance genes, Mrp1 and Mdr1b, and down-regulation of the organic anion transporter, Mrp2, and the bile salt transporter, Spgp, in endotoxemic rat liver. Hepatology 1998, 28:1637-1644.
    • (1998) Hepatology , vol.28 , pp. 1637-1644
    • Vos, T.A.1    Hooiveld, G.J.2    Koning, H.3    Childs, S.4    Meijer, D.K.5    Moshage, H.6
  • 276
    • 0030963906 scopus 로고    scopus 로고
    • The rat canalicular conjugate export pump (Mrp2) is down-regulated in intrahepatic and obstructive cholestasis
    • Trauner M, Arrese M, Soroka CJ, Ananthanarayanan M, Koeppel TA, Schlosser SF, et al. The rat canalicular conjugate export pump (Mrp2) is down-regulated in intrahepatic and obstructive cholestasis. Gastroenterology 1997, 113:255-264.
    • (1997) Gastroenterology , vol.113 , pp. 255-264
    • Trauner, M.1    Arrese, M.2    Soroka, C.J.3    Ananthanarayanan, M.4    Koeppel, T.A.5    Schlosser, S.F.6
  • 277
    • 0033746295 scopus 로고    scopus 로고
    • Intracellular trafficking and regulation of canalicular ATP-binding cassette transporters
    • Kipp H, Arias IM Intracellular trafficking and regulation of canalicular ATP-binding cassette transporters. Semin Liver Dis 2000, 20:339-351.
    • (2000) Semin Liver Dis , vol.20 , pp. 339-351
    • Kipp, H.1    Arias, I.M.2
  • 278
    • 0036196904 scopus 로고    scopus 로고
    • Trafficking of canalicular ABC transporters in hepatocytes
    • Kipp H, Arias IM Trafficking of canalicular ABC transporters in hepatocytes. Annu Rev Physiol 2002, 64:595-608.
    • (2002) Annu Rev Physiol , vol.64 , pp. 595-608
    • Kipp, H.1    Arias, I.M.2
  • 279
    • 33748758162 scopus 로고    scopus 로고
    • Transporters on demand: intracellular reservoirs and cycling of bile canalicular ABC transporters
    • Wakabayashi Y, Kipp H, Arias IM Transporters on demand: intracellular reservoirs and cycling of bile canalicular ABC transporters. J Biol Chem 2006, 281:27669-27673.
    • (2006) J Biol Chem , vol.281 , pp. 27669-27673
    • Wakabayashi, Y.1    Kipp, H.2    Arias, I.M.3
  • 280
    • 0025077050 scopus 로고
    • DBcAMP stimulates vesicle transport and HRP excretion in isolated perfused rat liver
    • Hayakawa T, Bruck R, Ng OC, Boyer JL DBcAMP stimulates vesicle transport and HRP excretion in isolated perfused rat liver. Am J Physiol 1990, 259:G727-G735.
    • (1990) Am J Physiol , vol.259
    • Hayakawa, T.1    Bruck, R.2    Ng, O.C.3    Boyer, J.L.4
  • 281
    • 0025358068 scopus 로고
    • Taurocholate stimulates transcytotic vesicular pathways labeled by horseradish peroxidase in the isolated perfused rat liver
    • Hayakawa T, Ng OC, Ma A, Boyer JL, Cheng O Taurocholate stimulates transcytotic vesicular pathways labeled by horseradish peroxidase in the isolated perfused rat liver. Gastroenterology 1990, 99:216-228.
    • (1990) Gastroenterology , vol.99 , pp. 216-228
    • Hayakawa, T.1    Ng, O.C.2    Ma, A.3    Boyer, J.L.4    Cheng, O.5
  • 282
    • 0030907544 scopus 로고    scopus 로고
    • Regulation and translocation of ATP-dependent apical membrane proteins in rat liver
    • Gatmaitan ZC, Nies AT, Arias IM Regulation and translocation of ATP-dependent apical membrane proteins in rat liver. Am J Physiol 1997, 272:G1041-G1049.
    • (1997) Am J Physiol , vol.272
    • Gatmaitan, Z.C.1    Nies, A.T.2    Arias, I.M.3
  • 283
    • 0032500601 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase in taurocholate-induced trafficking of ATP-dependent canalicular transporters in rat liver
    • Misra S, Gatmaitan Z, Varticovski L, Arias IM The role of phosphoinositide 3-kinase in taurocholate-induced trafficking of ATP-dependent canalicular transporters in rat liver. J Biol Chem 1998, 273:26638-26644.
    • (1998) J Biol Chem , vol.273 , pp. 26638-26644
    • Misra, S.1    Gatmaitan, Z.2    Varticovski, L.3    Arias, I.M.4
  • 284
    • 0035831541 scopus 로고    scopus 로고
    • Transporters on demand: intrahepatic pools of canalicular ATP binding cassette transporters in rat liver
    • Kipp H, Pichetshote N, Arias IM Transporters on demand: intrahepatic pools of canalicular ATP binding cassette transporters in rat liver. J Biol Chem 2001, 276:7218-7224.
    • (2001) J Biol Chem , vol.276 , pp. 7218-7224
    • Kipp, H.1    Pichetshote, N.2    Arias, I.M.3
  • 285
    • 0033620611 scopus 로고    scopus 로고
    • Evidence for apical endocytosis in polarized hepatic cells: phosphoinositide 3-kinase inhibitors lead to the lysosomal accumulation of resident apical plasma membrane proteins
    • Tuma PL, Finnegan CM, Yi JH, Hubbard AL Evidence for apical endocytosis in polarized hepatic cells: phosphoinositide 3-kinase inhibitors lead to the lysosomal accumulation of resident apical plasma membrane proteins. J Cell Biol 1999, 145:1089-1102.
    • (1999) J Cell Biol , vol.145 , pp. 1089-1102
    • Tuma, P.L.1    Finnegan, C.M.2    Yi, J.H.3    Hubbard, A.L.4
  • 286
    • 0032489801 scopus 로고    scopus 로고
    • Apical plasma membrane proteins and endolyn-78 travel through a subapical compartment in polarized WIF-B hepatocytes
    • Ihrke G, Martin GV, Shanks MR, Schrader M, Schroer TA, Hubbard AL Apical plasma membrane proteins and endolyn-78 travel through a subapical compartment in polarized WIF-B hepatocytes. J Cell Biol 1998, 141:115-133.
    • (1998) J Cell Biol , vol.141 , pp. 115-133
    • Ihrke, G.1    Martin, G.V.2    Shanks, M.R.3    Schrader, M.4    Schroer, T.A.5    Hubbard, A.L.6
  • 287
    • 3042720029 scopus 로고    scopus 로고
    • Intracellular trafficking of bile salt export pump (ABCB11) in polarized hepatic cells: constitutive cycling between the canalicular membrane and rab11-positive endosomes
    • Wakabayashi Y, Lippincott-Schwartz J, Arias IM Intracellular trafficking of bile salt export pump (ABCB11) in polarized hepatic cells: constitutive cycling between the canalicular membrane and rab11-positive endosomes. Mol Biol Cell 2004, 15:3485-3496.
    • (2004) Mol Biol Cell , vol.15 , pp. 3485-3496
    • Wakabayashi, Y.1    Lippincott-Schwartz, J.2    Arias, I.M.3
  • 288
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • Schafer DA Coupling actin dynamics and membrane dynamics during endocytosis. Curr Opin Cell Biol 2002, 14:76-81.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 76-81
    • Schafer, D.A.1
  • 289
    • 3543047295 scopus 로고    scopus 로고
    • Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells
    • Ortiz DF, Moseley J, Calderon G, Swift AL, Li S, Arias IM Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells. J Biol Chem 2004, 279:32761-32770.
    • (2004) J Biol Chem , vol.279 , pp. 32761-32770
    • Ortiz, D.F.1    Moseley, J.2    Calderon, G.3    Swift, A.L.4    Li, S.5    Arias, I.M.6
  • 292
    • 0033026760 scopus 로고    scopus 로고
    • Endogenous bile acids are ligands for the nuclear receptor FXR/BAR
    • Wang H, Chen J, Hollister K, Sowers LC, Forman BM Endogenous bile acids are ligands for the nuclear receptor FXR/BAR. Mol Cell 1999, 3:543-553.
    • (1999) Mol Cell , vol.3 , pp. 543-553
    • Wang, H.1    Chen, J.2    Hollister, K.3    Sowers, L.C.4    Forman, B.M.5
  • 294
    • 0035851148 scopus 로고    scopus 로고
    • Orphan nuclear receptors: the exotics of xenobiotics
    • Xie W, Evans RM Orphan nuclear receptors: the exotics of xenobiotics. J Biol Chem 2001, 276:37739-37742.
    • (2001) J Biol Chem , vol.276 , pp. 37739-37742
    • Xie, W.1    Evans, R.M.2
  • 295
    • 0036623233 scopus 로고    scopus 로고
    • Nuclear receptor regulation of hepatic function
    • Karpen SJ Nuclear receptor regulation of hepatic function. J Hepatol 2002, 36:832-850.
    • (2002) J Hepatol , vol.36 , pp. 832-850
    • Karpen, S.J.1
  • 296
    • 0036164154 scopus 로고    scopus 로고
    • BAREing it all. The adoption of lxr and fxr and their roles in lipid homeostasis
    • Edwards PA, Kast HR, Anisfeld AM BAREing it all. The adoption of lxr and fxr and their roles in lipid homeostasis. J Lipid Res 2002, 43:2-12.
    • (2002) J Lipid Res , vol.43 , pp. 2-12
    • Edwards, P.A.1    Kast, H.R.2    Anisfeld, A.M.3
  • 297
    • 0037169551 scopus 로고    scopus 로고
    • Regulation of multidrug resistance-associated protein 2 (ABCC2) by the nuclear receptors pregnane X receptor, farnesoid X-activated receptor, and constitutive androstane receptor
    • Kast HR, Goodwin B, Tarr PT, Jones SA, Anisfeld AM, Stoltz CM, et al. Regulation of multidrug resistance-associated protein 2 (ABCC2) by the nuclear receptors pregnane X receptor, farnesoid X-activated receptor, and constitutive androstane receptor. J Biol Chem 2002, 277:2908-2915.
    • (2002) J Biol Chem , vol.277 , pp. 2908-2915
    • Kast, H.R.1    Goodwin, B.2    Tarr, P.T.3    Jones, S.A.4    Anisfeld, A.M.5    Stoltz, C.M.6
  • 298
    • 0035800772 scopus 로고    scopus 로고
    • Human bile salt export pump promoter is transactivated by the farnesoid X receptor/bile acid receptor
    • Ananthanarayanan M, Balasubramanian N, Makishima M, Mangelsdorf DJ, Suchy FJ Human bile salt export pump promoter is transactivated by the farnesoid X receptor/bile acid receptor. J Biol Chem 2001, 276:28857-28865.
    • (2001) J Biol Chem , vol.276 , pp. 28857-28865
    • Ananthanarayanan, M.1    Balasubramanian, N.2    Makishima, M.3    Mangelsdorf, D.J.4    Suchy, F.J.5
  • 299
    • 0033637121 scopus 로고    scopus 로고
    • A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis
    • Goodwin B, Jones SA, Price RR, Watson MA, McKee DD, Moore LB, et al. A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. Mol Cell 2000, 6:517-526.
    • (2000) Mol Cell , vol.6 , pp. 517-526
    • Goodwin, B.1    Jones, S.A.2    Price, R.R.3    Watson, M.A.4    McKee, D.D.5    Moore, L.B.6
  • 300
    • 0033636789 scopus 로고    scopus 로고
    • Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors
    • Lu TT, Makishima M, Repa JJ, Schoonjans K, Kerr TA, Auwerx J, et al. Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors. Mol Cell 2000, 6:507-515.
    • (2000) Mol Cell , vol.6 , pp. 507-515
    • Lu, T.T.1    Makishima, M.2    Repa, J.J.3    Schoonjans, K.4    Kerr, T.A.5    Auwerx, J.6
  • 301
    • 0035834771 scopus 로고    scopus 로고
    • Transcriptional regulation of the human sterol 12alpha-hydroxylase gene (CYP8B1): roles of hepatocyte nuclear factor 4alpha in mediating bile acid repression
    • Zhang M, Chiang JY Transcriptional regulation of the human sterol 12alpha-hydroxylase gene (CYP8B1): roles of hepatocyte nuclear factor 4alpha in mediating bile acid repression. J Biol Chem 2001, 276:41690-41699.
    • (2001) J Biol Chem , vol.276 , pp. 41690-41699
    • Zhang, M.1    Chiang, J.Y.2
  • 302
    • 0035470833 scopus 로고    scopus 로고
    • Suppression of sterol 12alpha-hydroxylase transcription by the short heterodimer partner: insights into the repression mechanism
    • Castillo-Olivares A, Gil G Suppression of sterol 12alpha-hydroxylase transcription by the short heterodimer partner: insights into the repression mechanism. Nucleic Acids Res 2001, 29:4035-4042.
    • (2001) Nucleic Acids Res , vol.29 , pp. 4035-4042
    • Castillo-Olivares, A.1    Gil, G.2
  • 303
    • 0034950514 scopus 로고    scopus 로고
    • The orphan nuclear receptor, shp, mediates bile acid-induced inhibition of the rat bile acid transporter, ntcp
    • Denson LA, Sturm E, Echevarria W, Zimmerman TL, Makishima M, Mangelsdorf DJ, et al. The orphan nuclear receptor, shp, mediates bile acid-induced inhibition of the rat bile acid transporter, ntcp. Gastroenterology 2001, 121:140-147.
    • (2001) Gastroenterology , vol.121 , pp. 140-147
    • Denson, L.A.1    Sturm, E.2    Echevarria, W.3    Zimmerman, T.L.4    Makishima, M.5    Mangelsdorf, D.J.6
  • 304
    • 0142211282 scopus 로고    scopus 로고
    • Enterohepatic circulation of bile salts in farnesoid X receptor-deficient mice: efficient intestinal bile salt absorption in the absence of ileal bile acid-binding protein
    • Kok T, Hulzebos CV, Wolters H, Havinga R, Agellon LB, Stellaard F, et al. Enterohepatic circulation of bile salts in farnesoid X receptor-deficient mice: efficient intestinal bile salt absorption in the absence of ileal bile acid-binding protein. J Biol Chem 2003, 278:41930-41937.
    • (2003) J Biol Chem , vol.278 , pp. 41930-41937
    • Kok, T.1    Hulzebos, C.V.2    Wolters, H.3    Havinga, R.4    Agellon, L.B.5    Stellaard, F.6
  • 305
    • 0032498303 scopus 로고    scopus 로고
    • An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway
    • Kliewer SA, Moore JT, Wade L, Staudinger JL, Watson MA, Jones SA, et al. An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway. Cell 1998, 92:73-82.
    • (1998) Cell , vol.92 , pp. 73-82
    • Kliewer, S.A.1    Moore, J.T.2    Wade, L.3    Staudinger, J.L.4    Watson, M.A.5    Jones, S.A.6
  • 306
    • 0242665373 scopus 로고    scopus 로고
    • Complementary roles of farnesoid X receptor, pregnane X receptor, and constitutive androstane receptor in protection against bile acid toxicity
    • Guo GL, Lambert G, Negishi M, Ward JM, Brewer HB, Kliewer SA, et al. Complementary roles of farnesoid X receptor, pregnane X receptor, and constitutive androstane receptor in protection against bile acid toxicity. J Biol Chem 2003, 278:45062-45071.
    • (2003) J Biol Chem , vol.278 , pp. 45062-45071
    • Guo, G.L.1    Lambert, G.2    Negishi, M.3    Ward, J.M.4    Brewer, H.B.5    Kliewer, S.A.6
  • 307
    • 65549087088 scopus 로고
    • Metabolism of sulfobromophthalein sodium (BSP) in the rat
    • Krebs JS, Brauer RW Metabolism of sulfobromophthalein sodium (BSP) in the rat. Am J Physiol 1958, I94:37-43.
    • (1958) Am J Physiol , vol.I94 , pp. 37-43
    • Krebs, J.S.1    Brauer, R.W.2
  • 310
    • 84882532469 scopus 로고    scopus 로고
    • The involvement of PXR in hepatic gene regulation during inflammation in mice
    • Teng S, Piquette-Miller M The involvement of PXR in hepatic gene regulation during inflammation in mice. J Pharmacol Exp Ther 2004.
    • (2004) J Pharmacol Exp Ther
    • Teng, S.1    Piquette-Miller, M.2
  • 311
    • 1642454581 scopus 로고    scopus 로고
    • Identification of amino acids in rat pregnane X receptor that determine species-specific activation
    • Tirona RG, Leake BF, Podust LM, Kim RB Identification of amino acids in rat pregnane X receptor that determine species-specific activation. Mol Pharmacol 2004, 65:36-44.
    • (2004) Mol Pharmacol , vol.65 , pp. 36-44
    • Tirona, R.G.1    Leake, B.F.2    Podust, L.M.3    Kim, R.B.4
  • 312
    • 0346690402 scopus 로고    scopus 로고
    • Hepatoprotection by the farnesoid X receptor agonist GW4064 in rat models of intra-and extrahepatic cholestasis
    • Liu Y, Binz J, Numerick MJ, Dennis S, Luo G, Desai B, et al. Hepatoprotection by the farnesoid X receptor agonist GW4064 in rat models of intra-and extrahepatic cholestasis. J Clin Invest 2003, 112:1678-1687.
    • (2003) J Clin Invest , vol.112 , pp. 1678-1687
    • Liu, Y.1    Binz, J.2    Numerick, M.J.3    Dennis, S.4    Luo, G.5    Desai, B.6


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