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Volumn 90, Issue 4, 2008, Pages 322-332

Cloning and molecular characterization of apical efflux transporters (ABCB1, ABCB11 and ABCC2) in rainbow trout (Oncorhynchus mykiss) hepatocytes

Author keywords

ABC genes; Real time RT PCR; Trout hepatocytes

Indexed keywords

ABC TRANSPORTER; CALCEIN; CYCLOSPORIN A; MESSENGER RNA; MULTIDRUG RESISTANCE PROTEIN 1; RHODAMINE 123; TAUROCHENODEOXYCHOLIC ACID; TAUROCHOLIC ACID; VERAPAMIL; VERLUKAST; XENOBIOTIC AGENT;

EID: 56349129656     PISSN: 0166445X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.aquatox.2008.09.012     Document Type: Article
Times cited : (65)

References (46)
  • 1
    • 0036346357 scopus 로고    scopus 로고
    • Structural polarity and functional bile canaliculi in rat hepatocyte spheroids
    • Abu-Absi S.F., Friend J.R., Hansen L.K., and Hu W.S. Structural polarity and functional bile canaliculi in rat hepatocyte spheroids. Exp. Cell Res. 274 (2002) 56-67
    • (2002) Exp. Cell Res. , vol.274 , pp. 56-67
    • Abu-Absi, S.F.1    Friend, J.R.2    Hansen, L.K.3    Hu, W.S.4
  • 3
    • 0034001136 scopus 로고    scopus 로고
    • Multixenobiotic resistance as a cellular defense mechanism in aquatic organisms
    • Bard S.M. Multixenobiotic resistance as a cellular defense mechanism in aquatic organisms. Aquat. Toxicol. 48 (2000) 357-389
    • (2000) Aquat. Toxicol. , vol.48 , pp. 357-389
    • Bard, S.M.1
  • 4
    • 85163513522 scopus 로고    scopus 로고
    • Solving the problem of multidrug resistance: ABC transporters in clinical oncology
    • Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds), Academic Press, San Diego
    • Bates S.E. Solving the problem of multidrug resistance: ABC transporters in clinical oncology. In: Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds). ABC Proteins from Bacteria to Man (2003), Academic Press, San Diego 359-392
    • (2003) ABC Proteins from Bacteria to Man , pp. 359-392
    • Bates, S.E.1
  • 6
    • 0029022589 scopus 로고
    • Identification of a sister gene to P-glycoprotein
    • Childs S., Yeh R.L., Georges E., and Ling V. Identification of a sister gene to P-glycoprotein. Cancer Res. 55 (1995) 2029-2034
    • (1995) Cancer Res. , vol.55 , pp. 2029-2034
    • Childs, S.1    Yeh, R.L.2    Georges, E.3    Ling, V.4
  • 7
    • 0032942682 scopus 로고    scopus 로고
    • Altered expression of the xenobiotic transporter P-glycoprotein in liver and liver tumors of mummichog (Fundulus heteroclitus) from a creosote-contaminated environment
    • Cooper P.S., Vogelbein W.K., and Van Veld P.A. Altered expression of the xenobiotic transporter P-glycoprotein in liver and liver tumors of mummichog (Fundulus heteroclitus) from a creosote-contaminated environment. Biomarkers 4 (1999) 48-58
    • (1999) Biomarkers , vol.4 , pp. 48-58
    • Cooper, P.S.1    Vogelbein, W.K.2    Van Veld, P.A.3
  • 8
    • 0001463656 scopus 로고
    • Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150- to 170-kDa protein detected by photoaffinity labeling
    • Cornwell M.M., Safa A.R., Felsted R.L., Gottesman M.M., and Pastan I. Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150- to 170-kDa protein detected by photoaffinity labeling. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 3847-3850
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 3847-3850
    • Cornwell, M.M.1    Safa, A.R.2    Felsted, R.L.3    Gottesman, M.M.4    Pastan, I.5
  • 9
    • 0036233126 scopus 로고    scopus 로고
    • The fluorescent probe bodipy-verapamil is a substrate for both P-glycoprotein and multidrug resistance-related protein (MRP)-1
    • Crivellato E., Candussio L., Rosati A.M., Bartoli-Klugmann F., Mallardi F., and Decorti G. The fluorescent probe bodipy-verapamil is a substrate for both P-glycoprotein and multidrug resistance-related protein (MRP)-1. J. Histochem. Cytochem. 50 (2002) 731-734
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 731-734
    • Crivellato, E.1    Candussio, L.2    Rosati, A.M.3    Bartoli-Klugmann, F.4    Mallardi, F.5    Decorti, G.6
  • 10
    • 0034687719 scopus 로고    scopus 로고
    • Rhodamine 123 binds to multiple sites in the multidrug resistance protein (MRP1)
    • Daoud R., Kast C., Gros P., and Georges E. Rhodamine 123 binds to multiple sites in the multidrug resistance protein (MRP1). Biochemistry 39 (2000) 15344-15352
    • (2000) Biochemistry , vol.39 , pp. 15344-15352
    • Daoud, R.1    Kast, C.2    Gros, P.3    Georges, E.4
  • 11
    • 0034928631 scopus 로고    scopus 로고
    • Up-regulation of basolateral multidrug resistance protein 3 (Mrp3) in cholestatic rat liver
    • Donner M.G., and Keppler D. Up-regulation of basolateral multidrug resistance protein 3 (Mrp3) in cholestatic rat liver. Hepatology 34 (2001) 351-359
    • (2001) Hepatology , vol.34 , pp. 351-359
    • Donner, M.G.1    Keppler, D.2
  • 12
    • 56349126609 scopus 로고    scopus 로고
    • Use of multidrug transporters as first line of defense against toxins in aquatic organisms
    • Epel D. Use of multidrug transporters as first line of defense against toxins in aquatic organisms. Comp. Biochem. Physiol. A-Mol. Integr. Physiol. 134 (2003) 233-246
    • (2003) Comp. Biochem. Physiol. A-Mol. Integr. Physiol. , vol.134 , pp. 233-246
    • Epel, D.1
  • 13
    • 0343306779 scopus 로고    scopus 로고
    • Kinetic analysis of calcein and calcein-acetoxymethylester efflux mediated by multidrug resistance protein and P-glycoprotein
    • Essodaïgui M., Broxterman H.J., and Garnier-Suillerot A. Kinetic analysis of calcein and calcein-acetoxymethylester efflux mediated by multidrug resistance protein and P-glycoprotein. Biochemistry 37 (1998) 2243-2250
    • (1998) Biochemistry , vol.37 , pp. 2243-2250
    • Essodaïgui, M.1    Broxterman, H.J.2    Garnier-Suillerot, A.3
  • 16
    • 0029954843 scopus 로고    scopus 로고
    • P-glycoprotein-a mediator of multidrug resistance in tumour cells
    • Germann U.A. P-glycoprotein-a mediator of multidrug resistance in tumour cells. Eur. J. Cancer 32A (1996) 927-944
    • (1996) Eur. J. Cancer , vol.32 A , pp. 927-944
    • Germann, U.A.1
  • 17
    • 0029958849 scopus 로고    scopus 로고
    • Transport properties of multidrug resistance-associated protein (MRP) in human tumour cells
    • Holló Z., Homolya L., Hegedüs T., and Sarkadi B. Transport properties of multidrug resistance-associated protein (MRP) in human tumour cells. FEBS Lett. 383 (1996) 99-104
    • (1996) FEBS Lett. , vol.383 , pp. 99-104
    • Holló, Z.1    Homolya, L.2    Hegedüs, T.3    Sarkadi, B.4
  • 18
    • 0025964988 scopus 로고
    • Interaction of organic chemicals with P-glycoprotein in adrenal gland, kidney, and multidrug-resistant KB cell
    • Ichikawa M., Yoshimura A., Sumizawa T., Shudo N., Kuwazuru Y., Furukawa T., and Akiyama S. Interaction of organic chemicals with P-glycoprotein in adrenal gland, kidney, and multidrug-resistant KB cell. J. Biol. Chem. 266 (1991) 903-908
    • (1991) J. Biol. Chem. , vol.266 , pp. 903-908
    • Ichikawa, M.1    Yoshimura, A.2    Sumizawa, T.3    Shudo, N.4    Kuwazuru, Y.5    Furukawa, T.6    Akiyama, S.7
  • 19
    • 15844369734 scopus 로고    scopus 로고
    • Substrates and inhibitors of efflux proteins interfere with the MTT assay in cells and may lead to underestimation of drug toxicity
    • Kati-Sisko V., Honkakoski P., and Urtti A. Substrates and inhibitors of efflux proteins interfere with the MTT assay in cells and may lead to underestimation of drug toxicity. Eur. J. Pharmacol. Sci. 23 (2004) 181-188
    • (2004) Eur. J. Pharmacol. Sci. , vol.23 , pp. 181-188
    • Kati-Sisko, V.1    Honkakoski, P.2    Urtti, A.3
  • 20
    • 0345724724 scopus 로고    scopus 로고
    • The MRP family of drug efflux pumps
    • Kruh G.D., and Belinsky M.G. The MRP family of drug efflux pumps. Oncogene 22 (2003) 7537-7552
    • (2003) Oncogene , vol.22 , pp. 7537-7552
    • Kruh, G.D.1    Belinsky, M.G.2
  • 21
    • 0026728777 scopus 로고
    • The multixenobiotic resistance mechanisms in aquatic organisms
    • Kurelec B. The multixenobiotic resistance mechanisms in aquatic organisms. Crit. Rev. Toxicol. 22 (1992) 23-43
    • (1992) Crit. Rev. Toxicol. , vol.22 , pp. 23-43
    • Kurelec, B.1
  • 24
    • 0035813012 scopus 로고    scopus 로고
    • Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters
    • Leslie E.M., Deeley R.G., and Cole S.P.C. Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters. Toxicology 167 (2001) 3-23
    • (2001) Toxicology , vol.167 , pp. 3-23
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 25
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense
    • Leslie E.M., Deeley R.G., and Cole S.P.C. Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense. Toxicol. Appl. Pharmacol. 204 (2005) 216-237
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 26
    • 0034947674 scopus 로고    scopus 로고
    • From MDR to MXR: new understanding of multidrug resistance systems, their properties and clinical significance
    • Litman T., Druley T.E., Stein W.D., and Bates S.E. From MDR to MXR: new understanding of multidrug resistance systems, their properties and clinical significance. Cell. Mol. Life Sci. 58 (2001) 931-959
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 931-959
    • Litman, T.1    Druley, T.E.2    Stein, W.D.3    Bates, S.E.4
  • 27
    • 0031851557 scopus 로고    scopus 로고
    • The fate of organic xenobiotics in aquatic ecosystems: quantitative and qualitative differences in biotransformation by invertebrates and fish
    • Livingstone D.R. The fate of organic xenobiotics in aquatic ecosystems: quantitative and qualitative differences in biotransformation by invertebrates and fish. Comp. Biochem. Physiol. Part A 120 (1998) 43-49
    • (1998) Comp. Biochem. Physiol. Part A , vol.120 , pp. 43-49
    • Livingstone, D.R.1
  • 29
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 30
    • 0028284288 scopus 로고
    • Characterization of rhodamine 123 binding to P-glycoprotein in human multidrug-resistant cells
    • Nare B., Prichard R.K., and Georges E. Characterization of rhodamine 123 binding to P-glycoprotein in human multidrug-resistant cells. Mol. Pharmacol. 45 (1994) 1145-1152
    • (1994) Mol. Pharmacol. , vol.45 , pp. 1145-1152
    • Nare, B.1    Prichard, R.K.2    Georges, E.3
  • 31
    • 0036828271 scopus 로고    scopus 로고
    • Functional expression of the canalicular bile salt export pump of human liver
    • Noé J., Stieger B., and Meier P.J. Functional expression of the canalicular bile salt export pump of human liver. Gastroenterology 123 (2002) 1659-1666
    • (2002) Gastroenterology , vol.123 , pp. 1659-1666
    • Noé, J.1    Stieger, B.2    Meier, P.J.3
  • 32
    • 0023122543 scopus 로고
    • Tracing of xenobiotic contamination in water with the aid of fish bile metabolites: a filed study with caged rainbow trout (Salmo gairdneri)
    • Oikari A., and Kunnamo-Ojala T. Tracing of xenobiotic contamination in water with the aid of fish bile metabolites: a filed study with caged rainbow trout (Salmo gairdneri). Aquat. Toxicol. 9 (1987) 327-341
    • (1987) Aquat. Toxicol. , vol.9 , pp. 327-341
    • Oikari, A.1    Kunnamo-Ojala, T.2
  • 33
    • 0032101217 scopus 로고    scopus 로고
    • An assessment of Ah-inducible phase I and phase II enzymatic activities and oxidative stress indices in adult lake trout (Salvelinus namaycush) from Lake Ontario and Lake Superior
    • Palace V.P., Baron C.L., and Klaverkamp J.F. An assessment of Ah-inducible phase I and phase II enzymatic activities and oxidative stress indices in adult lake trout (Salvelinus namaycush) from Lake Ontario and Lake Superior. Aquat. Toxicol. 42 (1998) 149-168
    • (1998) Aquat. Toxicol. , vol.42 , pp. 149-168
    • Palace, V.P.1    Baron, C.L.2    Klaverkamp, J.F.3
  • 34
    • 0035896509 scopus 로고    scopus 로고
    • Role of the multidrug resistance protein 1 (MRP1) and glutathione S-transferase A1-1 in alkylating agent resistance: kinetics of glutathione conjugate formation and efflux govern differential cellular sensitivity to chlorambucil versus melphalan toxicity
    • Paumi C.M., Ledford B.G., Smitherman P.K., Towensend A.J., and Morrow C.S. Role of the multidrug resistance protein 1 (MRP1) and glutathione S-transferase A1-1 in alkylating agent resistance: kinetics of glutathione conjugate formation and efflux govern differential cellular sensitivity to chlorambucil versus melphalan toxicity. J. Biol. Chem. 276 (2001) 7952-7956
    • (2001) J. Biol. Chem. , vol.276 , pp. 7952-7956
    • Paumi, C.M.1    Ledford, B.G.2    Smitherman, P.K.3    Towensend, A.J.4    Morrow, C.S.5
  • 36
    • 0035011828 scopus 로고    scopus 로고
    • Regulation of cytochrome P450 in a primary culture of rainbow trout hepatocytes
    • Sadar M.D., and Andersson T.B. Regulation of cytochrome P450 in a primary culture of rainbow trout hepatocytes. In Vitro Cell. Dev. Biol.-Anim. 37 (2001) 180-184
    • (2001) In Vitro Cell. Dev. Biol.-Anim. , vol.37 , pp. 180-184
    • Sadar, M.D.1    Andersson, T.B.2
  • 37
    • 0042823385 scopus 로고    scopus 로고
    • Kinetic analysis of rhodamines efflux mediated by multidrug resistance proteins (MRP1)
    • Saengkhae C., Loetchutinat C., and Garnier-Suillerot A. Kinetic analysis of rhodamines efflux mediated by multidrug resistance proteins (MRP1). Biophys. J. 85 (2003) 2006-2014
    • (2003) Biophys. J. , vol.85 , pp. 2006-2014
    • Saengkhae, C.1    Loetchutinat, C.2    Garnier-Suillerot, A.3
  • 38
    • 2942541571 scopus 로고    scopus 로고
    • Identification of the multidrug resistance-associated protein (MRP) related gene in red mullet (Mullus barbatus)
    • Sauerborn R., Stupin-Polanec D., Zaja R., and Smital T. Identification of the multidrug resistance-associated protein (MRP) related gene in red mullet (Mullus barbatus). Mar. Environ. Res. 58 (2004) 199-204
    • (2004) Mar. Environ. Res. , vol.58 , pp. 199-204
    • Sauerborn, R.1    Stupin-Polanec, D.2    Zaja, R.3    Smital, T.4
  • 39
    • 0017101039 scopus 로고
    • Preparation of isolated rat liver cells
    • Segelen P.O. Preparation of isolated rat liver cells. Methods Cell. Biol. 13 (1976) 29-83
    • (1976) Methods Cell. Biol. , vol.13 , pp. 29-83
    • Segelen, P.O.1
  • 40
    • 0033567425 scopus 로고    scopus 로고
    • Interaction of the P-glycoprotein multidrug transporter (MDR1) with high affinity peptide chemosensitizers in isolated membranes, reconstituted systems, and intact cells
    • Sharom F.J., Yu X., Lu P., Liu R., Chu J.W.K., Szabó K., Müller M., Hose C.D., Monks A., Váradi A., Seprôdi J., and Sarkadi B. Interaction of the P-glycoprotein multidrug transporter (MDR1) with high affinity peptide chemosensitizers in isolated membranes, reconstituted systems, and intact cells. Biochem. Pharmacol. 58 (1999) 571-586
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 571-586
    • Sharom, F.J.1    Yu, X.2    Lu, P.3    Liu, R.4    Chu, J.W.K.5    Szabó, K.6    Müller, M.7    Hose, C.D.8    Monks, A.9    Váradi, A.10    Seprôdi, J.11    Sarkadi, B.12
  • 41
    • 0035427646 scopus 로고    scopus 로고
    • Prochloraz and nonylphenol diethoxylate inhibit an mdr1-like activity in vitro, but do not alter hepatic levels of P-glycoprotein in trout exposed in vivo
    • Sturm A., Cravedi J.P., and Segner H. Prochloraz and nonylphenol diethoxylate inhibit an mdr1-like activity in vitro, but do not alter hepatic levels of P-glycoprotein in trout exposed in vivo. Aquat. Toxicol. 53 (2001) 215-228
    • (2001) Aquat. Toxicol. , vol.53 , pp. 215-228
    • Sturm, A.1    Cravedi, J.P.2    Segner, H.3
  • 43
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 44
    • 0037379362 scopus 로고    scopus 로고
    • Bile salt transporters: molecular characterization, function, and regulation
    • Trauner M., and Boyer J.L. Bile salt transporters: molecular characterization, function, and regulation. Physiol. Rev. 83 (2003) 663-671
    • (2003) Physiol. Rev. , vol.83 , pp. 663-671
    • Trauner, M.1    Boyer, J.L.2
  • 45
    • 0035988699 scopus 로고    scopus 로고
    • Genetic and immunological characterisation of multixenobiotic resistance system in the turbot (Scophthalamus maximus)
    • Tutundjian R., Cachot J., Leboulenger F., and Minier C. Genetic and immunological characterisation of multixenobiotic resistance system in the turbot (Scophthalamus maximus). Comp. Biochem. Physiol. B 132 (2002) 463-471
    • (2002) Comp. Biochem. Physiol. B , vol.132 , pp. 463-471
    • Tutundjian, R.1    Cachot, J.2    Leboulenger, F.3    Minier, C.4
  • 46
    • 0037391057 scopus 로고    scopus 로고
    • Fluorescent substrates of sister-P-glycoprotein (BSEP) evaluated as markers of active transport and inhibition: evidence for contingent unequal binding sites
    • Wang E.J., Casciano C.N., Clement R.P., and Johnson W.W. Fluorescent substrates of sister-P-glycoprotein (BSEP) evaluated as markers of active transport and inhibition: evidence for contingent unequal binding sites. Pharmacol. Res. 20 (2003) 537-544
    • (2003) Pharmacol. Res. , vol.20 , pp. 537-544
    • Wang, E.J.1    Casciano, C.N.2    Clement, R.P.3    Johnson, W.W.4


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