메뉴 건너뛰기




Volumn 1788, Issue 2, 2009, Pages 402-409

The high turnover Drosophila multidrug resistance-associated protein shares the biochemical features of its human orthologues

Author keywords

ABC transporter; Substrate stimulated substrate inhibited ATPase activity; Substrate specificity; Transport activity

Indexed keywords

17 BETA DEXTRO GLUCURONIDE; ADENOSINE TRIPHOSPHATASE; CALCEIN; CARBOXYDICHLOROFLUORESCEIN; ESTRADIOL; FLUO 3; FLUORESCEIN; GLUCURONIDE; GLUTATHIONE; LEUKOTRIENE C4; MEMBRANE PROTEIN; MULTIDRUG RESISTANCE PROTEIN; MULTIDRUG RESISTANCE PROTEIN 1; MULTIDRUG RESISTANCE PROTEIN 2; MULTIDRUG RESISTANCE PROTEIN 3; MULTIDRUG RESISTANCE PROTEIN 6; MULTIDRUG RESISTANCE PROTEIN 7; N ETHYLMALEIMIDE; PROBENECID; PROTEIN DMRP; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 59249083025     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.11.007     Document Type: Article
Times cited : (19)

References (40)
  • 1
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland I.B., and Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 293 (1999) 381-399
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 2
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: physiology, structure and mechanism-an overview
    • Higgins C.F. ABC transporters: physiology, structure and mechanism-an overview. Res. Microbiol. 152 (2001) 205-210
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 3
    • 25844487733 scopus 로고    scopus 로고
    • Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates
    • Dean M., and Annilo T. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Annu. Rev. Genomics Hum. Genet. 6 (2005) 123-142
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.6 , pp. 123-142
    • Dean, M.1    Annilo, T.2
  • 5
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1 (1982) 945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 7
    • 0031026369 scopus 로고    scopus 로고
    • Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters
    • Tusnady G.E., Bakos E., Varadi A., and Sarkadi B. Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters. FEBS Lett. 402 (1997) 1-3
    • (1997) FEBS Lett. , vol.402 , pp. 1-3
    • Tusnady, G.E.1    Bakos, E.2    Varadi, A.3    Sarkadi, B.4
  • 9
    • 0034917716 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean M., Rzhetsky A., and Allikmets R. The human ATP-binding cassette (ABC) transporter superfamily. Genome Res. 11 (2001) 1156-1166
    • (2001) Genome Res. , vol.11 , pp. 1156-1166
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 10
    • 0032830934 scopus 로고    scopus 로고
    • A novel sulfonylurea receptor family member expressed in the embryonic Drosophila dorsal vessel and tracheal system
    • Nasonkin I., Alikasifoglu A., Ambrose C., Cahill P., Cheng M., Sarniak A., Egan M., and Thomas P.M. A novel sulfonylurea receptor family member expressed in the embryonic Drosophila dorsal vessel and tracheal system. J. Biol. Chem. 274 (1999) 29420-29425
    • (1999) J. Biol. Chem. , vol.274 , pp. 29420-29425
    • Nasonkin, I.1    Alikasifoglu, A.2    Ambrose, C.3    Cahill, P.4    Cheng, M.5    Sarniak, A.6    Egan, M.7    Thomas, P.M.8
  • 11
    • 4644242353 scopus 로고    scopus 로고
    • Conserved mechanisms of glucose sensing and regulation by Drosophila corpora cardiaca cells
    • Kim S.K., and Rulifson E.J. Conserved mechanisms of glucose sensing and regulation by Drosophila corpora cardiaca cells. Nature 431 (2004) 316-320
    • (2004) Nature , vol.431 , pp. 316-320
    • Kim, S.K.1    Rulifson, E.J.2
  • 12
    • 33747065251 scopus 로고    scopus 로고
    • The ATP-sensitive potassium (KATP) channel-encoded dSUR gene is required for Drosophila heart function and is regulated by tinman
    • Akasaka T., Klinedinst S., Ocorr K., Bustamante E.L., Kim S.K., and Bodmer R. The ATP-sensitive potassium (KATP) channel-encoded dSUR gene is required for Drosophila heart function and is regulated by tinman. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 11999-12004
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11999-12004
    • Akasaka, T.1    Klinedinst, S.2    Ocorr, K.3    Bustamante, E.L.4    Kim, S.K.5    Bodmer, R.6
  • 13
    • 5044225809 scopus 로고    scopus 로고
    • The dMRP/CG6214 gene of Drosophila is evolutionarily and functionally related to the human multidrug resistance-associated protein family
    • Tarnay J.N., Szeri F., Ilias A., Annilo T., Sung C., Le Saux O., Varadi A., Dean M., Boyd C.D., and Robinow S. The dMRP/CG6214 gene of Drosophila is evolutionarily and functionally related to the human multidrug resistance-associated protein family. Insect Mol. Biol. 13 (2004) 539-548
    • (2004) Insect Mol. Biol. , vol.13 , pp. 539-548
    • Tarnay, J.N.1    Szeri, F.2    Ilias, A.3    Annilo, T.4    Sung, C.5    Le Saux, O.6    Varadi, A.7    Dean, M.8    Boyd, C.D.9    Robinow, S.10
  • 15
    • 0030863293 scopus 로고    scopus 로고
    • Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus
    • Hipfner D.R., Almquist K.C., Leslie E.M., Gerlach J.H., Grant C.E., Deeley R.G., and Cole S.P. Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus. J. Biol. Chem. 272 (1997) 23623-23630
    • (1997) J. Biol. Chem. , vol.272 , pp. 23623-23630
    • Hipfner, D.R.1    Almquist, K.C.2    Leslie, E.M.3    Gerlach, J.H.4    Grant, C.E.5    Deeley, R.G.6    Cole, S.P.7
  • 16
    • 0030685129 scopus 로고    scopus 로고
    • Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence
    • Kast C., and Gros P. Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence. J. Biol. Chem. 272 (1997) 26479-26487
    • (1997) J. Biol. Chem. , vol.272 , pp. 26479-26487
    • Kast, C.1    Gros, P.2
  • 17
    • 0032562137 scopus 로고    scopus 로고
    • Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein
    • Kast C., and Gros P. Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein. Biochemistry 37 (1998) 2305-2313
    • (1998) Biochemistry , vol.37 , pp. 2305-2313
    • Kast, C.1    Gros, P.2
  • 18
    • 0037468860 scopus 로고    scopus 로고
    • The Drosophila melanogaster multidrug-resistance protein 1 (MRP1) homolog has a novel gene structure containing two variable internal exons
    • Grailles M., Brey P.T., and Roth C.W. The Drosophila melanogaster multidrug-resistance protein 1 (MRP1) homolog has a novel gene structure containing two variable internal exons. Gene 307 (2003) 41-50
    • (2003) Gene , vol.307 , pp. 41-50
    • Grailles, M.1    Brey, P.T.2    Roth, C.W.3
  • 19
    • 0034072174 scopus 로고    scopus 로고
    • Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions
    • Bakos E., Evers R., Sinko E., Varadi A., Borst P., and Sarkadi B. Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions. Mol. Pharmacol. 57 (2000) 760-768
    • (2000) Mol. Pharmacol. , vol.57 , pp. 760-768
    • Bakos, E.1    Evers, R.2    Sinko, E.3    Varadi, A.4    Borst, P.5    Sarkadi, B.6
  • 20
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi B., Price E.M., Boucher R.C., Germann U.A., and Scarborough G.A. Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase. J. Biol. Chem. 267 (1992) 4854-4858
    • (1992) J. Biol. Chem. , vol.267 , pp. 4854-4858
    • Sarkadi, B.1    Price, E.M.2    Boucher, R.C.3    Germann, U.A.4    Scarborough, G.A.5
  • 21
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun A., and Weinstein D. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70 (1976) 241-250
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 23
    • 0345505691 scopus 로고    scopus 로고
    • The role of multidrug transporters in drug availability, metabolism and toxicity
    • Bodo A., Bakos E., Szeri F., Varadi A., and Sarkadi B. The role of multidrug transporters in drug availability, metabolism and toxicity. Toxicol. Lett. 140-141 (2003) 133-143
    • (2003) Toxicol. Lett. , vol.140-141 , pp. 133-143
    • Bodo, A.1    Bakos, E.2    Szeri, F.3    Varadi, A.4    Sarkadi, B.5
  • 24
    • 0037053355 scopus 로고    scopus 로고
    • Loss of ATP-dependent transport activity in pseudoxanthoma elasticum-associated mutants of human ABCC6 (MRP6)
    • Ilias A., Urban Z., Seidl T.L., Le Saux O., Sinko E., Boyd C.D., Sarkadi B., and Varadi A. Loss of ATP-dependent transport activity in pseudoxanthoma elasticum-associated mutants of human ABCC6 (MRP6). J. Biol. Chem. 277 (2002) 16860-16867
    • (2002) J. Biol. Chem. , vol.277 , pp. 16860-16867
    • Ilias, A.1    Urban, Z.2    Seidl, T.L.3    Le Saux, O.4    Sinko, E.5    Boyd, C.D.6    Sarkadi, B.7    Varadi, A.8
  • 25
    • 0035823559 scopus 로고    scopus 로고
    • Transport of cyclic nucleotides and estradiol 17-beta-d-glucuronide by multidrug resistance protein 4. Resistance to 6-mercaptopurine and 6-thioguanine
    • Chen Z.S., Lee K., and Kruh G.D. Transport of cyclic nucleotides and estradiol 17-beta-d-glucuronide by multidrug resistance protein 4. Resistance to 6-mercaptopurine and 6-thioguanine. J. Biol. Chem. 276 (2001) 33747-33754
    • (2001) J. Biol. Chem. , vol.276 , pp. 33747-33754
    • Chen, Z.S.1    Lee, K.2    Kruh, G.D.3
  • 26
    • 0034730755 scopus 로고    scopus 로고
    • The multidrug resistance protein 5 functions as an ATP-dependent export pump for cyclic nucleotides
    • Jedlitschky G., Burchell B., and Keppler D. The multidrug resistance protein 5 functions as an ATP-dependent export pump for cyclic nucleotides. J. Biol. Chem. 275 (2000) 30069-30074
    • (2000) J. Biol. Chem. , vol.275 , pp. 30069-30074
    • Jedlitschky, G.1    Burchell, B.2    Keppler, D.3
  • 27
    • 0030063480 scopus 로고    scopus 로고
    • Transport of glutathione, glucuronate, and sulfate conjugates by the MRP gene-encoded conjugate export pump
    • Jedlitschky G., Leier I., Buchholz U., Barnouin K., Kurz G., and Keppler D. Transport of glutathione, glucuronate, and sulfate conjugates by the MRP gene-encoded conjugate export pump. Cancer Res. 56 (1996) 988-994
    • (1996) Cancer Res. , vol.56 , pp. 988-994
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Barnouin, K.4    Kurz, G.5    Keppler, D.6
  • 28
    • 0029918142 scopus 로고    scopus 로고
    • ATP-dependent 17 beta-estradiol 17-(beta-d-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids
    • Loe D.W., Almquist K.C., Cole S.P., and Deeley R.G. ATP-dependent 17 beta-estradiol 17-(beta-d-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids. J. Biol. Chem. 271 (1996) 9683-9689
    • (1996) J. Biol. Chem. , vol.271 , pp. 9683-9689
    • Loe, D.W.1    Almquist, K.C.2    Cole, S.P.3    Deeley, R.G.4
  • 29
    • 0345299165 scopus 로고    scopus 로고
    • Drug resistance and ATP-dependent conjugate transport mediated by the apical multidrug resistance protein, MRP2, permanently expressed in human and canine cells
    • Cui Y., Konig J., Buchholz J.K., Spring H., Leier I., and Keppler D. Drug resistance and ATP-dependent conjugate transport mediated by the apical multidrug resistance protein, MRP2, permanently expressed in human and canine cells. Mol. Pharmacol. 55 (1999) 929-937
    • (1999) Mol. Pharmacol. , vol.55 , pp. 929-937
    • Cui, Y.1    Konig, J.2    Buchholz, J.K.3    Spring, H.4    Leier, I.5    Keppler, D.6
  • 30
    • 0035824674 scopus 로고    scopus 로고
    • Characterization of drug transport by the human multidrug resistance protein 3 (ABCC3)
    • Zelcer N., Saeki T., Reid G., Beijnen J.H., and Borst P. Characterization of drug transport by the human multidrug resistance protein 3 (ABCC3). J. Biol. Chem. 276 (2001) 46400-46407
    • (2001) J. Biol. Chem. , vol.276 , pp. 46400-46407
    • Zelcer, N.1    Saeki, T.2    Reid, G.3    Beijnen, J.H.4    Borst, P.5
  • 31
    • 0034282991 scopus 로고    scopus 로고
    • Transport of amphipathic anions by human multidrug resistance protein 3
    • Zeng H., Liu G., Rea P.A., and Kruh G.D. Transport of amphipathic anions by human multidrug resistance protein 3. Cancer Res. 60 (2000) 4779-4784
    • (2000) Cancer Res. , vol.60 , pp. 4779-4784
    • Zeng, H.1    Liu, G.2    Rea, P.A.3    Kruh, G.D.4
  • 32
    • 0037311274 scopus 로고    scopus 로고
    • Characterization of the transport properties of human multidrug resistance protein 7 (MRP7, ABCC10)
    • Chen Z.S., Hopper-Borge E., Belinsky M.G., Shchaveleva I., Kotova E., and Kruh G.D. Characterization of the transport properties of human multidrug resistance protein 7 (MRP7, ABCC10). Mol. Pharmacol. 63 (2003) 351-358
    • (2003) Mol. Pharmacol. , vol.63 , pp. 351-358
    • Chen, Z.S.1    Hopper-Borge, E.2    Belinsky, M.G.3    Shchaveleva, I.4    Kotova, E.5    Kruh, G.D.6
  • 33
    • 0036829109 scopus 로고    scopus 로고
    • Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6)
    • Belinsky M.G., Chen Z.S., Shchaveleva I., Zeng H., and Kruh G.D. Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6). Cancer Res. 62 (2002) 6172-6177
    • (2002) Cancer Res. , vol.62 , pp. 6172-6177
    • Belinsky, M.G.1    Chen, Z.S.2    Shchaveleva, I.3    Zeng, H.4    Kruh, G.D.5
  • 34
    • 0037963557 scopus 로고    scopus 로고
    • Differential modulation of the human liver conjugate transporters MRP2 and MRP3 by bile acids and organic anions
    • Bodo A., Bakos E., Szeri F., Varadi A., and Sarkadi B. Differential modulation of the human liver conjugate transporters MRP2 and MRP3 by bile acids and organic anions. J. Biol. Chem. 278 (2003) 23529-23537
    • (2003) J. Biol. Chem. , vol.278 , pp. 23529-23537
    • Bodo, A.1    Bakos, E.2    Szeri, F.3    Varadi, A.4    Sarkadi, B.5
  • 35
    • 0027984511 scopus 로고
    • The MRP gene encodes an ATP-dependent export pump for leukotriene C4 and structurally related conjugates
    • Leier I., Jedlitschky G., Buchholz U., Cole S.P., Deeley R.G., and Keppler D. The MRP gene encodes an ATP-dependent export pump for leukotriene C4 and structurally related conjugates. J. Biol. Chem. 269 (1994) 27807-27810
    • (1994) J. Biol. Chem. , vol.269 , pp. 27807-27810
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Cole, S.P.4    Deeley, R.G.5    Keppler, D.6
  • 36
    • 0029074372 scopus 로고
    • ATP-dependent efflux of calcein by the multidrug resistance protein (MRP): no inhibition by intracellular glutathione depletion
    • Feller N., Broxterman H.J., Wahrer D.C., and Pinedo H.M. ATP-dependent efflux of calcein by the multidrug resistance protein (MRP): no inhibition by intracellular glutathione depletion. FEBS Lett. 368 (1995) 385-388
    • (1995) FEBS Lett. , vol.368 , pp. 385-388
    • Feller, N.1    Broxterman, H.J.2    Wahrer, D.C.3    Pinedo, H.M.4
  • 37
    • 0032855145 scopus 로고    scopus 로고
    • Export pumps for anionic conjugates encoded by MRP genes
    • Keppler D., Cui Y., Konig J., Leier I., and Nies A. Export pumps for anionic conjugates encoded by MRP genes. Adv. Enzyme Regul. 39 (1999) 237-246
    • (1999) Adv. Enzyme Regul. , vol.39 , pp. 237-246
    • Keppler, D.1    Cui, Y.2    Konig, J.3    Leier, I.4    Nies, A.5
  • 38
    • 34047197024 scopus 로고    scopus 로고
    • Expression of c-kit and Sca-1 and their relationship with multidrug resistance protein 1 in mouse bone marrow mononuclear cells
    • Kyle-Cezar F., dos Santos E.-L.J., Goldenberg R.C., and Rumjanek V.M. Expression of c-kit and Sca-1 and their relationship with multidrug resistance protein 1 in mouse bone marrow mononuclear cells. Immunology 121 (2007) 122-128
    • (2007) Immunology , vol.121 , pp. 122-128
    • Kyle-Cezar, F.1    dos Santos, E.-L.J.2    Goldenberg, R.C.3    Rumjanek, V.M.4
  • 39
    • 0031758818 scopus 로고    scopus 로고
    • Expression of the apical conjugate export pump, Mrp2, in the polarized hepatoma cell line, WIF-B
    • Nies A.T., Cantz T., Brom M., Leier I., and Keppler D. Expression of the apical conjugate export pump, Mrp2, in the polarized hepatoma cell line, WIF-B. Hepatology 28 (1998) 1332-1340
    • (1998) Hepatology , vol.28 , pp. 1332-1340
    • Nies, A.T.1    Cantz, T.2    Brom, M.3    Leier, I.4    Keppler, D.5
  • 40
    • 33644847437 scopus 로고    scopus 로고
    • Kinetic validation of the use of carboxydichlorofluorescein as a drug surrogate for MRP5-mediated transport
    • Pratt S., Chen V., Perry III W.I., Starling J.J., and Dantzig A.H. Kinetic validation of the use of carboxydichlorofluorescein as a drug surrogate for MRP5-mediated transport. Eur. J. Pharm. Sci. 27 (2006) 524-532
    • (2006) Eur. J. Pharm. Sci. , vol.27 , pp. 524-532
    • Pratt, S.1    Chen, V.2    Perry III, W.I.3    Starling, J.J.4    Dantzig, A.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.