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Volumn 273, Issue 3, 2000, Pages 913-919

Expression and characterization of the N- and C-terminal ATP-binding domains of MRP1

Author keywords

ABC transporters; ATP binding; ATPase activity; Multidrug resistance; Nucleotide binding domains

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MALTOSE BINDING PROTEIN; MULTIDRUG RESISTANCE PROTEIN; N ETHYLMALEIMIDE;

EID: 0343090423     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3040     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman M. M., Pastan I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem. 62:1993;385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 4
    • 0028001416 scopus 로고
    • ATP-dependent transport of glutathione S-conjugates by the multidrug resistance-associated protein
    • Jedlitschky G., Leier I., Buchholz U., Center M., Keppler D. ATP-dependent transport of glutathione S-conjugates by the multidrug resistance-associated protein. Cancer Res. 54:1994;4833-4836.
    • (1994) Cancer Res. , vol.54 , pp. 4833-4836
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Center, M.4    Keppler, D.5
  • 5
    • 0029958849 scopus 로고    scopus 로고
    • Transport properties of the multidrug resistance-associated protein
    • Holló Z., Homolya L., Hegedûs T., Sarkadi B. Transport properties of the multidrug resistance-associated protein. FEBS Lett. 383:1996;99-104.
    • (1996) FEBS Lett. , vol.383 , pp. 99-104
    • Holló, Z.1    Homolya, L.2    Hegedûs, T.3    Sarkadi, B.4
  • 6
    • 0033616684 scopus 로고    scopus 로고
    • Choroid plexus epithelial expression of MDR1 P glycoprotein and multidrug resistance-associated protein contribute to the blood-cerebrospinal-fluid drug-permeability barrier
    • Rao V. V., Dahlheimer J. L., Bardgett M. E., Snyder A. Z., Finch R. A., Sartorelli A. C., Piwnica-Worms D. Choroid plexus epithelial expression of MDR1 P glycoprotein and multidrug resistance-associated protein contribute to the blood-cerebrospinal-fluid drug-permeability barrier. Proc. Natl. Acad. Sci. USA. 96:1999;3900-3905.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3900-3905
    • Rao, V.V.1    Dahlheimer, J.L.2    Bardgett, M.E.3    Snyder, A.Z.4    Finch, R.A.5    Sartorelli, A.C.6    Piwnica-Worms, D.7
  • 7
    • 0032494133 scopus 로고    scopus 로고
    • Multidrug resistance protein 1 protects the oropharyngeal mucosal layer and the testicular tubules against drug-induced damage
    • Wijnholds J., Scheffer G. L., van der Valk M., van der Valk P., Beijnen J. H., Scheper R. J., Borst P. Multidrug resistance protein 1 protects the oropharyngeal mucosal layer and the testicular tubules against drug-induced damage. J. Exp. Med. 188:1998;797-808.
    • (1998) J. Exp. Med. , vol.188 , pp. 797-808
    • Wijnholds, J.1    Scheffer, G.L.2    Van Der Valk, M.3    Van Der Valk, P.4    Beijnen, J.H.5    Scheper, R.J.6    Borst, P.7
  • 10
    • 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., 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
  • 11
    • 0028059144 scopus 로고
    • Overexpression and purification of the carboxyl-terminal nucleotid binding domain from mouse P-glycoprotein
    • Baubichon-Cortay H., Bagetto L. G., Dayan G., Di Pietro A. Overexpression and purification of the carboxyl-terminal nucleotid binding domain from mouse P-glycoprotein. J. Biol. Chem. 269:1994;22983-22989.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22983-22989
    • Baubichon-Cortay, H.1    Bagetto, L.G.2    Dayan, G.3    Di Pietro, A.4
  • 13
    • 0029041911 scopus 로고
    • Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein
    • Sharma S., Rose D. R. Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein. J. Biol. Chem. 270:1995;14085-14093.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14085-14093
    • Sharma, S.1    Rose, D.R.2
  • 14
    • 0033557887 scopus 로고    scopus 로고
    • Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: Comparison of fusions to gluthation S-transferase, thioredoxin and maltose-binding protein
    • Wang C., Castro F. A., Wilkes D. M., Altenberg G. A. Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: comparison of fusions to gluthation S-transferase, thioredoxin and maltose-binding protein. Biochem. J. 338:1999;77-81.
    • (1999) Biochem. J. , vol.338 , pp. 77-81
    • Wang, C.1    Castro, F.A.2    Wilkes, D.M.3    Altenberg, G.A.4
  • 15
    • 0026702994 scopus 로고
    • Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product
    • Hartman J., Huang Z., Rado T. A., Peng S., Jilling T., Muccio D. D., Sorscher E. J. Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product. J. Biol. Chem. 267:1992;6455-6458.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6455-6458
    • Hartman, J.1    Huang, Z.2    Rado, T.A.3    Peng, S.4    Jilling, T.5    Muccio, D.D.6    Sorscher, E.J.7
  • 16
    • 0027524866 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator
    • Ko Y. H., Thomas P. J., Deleanoy M. R., Pedersen P. L. The cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 268:1993;24330-24338.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24330-24338
    • Ko, Y.H.1    Thomas, P.J.2    Deleanoy, M.R.3    Pedersen, P.L.4
  • 17
    • 0029113976 scopus 로고
    • The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase
    • Ko Y. H., Pedersen P. L. The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase. J. Biol. Chem. 270:1995;22093-22096.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22093-22096
    • Ko, Y.H.1    Pedersen, P.L.2
  • 18
    • 0030033151 scopus 로고    scopus 로고
    • A recombinant peptide model of the firstnucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: Comparison of wild-type and delta F508 mutant forms
    • Yike I., Ye J., Zhang Y., Manavalan P., Gerken T. A., Dearborn D. G. A recombinant peptide model of the firstnucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: Comparison of wild-type and delta F508 mutant forms. Protein Sci. 5:1996;89-97.
    • (1996) Protein Sci. , vol.5 , pp. 89-97
    • Yike, I.1    Ye, J.2    Zhang, Y.3    Manavalan, P.4    Gerken, T.A.5    Dearborn, D.G.6
  • 19
    • 0028150053 scopus 로고
    • Nucleotide binding to the hydrophilic C-terminal domain of the transporter associated with antigen processing (TAP)
    • Müller K. M., Ebensperger C., Tampé R. Nucleotide binding to the hydrophilic C-terminal domain of the transporter associated with antigen processing (TAP). J. Biol. Chem. 269:1994;14032-14037.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14032-14037
    • Müller, K.M.1    Ebensperger, C.2    Tampé, R.3
  • 20
    • 0030822352 scopus 로고    scopus 로고
    • Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium
    • Nikaido K., Liu P.-O., Ames G. F.-L. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. J. Biol. Chem. 272:1997;27745-27752.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27745-27752
    • Nikaido, K.1    Liu, P.-O.2    Ames, G.F.-L.3
  • 21
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung L. W., Wang I. X., Nikaido K., Liu P. Q., Ames G. F., Kim S. H. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature. 396:1998;703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu R., Sharom F. J. Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry. 35:1996;11865-11873.
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 24
    • 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., 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
  • 25
    • 0015894660 scopus 로고
    • Preparation and properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate
    • Hiratsuka T., Uchida K. Preparation and properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate. BBA. 320:1973;635-647.
    • (1973) BBA. , vol.320 , pp. 635-647
    • Hiratsuka, T.1    Uchida, K.2
  • 26
    • 0017180809 scopus 로고
    • Fluorescent properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate and its use in the study of binding to hevy meromyosin ATPase
    • Hiratsuka T. Fluorescent properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate and its use in the study of binding to hevy meromyosin ATPase. BBA. 453:1976;293-297.
    • (1976) BBA. , vol.453 , pp. 293-297
    • Hiratsuka, T.1
  • 27
    • 0034072174 scopus 로고    scopus 로고
    • Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions
    • Bakos É., Evers R., Sinkó E., Váradi A., Borst P., 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, É.1    Evers, R.2    Sinkó, E.3    Váradi, A.4    Borst, P.5    Sarkadi, B.6
  • 28
    • 0032508515 scopus 로고    scopus 로고
    • Stimulation of ATPase activity of purified multidrug resistance-associated protein by nucleoside diphosphates
    • Chang X. B., Hou Z. X., Riordan J. H. Stimulation of ATPase activity of purified multidrug resistance-associated protein by nucleoside diphosphates. J. Biol. Chem. 273:1998;23844-23848.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23844-23848
    • Chang, X.B.1    Hou, Z.X.2    Riordan, J.H.3
  • 29
    • 0033370596 scopus 로고    scopus 로고
    • ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells
    • Mao Q., Leslie E. M., Deeley R. G., Cole S. P. C. ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells. Biochim. Biophys. Acta. 1461:1999;69-82.
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 69-82
    • Mao, Q.1    Leslie, E.M.2    Deeley, R.G.3    Cole, S.P.C.4
  • 32
    • 0032560635 scopus 로고    scopus 로고
    • Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphatase activity
    • Beaudet L., Urbatsch I. L., Gros P. Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphatase activity. Biochemistry. 37:1998;9073-9082.
    • (1998) Biochemistry , vol.37 , pp. 9073-9082
    • Beaudet, L.1    Urbatsch, I.L.2    Gros, P.3
  • 33
    • 0028307625 scopus 로고
    • Covalent inhibitors of P-glycoprotein ATPase activity
    • Al-Shawi M. K., Urbatsch I. L., Senior A. E. Covalent inhibitors of P-glycoprotein ATPase activity. J. Biol. Chem. 269:1994;8986-8992.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8986-8992
    • Al-Shawi, M.K.1    Urbatsch, I.L.2    Senior, A.E.3
  • 34
    • 0029121417 scopus 로고
    • Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity
    • Loo T. W., Clarke D. M. Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J. Biol. Chem. 270:1995;22957-22961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 35
    • 0030609038 scopus 로고    scopus 로고
    • Photoaffinity labelling of P-glycoprotein catalytic sites
    • Sankaran B., Bhagat S., Senior A. E. Photoaffinity labelling of P-glycoprotein catalytic sites. FEBS Lett. 417:1997;119-122.
    • (1997) FEBS Lett. , vol.417 , pp. 119-122
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 36
    • 0031156388 scopus 로고    scopus 로고
    • ATP hydrolysis cycles and mechanism in P-glycoprotein and CFTR
    • Senior A. E., Gadsby D. C. ATP hydrolysis cycles and mechanism in P-glycoprotein and CFTR. Semin. Cancer Biol. 8:1997;143-151.
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 143-151
    • Senior, A.E.1    Gadsby, D.C.2
  • 37
    • 0031148758 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein ATPase activity by procedures involving trapping of nucleotide in catalytic sites
    • Sankaran B., Bhagat S., Senior A. E. Inhibition of P-glycoprotein ATPase activity by procedures involving trapping of nucleotide in catalytic sites. Arch. Biochem. Biophys. 341:1997;160-169.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 160-169
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 38
    • 0030995604 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein ATPase activity by beryllium fluoride
    • Sankaran B., Bhagat S., Senior A. E. Inhibition of P-glycoprotein ATPase activity by beryllium fluoride. Biochemistry. 36:1997;6847-6853.
    • (1997) Biochemistry , vol.36 , pp. 6847-6853
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 39
    • 0034724680 scopus 로고    scopus 로고
    • Comparison of the Functional Characteristics of the Nucleotide Binding Domains of Multidrug Resistance Protein 1
    • Gao M., Cui H-R., Loe D. W., Grant C. E., Almquist K. C., Cole S. P. C., Deeley R. G. Comparison of the Functional Characteristics of the Nucleotide Binding Domains of Multidrug Resistance Protein 1. J. Biol. Chem. 275:2000;13098-13108.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13098-13108
    • Gao, M.1    Cui, H.-R.2    Loe, D.W.3    Grant, C.E.4    Almquist, K.C.5    Cole, S.P.C.6    Deeley, R.G.7
  • 40
    • 0034617097 scopus 로고    scopus 로고
    • Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1
    • Hou Y.-X., Cui L., Riordan J. R., Chang X.-B. Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1. J. Biol. Chem. 2000.
    • (2000) J. Biol. Chem.
    • Hou, Y.-X.1    Cui, L.2    Riordan, J.R.3    Chang, X.-B.4
  • 41
    • 0034625350 scopus 로고    scopus 로고
    • Non-equivalent nucleotide trapping in the two nucleotide binding folds of the human multidrug resistance protein MRP1
    • Nagata K., Nishitani M., Matsuo M., Kioka N., Amachi T., Ueda K. Non-equivalent nucleotide trapping in the two nucleotide binding folds of the human multidrug resistance protein MRP1. J. Biol. Chem. 2000.
    • (2000) J. Biol. Chem.
    • Nagata, K.1    Nishitani, M.2    Matsuo, M.3    Kioka, N.4    Amachi, T.5    Ueda, K.6


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