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Volumn 58, Issue 1, 2000, Pages 37-47

Functional analysis of a tryptophan-less P-glycoprotein: A tool for tryptophan insertion and fluorescence spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CALCEIN; COLCHICINE; DACTINOMYCIN; DOXORUBICIN; GLYCOPROTEIN P; VINBLASTINE;

EID: 0033924206     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.58.1.37     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0024307162 scopus 로고
    • Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance
    • Azzaria M, Schurr E and Gros P (1989) Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance. Mol Cell Biol 9:5289-5297.
    • (1989) Mol Cell Biol , vol.9 , pp. 5289-5297
    • Azzaria, M.1    Schurr, E.2    Gros, P.3
  • 2
    • 0028982951 scopus 로고
    • Functional dissection of p-glycoprotein nucleotide-binding domains in chimeric and mutant proteins: Modulation of drug resistance profiles
    • Beaudet L and Gros P (1995) Functional dissection of P-glycoprotein nucleotide-binding domains in chimeric and mutant proteins: Modulation of drug resistance profiles. J Biol Chem 270:17159-17170.
    • (1995) J Biol Chem , vol.270 , pp. 17159-17170
    • Beaudet, L.1    Gros, P.2
  • 3
    • 0028720467 scopus 로고
    • Cytomegalovirus plasmid vectors for permanent lines of polarized epithelial cells
    • Brewer CB (1994) Cytomegalovirus plasmid vectors for permanent lines of polarized epithelial cells. Methods Cell Biol 43:233-245.
    • (1994) Methods Cell Biol , vol.43 , pp. 233-245
    • Brewer, C.B.1
  • 4
    • 0025253133 scopus 로고
    • Two members of the mouse mdr gene family confer multidrug resistance with overlapping but distinct drug specificities
    • Devault A and Gros P (1990) Two members of the mouse mdr gene family confer multidrug resistance with overlapping but distinct drug specificities. Mol Cell Biol 10:1652-1663.
    • (1990) Mol Cell Biol , vol.10 , pp. 1652-1663
    • Devault, A.1    Gros, P.2
  • 5
    • 0026556302 scopus 로고
    • Amino acid substitutions in the sixth transmembrane domain of P-glycoprotein alter multidrug resistance
    • Devine SE, Ling V and Melera PW (1992) Amino acid substitutions in the sixth transmembrane domain of P-glycoprotein alter multidrug resistance. Proc Natl Acad Sci USA 89:4564-4568.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4564-4568
    • Devine, S.E.1    Ling, V.2    Melera, P.W.3
  • 6
    • 0343306779 scopus 로고    scopus 로고
    • Kinetic analysis of calcein and calcein-acetoxymethylester efflux mediated by the multidrug resistance protein and P-glycoprotein
    • Essodaigui M, Broxterman HJ and Garnier-Suillerot A (1998) Kinetic analysis of calcein and calcein-acetoxymethylester efflux mediated by the multidrug resistance protein and P-glycoprotein. Biochemistry 37:2243-2250.
    • (1998) Biochemistry , vol.37 , pp. 2243-2250
    • Essodaigui, M.1    Broxterman, H.J.2    Garnier-Suillerot, A.3
  • 7
    • 0027216104 scopus 로고
    • Major photoaffinity drug labeling sites for iodoaryl azido-prazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12
    • Greenberger LM (1993) Major photoaffinity drug labeling sites for iodoaryl azido-prazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12. J Biol Chem 268:11417-11425.
    • (1993) J Biol Chem , vol.268 , pp. 11417-11425
    • Greenberger, L.M.1
  • 8
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: Complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros P, Croop J and Housman D (1986) Mammalian multidrug resistance gene: Complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47:371-380.
    • (1986) Cell , vol.47 , pp. 371-380
    • Gros, P.1    Croop, J.2    Housman, D.3
  • 9
    • 0032541975 scopus 로고    scopus 로고
    • Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein
    • Hafkemeyer P, Dey S, Ambudkar SV, Hrycyna CA, Pastan I and Gottesman MM (1998) Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein. Biochemistry 37: 16400-16409.
    • (1998) Biochemistry , vol.37 , pp. 16400-16409
    • Hafkemeyer, P.1    Dey, S.2    Ambudkar, S.V.3    Hrycyna, C.A.4    Pastan, I.5    Gottesman, M.M.6
  • 10
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning
    • Hanna M, Brault M, Kwan T, Kast C and Gros P (1996) Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning. Biochemistry 35:3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1    Brault, M.2    Kwan, T.3    Kast, C.4    Gros, P.5
  • 12
  • 13
    • 0021852930 scopus 로고
    • Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies
    • Kartner N, Evernden-Porelle D, Bradley G and Ling V (1985) Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies. Nature (Lond) 316:820-823.
    • (1985) Nature (Lond) , vol.316 , pp. 820-823
    • Kartner, N.1    Evernden-Porelle, D.2    Bradley, G.3    Ling, V.4
  • 14
    • 0028950653 scopus 로고
    • Membrane topology of P-glycoprotein as determined by epitope insertion: Transmembrane organization of the N-terminal domain of mdr3
    • Kast C, Canfield V, Levenson R and Gros P (1995) Membrane topology of P-glycoprotein as determined by epitope insertion: Transmembrane organization of the N-terminal domain of mdr3. Biochemistry 34:4402-4411.
    • (1995) Biochemistry , vol.34 , pp. 4402-4411
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 15
    • 0029918133 scopus 로고    scopus 로고
    • Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence
    • Kast C, Canfield V, Levenson R and Gros P (1996) Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence. J Biol Chem 271:9240-9248.
    • (1996) J Biol Chem , vol.271 , pp. 9240-9248
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 16
    • 0033520934 scopus 로고    scopus 로고
    • Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins
    • Lerner-Marmarosh N, Gimi K, Urbatsch IL, Gros P and Senior AE (1999) Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins. J Biol Chem 274:34711-34718.
    • (1999) J Biol Chem , vol.274 , pp. 34711-34718
    • Lerner-Marmarosh, N.1    Gimi, K.2    Urbatsch, I.L.3    Gros, P.4    Senior, A.E.5
  • 17
    • 0030738677 scopus 로고    scopus 로고
    • Multidrug resistance: Molecular mechanisms and clinical relevance
    • Ling V (1997) Multidrug resistance: Molecular mechanisms and clinical relevance. Cancer Chemother Pharmacol 40:S3-S8.
    • (1997) Cancer Chemother Pharmacol , vol.40
    • Ling, V.1
  • 18
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu R and Sharom FJ (1996) Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry 35:11865-11873.
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 19
    • 0032485855 scopus 로고    scopus 로고
    • Proximity of the nucleotide binding domains of the P-glycoprotein multidrug transporter to the membrane surface: A resonance energy transfer study
    • Liu R and Sharom FJ (1998) Proximity of the nucleotide binding domains of the P-glycoprotein multidrug transporter to the membrane surface: A resonance energy transfer study. Biochemistry 37:6503-6512.
    • (1998) Biochemistry , vol.37 , pp. 6503-6512
    • Liu, R.1    Sharom, F.J.2
  • 20
    • 0027997698 scopus 로고
    • Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein
    • Loo TW and Clarke DM (1994) Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein. Biochemistry 33:14049-14057.
    • (1994) Biochemistry , vol.33 , pp. 14049-14057
    • Loo, T.W.1    Clarke, D.M.2
  • 21
    • 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 TW and Clarke DM (1995a) Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J Biol Chem 270:22957-22961.
    • (1995) J Biol Chem , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 22
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo TW and Clarke DM (1995b) Membrane topology of a cysteine-less mutant of human P-glycoprotein. J Biol Chem 270:843-848.
    • (1995) J Biol Chem , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 23
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo TW and Clarke DM (1996) Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J Biol Chem 271:27482-27487.
    • (1996) J Biol Chem , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 24
    • 0030779102 scopus 로고    scopus 로고
    • Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12
    • Loo TW and Clarke DM (1997a) Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12. J Biol Chem 272:20986-20989.
    • (1997) J Biol Chem , vol.272 , pp. 20986-20989
    • Loo, T.W.1    Clarke, D.M.2
  • 25
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate
    • Loo TW and Clarke DM (1997b) Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J Biol Chem 272:31945-31948.
    • (1997) J Biol Chem , vol.272 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 26
    • 0026585065 scopus 로고
    • Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene
    • Raymond M, Gros P, Whiteway M and Thomas DY (1992) Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene. Science (Wash DC) 256:232-234.
    • (1992) Science (Wash DC) , vol.256 , pp. 232-234
    • Raymond, M.1    Gros, P.2    Whiteway, M.3    Thomas, D.Y.4
  • 27
    • 0027955136 scopus 로고
    • Functional expression of P-glycoprotein in saccharomyces cerevisiae confers cellular resistance to the immunosuppressive and antifungal agent FK520
    • Raymond M, Ruetz S, Thomas DY and Gros P (1994) Functional expression of P-glycoprotein in Saccharomyces cerevisiae confers cellular resistance to the immunosuppressive and antifungal agent FK520. Mol Cell Biol 14:277-286.
    • (1994) Mol Cell Biol , vol.14 , pp. 277-286
    • Raymond, M.1    Ruetz, S.2    Thomas, D.Y.3    Gros, P.4
  • 28
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg MF, Callaghan R, Ford RC and Higgins CF (1997) Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J Biol Chem 272:10685-10694.
    • (1997) J Biol Chem , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 29
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • Ruetz S and Gros P (1994) Phosphatidylcholine translocase: A physiological role for the mdr2 gene. Cell 77:1071-1081.
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 31
    • 0032129974 scopus 로고    scopus 로고
    • Catalytic mechanism of P-glycoprotein
    • Senior AE (1998) Catalytic mechanism of P-glycoprotein. Acta Physiol Scand Suppl 643:213-218.
    • (1998) Acta Physiol Scand Suppl , vol.643 , pp. 213-218
    • Senior, A.E.1
  • 32
    • 0032130787 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent multidrug transport by P-glycoprotein
    • Shapiro AB and Ling V (1998) The mechanism of ATP-dependent multidrug transport by P-glycoprotein. Acta Physiol Scand Suppl 643:227-234.
    • (1998) Acta Physiol Scand Suppl , vol.643 , pp. 227-234
    • Shapiro, A.B.1    Ling, V.2
  • 33
    • 0027303904 scopus 로고
    • The nitrogen of the acetamido group of colchicine modulates P-glycoprotein-mediated multidrug resistance
    • Tang-Wai DF, Brossi A, Arnold LD and Gros P (1993) The nitrogen of the acetamido group of colchicine modulates P-glycoprotein-mediated multidrug resistance. Biochemistry 32:6470-6476.
    • (1993) Biochemistry , vol.32 , pp. 6470-6476
    • Tang-Wai, D.F.1    Brossi, A.2    Arnold, L.D.3    Gros, P.4
  • 34
    • 0032584289 scopus 로고    scopus 로고
    • Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotide at both sites
    • Urbatsch IL, Beaudet L, Carrier I and Gros P (1998) Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotide at both sites. Biochemistry 37:4592-4602.
    • (1998) Biochemistry , vol.37 , pp. 4592-4602
    • Urbatsch, I.L.1    Beaudet, L.2    Carrier, I.3    Gros, P.4
  • 35
    • 0007544439 scopus 로고    scopus 로고
    • Mdr1 P-glycoprotein is a lipid translocase of broad specificity, while mdr3 P-glycoprotein specifically translocates phosphatidylcholine
    • Vanhelvoort A, Smith AJ, Sprong H, Fritzsche I, Schinkel AH, Borst P and Vanmeer G (1996) mdr1 P-glycoprotein is a lipid translocase of broad specificity, while mdr3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87:507-517.
    • (1996) Cell , vol.87 , pp. 507-517
    • Vanhelvoort, A.1    Smith, A.J.2    Sprong, H.3    Fritzsche, I.4    Schinkel, A.H.5    Borst, P.6    Vanmeer, G.7
  • 36
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet T, Dignard D and Thomas DY (1987) A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 37
    • 0030698195 scopus 로고    scopus 로고
    • Ligand-induced movement of helix X in the lactose permease from Escherichia coli: A fluorescence quenching study
    • Wang Q, Matsushita K, de Foresta B, le Maire M and Kaback HR (1997) Ligand-induced movement of helix X in the lactose permease from Escherichia coli: A fluorescence quenching study. Biochemistry 36:14120-14127.
    • (1997) Biochemistry , vol.36 , pp. 14120-14127
    • Wang, Q.1    Matsushita, K.2    De Foresta, B.3    Le Maire, M.4    Kaback, H.R.5
  • 38
    • 0032167938 scopus 로고    scopus 로고
    • Tryptophan substitutions surrounding the nucleotide in catalytic sites of F1-ATPase
    • Weber J, Wilke-Mounts S, Hammond ST and Senior AE (1998) Tryptophan substitutions surrounding the nucleotide in catalytic sites of F1-ATPase. Biochemistry 37:12042-12050.
    • (1998) Biochemistry , vol.37 , pp. 12042-12050
    • Weber, J.1    Wilke-Mounts, S.2    Hammond, S.T.3    Senior, A.E.4
  • 39
    • 0024441318 scopus 로고
    • Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies
    • Yoshimura A, Kuwazuru Y, Sumizawa T, Ichikawa M, Ikeda S, Uda T and Akiyama S (1989) Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies. J Biol Chem 264:16282-16291.
    • (1989) J Biol Chem , vol.264 , pp. 16282-16291
    • Yoshimura, A.1    Kuwazuru, Y.2    Sumizawa, T.3    Ichikawa, M.4    Ikeda, S.5    Uda, T.6    Akiyama, S.7
  • 40
    • 0030795417 scopus 로고    scopus 로고
    • Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase
    • Zhou T and Rosen BP (1997) Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase. J Biol Chem 272:19731-19737.
    • (1997) J Biol Chem , vol.272 , pp. 19731-19737
    • Zhou, T.1    Rosen, B.P.2


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