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Volumn 243, Issue , 2002, Pages 54-68

P glycoprotein and the mechanism of multidrug resistance

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; GLYCOPROTEIN P;

EID: 0036361915     PISSN: None     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (29)

References (44)
  • 1
    • 0026662530 scopus 로고
    • Partial purification and reconstitution of the human multidrug-resistance pump: Characterization of the drug-stimulatable ATP hydrolysis
    • USA
    • Ambudkar SV, Lelong IH, Zhang J, Cardarelli CO, Gottesman MM, Pastan I 1992 Partial purification and reconstitution of the human multidrug-resistance pump: characterization of the drug-stimulatable ATP hydrolysis. Proc Natl Acad Sci USA 89:8472-8476
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 8472-8476
    • Ambudkar, S.V.1    Lelong, I.H.2    Zhang, J.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 3
    • 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, 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
  • 4
    • 0031007555 scopus 로고    scopus 로고
    • Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region
    • Bakos É, Klein I, Welker E et al 1997 Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region. Biochem J 323: 777-783
    • (1997) Biochem J , vol.323 , pp. 777-783
    • É, B.1    Klein, I.2    Welker, E.3
  • 5
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen CJ, Chin JE, Ueda K et al 1986 Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47:381-389
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.J.1    Chin, J.E.2    Ueda, K.3
  • 6
    • 0000712439 scopus 로고
    • Multidrug-resistance gene (P-glycoprotein) is expressed by endothelial cells at blood-brain barrier sites
    • USA
    • Cordon-Cardo C, O'Brien JP, Casals D et al 1989 Multidrug-resistance gene (P-glycoprotein) is expressed by endothelial cells at blood-brain barrier sites. Proc Natl Acad Sci USA 86:695-698
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 695-698
    • Cordon-Cardo, C.1    O'Brien, J.P.2    Casals, D.3
  • 7
    • 0023553574 scopus 로고
    • ATP-binding properties of P glycoprotein from multidrug-resistant KB cells
    • Cornwell MM, Tsuruo T, Gottesman MM, Pastan I 1987 ATP-binding properties of P glycoprotein from multidrug-resistant KB cells. FASEB J 1:51-54
    • (1987) FASEB J , vol.1 , pp. 51-54
    • Cornwell, M.M.1    Tsuruo, T.2    Gottesman, M.M.3    Pastan, I.4
  • 8
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs K, Diez J, Greller G et al 2000 Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J 19: 5951-5961
    • (2000) EMBO J , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3
  • 9
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: Complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros P, Croop J, 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
  • 10
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of the Rad50 ATPase. ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner KP, Karcher A, Shin DS et al 2000 Structural biology of the Rad50 ATPase. ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101:789-800
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3
  • 11
    • 0032479280 scopus 로고    scopus 로고
    • Mechanism of action of human P-glycoprotein ATPase activity: Photochemical cleavage during a catalytic transition state using othovanadate reveals cross-talk between the two ATP sites
    • Hrycyna CA, Ramachandra M, Ambudkar SV et al 1998a Mechanism of action of human P-glycoprotein ATPase activity: photochemical cleavage during a catalytic transition state using othovanadate reveals cross-talk between the two ATP sites. J Biol Chem 273: 16631-16634
    • (1998) J Biol Chem , vol.273 , pp. 16631-16634
    • Hrycyna, C.A.1    Ramachandra, M.2    Ambudkar, S.V.3
  • 12
    • 0032578434 scopus 로고    scopus 로고
    • Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport
    • Hrycyna CA, Airan LE, Germann UA, Ambudkar SV, Pastan I, Gottesman MM 1998b Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport. Biochemistry 37:13660-13673
    • (1998) Biochemistry , vol.37 , pp. 13660-13673
    • Hrycyna, C.A.1    Airan, L.E.2    Germann, U.A.3    Ambudkar, S.V.4    Pastan, I.5    Gottesman, M.M.6
  • 13
  • 14
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones PM, George AM 1999 Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiol Lett 179:187-202
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 16
    • 0032716822 scopus 로고    scopus 로고
    • Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters
    • Krupka RM 1999 Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters. J Membr Biol 127:129-143
    • (1999) J Membr Biol , vol.127 , pp. 129-143
    • Krupka, R.M.1
  • 17
    • 0033609856 scopus 로고    scopus 로고
    • The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface
    • Loo TW, Clarke DM 1999 The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface. J Biol Chem 274:24759-24765
    • (1999) J Biol Chem , vol.274 , pp. 24759-24765
    • Loo, T.W.1    Clarke, D.M.2
  • 18
    • 0030026629 scopus 로고    scopus 로고
    • Altered drug-stimulated ATPase activity in mutants of the human multidrug resistance protein
    • Müller M, Bakos É, Welker E et al 1996 Altered drug-stimulated ATPase activity in mutants of the human multidrug resistance protein. J Biol Chem 271:1877-1883
    • (1996) J Biol Chem , vol.271 , pp. 1877-1883
    • Müller, M.1    É, B.2    Welker, E.3
  • 19
    • 0035814802 scopus 로고    scopus 로고
    • FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated
    • Qu Q, Sharom SJ 2001 FRET Analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated. Biochemistry 40:1413-1422
    • (2001) Biochemistry , vol.40 , pp. 1413-1422
    • Qu, Q.1    Sharom, S.J.2
  • 20
    • 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
    • USA
    • Rao VV, Dahlheimer JL, Bardgett ME et al 1999 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 96:3900-3905
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 3900-3905
    • Rao, V.V.1    Dahlheimer, J.L.2    Bardgett, M.E.3
  • 21
    • 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, 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
  • 22
    • 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 AE 1997a Inhibition of P-glycoprotein ATPase activity by procedures involving trapping of nucleotide in catalytic sites. Arch Biochem Biophys 341:160-169
    • (1997) Arch Biochem Biophys , vol.341 , pp. 160-169
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 23
    • 0030995604 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein ATPase activity by beryllium fluoride
    • Sankaran B, Bhagat S, Senior AE 1997b Inhibition of P-glycoprotein ATPase activity by beryllium fluoride. Biochemistry 36:6847-6853
    • (1997) Biochemistry , vol.36 , pp. 6847-6853
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 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 EM, Boucher RC, Germann UA, Scarborough GA 1992 Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase. J Biol Chem 267:4854-4858
    • (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
    • 0034646468 scopus 로고    scopus 로고
    • Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein
    • USA
    • Sauna ZE, Ambudkar SV 2000 Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein. Proc Natl Acad Sci USA 97:2515-2520
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 2515-2520
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 26
    • 0028229150 scopus 로고
    • Disruption of the mouse mdr1a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs
    • Schinkel AH, Smit JJ, van Tellingen O et al 1994 Disruption of the mouse mdr1a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs. Cell 77:491-502
    • (1994) Cell , vol.77 , pp. 491-502
    • Schinkel, A.H.1    Smit, J.J.2    Van Tellingen, O.3
  • 27
    • 4243801613 scopus 로고    scopus 로고
    • Normal viability and altered pharmacokinetics in mice lacking mdr1-type (drug-transporting) P-glycoproteins
    • USA
    • Schinkel AH, Mayer U, Wagenaar E et al 1997 Normal viability and altered pharmacokinetics in mice lacking mdr1-type (drug-transporting) P-glycoproteins. Proc Natl Acad Sci USA 94:4028-4033
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 4028-4033
    • Schinkel, A.H.1    Mayer, U.2    Wagenaar, E.3
  • 29
    • 0031156388 scopus 로고    scopus 로고
    • ATP hydrolysis cycles and mechanism in P-glycoprotein and CFTR
    • Senior AE, Gadsby DC 1997 ATP hydrolysis cycles and mechanism in P-glycoprotein and CFTR. Semin Cancer Biol 8:143-150
    • (1997) Semin Cancer Biol , vol.8 , pp. 143-150
    • Senior, A.E.1    Gadsby, D.C.2
  • 30
    • 0029041911 scopus 로고
    • Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein
    • Sharma S, Rose DR 1995 Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein. J Biol Chem 270:14085-14093
    • (1995) J Biol Chem , vol.270 , pp. 14085-14093
    • Sharma, S.1    Rose, D.R.2
  • 32
    • 0032562795 scopus 로고    scopus 로고
    • Drug-stimulated nucleotide trapping in the human multidrug transporter MDR1: Cooperation of the nucleotide binding domains
    • Szabó K, Welker E, Bakos É et al 1998 Drug-stimulated nucleotide trapping in the human multidrug transporter MDR1: cooperation of the nucleotide binding domains. J Biol Chem 273:10132-10138
    • (1998) J Biol Chem , vol.273 , pp. 10132-10138
    • Szabó, K.1    Welker, E.2    É, B.3
  • 34
    • 0035874464 scopus 로고    scopus 로고
    • Role of the conserved Gly residue in the ABC-signature motif of human MDR1 in the drug-induced allosteric control of ATPase activity
    • Szakács G, Özvegy CS, Bakos É, Sarkadi B, Váradi A 2001 Role of the conserved Gly residue in the ABC-signature motif of human MDR1 in the drug-induced allosteric control of ATPase activity. Biochem J 356:71-75
    • (2001) Biochem J , vol.356 , pp. 71-75
    • Szakács, G.1    Özvegy, C.S.2    É, B.3    Sarkadi, B.4    Váradi, A.5
  • 35
    • 0023447098 scopus 로고
    • Cellular localization of the multidrug-resistance gene product P-glycoprotein in normal human tissues
    • USA
    • Thiebaut F, Tsuruo T, Hamada H, Gottesman MM, Pastan I, Willingham MC 1987 Cellular localization of the multidrug-resistance gene product P-glycoprotein in normal human tissues. Proc Natl Acad Sci USA 84:7735-7738
    • (1987) Proc Natl Acad Sci , vol.84 , pp. 7735-7738
    • Thiebaut, F.1    Tsuruo, T.2    Hamada, H.3    Gottesman, M.M.4    Pastan, I.5    Willingham, M.C.6
  • 36
    • 0034637483 scopus 로고    scopus 로고
    • Conserved Walker A Ser residues in the catalytic sites of P-glycoprotein are critical for catalysis and involved primarily at the transition state step
    • Urbatsch IL, Gimi K, Wilke-Mounts S, Senior AE 2000a Conserved Walker A Ser residues in the catalytic sites of P-glycoprotein are critical for catalysis and involved primarily at the transition state step. J Biol Chem 275:25031-25038
    • (2000) J Biol Chem , vol.275 , pp. 25031-25038
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 37
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • Urbatsch IL, Gimi K, Wilke-Mounts S, Senior AE 2000b Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein. Biochemistry 39:11921-11927
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 38
    • 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, 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
  • 39
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch IL, Sankaran B, Weber J, Senior AE 1995a P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J Biol Chem 270:19383-19390
    • (1995) J Biol Chem , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 40
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch IL, Sankaran B, Bhagat S, Senior AE 1995b Both P-glycoprotein nucleotide-binding sites are catalytically active. J Biol Chem 270:26956-26961
    • (1995) J Biol Chem , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 41
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • van Helvoort A, Smith AJ, Sprong H et al 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
    • Van Helvoort, A.1    Smith, A.J.2    Sprong, H.3
  • 42
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myoisn, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ 1982 Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myoisn, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1:945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 43
    • 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 FA, Wilkes DM, Altenberg G A 1999 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 338:77-81
    • (1999) Biochem J , vol.338 , pp. 77-81
    • Wang, C.1    Castro, F.A.2    Wilkes, D.M.3    Altenberg, G.A.4
  • 44
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter
    • Zheleznova EE, Markham PN, Neyfakh AA, Brennan RG 1999 Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter. Cell 96:353-336
    • (1999) Cell , vol.96 , pp. 353-1336
    • Zheleznova, E.E.1    Markham, P.N.2    Neyfakh, A.A.3    Brennan, R.G.4


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