메뉴 건너뛰기




Volumn 72, Issue 2, 2006, Pages 145-155

Biochemical and pharmacological properties of an allosteric modulator site of the human P-glycoprotein (ABCB1)

Author keywords

125I iodoarylazidoprazosin (or 125I IAAP); Flupentixol; Multidrug resistance; Phenothiazine; Thioxanthene

Indexed keywords

CYCLOSPORIN A; FLUPENTIXOL; GLYCOPROTEIN P; PHENOTHIAZINE DERIVATIVE; THIOXANTHENE DERIVATIVE; VINBLASTINE;

EID: 33744942933     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.04.008     Document Type: Article
Times cited : (14)

References (42)
  • 3
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen C.-j., Chin J.E., Ueda K., Clark D.P., Pastan I., Gottesman M.M., et al. Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47 (1986) 381-389
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.-j.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6
  • 4
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman M.M., and 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
  • 5
    • 0028229881 scopus 로고
    • Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides
    • Loo T.W., and Clarke D.M. Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides. J Biol Chem 269 (1994) 7750-7755
    • (1994) J Biol Chem , vol.269 , pp. 7750-7755
    • Loo, T.W.1    Clarke, D.M.2
  • 6
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities
    • Loo T.W., and Clarke D.M. Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities. J Biol Chem 270 (1995) 21449-21452
    • (1995) J Biol Chem , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 7
    • 0027408359 scopus 로고
    • N-glycosylation and deletion mutants of the human P-glycoprotein
    • Schinkel A.H., Kemp S., Dolle M., Rudenko G., and Wagenaar E. N-glycosylation and deletion mutants of the human P-glycoprotein. J Biol Chem 268 (1993) 7474-7481
    • (1993) J Biol Chem , vol.268 , pp. 7474-7481
    • Schinkel, A.H.1    Kemp, S.2    Dolle, M.3    Rudenko, G.4    Wagenaar, E.5
  • 8
    • 0035813143 scopus 로고    scopus 로고
    • Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers
    • Loo T.W., and Clarke D.M. Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers. J Biol Chem 276 (2001) 36877-36880
    • (2001) J Biol Chem , vol.276 , pp. 36877-36880
    • Loo, T.W.1    Clarke, D.M.2
  • 9
    • 0035805573 scopus 로고    scopus 로고
    • Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil MTS-verapamil
    • Loo T.W., and Clarke D.M. Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analog of verapamil MTS-verapamil. J Biol Chem 276 (2001) 14972-14979
    • (2001) J Biol Chem , vol.276 , pp. 14972-14979
    • Loo, T.W.1    Clarke, D.M.2
  • 10
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv Y., Pollard H.B., Bruggemann E.P., Pastan I., and Gottesman M.M. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. J Biol Chem 265 (1990) 3975-3980
    • (1990) J Biol Chem , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 11
    • 0024971222 scopus 로고
    • Two different regions of P-glycoprotein are photoaffinity labeled by azidopine
    • Bruggemann E.P., Germann U.A., Gottesman M.M., and Pastan I. Two different regions of P-glycoprotein are photoaffinity labeled by azidopine. J Biol Chem 264 (1989) 15483-15488
    • (1989) J Biol Chem , vol.264 , pp. 15483-15488
    • Bruggemann, E.P.1    Germann, U.A.2    Gottesman, M.M.3    Pastan, I.4
  • 12
    • 0028128286 scopus 로고
    • Localization of the forskolin labeling sites to both halves of P-glycoprotein: similarity of the sites labeled by forskolin and prazosin
    • Morris D.I., Greenberger L.M., Bruggemann E.P., Cardarelli C.O., Gottesman M.M., Pastan I., et al. Localization of the forskolin labeling sites to both halves of P-glycoprotein: similarity of the sites labeled by forskolin and prazosin. Mol Pharmacol 46 (1994) 329-337
    • (1994) Mol Pharmacol , vol.46 , pp. 329-337
    • Morris, D.I.1    Greenberger, L.M.2    Bruggemann, E.P.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 13
    • 0025872032 scopus 로고
    • Domain mapping of the photoaffinity drug-binding sites in P-glycoprotein encoded by mouse mdr1b
    • Greenberger L.M., Lisanti C.J., Silva J.T., and Horwitz S.B. Domain mapping of the photoaffinity drug-binding sites in P-glycoprotein encoded by mouse mdr1b. J Biol Chem 266 (1991) 20744-20751
    • (1991) J Biol Chem , vol.266 , pp. 20744-20751
    • Greenberger, L.M.1    Lisanti, C.J.2    Silva, J.T.3    Horwitz, S.B.4
  • 14
    • 0027216104 scopus 로고
    • Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12
    • Greenberger L.M. Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12. J Biol Chem 268 (1993) 11417-11425
    • (1993) J Biol Chem , vol.268 , pp. 11417-11425
    • Greenberger, L.M.1
  • 16
    • 0029939665 scopus 로고    scopus 로고
    • Experimental reversal of P-glycoprotein-mediated multidrug resistance by pharmacological chemosensitisers
    • Ford J.M. Experimental reversal of P-glycoprotein-mediated multidrug resistance by pharmacological chemosensitisers. Eur J Cancer 32A (1996) 991-1001
    • (1996) Eur J Cancer , vol.32 A , pp. 991-1001
    • Ford, J.M.1
  • 17
    • 0027290876 scopus 로고
    • Restricted transport of Cyclosporin-A across the blood brain barrier by a multidrug transporter, p-glycoprotein
    • Tsuji A., Tamai I., Sakata A., Tenda Y., and Terasaki T. Restricted transport of Cyclosporin-A across the blood brain barrier by a multidrug transporter, p-glycoprotein. Biochem Pharmacol 46 (1993) 1096-1099
    • (1993) Biochem Pharmacol , vol.46 , pp. 1096-1099
    • Tsuji, A.1    Tamai, I.2    Sakata, A.3    Tenda, Y.4    Terasaki, T.5
  • 18
    • 0027418815 scopus 로고
    • Human P-Glycoprotein transports Cyclosporin-A and FK506
    • Saeki T., Ueda K., Tanigawara Y., Hori R., and Komano T. Human P-Glycoprotein transports Cyclosporin-A and FK506. J Biol Chem 268 (1993) 6077-6080
    • (1993) J Biol Chem , vol.268 , pp. 6077-6080
    • Saeki, T.1    Ueda, K.2    Tanigawara, Y.3    Hori, R.4    Komano, T.5
  • 19
    • 0032322661 scopus 로고    scopus 로고
    • Photoaffinity labeling of human P-glycoprotein: effect of modulator interaction and ATP hydrolysis on substrate binding
    • Dey S., Ramachandra M., Pastan I., Gottesman M.M., and Ambudkar S.V. Photoaffinity labeling of human P-glycoprotein: effect of modulator interaction and ATP hydrolysis on substrate binding. Methods Enzymol 292 (1998) 318-328
    • (1998) Methods Enzymol , vol.292 , pp. 318-328
    • Dey, S.1    Ramachandra, M.2    Pastan, I.3    Gottesman, M.M.4    Ambudkar, S.V.5
  • 20
    • 0033580634 scopus 로고    scopus 로고
    • A single amino acid residue contributes to distinct mechanisms of inhibition of the human multidrug transporter by stereoisomers of the dopamine receptor antagonist flupentixol
    • Dey S., Hafkemeyer P., Pastan I., and Gottesman M.M. A single amino acid residue contributes to distinct mechanisms of inhibition of the human multidrug transporter by stereoisomers of the dopamine receptor antagonist flupentixol. Biochemistry 38 (1999) 6630-6639
    • (1999) Biochemistry , vol.38 , pp. 6630-6639
    • Dey, S.1    Hafkemeyer, P.2    Pastan, I.3    Gottesman, M.M.4
  • 21
    • 0032881342 scopus 로고    scopus 로고
    • The molecular interaction of the high affinity reversal agent XR9576 with P-glycoprotein
    • Martin C., Berridge G., Mistry P., Higgins C., Charlton P., and Callaghan R. The molecular interaction of the high affinity reversal agent XR9576 with P-glycoprotein. Br J Pharmacol 128 (1999) 403-411
    • (1999) Br J Pharmacol , vol.128 , pp. 403-411
    • Martin, C.1    Berridge, G.2    Mistry, P.3    Higgins, C.4    Charlton, P.5    Callaghan, R.6
  • 22
    • 0030697879 scopus 로고    scopus 로고
    • The multi-drug resistance reversal agent SR33557 and modulation of vinca alkaloid binding to P-glycoprotein by an allosteric interaction
    • Martin C., Berridge G., Higgins C.F., and Callaghan R. The multi-drug resistance reversal agent SR33557 and modulation of vinca alkaloid binding to P-glycoprotein by an allosteric interaction. Br J Pharmacol 122 (1997) 765-771
    • (1997) Br J Pharmacol , vol.122 , pp. 765-771
    • Martin, C.1    Berridge, G.2    Higgins, C.F.3    Callaghan, R.4
  • 23
    • 0030069428 scopus 로고    scopus 로고
    • Reversible labeling of a chemosensitizer binding domain of p-glycoprotein with a novel 1,4-dihydropyridine drug transport inhibitor
    • Boer R., Dichtl M., Borchers C., Ulrich W.R., Marecek J.F., Prestwich G.D., et al. Reversible labeling of a chemosensitizer binding domain of p-glycoprotein with a novel 1,4-dihydropyridine drug transport inhibitor. Biochemistry 35 (1996) 1387-1396
    • (1996) Biochemistry , vol.35 , pp. 1387-1396
    • Boer, R.1    Dichtl, M.2    Borchers, C.3    Ulrich, W.R.4    Marecek, J.F.5    Prestwich, G.D.6
  • 24
    • 0028978838 scopus 로고
    • Allosteric regulation of [3H]vinblastine binding to P-glycoprotein of MCF-7 ADR cells by dexniguldipine
    • Ferry D.R., Malkhandi P.J., Russell M.A., and Kerr D.J. Allosteric regulation of [3H]vinblastine binding to P-glycoprotein of MCF-7 ADR cells by dexniguldipine. Biochem Pharmacol 49 (1995) 1851-1861
    • (1995) Biochem Pharmacol , vol.49 , pp. 1851-1861
    • Ferry, D.R.1    Malkhandi, P.J.2    Russell, M.A.3    Kerr, D.J.4
  • 25
    • 0038043182 scopus 로고    scopus 로고
    • Allosteric modulation of human P-glycoprotein. Inhibition of transport by preventing substrate translocation and dissociation
    • Maki N., Hafkemeyer P., and Dey S. Allosteric modulation of human P-glycoprotein. Inhibition of transport by preventing substrate translocation and dissociation. J Biol Chem 278 (2003) 18132-18139
    • (2003) J Biol Chem , vol.278 , pp. 18132-18139
    • Maki, N.1    Hafkemeyer, P.2    Dey, S.3
  • 26
    • 33644538904 scopus 로고    scopus 로고
    • Modulator-induced interference in the functional cross talk between the substrate and the ATP sites of human P-glycoprotein
    • Maki N., Moitra K., Silver C., Ghosh P., Chattopadhyay A., and Dey S. Modulator-induced interference in the functional cross talk between the substrate and the ATP sites of human P-glycoprotein. Biochemistry 45 (2006) 2739-2751
    • (2006) Biochemistry , vol.45 , pp. 2739-2751
    • Maki, N.1    Moitra, K.2    Silver, C.3    Ghosh, P.4    Chattopadhyay, A.5    Dey, S.6
  • 27
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra M., Ambudkar S.V., Chen D., Hrycyna C.A., Dey S., Gottesman M.M., et al. Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 37 (1998) 5010-5019
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6
  • 28
    • 0025246330 scopus 로고
    • Expression of the human multidrug transporter in insect cells by a recombinant baculovirus
    • Germann U.A., Willingham M.C., Pastan I., and Gottesman M.M. Expression of the human multidrug transporter in insect cells by a recombinant baculovirus. Biochemistry 29 (1990) 2295-2303
    • (1990) Biochemistry , vol.29 , pp. 2295-2303
    • Germann, U.A.1    Willingham, M.C.2    Pastan, I.3    Gottesman, M.M.4
  • 29
    • 33744921728 scopus 로고    scopus 로고
    • Bailey JL. New York: Elsevier Publishing Co.; 1967. p. 340-41
  • 30
    • 0032479280 scopus 로고    scopus 로고
    • Mechanism of action of human P-glycoprotein ATPase activity. Photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites
    • Hrycyna C.A., Ramachandra M., Ambudkar S.V., Ko Y.H., Pedersen P.L., Pastan I., et al. Mechanism of action of human P-glycoprotein ATPase activity. Photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites. J Biol Chem 273 (1998) 16631-16634
    • (1998) J Biol Chem , vol.273 , pp. 16631-16634
    • Hrycyna, C.A.1    Ramachandra, M.2    Ambudkar, S.V.3    Ko, Y.H.4    Pedersen, P.L.5    Pastan, I.6
  • 31
    • 0030067789 scopus 로고    scopus 로고
    • Characterization of phosphorylation-defective mutants of human P-glycoprotein expressed in mammalian cells
    • Germann U.A., Chambers T.C., Ambudkar S.V., Licht T., Cardarelli C.O., Pastan I., et al. Characterization of phosphorylation-defective mutants of human P-glycoprotein expressed in mammalian cells. J Biol Chem 271 (1996) 1708-1716
    • (1996) J Biol Chem , vol.271 , pp. 1708-1716
    • Germann, U.A.1    Chambers, T.C.2    Ambudkar, S.V.3    Licht, T.4    Cardarelli, C.O.5    Pastan, I.6
  • 32
    • 0019980821 scopus 로고
    • Inhibition of calmodulin by phenothiazines and related drugs: structure-activity relationships
    • Prozialeck W.C., and Weiss B. Inhibition of calmodulin by phenothiazines and related drugs: structure-activity relationships. J Pharmacol Exp Ther 222 (1982) 509-516
    • (1982) J Pharmacol Exp Ther , vol.222 , pp. 509-516
    • Prozialeck, W.C.1    Weiss, B.2
  • 33
    • 0021682498 scopus 로고
    • Interaction of quaternary phenothiazine salts with calmodulin
    • Prozialeck W.C. Interaction of quaternary phenothiazine salts with calmodulin. J Pharmacol Exp Ther 231 (1984) 473-479
    • (1984) J Pharmacol Exp Ther , vol.231 , pp. 473-479
    • Prozialeck, W.C.1
  • 34
    • 0028818393 scopus 로고
    • Partial inhibition of multidrug resistance by safingol is independent of modulation of P-glycoprotein substrate activities and correlated with inhibition of protein kinase C
    • Sachs C.W., Safa A.R., Harrison S.D., and Fine R.L. Partial inhibition of multidrug resistance by safingol is independent of modulation of P-glycoprotein substrate activities and correlated with inhibition of protein kinase C. J Biol Chem 270 (1995) 26639-26648
    • (1995) J Biol Chem , vol.270 , pp. 26639-26648
    • Sachs, C.W.1    Safa, A.R.2    Harrison, S.D.3    Fine, R.L.4
  • 35
    • 0029683163 scopus 로고    scopus 로고
    • Interaction of P-glycoprotein with protein kinase C in human multidrug resistant carcinoma cells
    • Yang J.M., Chin K.V., and Hait W.N. Interaction of P-glycoprotein with protein kinase C in human multidrug resistant carcinoma cells. Cancer Res 56 (1996) 3490-3494
    • (1996) Cancer Res , vol.56 , pp. 3490-3494
    • Yang, J.M.1    Chin, K.V.2    Hait, W.N.3
  • 36
    • 0030800860 scopus 로고    scopus 로고
    • Phosphorylation site mutations in the human multidrug transporter modulate its drug-stimulated ATPase activity
    • Szabo K., Bakos E., Welker E., Muller M., Goodfellow H.R., Higgins C.F., et al. Phosphorylation site mutations in the human multidrug transporter modulate its drug-stimulated ATPase activity. J Biol Chem 272 (1997) 23165-23171
    • (1997) J Biol Chem , vol.272 , pp. 23165-23171
    • Szabo, K.1    Bakos, E.2    Welker, E.3    Muller, M.4    Goodfellow, H.R.5    Higgins, C.F.6
  • 37
    • 0029011872 scopus 로고
    • Functional modulation of multidrug resistance-related P-glycoprotein by Ca(2+)-calmodulin
    • Schlemmer S.R., Yang C.H., and Sirotnak F.M. Functional modulation of multidrug resistance-related P-glycoprotein by Ca(2+)-calmodulin. J Biol Chem 270 (1995) 11040-11042
    • (1995) J Biol Chem , vol.270 , pp. 11040-11042
    • Schlemmer, S.R.1    Yang, C.H.2    Sirotnak, F.M.3
  • 38
    • 0026662530 scopus 로고
    • Partial purification and reconstitution of the human multidrug-resistance pump-characterization of the drug-stimulatable ATP hydrolysis
    • Ambudkar S.V., Lelong I.H., Zhang J.P., Cardarelli C.O., Gottesman M.M., and Pastan I. Partial purification and reconstitution of the human multidrug-resistance pump-characterization of the drug-stimulatable ATP hydrolysis. Proc Natl Acad Sci USA 89 (1992) 8472-8476
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8472-8476
    • Ambudkar, S.V.1    Lelong, I.H.2    Zhang, J.P.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166 (1987) 368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 40
    • 0028028295 scopus 로고
    • Reversal of multidrug resistance in murine fibrosarcoma cells by thioxanthene flupentixol
    • Fan D., Poste G., Seid C., Earnest L.E., Bull T., Clyne R.K., et al. Reversal of multidrug resistance in murine fibrosarcoma cells by thioxanthene flupentixol. Invest New Drugs 12 (1994) 185-195
    • (1994) Invest New Drugs , vol.12 , pp. 185-195
    • Fan, D.1    Poste, G.2    Seid, C.3    Earnest, L.E.4    Bull, T.5    Clyne, R.K.6
  • 41
    • 0031012175 scopus 로고    scopus 로고
    • Chemosensitization of cancer cells by the staurosporine derivative CGP 41251 in association with decreased P-glycoprotein phosphorylation
    • Beltran P.J., Fan D., Fidler I.J., and O'Brian C.A. Chemosensitization of cancer cells by the staurosporine derivative CGP 41251 in association with decreased P-glycoprotein phosphorylation. Biochem Pharmacol 53 (1997) 245-247
    • (1997) Biochem Pharmacol , vol.53 , pp. 245-247
    • Beltran, P.J.1    Fan, D.2    Fidler, I.J.3    O'Brian, C.A.4
  • 42
    • 0026512425 scopus 로고
    • Rational design and pre-clinical pharmacology of drugs for reversing multidrug resistance
    • Hait W.N., and Aftab D.T. Rational design and pre-clinical pharmacology of drugs for reversing multidrug resistance. Biochem Pharmacol 43 (1992) 103-107
    • (1992) Biochem Pharmacol , vol.43 , pp. 103-107
    • Hait, W.N.1    Aftab, D.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.