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Volumn 1853, Issue 10, 2015, Pages 2361-2370

Revealing the fate of cell surface human P-glycoprotein (ABCB1): The lysosomal degradation pathway

Author keywords

Degradation; Endosome; Half life; Lysosome; P glycoprotein; Proteasome

Indexed keywords

BAFILOMYCIN A1; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CELL SURFACE PROTEIN; LACTACYSTIN; MULTIDRUG RESISTANCE PROTEIN 1; RHODAMINE 123; ABCB1 PROTEIN, HUMAN; ANTIFUNGAL AGENT; MACROLIDE; MULTIDRUG RESISTANCE PROTEIN; PROTEASOME INHIBITOR;

EID: 84938125626     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.06.001     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: role of ATP-dependent transporters
    • Gottesman M.M., Fojo T., Bates S.E. Multidrug resistance in cancer: role of ATP-dependent transporters. Nat. Rev. Cancer 2002, 2:48-58.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 2
    • 0036176510 scopus 로고    scopus 로고
    • Mechanisms of cancer drug resistance
    • Gottesman M.M. Mechanisms of cancer drug resistance. Annu. Rev. Med. 2002, 53:615-627.
    • (2002) Annu. Rev. Med. , vol.53 , pp. 615-627
    • Gottesman, M.M.1
  • 3
    • 33644840984 scopus 로고    scopus 로고
    • The power of the pump: mechanisms of action of P-glycoprotein (ABCB1)
    • Ambudkar S.V., Kim I.W., Sauna Z.E. The power of the pump: mechanisms of action of P-glycoprotein (ABCB1). Eur. J. Pharm. Sci. 2006, 27:392-400.
    • (2006) Eur. J. Pharm. Sci. , vol.27 , pp. 392-400
    • Ambudkar, S.V.1    Kim, I.W.2    Sauna, Z.E.3
  • 6
    • 0141994817 scopus 로고    scopus 로고
    • Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein
    • Loo T.W., Bartlett M.C., Clarke D.M. Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein. J. Biol. Chem. 2003, 278:39706-39710.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39706-39710
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 7
    • 27144451192 scopus 로고    scopus 로고
    • Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: evidence for simultaneous binding of both drugs
    • Lugo M.R., Sharom F.J. Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: evidence for simultaneous binding of both drugs. Biochemistry 2005, 44:14020-14029.
    • (2005) Biochemistry , vol.44 , pp. 14020-14029
    • Lugo, M.R.1    Sharom, F.J.2
  • 8
    • 84871685846 scopus 로고    scopus 로고
    • Two ATPases
    • Senior A.E. Two ATPases. J. Biol. Chem. 2012, 287:30049-30062.
    • (2012) J. Biol. Chem. , vol.287 , pp. 30049-30062
    • Senior, A.E.1
  • 10
    • 34249679271 scopus 로고    scopus 로고
    • ABC transporters and drug resistance in leukemia: was P-gp nothing but the first head of the Hydra?
    • Steinbach D., Legrand O. ABC transporters and drug resistance in leukemia: was P-gp nothing but the first head of the Hydra?. Leukemia 2007, 21:1172-1176.
    • (2007) Leukemia , vol.21 , pp. 1172-1176
    • Steinbach, D.1    Legrand, O.2
  • 11
    • 84864050140 scopus 로고    scopus 로고
    • Analysis of the interaction of induction regimens with p-glycoprotein expression in patients with acute myeloid leukaemia: results from the MRC AML15 trial
    • Pallis M., Hills R., White P., Grundy M., Russell N., Burnett A. Analysis of the interaction of induction regimens with p-glycoprotein expression in patients with acute myeloid leukaemia: results from the MRC AML15 trial. Blood Cancer J. 2011, 1:e23.
    • (2011) Blood Cancer J. , vol.1 , pp. e23
    • Pallis, M.1    Hills, R.2    White, P.3    Grundy, M.4    Russell, N.5    Burnett, A.6
  • 13
    • 0025914062 scopus 로고
    • Multidrug resistance (mdr1) gene expression in adult acute leukemias: correlations with treatment outcome and in vitro drug sensitivity
    • Marie J.P., Zittoun R., Sikic B.I. Multidrug resistance (mdr1) gene expression in adult acute leukemias: correlations with treatment outcome and in vitro drug sensitivity. Blood 1991, 78:586-592.
    • (1991) Blood , vol.78 , pp. 586-592
    • Marie, J.P.1    Zittoun, R.2    Sikic, B.I.3
  • 15
    • 0026602155 scopus 로고
    • Clinical significance of multidrug resistance P-glycoprotein expression on acute nonlymphoblastic leukemia cells at diagnosis
    • Campos L., Guyotat D., Archimbaud E., Calmard-Oriol P., Tsuruo T., Troncy J., Treille D., Fiere D. Clinical significance of multidrug resistance P-glycoprotein expression on acute nonlymphoblastic leukemia cells at diagnosis. Blood 1992, 79:473-476.
    • (1992) Blood , vol.79 , pp. 473-476
    • Campos, L.1    Guyotat, D.2    Archimbaud, E.3    Calmard-Oriol, P.4    Tsuruo, T.5    Troncy, J.6    Treille, D.7    Fiere, D.8
  • 16
    • 0026699910 scopus 로고
    • Relevance of mdr1 gene expression in acute myeloid leukemia and comparison of different diagnostic methods
    • Zhou D.C., Marie J.P., Suberville A.M., Zittoun R. Relevance of mdr1 gene expression in acute myeloid leukemia and comparison of different diagnostic methods. Leukemia 1992, 6:879-885.
    • (1992) Leukemia , vol.6 , pp. 879-885
    • Zhou, D.C.1    Marie, J.P.2    Suberville, A.M.3    Zittoun, R.4
  • 17
    • 0028244591 scopus 로고
    • P-glycoprotein expression on acute myeloid leukaemia blast cells at diagnosis predicts response to chemotherapy and survival
    • Wood P., Burgess R., MacGregor A., Yin J.A. P-glycoprotein expression on acute myeloid leukaemia blast cells at diagnosis predicts response to chemotherapy and survival. Br. J. Haematol. 1994, 87:509-514.
    • (1994) Br. J. Haematol. , vol.87 , pp. 509-514
    • Wood, P.1    Burgess, R.2    MacGregor, A.3    Yin, J.A.4
  • 18
    • 0028178091 scopus 로고
    • P-glycoprotein expression as unfavorable prognostic factor in acute myeloid leukemia
    • Zochbauer S., Gsur A., Brunner R., Kyrle P.A., Lechner K., Pirker R. P-glycoprotein expression as unfavorable prognostic factor in acute myeloid leukemia. Leukemia 1994, 8:974-977.
    • (1994) Leukemia , vol.8 , pp. 974-977
    • Zochbauer, S.1    Gsur, A.2    Brunner, R.3    Kyrle, P.A.4    Lechner, K.5    Pirker, R.6
  • 20
    • 78649834084 scopus 로고    scopus 로고
    • Exploring the P-glycoprotein binding cavity with polyoxyethylene alkyl ethers
    • Li-Blatter X., Seelig A. Exploring the P-glycoprotein binding cavity with polyoxyethylene alkyl ethers. Biophys. J. 2010, 99:3589-3598.
    • (2010) Biophys. J. , vol.99 , pp. 3589-3598
    • Li-Blatter, X.1    Seelig, A.2
  • 21
    • 73649111071 scopus 로고    scopus 로고
    • Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1
    • Gutmann D.A., Ward A., Urbatsch I.L., Chang G., van Veen H.W. Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1. Trends Biochem. Sci. 2010, 35:36-42.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 36-42
    • Gutmann, D.A.1    Ward, A.2    Urbatsch, I.L.3    Chang, G.4    van Veen, H.W.5
  • 22
    • 84856271899 scopus 로고    scopus 로고
    • The P-glycoprotein multidrug transporter
    • Sharom F.J. The P-glycoprotein multidrug transporter. Essays Biochem. 2011, 50:161-178.
    • (2011) Essays Biochem. , vol.50 , pp. 161-178
    • Sharom, F.J.1
  • 23
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoprotein-mediated multidrug resistance
    • Endicott J.A., Ling V. The biochemistry of P-glycoprotein-mediated multidrug resistance. Annu. Rev. Biochem. 1989, 58:137-171.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 137-171
    • Endicott, J.A.1    Ling, V.2
  • 24
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: implications for metabolism
    • Mizushima N., Klionsky D.J. Protein turnover via autophagy: implications for metabolism. Annu. Rev. Nutr. 2007, 27:19-40.
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 26
    • 13944258097 scopus 로고    scopus 로고
    • Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells
    • Bright N.A., Gratian M.J., Luzio J.P. Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells. Curr. Biol. 2005, 15:360-365.
    • (2005) Curr. Biol. , vol.15 , pp. 360-365
    • Bright, N.A.1    Gratian, M.J.2    Luzio, J.P.3
  • 27
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • Smalle J., Vierstra R.D. The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 2004, 55:555-590.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 28
    • 14144255733 scopus 로고    scopus 로고
    • Lysosomal storage disorders
    • Vellodi A. Lysosomal storage disorders. Br. J. Haematol. 2005, 128:413-431.
    • (2005) Br. J. Haematol. , vol.128 , pp. 413-431
    • Vellodi, A.1
  • 29
    • 0021040946 scopus 로고
    • Lysosomes revisited
    • de Duve C. Lysosomes revisited. Eur. J. Biochem. 1983, 137:391-397.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 391-397
    • de Duve, C.1
  • 30
    • 0030137994 scopus 로고    scopus 로고
    • Intracellular trafficking of lysosomal membrane proteins
    • Hunziker W., Geuze H.J. Intracellular trafficking of lysosomal membrane proteins. Bioessays 1996, 18:379-389.
    • (1996) Bioessays , vol.18 , pp. 379-389
    • Hunziker, W.1    Geuze, H.J.2
  • 31
    • 62949097187 scopus 로고    scopus 로고
    • Delivery of endocytosed membrane proteins to the lysosome
    • Pryor P.R., Luzio J.P. Delivery of endocytosed membrane proteins to the lysosome. Biochim. Biophys. Acta 2009, 1793:615-624.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 615-624
    • Pryor, P.R.1    Luzio, J.P.2
  • 33
    • 0028172728 scopus 로고
    • Modulation of adriamycin accumulation and efflux by flavonoids in HCT-15 colon cells. Activation of P-glycoprotein as a putative mechanism
    • Critchfield J.W., Welsh C.J., Phang J.M., Yeh G.C. Modulation of adriamycin accumulation and efflux by flavonoids in HCT-15 colon cells. Activation of P-glycoprotein as a putative mechanism. Biochem. Pharmacol. 1994, 48:1437-1445.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1437-1445
    • Critchfield, J.W.1    Welsh, C.J.2    Phang, J.M.3    Yeh, G.C.4
  • 36
    • 84855998504 scopus 로고    scopus 로고
    • Use of baculovirus BacMam vectors for expression of ABC drug transporters in mammalian cells
    • Shukla S., Schwartz C., Kapoor K., Kouanda A., Ambudkar S.V. Use of baculovirus BacMam vectors for expression of ABC drug transporters in mammalian cells. Drug Metab. Dispos. 2012, 40:304-312.
    • (2012) Drug Metab. Dispos. , vol.40 , pp. 304-312
    • Shukla, S.1    Schwartz, C.2    Kapoor, K.3    Kouanda, A.4    Ambudkar, S.V.5
  • 37
    • 0034142125 scopus 로고    scopus 로고
    • Functional characterization of glycosylation-deficient human P-glycoprotein using a vaccinia virus expression system
    • Gribar J.J., Ramachandra M., Hrycyna C.A., Dey S., Ambudkar S.V. Functional characterization of glycosylation-deficient human P-glycoprotein using a vaccinia virus expression system. J. Membr. Biol. 2000, 173:203-214.
    • (2000) J. Membr. Biol. , vol.173 , pp. 203-214
    • Gribar, J.J.1    Ramachandra, M.2    Hrycyna, C.A.3    Dey, S.4    Ambudkar, S.V.5
  • 38
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • Skach W.R., Calayag M.C., Lingappa V.R. Evidence for an alternate model of human P-glycoprotein structure and biogenesis. J. Biol. Chem. 1993, 268:6903-6908.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6903-6908
    • Skach, W.R.1    Calayag, M.C.2    Lingappa, V.R.3
  • 39
    • 77954888748 scopus 로고    scopus 로고
    • Pim-1 kinase protects P-glycoprotein from degradation and enables its glycosylation and cell surface expression
    • Xie Y., Burcu M., Linn D.E., Qiu Y., Baer M.R. Pim-1 kinase protects P-glycoprotein from degradation and enables its glycosylation and cell surface expression. Mol. Pharmacol. 2010, 78:310-318.
    • (2010) Mol. Pharmacol. , vol.78 , pp. 310-318
    • Xie, Y.1    Burcu, M.2    Linn, D.E.3    Qiu, Y.4    Baer, M.R.5
  • 40
    • 0037108987 scopus 로고    scopus 로고
    • Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation
    • Hirsch J.D., Eslamizar L., Filanoski B.J., Malekzadeh N., Haugland R.P., Beechem J.M., Haugland R.P. Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation. Anal. Biochem. 2002, 308:343-357.
    • (2002) Anal. Biochem. , vol.308 , pp. 343-357
    • Hirsch, J.D.1    Eslamizar, L.2    Filanoski, B.J.3    Malekzadeh, N.4    Haugland, R.P.5    Beechem, J.M.6    Haugland, R.P.7
  • 41
    • 47749105733 scopus 로고    scopus 로고
    • Protein-protein interaction detection in vitro and in cells by proximity biotinylation
    • Fernandez-Suarez M., Chen T.S., Ting A.Y. Protein-protein interaction detection in vitro and in cells by proximity biotinylation. J. Am. Chem. Soc. 2008, 130:9251-9253.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9251-9253
    • Fernandez-Suarez, M.1    Chen, T.S.2    Ting, A.Y.3
  • 42
    • 0011913143 scopus 로고
    • Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman E.J., Siebers A., Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. U. S. A. 1988, 85:7972-7976.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 43
    • 0024991786 scopus 로고
    • Kinetic studies of chromaffin granule H+-ATPase and effects of bafilomycin A1
    • Hanada H., Moriyama Y., Maeda M., Futai M. Kinetic studies of chromaffin granule H+-ATPase and effects of bafilomycin A1. Biochem. Biophys. Res. Commun. 1990, 170:873-878.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 873-878
    • Hanada, H.1    Moriyama, Y.2    Maeda, M.3    Futai, M.4
  • 44
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: valuable new tools for cell biologists
    • Lee D.H., Goldberg A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 1998, 8:397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 45
    • 0026046284 scopus 로고
    • Ammonium chloride, an inhibitor of phagosome-lysosome fusion in macrophages, concurrently induces phagosome-endosome fusion, and opens a novel pathway: studies of a pathogenic mycobacterium and a nonpathogenic yeast
    • Hart P.D., Young M.R. Ammonium chloride, an inhibitor of phagosome-lysosome fusion in macrophages, concurrently induces phagosome-endosome fusion, and opens a novel pathway: studies of a pathogenic mycobacterium and a nonpathogenic yeast. J. Exp. Med. 1991, 174:881-889.
    • (1991) J. Exp. Med. , vol.174 , pp. 881-889
    • Hart, P.D.1    Young, M.R.2
  • 46
    • 78650122336 scopus 로고    scopus 로고
    • Dynamic vs static ABCG2 inhibitors to sensitize drug resistant cancer cells
    • Peng H., Qi J., Dong Z., Zhang J.T. Dynamic vs static ABCG2 inhibitors to sensitize drug resistant cancer cells. PLoS One 2010, 5:e15276.
    • (2010) PLoS One , vol.5 , pp. e15276
    • Peng, H.1    Qi, J.2    Dong, Z.3    Zhang, J.T.4


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