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Volumn 4, Issue 5, 2013, Pages 391-401

Identification Of Caveolin-1 As A Potential Causative Factor In The Generation Of Trastuzumab Resistance In Breast Cancer Cells

Author keywords

Antibody dependent cell mediated cytotoxicity (ADCC); Ec eGFP; ErbB2, Caveolin 1; Internalization; Trastuzumab.

Indexed keywords

CAVEOLIN 1; EPIDERMAL GROWTH FACTOR RECEPTOR 2; LIGAND; PROTEIN TYROSINE KINASE; TRASTUZUMAB;

EID: 84882959371     PISSN: None     EISSN: 18379664     Source Type: Journal    
DOI: 10.7150/jca.6470     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 77953896432 scopus 로고    scopus 로고
    • Cell signalling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. Cell signalling by receptor tyrosine kinases. Cell. 2010; 141: 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 3
    • 33847696075 scopus 로고    scopus 로고
    • Receptor tyrosine kinases: mechanisms of activation and signalling
    • Hubbard R, Miller WT. Receptor tyrosine kinases: mechanisms of activation and signalling. Current Opinion in Cell Biology. 2007; 19: 117-123.
    • (2007) Current Opinion in Cell Biology , vol.19 , pp. 117-123
    • Hubbard, R.1    Miller, W.T.2
  • 5
    • 67649472398 scopus 로고    scopus 로고
    • Novel anticancer targets: revisiting ERBB2 and discovering ERBB3
    • Baselga J, Swain SM. Novel anticancer targets: revisiting ERBB2 and discovering ERBB3. Nature Reviews Cancer. 2009; 9: 463-475.
    • (2009) Nature Reviews Cancer , vol.9 , pp. 463-475
    • Baselga, J.1    Swain, S.M.2
  • 6
    • 0024478054 scopus 로고
    • p185HER2 monoclonal antibody has anti proliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor
    • Hudziak R M, Lewis GD, Winget M, et al. p185HER2 monoclonal antibody has anti proliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor. Molecular Cell Biology. 1989; 9: 1165-1172.
    • (1989) Molecular Cell Biology , vol.9 , pp. 1165-1172
    • Hudziak, R.M.1    Lewis, G.D.2    Winget, M.3
  • 7
    • 0026610881 scopus 로고
    • Humanization of an anti-p185HER2 antibody for human cancer therapy
    • Carter P, Presta L, Gorman CM, Ridgway JB, et al. Humanization of an anti-p185HER2 antibody for human cancer therapy. Proc. Natl. Acad. Sci. 1992; 89: 4285-4289.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 4285-4289
    • Carter, P.1    Presta, L.2    Gorman, C.M.3    Ridgway, J.B.4
  • 8
    • 0033996361 scopus 로고    scopus 로고
    • ErbB2 Potentiates Breast Tumor Proliferation through Modulation of p27 Kip1-Cdk2 Complex Formation: Receptor Over expression Does Not Determine Growth Dependency
    • Lane H A, Beuvink I, Motoyama A B, et al. ErbB2 Potentiates Breast Tumor Proliferation through Modulation of p27 Kip1-Cdk2 Complex Formation: Receptor Over expression Does Not Determine Growth Dependency. Molecular Cell Biology. 2000; 20: 3210- 3223.
    • (2000) Molecular Cell Biology , vol.20 , pp. 3210-3223
    • Lane, H.A.1    Beuvink, I.2    Motoyama, A.B.3
  • 9
    • 65349101151 scopus 로고    scopus 로고
    • Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941
    • Junttila TT, Akita RW, Parsons K, et al. Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. Cancer Cell. 2009; 15: 429-440.
    • (2009) Cancer Cell , vol.15 , pp. 429-440
    • Junttila, T.T.1    Akita, R.W.2    Parsons, K.3
  • 10
    • 0035874981 scopus 로고    scopus 로고
    • Trastuzumab (Herceptin), a Humanized Anti-HER2 Receptor Monoclonal Antibody, Inhibits Basal and Activated HER2 Ectodomain Cleavage in Breast Cancer Cells
    • Molina MA, Codony-servat J, Albanell J, et al. Trastuzumab (Herceptin), a Humanized Anti-HER2 Receptor Monoclonal Antibody, Inhibits Basal and Activated HER2 Ectodomain Cleavage in Breast Cancer Cells. Cancer Research. 2001; 61: 4744 -4749.
    • (2001) Cancer Research , vol.61
    • Molina, M.A.1    Codony-servat, J.2    Albanell, J.3
  • 11
    • 48549094102 scopus 로고    scopus 로고
    • Effector mechanisms of therapeutic antibodies against ErbB receptors
    • Peipp M, Dechant M, Valerius T. Effector mechanisms of therapeutic antibodies against ErbB receptors. Current Opinion in Immunology. 2008; 20: 436-443.
    • (2008) Current Opinion in Immunology , vol.20 , pp. 436-443
    • Peipp, M.1    Dechant, M.2    Valerius, T.3
  • 12
    • 31444451572 scopus 로고    scopus 로고
    • Trastuzumab-based treatment of HER2-positive breast cancer: an antibody-dependent cellular cytotoxicity mechanism?
    • Arnould L, Gelly M, Penault-Llorca F, et al. Trastuzumab-based treatment of HER2-positive breast cancer: an antibody-dependent cellular cytotoxicity mechanism? British Journal of Cancer. 2006; 94: 259- 67.
    • (2006) British Journal of Cancer , vol.94 , pp. 259-67
    • Arnould, L.1    Gelly, M.2    Penault-Llorca, F.3
  • 13
    • 0034076307 scopus 로고    scopus 로고
    • Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets
    • Clynes RA, Towers TL, Presta LG, Ravetch JV. Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets. Nature Medicine. 2000; 6: 443-6.
    • (2000) Nature Medicine , vol.6 , pp. 443-6
    • Clynes, R.A.1    Towers, T.L.2    Presta, LG.3    Ravetch, J.V.4
  • 14
    • 36248988538 scopus 로고    scopus 로고
    • Ligand-dependent responses of the ErbB signaling network: experimental and modeling analyses
    • Birtwistle MR, Hatakeyama M, Yumoto N B, et al. Ligand-dependent responses of the ErbB signaling network: experimental and modeling analyses. Molecular Systems Biology. 2007; 3: 144.
    • (2007) Molecular Systems Biology , vol.3 , pp. 144
    • Birtwistle, M.R.1    Hatakeyama, M.2    Yumoto, N.B.3
  • 15
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin A, Goh LK. Endocytosis and intracellular trafficking of ErbBs. Experimental Cell Research. 2009; 315: 683- 696.
    • (2009) Experimental Cell Research , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 16
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida J, Kraus MH, Alimandi M, et al. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. The Journal of Biological Chemistry. 1996; 271: 5251-7.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 5251-7
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3
  • 17
    • 42449114402 scopus 로고    scopus 로고
    • Endocytic downregulation of ErbB receptors: mechanisms and relevance in cancer
    • Roepstorff K, Grøvdal L, Grandal M, et al. Endocytic downregulation of ErbB receptors: mechanisms and relevance in cancer. Histochemistry and Cell Biology. 2008; 129: 563-578.
    • (2008) Histochemistry and Cell Biology , vol.129 , pp. 563-578
    • Roepstorff, K.1    Grøvdal, L.2    Grandal, M.3
  • 18
    • 39149137183 scopus 로고    scopus 로고
    • Identification of the domain in ErbB2 that restricts ligand-induced degradation
    • Shen F, Lin Q, Childress C, Yang W. Identification of the domain in ErbB2 that restricts ligand-induced degradation. Cellular Signalling. 2008; 20: 779- 86.
    • (2008) Cellular Signalling , vol.20
    • Shen, F.1    Lin, Q.2    Childress, C.3    Yang, W.4
  • 19
    • 1642422374 scopus 로고    scopus 로고
    • Association with Membrane Protrusions Makes ErbB2 an Internalization-resistant Receptor
    • Hommelgaard AM, Lerdrup M, Deurs BV. Association with Membrane Protrusions Makes ErbB2 an Internalization-resistant Receptor. Molecular Biology of the Cell. 2004; 15: 1557-1567.
    • (2004) Molecular Biology of the Cell , vol.15 , pp. 1557-1567
    • Hommelgaard, A.M.1    Lerdrup, M.2    Deurs, BV.3
  • 20
    • 28644439423 scopus 로고    scopus 로고
    • The Inhibitory Effect of ErbB2 on Epidermal Growth Factor-induced Formation of Clathrin-coated Pits Correlates with Retention of Epidermal Growth Factor Receptor-ErbB2 Oligomeric Complexes at the Plasma Membrane
    • Haslekås C, Breen K, Pedersen KW, et al. The Inhibitory Effect of ErbB2 on Epidermal Growth Factor-induced Formation of Clathrin-coated Pits Correlates with Retention of Epidermal Growth Factor Receptor-ErbB2 Oligomeric Complexes at the Plasma Membrane. Molecular Biology of the Cell. 2005; 16: 5832-5842.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 5832-5842
    • Haslekås, C.1    Breen, K.2    Pedersen, K.W.3
  • 21
    • 14544306526 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis of ubiquitinated cargos
    • Sigismund S, Woelk T, Puri C, et al. Clathrin-independent endocytosis of ubiquitinated cargos. Proc. Natl. Acad. Sci. 2005; 102: 2760-2765.
    • (2005) Proc Natl. Acad. Sci. , vol.102 , pp. 2760-2765
    • Sigismund, S.1    Woelk, T.2    Puri, C.3
  • 22
    • 0037145061 scopus 로고    scopus 로고
    • Dimerization and activation of EGF receptor
    • Schlessinger J. Dimerization and activation of EGF receptor. Cell. 2002; 110: 669-672.
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 23
    • 0037112996 scopus 로고    scopus 로고
    • Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2
    • Nagy P, Vereb G, Sebestyén Z, et al. Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2. Journal of Cell Science. 2002; 115: 4251-4262.
    • (2002) Journal of Cell Science , vol.115 , pp. 4251-4262
    • Nagy, P.1    Vereb, G.2    Sebestyén, Z.3
  • 24
    • 78049239930 scopus 로고    scopus 로고
    • Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis
    • Nagy P, Claus J, Jovin TM, Arndt Jovin DJ. Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis. Proc. Natl. Acad. Sci. 2010; 107: 16524-16529.
    • (2010) Proc Natl. Acad. Sci , vol.107 , pp. 16524-16529
    • Nagy, P.1    Claus, J.2    Jovin, T.M.3    Arndt Jovin, D.J.4
  • 25
    • 33644838018 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham M, Parton RG. Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers. Biochimica et Biophysica Acta (BBA)-Biomembranes. 2005; 1746: 350-363.
    • (2005) Biochimica et Biophysica Acta (BBA)-Biomembranes , vol.1746 , pp. 350-363
    • Kirkham, M.1    Parton, R.G.2
  • 26
    • 84880920639 scopus 로고    scopus 로고
    • Flotillins as regulators of ErbB2 levels in breast cancer
    • Pust S, Klokk TI, Musa N, et al. Flotillins as regulators of ErbB2 levels in breast cancer. Oncogene. 2012;: 1-9.
    • (2012) Oncogene , pp. 1-9
    • Pust, S.1    Klokk, TI.2    Musa, N.3
  • 27
    • 9444252957 scopus 로고    scopus 로고
    • Endocytosis and Sorting of ErbB2 and the Site of Action of Cancer Therapeutics Trastuzumab and Geldanamycin
    • Austin CD, Mazie AM, Pisacane PI, et al. Endocytosis and Sorting of ErbB2 and the Site of Action of Cancer Therapeutics Trastuzumab and Geldanamycin. Molecular Biology of the Cell. 2004; 15: 5268-5282.
    • (2004) Molecular Biology of the Cell , vol.15 , pp. 5268-5282
    • Austin, C.D.1    Mazie, A.M.2    Pisacane, P.I.3
  • 28
    • 23844436643 scopus 로고    scopus 로고
    • Caveolae: stable membrane domains with a potential for internalization
    • Hommelgaard AM, Roepstorff K, Vilhardt F. Caveolae: stable membrane domains with a potential for internalization. Traffic. 2005; 6: 720-4.
    • (2005) Traffic , vol.6 , pp. 720-4
    • Hommelgaard, A.M.1    Roepstorff, K.2    Vilhardt, F.3
  • 29
    • 77049128273 scopus 로고    scopus 로고
    • Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis
    • Römer W, Pontani LL, Sorre B, et al. Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis. Cell. 2010; 140: 540-53.
    • (2010) Cell , vol.140 , pp. 540-53
    • Römer, W.1    Pontani, LL.2    Sorre, B.3
  • 30
    • 77954187308 scopus 로고    scopus 로고
    • Caveolin-1 Induces Formation of Membrane Tubules That Sense Actomyosin Tension and Are Inhibited by Polymerase I and Transcript Release Factor/Cavin-1
    • Verma P, Ostermeyer-fay AG, Brown DA. Caveolin-1 Induces Formation of Membrane Tubules That Sense Actomyosin Tension and Are Inhibited by Polymerase I and Transcript Release Factor/Cavin-1. Molecular Biology of Cell. 2010; 21: 2226-2240.
    • (2010) Molecular Biology of Cell , vol.21 , pp. 2226-2240
    • Verma, P.1    Ostermeyer-fay, A.G.2    Brown, D.A.3
  • 32
    • 17344363636 scopus 로고    scopus 로고
    • Reciprocal Regulation of Neu Tyrosine Kinase Activity and Caveolin-1 Protein Expression in Vitro and in Vivo
    • Engelman JA, Lee RJ, Karnezis A, et al. Reciprocal Regulation of Neu Tyrosine Kinase Activity and Caveolin-1 Protein Expression in Vitro and in Vivo. The Journal of Biological Chemistry. 1998; 273: 20448-20455.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 20448-20455
    • Engelman, J.A.1    Lee, R.J.2    Karnezis, A.3
  • 33
    • 4143068213 scopus 로고    scopus 로고
    • Identification of a small peptide that inhibits the phosphorylation of ErbB2 and proliferation of ErbB2 overexpressing breast cancer cells
    • Pero SC, Shukla GS, Armstrong AL, et al. Identification of a small peptide that inhibits the phosphorylation of ErbB2 and proliferation of ErbB2 overexpressing breast cancer cells. International Journal of Cancer. 2004; 111: 951-60.
    • (2004) International Journal of Cancer , vol.111 , pp. 951-60
    • Pero, S.C.1    Shukla, G.S.2    Armstrong, A.L.3
  • 34
    • 44549087930 scopus 로고    scopus 로고
    • Cell type dependent endocytic internalization of ErbB2 with an artificial peptide ligand that binds to ErbB2
    • Hashizume T, Fukuda T, Nagaoka T, et al. Cell type dependent endocytic internalization of ErbB2 with an artificial peptide ligand that binds to ErbB2. Cell Biology International. 2008; 32: 814 -26.
    • (2008) Cell Biology International , vol.32 , pp. 814-26
    • Hashizume, T.1    Fukuda, T.2    Nagaoka, T.3
  • 35
    • 79953793965 scopus 로고    scopus 로고
    • Enhanced internalization of ErbB2 in SK-BR-3 cells with multivalent forms of an artificial ligand
    • Vaidyanath A, Hashizume T, Nagaoka T, et al. Enhanced internalization of ErbB2 in SK-BR-3 cells with multivalent forms of an artificial ligand. Journal of Cellular and Molecular Medicine. 2011; 15: 2525-38.
    • (2011) Journal of Cellular and Molecular Medicine , vol.15 , pp. 2525-38
    • Vaidyanath, A.1    Hashizume, T.2    Nagaoka, T.3
  • 36
    • 55449129956 scopus 로고    scopus 로고
    • Clathrin- independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells
    • Barr DJ, Ostermeyer-Fay AG, Matundan RA, Brown DA. Clathrin-independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells. Journal of Cell Science. 2008; 121: 3155-66.
    • (2008) Journal of Cell Science , vol.121 , pp. 3155-66
    • Barr, D.J.1    Ostermeyer-Fay, A.G.2    Matundan, R.A.3    Brown, D.A.4
  • 37
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • Pelkmans L, Bürli T, Zerial M, Helenius A. Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic. Cell. 2004; 118: 767-780.
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Bürli, T.2    Zerial, M.3    Helenius, A.4
  • 38
    • 33646204681 scopus 로고    scopus 로고
    • Mouse Polyomavirus Enters Early Endosomes, Requires Their Acidic pH for Productive Infection, and Meets Transferrin Cargo in Rab11-Positive Endosomes
    • Liebl D, Difato F, et al. Mouse Polyomavirus Enters Early Endosomes, Requires Their Acidic pH for Productive Infection, and Meets Transferrin Cargo in Rab11-Positive Endosomes. Journal of Virology. 2006; 80: 4610-4622.
    • (2006) Journal of Virology , vol.80 , pp. 4610-4622
    • Liebl, D.1    Difato, F.2
  • 39
    • 27744584125 scopus 로고    scopus 로고
    • Biological properties of a human compact anti-ErbB2 antibody
    • De LC, Cozzolino R, et al. Biological properties of a human compact anti-ErbB2 antibody. Carcinogenesis. 2005; 26: 1890- 1895.
    • (2005) Carcinogenesis , vol.26
    • De, L.C.1    Cozzolino, R.2
  • 41
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature ErbB2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu W, Mimnaugh E, Rosser MF, et al. Sensitivity of mature ErbB2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. The Journal of Biological Chemistry. 2001; 276: 3702-8.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 3702-8
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3
  • 42
    • 40949133268 scopus 로고    scopus 로고
    • Geldanamycin- induced down-regulation of ErbB2 from the plasma membrane is clathrin dependent but proteasomal activity independent
    • Pedersen NM, Madshus IH, Haslekås C, Stang E. Geldanamycin- induced down-regulation of ErbB2 from the plasma membrane is clathrin dependent but proteasomal activity independent. Molecular Cancer Research. 2008; 6: 1-500.
    • (2008) Molecular Cancer Research , vol.6 , pp. 1-500
    • Pedersen, N.M.1    Madshus, I.H.2    Haslekås, C.3    Stang, E.4
  • 44
    • 0038353161 scopus 로고    scopus 로고
    • Caveolin-1 as tumor suppressor gene in breast cancer
    • Hino M, Doihara H, Kobayashi K, et al. Caveolin-1 as tumor suppressor gene in breast cancer. Surgery Today. 2003; 33: 486-90.
    • (2003) Surgery Today , vol.33 , pp. 486-90
    • Hino, M.1    Doihara, H.2    Kobayashi, K.3
  • 45
    • 0032546319 scopus 로고    scopus 로고
    • Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells
    • Lee SW, Reimer CL, Phil Oh, et al. Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells. Oncogene.1998; 16: 1391-1397.
    • (1998) Oncogene , vol.16 , pp. 1391-1397
    • Lee, S.W.1    Reimer, C.L.2    Phil, O.H.3
  • 46
    • 4644345009 scopus 로고    scopus 로고
    • Clinical significance of Caveolin- 1, Caveolin-2 and HER2/neu mRNA expression in human breast cancer
    • Sagara Y, Mimori K, Yoshinaga K, et al. Clinical significance of Caveolin- 1, Caveolin-2 and HER2/neu mRNA expression in human breast cancer. British journal of Cancer. 2004; 91: 959-965.
    • (2004) British journal of Cancer , vol.91 , pp. 959-965
    • Sagara, Y.1    Mimori, K.2    Yoshinaga, K.3
  • 47
    • 28844441371 scopus 로고    scopus 로고
    • Caveolin-1 is down-regulated and inversely correlated with HER2 and EGFR expression status in invasive ductal carcinoma of the breast
    • Park SS, Kim JE, Kim YA, et al. Caveolin-1 is down-regulated and inversely correlated with HER2 and EGFR expression status in invasive ductal carcinoma of the breast. Histopathology. 2005; 47: 625-630.
    • (2005) Histopathology , vol.47 , pp. 625-630
    • Park, S.S.1    Kim, J.E.2    Kim, Y.A.3
  • 49
    • 66749106907 scopus 로고    scopus 로고
    • Stromal cell expression of caveolin- 1 predicts outcome in breast cancer
    • Sloan E K, Ciocca DR, Pouliot N, et al. Stromal cell expression of caveolin- 1 predicts outcome in breast cancer. The American Journal of Pathology. 2009; 174: 2035-43
    • (2009) The American Journal of Pathology , vol.174 , pp. 2035-2043
    • Sloan, E.K.1    Ciocca, D.R.2    Pouliot, N.3


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