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Volumn 25, Issue 6, 2009, Pages 417-423

Affibody-mediated retention of the epidermal growth factor receptor in the secretory compartments leads to inhibition of phosphorylation in the kinase domain

Author keywords

[No Author keywords available]

Indexed keywords

CELL LYSATES; CELL SURFACES; EPIDERMAL GROWTH FACTOR RECEPTORS; FLUORESCENT STAINING; HIGH AFFINITY; KINASE DOMAINS; LOCALISATION; PROLIFERATION RATE; SPECIFIC INTERACTION; SURFACE DEPLETION;

EID: 70449523599     PISSN: 18716784     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbt.2009.02.001     Document Type: Article
Times cited : (6)

References (38)
  • 1
    • 0037429737 scopus 로고    scopus 로고
    • Epidermal growth factor receptor: mechanisms of activation and signalling
    • Jorissen R.N., et al. Epidermal growth factor receptor: mechanisms of activation and signalling. Exp. Cell Res. 284 (2003) 31-53
    • (2003) Exp. Cell Res. , vol.284 , pp. 31-53
    • Jorissen, R.N.1
  • 2
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: the complexity of targeted inhibitors
    • Hynes N.E., and Lane H.A. ERBB receptors and cancer: the complexity of targeted inhibitors. Nat. Rev. Cancer 5 (2005) 341-354
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 3
    • 0034773992 scopus 로고    scopus 로고
    • The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities
    • Yarden Y. The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities. Eur. J. Cancer 37 Suppl. 4 (2001) S3-8
    • (2001) Eur. J. Cancer , vol.37 , Issue.SUPPL. 4
    • Yarden, Y.1
  • 5
    • 11244258222 scopus 로고    scopus 로고
    • Epidermal growth factor receptor inhibition strategies in oncology
    • Harari P.M. Epidermal growth factor receptor inhibition strategies in oncology. Endocr. Relat. Cancer 11 (2004) 689-708
    • (2004) Endocr. Relat. Cancer , vol.11 , pp. 689-708
    • Harari, P.M.1
  • 7
    • 28444468144 scopus 로고    scopus 로고
    • EGFR inhibitors: what have we learned from the treatment of lung cancer?
    • Giaccone G., and Rodriguez J.A. EGFR inhibitors: what have we learned from the treatment of lung cancer?. Nat. Clin. Pract. Oncol. 2 (2005) 554-561
    • (2005) Nat. Clin. Pract. Oncol. , vol.2 , pp. 554-561
    • Giaccone, G.1    Rodriguez, J.A.2
  • 8
    • 0141521636 scopus 로고    scopus 로고
    • Intrabody and intrakine strategies for molecular therapy
    • Wheeler Y.Y., Chen S.Y., and Sane D.C. Intrabody and intrakine strategies for molecular therapy. Mol. Ther. 8 (2003) 355-366
    • (2003) Mol. Ther. , vol.8 , pp. 355-366
    • Wheeler, Y.Y.1    Chen, S.Y.2    Sane, D.C.3
  • 9
    • 41849131453 scopus 로고    scopus 로고
    • RNA and transcriptional modulation of gene expression
    • Hawkins P.G., and Morris K.V. RNA and transcriptional modulation of gene expression. Cell Cycle 7 (2008) 602-607
    • (2008) Cell Cycle , vol.7 , pp. 602-607
    • Hawkins, P.G.1    Morris, K.V.2
  • 10
    • 3242707674 scopus 로고    scopus 로고
    • Intracellular antibodies as specific reagents for functional ablation: future therapeutic molecules
    • Lobato M.N., and Rabbitts T.H. Intracellular antibodies as specific reagents for functional ablation: future therapeutic molecules. Curr. Mol. Med. 4 (2004) 519-528
    • (2004) Curr. Mol. Med. , vol.4 , pp. 519-528
    • Lobato, M.N.1    Rabbitts, T.H.2
  • 11
    • 22544471858 scopus 로고    scopus 로고
    • Intrabodies as drug discovery tools and therapeutics
    • Stocks M. Intrabodies as drug discovery tools and therapeutics. Curr. Opin. Chem. Biol. 9 (2005) 359-365
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 359-365
    • Stocks, M.1
  • 12
    • 33947315300 scopus 로고    scopus 로고
    • Blocking translocation of cell surface molecules from the ER to the cell surface by intracellular antibodies targeted to the ER
    • Boldicke T. Blocking translocation of cell surface molecules from the ER to the cell surface by intracellular antibodies targeted to the ER. J. Cell. Mol. Med. 11 (2007) 54-70
    • (2007) J. Cell. Mol. Med. , vol.11 , pp. 54-70
    • Boldicke, T.1
  • 13
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S., and Pelham H.R. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48 (1987) 899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 14
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis M.J., and Pelham H.R. A human homologue of the yeast HDEL receptor. Nature 348 (1990) 162-163
    • (1990) Nature , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.2
  • 15
    • 0141429975 scopus 로고    scopus 로고
    • The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus
    • Cabrera M., et al. The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus. Mol. Biol. Cell 14 (2003) 4114-4125
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4114-4125
    • Cabrera, M.1
  • 16
    • 33646261864 scopus 로고    scopus 로고
    • Tumor imaging using a picomolar affinity HER2 binding affibody molecule
    • Orlova A., et al. Tumor imaging using a picomolar affinity HER2 binding affibody molecule. Cancer Res. 66 (2006) 4339-4348
    • (2006) Cancer Res. , vol.66 , pp. 4339-4348
    • Orlova, A.1
  • 17
    • 50949094371 scopus 로고    scopus 로고
    • Affinity-based entrapment of the HER2 receptor in the endoplasmic reticulum using an affibody molecule
    • Vernet E., et al. Affinity-based entrapment of the HER2 receptor in the endoplasmic reticulum using an affibody molecule. J. Immunol. Methods 338 (2008) 1-6
    • (2008) J. Immunol. Methods , vol.338 , pp. 1-6
    • Vernet, E.1
  • 18
    • 70449525168 scopus 로고    scopus 로고
    • Phage display selection of Affibody molecules with specific binding to the extracellular domain of the epidermal growth factor receptor
    • Friedman M., et al. Phage display selection of Affibody molecules with specific binding to the extracellular domain of the epidermal growth factor receptor. Protein Eng. Des. Sel. 23 (2007) 23
    • (2007) Protein Eng. Des. Sel. , vol.23 , pp. 23
    • Friedman, M.1
  • 19
    • 39149087035 scopus 로고    scopus 로고
    • Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule
    • Friedman M., et al. Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule. J. Mol. Biol. 376 (2008) 1388-1402
    • (2008) J. Mol. Biol. , vol.376 , pp. 1388-1402
    • Friedman, M.1
  • 20
    • 43849098417 scopus 로고    scopus 로고
    • In vivo and in vitro uptake of 111In, delivered with the affibody molecule (ZEGFR:955)2, in EGFR expressing tumour cells
    • Nordberg E., et al. In vivo and in vitro uptake of 111In, delivered with the affibody molecule (ZEGFR:955)2, in EGFR expressing tumour cells. Oncol. Rep. 19 (2008) 853-857
    • (2008) Oncol. Rep. , vol.19 , pp. 853-857
    • Nordberg, E.1
  • 21
    • 0034658319 scopus 로고    scopus 로고
    • Comparative analysis of genetically modified dendritic cells and tumor cells as therapeutic cancer vaccines
    • Klein C., Bueler H., and Mulligan R.C. Comparative analysis of genetically modified dendritic cells and tumor cells as therapeutic cancer vaccines. J. Exp. Med. 191 (2000) 1699-1708
    • (2000) J. Exp. Med. , vol.191 , pp. 1699-1708
    • Klein, C.1    Bueler, H.2    Mulligan, R.C.3
  • 22
    • 0032717780 scopus 로고    scopus 로고
    • Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling
    • Gunneriusson E., et al. Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling. Protein Eng. 12 (1999) 873-878
    • (1999) Protein Eng. , vol.12 , pp. 873-878
    • Gunneriusson, E.1
  • 23
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain
    • Nord K., et al. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nat. Biotechnol. 15 (1997) 772-777
    • (1997) Nat. Biotechnol. , vol.15 , pp. 772-777
    • Nord, K.1
  • 24
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 25
    • 3142693955 scopus 로고    scopus 로고
    • Intracellular antibodies for proteomics
    • Visintin M., et al. Intracellular antibodies for proteomics. J. Immunol. Methods 290 (2004) 135-153
    • (2004) J. Immunol. Methods , vol.290 , pp. 135-153
    • Visintin, M.1
  • 26
    • 0029812091 scopus 로고    scopus 로고
    • Intracellular expression of a single-chain antibody directed to the EGFR leads to growth inhibition of tumor cells
    • Jannot C.B., et al. Intracellular expression of a single-chain antibody directed to the EGFR leads to growth inhibition of tumor cells. Oncogene 13 (1996) 275-282
    • (1996) Oncogene , vol.13 , pp. 275-282
    • Jannot, C.B.1
  • 27
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta D., et al. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 16 (1997) 1647-1655
    • (1997) EMBO J. , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1
  • 28
    • 0346220285 scopus 로고    scopus 로고
    • Intradiabodies, bispecific, tetravalent antibodies for the simultaneous functional knockout of two cell surface receptors
    • Jendreyko N., et al. Intradiabodies, bispecific, tetravalent antibodies for the simultaneous functional knockout of two cell surface receptors. J. Biol. Chem. 278 (2003) 47812-47819
    • (2003) J. Biol. Chem. , vol.278 , pp. 47812-47819
    • Jendreyko, N.1
  • 29
    • 20444391361 scopus 로고    scopus 로고
    • Phenotypic knockout of VEGF-R2 and Tie-2 with an intradiabody reduces tumor growth and angiogenesis in vivo
    • Jendreyko N., et al. Phenotypic knockout of VEGF-R2 and Tie-2 with an intradiabody reduces tumor growth and angiogenesis in vivo. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 8293-8298
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8293-8298
    • Jendreyko, N.1
  • 30
    • 0028823802 scopus 로고
    • Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2
    • Beerli R.R., et al. Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2. Mol. Cell. Biol. 15 (1995) 6496-6505
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6496-6505
    • Beerli, R.R.1
  • 31
    • 0028893444 scopus 로고
    • Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling
    • Graus-Porta D., Beerli R.R., and Hynes N.E. Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling. Mol. Cell. Biol. 15 (1995) 1182-1191
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1182-1191
    • Graus-Porta, D.1    Beerli, R.R.2    Hynes, N.E.3
  • 32
    • 34247348232 scopus 로고    scopus 로고
    • Role of epidermal growth factor and ErbB2 receptors in 3T3-L1 adipogenesis
    • Harrington M., Pond-Tor S., and Boney C.M. Role of epidermal growth factor and ErbB2 receptors in 3T3-L1 adipogenesis. Obesity (Silver Spring) 15 (2007) 563-571
    • (2007) Obesity (Silver Spring) , vol.15 , pp. 563-571
    • Harrington, M.1    Pond-Tor, S.2    Boney, C.M.3
  • 33
    • 0033543544 scopus 로고    scopus 로고
    • The role of individual SH2 domains in mediating association of phospholipase C-gamma1 with the activated EGF receptor
    • Chattopadhyay A., et al. The role of individual SH2 domains in mediating association of phospholipase C-gamma1 with the activated EGF receptor. J. Biol.Chem. 274 (1999) 26091-26097
    • (1999) J. Biol.Chem. , vol.274 , pp. 26091-26097
    • Chattopadhyay, A.1
  • 34
    • 0032478610 scopus 로고    scopus 로고
    • Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C
    • Marais R., et al. Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C. Science 280 (1998) 109-112
    • (1998) Science , vol.280 , pp. 109-112
    • Marais, R.1
  • 35
    • 54049086648 scopus 로고    scopus 로고
    • HER receptor signaling confers resistance to the insulin-like growth factor-I receptor inhibitor, BMS-536924
    • Haluska P., et al. HER receptor signaling confers resistance to the insulin-like growth factor-I receptor inhibitor, BMS-536924. Mol. Cancer Ther. 7 9 (2008) 2589-2598
    • (2008) Mol. Cancer Ther. , vol.7 , Issue.9 , pp. 2589-2598
    • Haluska, P.1
  • 36
    • 34147130694 scopus 로고    scopus 로고
    • The role of VEGF and EGFR inhibition: implications for combining anti-VEGF and anti-EGFR agents
    • Tabernero J. The role of VEGF and EGFR inhibition: implications for combining anti-VEGF and anti-EGFR agents. Mol. Cancer Res. 5 (2007) 203-220
    • (2007) Mol. Cancer Res. , vol.5 , pp. 203-220
    • Tabernero, J.1
  • 37
    • 21244441508 scopus 로고    scopus 로고
    • A fully human recombinant IgG-like bispecific antibody to both the epidermal growth factor receptor and the insulin-like growth factor receptor for enhanced antitumor activity
    • Lu D., et al. A fully human recombinant IgG-like bispecific antibody to both the epidermal growth factor receptor and the insulin-like growth factor receptor for enhanced antitumor activity. J. Biol. Chem. 280 (2005) 19665-19672
    • (2005) J. Biol. Chem. , vol.280 , pp. 19665-19672
    • Lu, D.1
  • 38
    • 0036498811 scopus 로고    scopus 로고
    • Construction and characterization of affibody-Fc chimeras produced in Escherichia coli
    • Ronnmark J., et al. Construction and characterization of affibody-Fc chimeras produced in Escherichia coli. J. Immunol. Methods 261 (2002) 199-211
    • (2002) J. Immunol. Methods , vol.261 , pp. 199-211
    • Ronnmark, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.