메뉴 건너뛰기




Volumn 422, Issue 4, 2012, Pages 532-544

Triepitopic antibody fusions inhibit cetuximab-resistant BRAF and KRAS mutant tumors via EGFR signal repression

Author keywords

cancer; downregulation; ErbB1; fibronectin; multispecific

Indexed keywords

ANTIBODY 10TH TYPE 3 DOMAIN OF HUMAN FIBRONECTIN FUSION PROTEIN; ANTINEOPLASTIC AGENT; B RAF KINASE; CETUXIMAB; EPIDERMAL GROWTH FACTOR RECEPTOR; EPITOPE; K RAS PROTEIN; MEMBRANE FUSION PROTEIN; UNCLASSIFIED DRUG;

EID: 84865513993     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.014     Document Type: Article
Times cited : (35)

References (40)
  • 2
    • 0028955388 scopus 로고
    • Epidermal growth factor-related peptides and their receptors in human malignancies
    • D.S. Salomon, R. Brandt, F. Ciardiello, and N. Normanno Epidermal growth factor-related peptides and their receptors in human malignancies Crit. Rev. Oncol./Hematol. 19 1995 183 232
    • (1995) Crit. Rev. Oncol./Hematol. , vol.19 , pp. 183-232
    • Salomon, D.S.1    Brandt, R.2    Ciardiello, F.3    Normanno, N.4
  • 5
    • 0025838675 scopus 로고
    • Regulators and effectors of ras proteins
    • G. Bollag, and F. McCormick Regulators and effectors of ras proteins Annu. Rev. Cell Biol. 7 1991 601 632
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 601-632
    • Bollag, G.1    McCormick, F.2
  • 6
    • 78650026316 scopus 로고    scopus 로고
    • KRAS and BRAF: Drug targets and predictive biomarkers
    • E. Vakiani, and D.B. Solit KRAS and BRAF: drug targets and predictive biomarkers J. Pathol. 223 2011 219 229
    • (2011) J. Pathol. , vol.223 , pp. 219-229
    • Vakiani, E.1    Solit, D.B.2
  • 7
    • 33646228635 scopus 로고    scopus 로고
    • KRAS mutation status is predictive of response to cetuximab therapy in colorectal cancer
    • A. Lievre, J.B. Bachet, D. Le Corre, V. Boige, B. Landi, and J.F. Emile KRAS mutation status is predictive of response to cetuximab therapy in colorectal cancer Cancer Res. 66 2006 3992 3995
    • (2006) Cancer Res. , vol.66 , pp. 3992-3995
    • Lievre, A.1    Bachet, J.B.2    Le Corre, D.3    Boige, V.4    Landi, B.5    Emile, J.F.6
  • 8
    • 42649145667 scopus 로고    scopus 로고
    • Wild-type KRAS is required for panitumumab efficacy in patients with metastatic colorectal cancer
    • R.G. Amado, M. Wolf, M. Peeters, E. Van Cutsem, S. Siena, and D.J. Freeman Wild-type KRAS is required for panitumumab efficacy in patients with metastatic colorectal cancer J. Clin. Oncol. 26 2008 1626 1634
    • (2008) J. Clin. Oncol. , vol.26 , pp. 1626-1634
    • Amado, R.G.1    Wolf, M.2    Peeters, M.3    Van Cutsem, E.4    Siena, S.5    Freeman, D.J.6
  • 11
    • 76549085643 scopus 로고    scopus 로고
    • Sym004: A novel synergistic anti-epidermal growth factor receptor antibody mixture with superior anticancer efficacy
    • M.W. Pedersen, H.J. Jacobsen, K. Koefoed, A. Hey, C. Pyke, J.S. Haurum, and M. Kragh Sym004: a novel synergistic anti-epidermal growth factor receptor antibody mixture with superior anticancer efficacy Cancer Res. 70 2010 588 597
    • (2010) Cancer Res. , vol.70 , pp. 588-597
    • Pedersen, M.W.1    Jacobsen, H.J.2    Koefoed, K.3    Hey, A.4    Pyke, C.5    Haurum, J.S.6    Kragh, M.7
  • 14
    • 34547457742 scopus 로고    scopus 로고
    • Monobodies: Antibody mimics based on the scaffold of the fibronectin type III domain
    • A. Koide, and S. Koide Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain Methods Mol. Biol. 352 2007 95 109
    • (2007) Methods Mol. Biol. , vol.352 , pp. 95-109
    • Koide, A.1    Koide, S.2
  • 15
    • 84856295686 scopus 로고    scopus 로고
    • Epidermal growth factor receptor downregulation by small heterodimeric binding proteins
    • B.J. Hackel, J.R. Neil, F.M. White, and K.D. Wittrup Epidermal growth factor receptor downregulation by small heterodimeric binding proteins Protein Eng., Des. Sel. 25 2012 47 57
    • (2012) Protein Eng., Des. Sel. , vol.25 , pp. 47-57
    • Hackel, B.J.1    Neil, J.R.2    White, F.M.3    Wittrup, K.D.4
  • 16
    • 0022393612 scopus 로고
    • Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor
    • J. Downward, M.D. Waterfield, and P.J. Parker Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor. Effect on tyrosine kinase activity and ligand binding affinity J. Biol. Chem. 260 1985 14538 14546 (Pubitemid 16210976)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.27 , pp. 14538-14546
    • Downward, J.1    Waterfield, M.D.2    Parker, P.J.3
  • 17
    • 0024316019 scopus 로고
    • All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor
    • B.L. Margolis, I. Lax, R. Kris, M. Dombalagian, A.M. Honegger, and R. Howk All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor J. Biol. Chem. 264 1989 10667 10671 (Pubitemid 19161640)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.18 , pp. 10667-10671
    • Margolis, B.L.1    Lax, I.2    Kris, R.3    Dombalagian, M.4    Honegger, A.M.5    Howk, R.6    Givol, D.7    Ullrich, A.8    Schlessinger, J.9
  • 18
    • 0028970465 scopus 로고
    • C-Src phosphorylates epidermal growth factor receptor on tyrosine 845
    • K. Sato, A. Sato, M. Aoto, and Y. Fukami c-Src phosphorylates epidermal growth factor receptor on tyrosine 845 Biochem. Biophys. Res. Commun. 215 1995 1078 1087
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 1078-1087
    • Sato, K.1    Sato, A.2    Aoto, M.3    Fukami, Y.4
  • 19
    • 0026503685 scopus 로고
    • Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase
    • J.L. Countaway, A.C. Nairn, and R.J. Davis Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase J. Biol. Chem. 267 1992 1129 1140
    • (1992) J. Biol. Chem. , vol.267 , pp. 1129-1140
    • Countaway, J.L.1    Nairn, A.C.2    Davis, R.J.3
  • 21
    • 1642421130 scopus 로고    scopus 로고
    • Target-based agents against ErbB receptors and their ligands: A novel approach to cancer treatment
    • DOI 10.1677/erc.0.0100001
    • N. Normanno, C. Bianco, A. De Luca, M.R. Maiello, and D.S. Salomon Target-based agents against ErbB receptors and their ligands: a novel approach to cancer treatment Endocr.-Relat. Cancer 10 2003 1 21 (Pubitemid 36457237)
    • (2003) Endocrine-Related Cancer , vol.10 , Issue.1 , pp. 1-21
    • Normanno, N.1    Bianco, C.2    De Luca, A.3    Maiello, M.R.4    Salomon, D.S.5
  • 23
    • 36249012382 scopus 로고    scopus 로고
    • EGF-receptor-mediated mammary epithelial cell migration is driven by sustained ERK signaling from autocrine stimulation
    • DOI 10.1242/jcs.010488
    • E.J. Joslin, L.K. Opresko, A. Wells, H.S. Wiley, and D.A. Lauffenburger EGF-receptor-mediated mammary epithelial cell migration is driven by sustained ERK signaling from autocrine stimulation J. Cell Sci. 120 2007 3688 3699 (Pubitemid 350120960)
    • (2007) Journal of Cell Science , vol.120 , Issue.20 , pp. 3688-3699
    • Joslin, E.J.1    Opresko, L.K.2    Wells, A.3    Wiley, H.S.4    Lauffenburger, D.A.5
  • 24
    • 0028819660 scopus 로고
    • Biological efficacy of a chimeric antibody to the epidermal growth factor receptor in a human tumor xenograft model
    • N.I. Goldstein, M. Prewett, K. Zuklys, P. Rockwell, and J. Mendelsohn Biological efficacy of a chimeric antibody to the epidermal growth factor receptor in a human tumor xenograft model Clin. Cancer Res. 1 1995 1311 1318
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1311-1318
    • Goldstein, N.I.1    Prewett, M.2    Zuklys, K.3    Rockwell, P.4    Mendelsohn, J.5
  • 25
    • 17444403242 scopus 로고    scopus 로고
    • Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
    • DOI 10.1016/j.ccr.2005.03.003
    • S. Li, K.R. Schmitz, P.D. Jeffrey, J.J. Wiltzius, P. Kussie, and K.M. Ferguson Structural basis for inhibition of the epidermal growth factor receptor by cetuximab Cancer Cell 7 2005 301 311 (Pubitemid 40544648)
    • (2005) Cancer Cell , vol.7 , Issue.4 , pp. 301-311
    • Li, S.1    Schmitz, K.R.2    Jeffrey, P.D.3    Wiltzius, J.J.W.4    Kussie, P.5    Ferguson, K.M.6
  • 26
    • 70649084992 scopus 로고    scopus 로고
    • The state of the art: Immune-mediated mechanisms of monoclonal antibodies in cancer therapy
    • J. Griggs, and K. Zinkewich-Peotti The state of the art: immune-mediated mechanisms of monoclonal antibodies in cancer therapy Br. J. Cancer 101 2009 1807 1812
    • (2009) Br. J. Cancer , vol.101 , pp. 1807-1812
    • Griggs, J.1    Zinkewich-Peotti, K.2
  • 28
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR
    • R.L. Shields, A.K. Namenuk, K. Hong, Y.G. Meng, J. Rae, and J. Briggs High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR J. Biol. Chem. 276 2001 6591 6604
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6
  • 29
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • A. Sorkin, and L.K. Goh Endocytosis and intracellular trafficking of ErbBs Exp. Cell Res. 315 2009 683 696
    • (2009) Exp. Cell Res. , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 30
    • 25444503249 scopus 로고    scopus 로고
    • Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis
    • DOI 10.1074/jbc.M503833200
    • J.X. Zhu, S. Goldoni, G. Bix, R.T. Owens, D.J. McQuillan, C.C. Reed, and R.V. Iozzo Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis J. Biol. Chem. 280 2005 32468 32479 (Pubitemid 41361859)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32468-32479
    • Zhu, J.-X.1    Goldoni, S.2    Bix, G.3    Owens, R.T.4    McQuillan, D.J.5    Reed, C.6    Iozzo, R.V.7
  • 32
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic ras mutants
    • DOI 10.1126/science.277.5324.333
    • K. Scheffzek, M.R. Ahmadian, W. Kabsch, L. Wiesmuller, A. Lautwein, F. Schmitz, and A. Wittinghofer The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants Science 277 1997 333 338 (Pubitemid 27450699)
    • (1997) Science , vol.277 , Issue.5324 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Kabsch, W.3    Wiesmuller, L.4    Lautwein, A.5    Schmitz, F.6    Wittinghofer, A.7
  • 34
    • 48549098958 scopus 로고    scopus 로고
    • Complement-dependent tumor cell lysis triggered by combinations of epidermal growth factor receptor antibodies
    • M. Dechant, W. Weisner, S. Berger, M. Peipp, T. Beyer, and T. Schneider-Merck Complement-dependent tumor cell lysis triggered by combinations of epidermal growth factor receptor antibodies Cancer Res. 68 2008 4998 5003
    • (2008) Cancer Res. , vol.68 , pp. 4998-5003
    • Dechant, M.1    Weisner, W.2    Berger, S.3    Peipp, M.4    Beyer, T.5    Schneider-Merck, T.6
  • 35
    • 14444288522 scopus 로고    scopus 로고
    • The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling
    • DOI 10.1074/jbc.272.5.2927
    • H.S. Huang, M. Nagane, C.K. Klingbeil, H. Lin, R. Nishikawa, and X.D. Ji The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling J. Biol. Chem. 272 1997 2927 2935 (Pubitemid 27053343)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.5 , pp. 2927-2935
    • Su Huang, H.-J.1    Nagane, M.2    Klingbeil, C.K.3    Lin, H.4    Nishikawa, R.5    Ji, X.-D.6    Huang, C.-M.7    Gill, G.N.8    Wiley, H.S.9    Cavenee, W.K.10
  • 37
    • 0031409362 scopus 로고    scopus 로고
    • Epidermal growth factor receptor inhibition by a monoclonal antibody as anticancer therapy
    • J. Mendelsohn Epidermal growth factor receptor inhibition by a monoclonal antibody as anticancer therapy Clin. Cancer Res. 3 1997 2703 2707 (Pubitemid 28133130)
    • (1997) Clinical Cancer Research , vol.3 , Issue.12 , pp. 2703-2707
    • Mendelsohn, J.1
  • 38
    • 0019427474 scopus 로고
    • Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts
    • S.K. Basu, J.L. Goldstein, R.G. Anderson, and M.S. Brown Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts Cell 24 1981 493 502
    • (1981) Cell , vol.24 , pp. 493-502
    • Basu, S.K.1    Goldstein, J.L.2    Anderson, R.G.3    Brown, M.S.4
  • 39
    • 0029803056 scopus 로고    scopus 로고
    • A combined assay of cell viability and in vitro cytotoxicity with a highly water-soluble tetrazolium salt, neutral red and crystal violet
    • M. Ishiyama, H. Tominaga, M. Shiga, K. Sasamoto, Y. Ohkura, and K. Ueno A combined assay of cell viability and in vitro cytotoxicity with a highly water-soluble tetrazolium salt, neutral red and crystal violet Biol. Pharm. Bull. 19 1996 1518 1520 (Pubitemid 26403266)
    • (1996) Biological and Pharmaceutical Bulletin , vol.19 , Issue.11 , pp. 1518-1520
    • Ishiyama, M.1    Tominaga, H.2    Shiga, M.3    Sasamoto, K.4    Ohkura, Y.5    Ueno, K.6
  • 40
    • 0029924424 scopus 로고    scopus 로고
    • A biological method for the quantitative measurement of tetrodotoxin (TTX): Tissue culture bioassay in combination with a water-soluble tetrazolium salt
    • DOI 10.1016/0041-0101(95)00151-4
    • K. Hamasaki, K. Kogure, and K. Ohwada A biological method for the quantitative measurement of tetrodotoxin (TTX): tissue culture bioassay in combination with a water-soluble tetrazolium salt Toxicon 34 1996 490 495 (Pubitemid 26130128)
    • (1996) Toxicon , vol.34 , Issue.4 , pp. 490-495
    • Hamasaki, K.1    Kogure, K.2    Ohwada, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.