메뉴 건너뛰기




Volumn 18, Issue 2, 2000, Pages 194-198

Rationally designed anti-HER2/neu peptide mimetic disables p185(HER2/neu) tyrosine kinases in vitro and in vivo

Author keywords

radiation; Doxorubicin; ErbB2; Her2; Herceptin; Mimetic; Neu; Tumor therapy

Indexed keywords

MONOCLONAL ANTIBODY; PROTEIN TYROSINE KINASE INHIBITOR;

EID: 0033953634     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/72651     Document Type: Article
Times cited : (171)

References (43)
  • 1
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon, D.J. et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235, 177-182 (1987).
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1
  • 2
    • 0024563889 scopus 로고
    • Expression pattern of the neu (NGL) gene-encoded growth factor receptor protein (p185neu) in normal and transformed epithelial tissues of the digestive tract
    • Cohen, J.A. et al. Expression pattern of the neu (NGL) gene-encoded growth factor receptor protein (p185neu) in normal and transformed epithelial tissues of the digestive tract. Oncogene 4, 81-88 (1989).
    • (1989) Oncogene , vol.4 , pp. 81-88
    • Cohen, J.A.1
  • 4
    • 0023943270 scopus 로고
    • Monoclonal antibodies specific for the neu oncogene product directly mediate anti-tumor effects in vivo
    • Drebin, J.A., Link, V.C. & Greene, M.I. Monoclonal antibodies specific for the neu oncogene product directly mediate anti-tumor effects in vivo. Oncogene 2, 387-394 (1988).
    • (1988) Oncogene , vol.2 , pp. 387-394
    • Drebin, J.A.1    Link, V.C.2    Greene, M.I.3
  • 5
    • 0032127350 scopus 로고    scopus 로고
    • Recombinant humanized anti-HER2 antibody (Herceptin) enhances the antitumor activity of paclitaxel and doxorubicin against HER2/neu overexpressing human breast cancer xenografts
    • Baselga, J., Norton, L., Albanell, J., Kim, Y.M. & Mendelsohn, J. Recombinant humanized anti-HER2 antibody (Herceptin) enhances the antitumor activity of paclitaxel and doxorubicin against HER2/neu overexpressing human breast cancer xenografts. Cancer Res. 58, 2825-2831 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 2825-2831
    • Baselga, J.1    Norton, L.2    Albanell, J.3    Kim, Y.M.4    Mendelsohn, J.5
  • 6
    • 0026610881 scopus 로고
    • Humanization of an anti-p185HER2 antibody for human cancer therapy
    • Carter, P. et al. Humanization of an anti-p185HER2 antibody for human cancer therapy. Proc. Natl. Acad. Sci. USA 89, 4285-4289 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4285-4289
    • Carter, P.1
  • 7
    • 0025318271 scopus 로고
    • Characterization of murine monoclonal antibodies reactive to either the human epidermal growth factor receptor or HER2/neu gene product
    • Fendly, B.M. et al. Characterization of murine monoclonal antibodies reactive to either the human epidermal growth factor receptor or HER2/neu gene product. Cancer Res. 50, 1550-1558 (1990).
    • (1990) Cancer Res. , vol.50 , pp. 1550-1558
    • Fendly, B.M.1
  • 8
    • 0024478054 scopus 로고
    • P185HER2 monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor
    • Hudziak, R.M. et al. p185HER2 monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor. Mol. Cell Biol. 9, 1165-1172 (1989).
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1165-1172
    • Hudziak, R.M.1
  • 9
    • 0021680507 scopus 로고
    • Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene
    • Drebin, J.A., Stern, D.F., Link, V.C., Weinberg, R.A. & Greene, M.I. Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene. Nature 312, 545-548 (1984).
    • (1984) Nature , vol.312 , pp. 545-548
    • Drebin, J.A.1    Stern, D.F.2    Link, V.C.3    Weinberg, R.A.4    Greene, M.I.5
  • 10
    • 3543024857 scopus 로고
    • Inhibition of tumor growth by a monoclonal antibody reactive with an oncogene-encoded tumor antigen
    • Drebin, J.A., Link, V.C., Weinberg, R.A. & Greene, M.I. Inhibition of tumor growth by a monoclonal antibody reactive with an oncogene-encoded tumor antigen. Proc. Natl. Acad. Sci. USA 83, 9129-9133 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9129-9133
    • Drebin, J.A.1    Link, V.C.2    Weinberg, R.A.3    Greene, M.I.4
  • 11
    • 0029944347 scopus 로고    scopus 로고
    • Macramolecular versus small-molecule therapeutics: Drug discovery, development and clinical considerations
    • Cho, M.J. & Juliano, R. Macramolecular versus small-molecule therapeutics: drug discovery, development and clinical considerations. Trends Biotechnol. 14, 153-158 (1996).
    • (1996) Trends Biotechnol. , vol.14 , pp. 153-158
    • Cho, M.J.1    Juliano, R.2
  • 12
    • 0027626855 scopus 로고
    • Conformational and topographical considerations in the design of biologically active peptides
    • Hruby, V.J. Conformational and topographical considerations in the design of biologically active peptides. Biopolymers 33, 1073-1082 (1993).
    • (1993) Biopolymers , vol.33 , pp. 1073-1082
    • Hruby, V.J.1
  • 13
    • 0030879919 scopus 로고    scopus 로고
    • Peptidomimetics and small molecule design
    • Langston, S. Peptidomimetics and small molecule design. Drug Discov. Today 2, 254-256 (1997).
    • (1997) Drug Discov. Today , vol.2 , pp. 254-256
    • Langston, S.1
  • 15
    • 0031942763 scopus 로고    scopus 로고
    • Structure-based design of immunologically active therapeutic peptides
    • Murali, R. & Greene, M.I. Structure-based design of immunologically active therapeutic peptides. Immunol. Res. 17, 163-169 (1998).
    • (1998) Immunol. Res. , vol.17 , pp. 163-169
    • Murali, R.1    Greene, M.I.2
  • 16
    • 0028293066 scopus 로고
    • Designing peptide mimetics
    • Moore, G.J. Designing peptide mimetics. Trends Pharmacol. Sci. 15, 124-129 (1994).
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 124-129
    • Moore, G.J.1
  • 18
    • 0025850422 scopus 로고
    • Design and synthesis of a mimetic from an antibody complementarity-determining region
    • Saragovi, H.U. et al. Design and synthesis of a mimetic from an antibody complementarity-determining region. Science 253, 792-795 (1991).
    • (1991) Science , vol.253 , pp. 792-795
    • Saragovi, H.U.1
  • 19
    • 0029670575 scopus 로고    scopus 로고
    • Synthetic Cd4 exocyclic peptides antagonize Cd4 holoreceptor binding and T-cell activation
    • Zhang, X. et al. Synthetic Cd4 exocyclic peptides antagonize Cd4 holoreceptor binding and T-cell activation. Nat. Biotechnol. 14, 472-475. (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 472-475
    • Zhang, X.1
  • 20
    • 0030687562 scopus 로고    scopus 로고
    • Structure-based design and characterization of exocyclic peptidomimetics that inhibit TNF alpha binding to its receptor
    • Takasaki, W., Kajino, Y., Kajino, K., Murali, R. & Greene, M.I. Structure-based design and characterization of exocyclic peptidomimetics that inhibit TNF alpha binding to its receptor. Nat. Biotechnol. 15, 1266-1270 (1997).
    • (1997) Nat. Biotechnol. , vol.15 , pp. 1266-1270
    • Takasaki, W.1    Kajino, Y.2    Kajino, K.3    Murali, R.4    Greene, M.I.5
  • 21
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia, C. & Lesk, A.M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196, 901-917 (1987).
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 22
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum, R.M., Martin, A.C. & Thornton, J.M. Antibody-antigen interactions: contact analysis and binding site topography. J. Mol. Biol. 262, 732-745 (1996).
    • (1996) J. Mol. Biol. , vol.262 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 24
    • 0007057553 scopus 로고
    • Nucleic acid sequence of an internal image-bearing monoclonal anti-idiotype and its comparison to the sequence of the external antigen
    • Bruck, C. et al. Nucleic acid sequence of an internal image-bearing monoclonal anti-idiotype and its comparison to the sequence of the external antigen. Proc. Natl. Acad. Sci. USA 83, 6578-6582 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6578-6582
    • Bruck, C.1
  • 25
    • 0027467623 scopus 로고
    • X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling
    • Eigenbrot, C., Randal, M., Presta, L., Carter, P. & Kossiakoff, A.A. X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling. J. Mol. Biol. 229, 969-995 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 969-995
    • Eigenbrot, C.1    Randal, M.2    Presta, L.3    Carter, P.4    Kossiakoff, A.A.5
  • 26
    • 0027955736 scopus 로고
    • X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: Structural indications of the key role of VH residues 59 to 65
    • Eigenbrot, C. et al. X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: structural indications of the key role of VH residues 59 to 65. Proteins 18, 49-62 (1994).
    • (1994) Proteins , vol.18 , pp. 49-62
    • Eigenbrot, C.1
  • 27
    • 0032818387 scopus 로고    scopus 로고
    • Pathobiological features of shared antigenic epitopes and biological functions of distinct and humanized anti-p185her2/neu monoclonal antibodies
    • Zhang, H. et al. Pathobiological features of shared antigenic epitopes and biological functions of distinct and humanized anti-p185her2/neu monoclonal antibodies. Exp. Mol. Pathol. 67, 15-25 (1999).
    • (1999) Exp. Mol. Pathol. , vol.67 , pp. 15-25
    • Zhang, H.1
  • 28
    • 0031052394 scopus 로고    scopus 로고
    • Synthetic Cd4 exocyclics inhibit binding of human-immunodeficiency-virus type-1 envelope to Cd4 and virus-replication in T-lymphocytes
    • Zhang, X. et al. Synthetic Cd4 exocyclics inhibit binding of human-immunodeficiency-virus type-1 envelope to Cd4 and virus-replication in T-lymphocytes. Nat. Biotechnol. 15, 150-154. (1997).
    • (1997) Nat. Biotechnol. , vol.15 , pp. 150-154
    • Zhang, X.1
  • 30
    • 0031031166 scopus 로고    scopus 로고
    • Potent inhibition of protein-tyrosine phosphatase by phosphotyrosine-mimic containing cyclic peptides
    • Akamatsu, M. et al. Potent inhibition of protein-tyrosine phosphatase by phosphotyrosine-mimic containing cyclic peptides. Bioorg. Med. Chem. 5, 157-163 (1997).
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 157-163
    • Akamatsu, M.1
  • 31
    • 0028506408 scopus 로고
    • Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics
    • Graciani, N.R., Tsang, K.Y., McCutchen, S.L. & Kelly, J.W. Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics. Bioorg. Med. Chem. 2, 999-1006 (1994).
    • (1994) Bioorg. Med. Chem. , vol.2 , pp. 999-1006
    • Graciani, N.R.1    Tsang, K.Y.2    McCutchen, S.L.3    Kelly, J.W.4
  • 32
    • 0030756977 scopus 로고    scopus 로고
    • Solution structures of Fc epsilon RI alpha-chain mimics: A beta-hairpin peptide and its retroenantiomer
    • McDonnell, J.M., Fushman, D., Cahill, S.M., Sutton, B.J. & Cowburn, D. Solution structures of Fc epsilon RI alpha-chain mimics: a beta-hairpin peptide and its retroenantiomer. J. Am. Chem. Soc. 119, 5321-5328 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5321-5328
    • McDonnell, J.M.1    Fushman, D.2    Cahill, S.M.3    Sutton, B.J.4    Cowburn, D.5
  • 33
    • 0032522565 scopus 로고    scopus 로고
    • Phosphinic peptides, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors
    • Yiallouros, I. et al. Phosphinic peptides, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors. Biochem. J. 331, 375-379 (1998).
    • (1998) Biochem. J. , vol.331 , pp. 375-379
    • Yiallouros, I.1
  • 34
    • 0025737863 scopus 로고
    • Structure-activity analysis of binding kinetics for NMDA receptor competitive antagonists: The influence of conformational restriction
    • Benveniste, M. & Mayer, M.L. Structure-activity analysis of binding kinetics for NMDA receptor competitive antagonists: the influence of conformational restriction. Br. J. Pharmacol. 104, 207-221 (1991).
    • (1991) Br. J. Pharmacol. , vol.104 , pp. 207-221
    • Benveniste, M.1    Mayer, M.L.2
  • 35
    • 0030013085 scopus 로고    scopus 로고
    • Characterization of different soluble TNF receptor (TNFR80) derivatives: Positive influence of the intracellular domain on receptor/ligand interaction and TNF neutralization capacity
    • Moosmayer, D. et al. Characterization of different soluble TNF receptor (TNFR80) derivatives: positive influence of the intracellular domain on receptor/ligand interaction and TNF neutralization capacity. J. Interf. Cytok. Res. 16, 471-477 (1996).
    • (1996) J. Interf. Cytok. Res. , vol.16 , pp. 471-477
    • Moosmayer, D.1
  • 36
    • 0022102126 scopus 로고
    • Down-modulation of an oncogene protein product and reversion of the transformed phenotype by monoclonal antibodies
    • Drebin, J.A., Link, V.C., Stern, D.F., Weinberg, R.A. & Greene, M.I. Down-modulation of an oncogene protein product and reversion of the transformed phenotype by monoclonal antibodies. Cell 41, 697-706 (1985).
    • (1985) Cell , vol.41 , pp. 697-706
    • Drebin, J.A.1    Link, V.C.2    Stern, D.F.3    Weinberg, R.A.4    Greene, M.I.5
  • 37
    • 0031283001 scopus 로고    scopus 로고
    • Identification of p185neu sequences required for monoclonal antibody- Or ligand-mediated receptor signal attenuation
    • Qian, X. et al. Identification of p185neu sequences required for monoclonal antibody- or ligand-mediated receptor signal attenuation. DNA Cell Biol. 16, 1395-1405 (1997).
    • (1997) DNA Cell Biol. , vol.16 , pp. 1395-1405
    • Qian, X.1
  • 38
    • 0024595042 scopus 로고
    • Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill
    • Hansen, M.B., Nielsen, S.E. & Berg, K. Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill. J. Immunol. Methods 119, 203-210 (1989).
    • (1989) J. Immunol. Methods , vol.119 , pp. 203-210
    • Hansen, M.B.1    Nielsen, S.E.2    Berg, K.3
  • 39
    • 0025804023 scopus 로고
    • Monoclonal antibody therapy of human cancer: Taking the HER2 protooncogene to the clinic
    • Shepard, H.M. et al. Monoclonal antibody therapy of human cancer: taking the HER2 protooncogene to the clinic. [Review]. J. Clin. Immunol. 11, 117-127 (1991).
    • (1991) J. Clin. Immunol. , vol.11 , pp. 117-127
    • Shepard, H.M.1
  • 40
    • 0032168534 scopus 로고    scopus 로고
    • Conversion of a radioresistant phenotype to a more sensitive one by disabling erbB receptor signaling in human cancer cells
    • O'Rourke, D.M. et al. Conversion of a radioresistant phenotype to a more sensitive one by disabling erbB receptor signaling in human cancer cells. Proc. Natl. Acad. Sci. USA 95, 10842-10847 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10842-10847
    • O'Rourke, D.M.1
  • 41
    • 0030842655 scopus 로고    scopus 로고
    • Cell-cycle arrest versus cell death in cancer therapy
    • Waldman, T. et al. Cell-cycle arrest versus cell death in cancer therapy. Nat. Med. 3, 1034-1036 (1997).
    • (1997) Nat. Med. , vol.3 , pp. 1034-1036
    • Waldman, T.1
  • 42
    • 0029041003 scopus 로고
    • Prevention of breast tumour development in vivo by down-regulation of the p185neu receptor
    • Katsumata, M. et al. Prevention of breast tumour development in vivo by down-regulation of the p185neu receptor. Nat. Med. 1, 644-648 (1995).
    • (1995) Nat. Med. , vol.1 , pp. 644-648
    • Katsumata, M.1
  • 43
    • 0028205406 scopus 로고
    • Kinase-deficient neu proteins suppress epidermal growth factor receptor function and abolish cell transformation
    • Qian, X., Dougall, W.C., Hellman, M.E. & Greene, M.I. Kinase-deficient neu proteins suppress epidermal growth factor receptor function and abolish cell transformation. Oncogene 9, 1507-1514 (1994).
    • (1994) Oncogene , vol.9 , pp. 1507-1514
    • Qian, X.1    Dougall, W.C.2    Hellman, M.E.3    Greene, M.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.