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Volumn 408, Issue 4, 2011, Pages 692-696

Single-domain antibodies that compete with the natural ligand fibroblast growth factor block the internalization of the fibroblast growth factor receptor 1

Author keywords

Competitive elution; Fibroblast growth factor receptor 1; Llama VHH; MCF7 cells; Receptor internalization; Single domain antibodies

Indexed keywords

EPITOPE; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR 1; HEPARIN; RECOMBINANT ANTIBODY; RECOMBINANT ANTIBODY VHH; UNCLASSIFIED DRUG;

EID: 79956188243     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.04.090     Document Type: Article
Times cited : (18)

References (30)
  • 1
    • 0030834170 scopus 로고    scopus 로고
    • Differential expression of the fibroblast growth factor receptor (FGFR) multigene family in normal human adult tissues
    • Hughes S.E. Differential expression of the fibroblast growth factor receptor (FGFR) multigene family in normal human adult tissues. J. Histochem. Cytochem. 1997, 45:1005-1019.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1005-1019
    • Hughes, S.E.1
  • 3
    • 0032954333 scopus 로고    scopus 로고
    • Alterations in expression of basic fibroblast growth factor (FGF) 2 and its receptor FGFR-1 in human prostate cancer
    • Giri D., Ropiquet F., Ittmann M. Alterations in expression of basic fibroblast growth factor (FGF) 2 and its receptor FGFR-1 in human prostate cancer. Clin. Cancer Res. 1999, 5:1063-1071.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 1063-1071
    • Giri, D.1    Ropiquet, F.2    Ittmann, M.3
  • 5
    • 2442675495 scopus 로고    scopus 로고
    • Blocking of FGFR signaling inhibits breast cancer proliferation through downregulation of D-type cyclins
    • Koziczak M., Holbro T., Hynes N.E. Blocking of FGFR signaling inhibits breast cancer proliferation through downregulation of D-type cyclins. Oncogene 2004, 23:3501-3508.
    • (2004) Oncogene , vol.23 , pp. 3501-3508
    • Koziczak, M.1    Holbro, T.2    Hynes, N.E.3
  • 7
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon A., Klagsbrun M., Esko J.D., Leder P., Ornitz D.M. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 1991, 64:841-848.
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 8
    • 0025835670 scopus 로고
    • Requirement of heparin sulfate for FGF-2-mediated fibroblast growth and myoblast differentiation
    • Rapraeger A.C., Krufka A., Olwin B.B. Requirement of heparin sulfate for FGF-2-mediated fibroblast growth and myoblast differentiation. Science 1991, 252:1705-1708.
    • (1991) Science , vol.252 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 9
    • 0034674223 scopus 로고    scopus 로고
    • Ligand binding properties of binary complexes of heparin and immunoglobulin-like modules of FGF receptor 2
    • Uematsu F., Kan M., Wang F., Jang J.H., Luo Y., McKeehan W.L. Ligand binding properties of binary complexes of heparin and immunoglobulin-like modules of FGF receptor 2. Biochem. Biophys. Res. Commun. 2000, 272:830-836.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 830-836
    • Uematsu, F.1    Kan, M.2    Wang, F.3    Jang, J.H.4    Luo, Y.5    McKeehan, W.L.6
  • 10
    • 0029954235 scopus 로고    scopus 로고
    • Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2
    • Maher P.A. Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2. J. Cell Biol. 1996, 134:529-536.
    • (1996) J. Cell Biol. , vol.134 , pp. 529-536
    • Maher, P.A.1
  • 11
    • 0034855942 scopus 로고    scopus 로고
    • Nuclear localization of EGF receptor and its potential new role as a transcription factor
    • Lin S.Y., Makino K., Xia W.M., Matin A., Wen Y., Kwong L K.Y., Hung M.C. Nuclear localization of EGF receptor and its potential new role as a transcription factor. Nat. Cell. Biol. 2001, 3:802-808.
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 802-808
    • Lin, S.Y.1    Makino, K.2    Xia, W.M.3    Matin, A.4    Wen, Y.5    Kwong L, K.Y.6    Hung, M.C.7
  • 13
    • 11144274556 scopus 로고    scopus 로고
    • Regulation of endocytosis, nuclear translocation, and signaling of Fibroblast Growth Factor Receptor 1 by E-Cadherin
    • Bryant D.M., Wylie F.G., Stow J.L. Regulation of endocytosis, nuclear translocation, and signaling of Fibroblast Growth Factor Receptor 1 by E-Cadherin. Mol. Biol. Cell 2005, 16:14-23.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 14-23
    • Bryant, D.M.1    Wylie, F.G.2    Stow, J.L.3
  • 14
    • 78349296066 scopus 로고    scopus 로고
    • The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins
    • ID: 658954
    • M. Aliprandi, E. Sparacio, F. Pivetta, G. Ossolengo, R. Maestro, A. de Marco, The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins, J. Biomed. Biotech. (2010) ID: 658954.
    • (2010) J. Biomed. Biotech.
    • Aliprandi, M.1    Sparacio, E.2    Pivetta, F.3    Ossolengo, G.4    Maestro, R.5    de Marco, A.6
  • 15
    • 79956191530 scopus 로고    scopus 로고
    • Epitope mapping of protein antigens by competition ELISA
    • Humana Press, Inc., Totowa, NJ, J.M. Walker (Ed.)
    • Morris G.E. Epitope mapping of protein antigens by competition ELISA. The Protein Protocols Handbook 1996, 595-600. Humana Press, Inc., Totowa, NJ. J.M. Walker (Ed.).
    • (1996) The Protein Protocols Handbook , pp. 595-600
    • Morris, G.E.1
  • 16
    • 78649992510 scopus 로고    scopus 로고
    • Effective suppression of vascular network formation by combination of antibodies blocking VEGFR ligand binding and receptor dimerization
    • Tvorogov D., Anisimov A., Zheng W., Leppänen V.-M., Tammela T., Laurinavicius S., et al. Effective suppression of vascular network formation by combination of antibodies blocking VEGFR ligand binding and receptor dimerization. Cancer Cell 2010, 18:630-640.
    • (2010) Cancer Cell , vol.18 , pp. 630-640
    • Tvorogov, D.1    Anisimov, A.2    Zheng, W.3    Leppänen, V.-M.4    Tammela, T.5    Laurinavicius, S.6
  • 17
    • 62149129236 scopus 로고    scopus 로고
    • Therapeutic antibodies: successes, limitations and hopes for the future
    • Chames P., Van Regenmortel M., Weiss E., Baty D. Therapeutic antibodies: successes, limitations and hopes for the future. Br. J. Pharmacol. 2009, 157:220-233.
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 220-233
    • Chames, P.1    Van Regenmortel, M.2    Weiss, E.3    Baty, D.4
  • 18
    • 79953782986 scopus 로고    scopus 로고
    • Combining epitope-distinct antibodies to HER2: cooperative inhibitory effects on invasive growth
    • Emde A., Pradeep C.-R., Ferraro D.A., Ben-Chetrit N., Sela M., Ribba B., et al. Combining epitope-distinct antibodies to HER2: cooperative inhibitory effects on invasive growth. Oncogene 2011, 30:1631-1642.
    • (2011) Oncogene , vol.30 , pp. 1631-1642
    • Emde, A.1    Pradeep, C.-R.2    Ferraro, D.A.3    Ben-Chetrit, N.4    Sela, M.5    Ribba, B.6
  • 19
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: the power of in vitro display technologies
    • Bradbury A.R.M., Sidhu S., Dübel S., McCafferty J. Beyond natural antibodies: the power of in vitro display technologies. Nat. Biotechnol. 2011, 29:245-254.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 245-254
    • Bradbury, A.R.M.1    Sidhu, S.2    Dübel, S.3    McCafferty, J.4
  • 20
    • 33846979756 scopus 로고    scopus 로고
    • Heating represents a rapid purification method for recovering correctly folded thermo tolerant VH and VHH domains
    • Olichon A., Schweizer D., Muyldermans S., de Marco A. Heating represents a rapid purification method for recovering correctly folded thermo tolerant VH and VHH domains. BMC Biotechnol. 2007, 7:7.
    • (2007) BMC Biotechnol. , vol.7 , pp. 7
    • Olichon, A.1    Schweizer, D.2    Muyldermans, S.3    de Marco, A.4
  • 22
    • 74949120905 scopus 로고    scopus 로고
    • Single domain antibodies are specially suited for quantitative determination of gliadins under denaturing conditions
    • Doňa V., Urrutia M., Bayardo M., Alzogaray V., Goldbaum F.A., Chirdo F.G. Single domain antibodies are specially suited for quantitative determination of gliadins under denaturing conditions. J. Agric. Food Chem. 2010, 58:918-926.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 918-926
    • Doňa, V.1    Urrutia, M.2    Bayardo, M.3    Alzogaray, V.4    Goldbaum, F.A.5    Chirdo, F.G.6
  • 23
    • 78650573881 scopus 로고    scopus 로고
    • CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells
    • Jähnichen S., Blanchetot C., Maussang D., Gonzalez-Pajuelo M., Chow K.Y., Bosch L., et al. CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells. Proc. Natl. Acad. Sci. USA 2010, 107:20565-20570.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 20565-20570
    • Jähnichen, S.1    Blanchetot, C.2    Maussang, D.3    Gonzalez-Pajuelo, M.4    Chow, K.Y.5    Bosch, L.6
  • 24
    • 57349165849 scopus 로고    scopus 로고
    • Llama antibody fragments with cross-subtype human immunodeficiency virus type 1 (HIV-1)-neutralizing properties and high affinity for HIV-1 gp120
    • Forsman A., Beirnaert E., Aasa-Chapman M.M.I., Hoorelbeke B., Hijazi K., Koh W., et al. Llama antibody fragments with cross-subtype human immunodeficiency virus type 1 (HIV-1)-neutralizing properties and high affinity for HIV-1 gp120. J. Virol. 2008, 82:12069-12081.
    • (2008) J. Virol. , vol.82 , pp. 12069-12081
    • Forsman, A.1    Beirnaert, E.2    Aasa-Chapman, M.M.I.3    Hoorelbeke, B.4    Hijazi, K.5    Koh, W.6
  • 25
    • 74049140009 scopus 로고    scopus 로고
    • An improved phage-display panning method to produce an HM-1 killer toxin anti-idiotypic antibody
    • Kabir M.E., Krishnaswamy S., Miyamoto M., Furuichi Y., Komiyama T. An improved phage-display panning method to produce an HM-1 killer toxin anti-idiotypic antibody. BMC Biotechnol. 2009, 9:99.
    • (2009) BMC Biotechnol. , vol.9 , pp. 99
    • Kabir, M.E.1    Krishnaswamy, S.2    Miyamoto, M.3    Furuichi, Y.4    Komiyama, T.5
  • 26
    • 78650481700 scopus 로고    scopus 로고
    • Anti-angiogenic activity of a neutralizing human single-chain antibody fragment against fibroblast growth factor receptor 1
    • Ronca R., Benzoni P., Leali D., Urbinati C., Belleri M., Corsini M., et al. Anti-angiogenic activity of a neutralizing human single-chain antibody fragment against fibroblast growth factor receptor 1. Mol. Cancer Ther. 2010, 9:3244-3253.
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 3244-3253
    • Ronca, R.1    Benzoni, P.2    Leali, D.3    Urbinati, C.4    Belleri, M.5    Corsini, M.6
  • 27
    • 0035911965 scopus 로고    scopus 로고
    • Importin β-mediated nuclear import of fibroblast growth factor receptor: role in cell proliferation
    • Reilly J.F., Maher P.A. Importin β-mediated nuclear import of fibroblast growth factor receptor: role in cell proliferation. J. Cell Biol. 2001, 152:1307-1312.
    • (2001) J. Cell Biol. , vol.152 , pp. 1307-1312
    • Reilly, J.F.1    Maher, P.A.2
  • 28
    • 79959565723 scopus 로고    scopus 로고
    • Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidase
    • in press, doi:10.1016/j.pep.2011.03.005
    • G. Veggiani, A. de Marco, Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidase, Prot. Expr. Purif., in press, doi:10.1016/j.pep.2011.03.005.
    • Prot. Expr. Purif.
    • Veggiani, G.1    de Marco, A.2
  • 29
    • 78650965365 scopus 로고    scopus 로고
    • Pre-expression of sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. coli
    • Nguyen V.D., Hatahet F., Salo K.E., Enlund E., Zhang C., Ruddock L.W. Pre-expression of sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. coli. Microb. Cell Fact. 2011, 10:1-13.
    • (2011) Microb. Cell Fact. , vol.10 , pp. 1-13
    • Nguyen, V.D.1    Hatahet, F.2    Salo, K.E.3    Enlund, E.4    Zhang, C.5    Ruddock, L.W.6
  • 30
    • 75149170979 scopus 로고    scopus 로고
    • Fibroblast growth factor signaling: from development to cancer
    • Turner N., Grose R. Fibroblast growth factor signaling: from development to cancer. Nat. Rev. Cancer 2010, 10:116-129.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 116-129
    • Turner, N.1    Grose, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.