메뉴 건너뛰기




Volumn 326, Issue 5, 2003, Pages 1475-1488

Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human αvβ3 integrin

Author keywords

Fibronectin type III domain; Integrin; Phage display; RGD; Scaffold

Indexed keywords

ALANINE; BINDING PROTEIN; CELL SURFACE RECEPTOR; FIBRONECTIN; FIBRONECTIN TYPE III; GLUTAMIC ACID; INTEGRIN; MONOCLONAL ANTIBODY; SCLEROPROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0037424598     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00082-2     Document Type: Article
Times cited : (59)

References (42)
  • 1
    • 0031876195 scopus 로고    scopus 로고
    • Phage display: Applications, innovations, and issues in phage and host biology
    • Wilson D.R., Finlay B.B. Phage display: applications, innovations, and issues in phage and host biology. Can. J. Microbiol. 44:1998;313-329.
    • (1998) Can. J. Microbiol. , vol.44 , pp. 313-329
    • Wilson, D.R.1    Finlay, B.B.2
  • 2
    • 0033638492 scopus 로고    scopus 로고
    • Phage display in pharmaceutical biotechnology
    • Sidhu S.S. Phage display in pharmaceutical biotechnology. Curr. Opin. Biotechnol. 11:2000;610-616.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 610-616
    • Sidhu, S.S.1
  • 3
    • 0030976150 scopus 로고    scopus 로고
    • Bacteriophage display and discovery of peptide leads for drug development
    • Lowman H.B. Bacteriophage display and discovery of peptide leads for drug development. Annu. Rev. Biophys. Biomol. Struct. 26:1997;401-424.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 401-424
    • Lowman, H.B.1
  • 5
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 71:1992;671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 6
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr P.A., Erickson H.P., Palmer A.G. III. Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure. 5:1997;949-959.
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer A.G. III3
  • 7
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide A., Bailey C.W., Huang X., Koide S. The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 284:1998;1141-1151.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 8
    • 0035167115 scopus 로고    scopus 로고
    • Osteopontin is involved in the initiation of cutaneous contact hypersensitivity by inducing Langerhans and dendritic cell migration to lymph nodes
    • Weiss J.M., Renkl A.C., Maier C.S., Kimmig M., Liaw L., Ahrens T., et al. Osteopontin is involved in the initiation of cutaneous contact hypersensitivity by inducing Langerhans and dendritic cell migration to lymph nodes. J. Expt. Med. 194:2001;1219-1229.
    • (2001) J. Expt. Med. , vol.194 , pp. 1219-1229
    • Weiss, J.M.1    Renkl, A.C.2    Maier, C.S.3    Kimmig, M.4    Liaw, L.5    Ahrens, T.6
  • 9
    • 0030873859 scopus 로고    scopus 로고
    • The alpha v beta 3 integrin "vitronectin receptor"
    • Horton M.A. The alpha v beta 3 integrin "vitronectin receptor" Int. J. Biochem. Cell. Biol. 29:1997;721-725.
    • (1997) Int. J. Biochem. Cell. Biol. , vol.29 , pp. 721-725
    • Horton, M.A.1
  • 11
    • 15844420283 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
    • Brooks P.C., Stromblad S., Sanders L.C., von Schalscha T.L., Aimes R.T., Stetler-Stevenson W.G., et al. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell. 85:1996;683-693.
    • (1996) Cell , vol.85 , pp. 683-693
    • Brooks, P.C.1    Stromblad, S.2    Sanders, L.C.3    Von Schalscha, T.L.4    Aimes, R.T.5    Stetler-Stevenson, W.G.6
  • 12
    • 0035793037 scopus 로고    scopus 로고
    • Disruption of matrix metalloproteinase 2 binding to integrin alpha vbeta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo
    • Silletti S., Kessler T., Goldberg J., Boger D.L., Cheresh D.A. Disruption of matrix metalloproteinase 2 binding to integrin alpha vbeta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc. Natl Acad. Sci. USA. 98:2001;119-124.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 119-124
    • Silletti, S.1    Kessler, T.2    Goldberg, J.3    Boger, D.L.4    Cheresh, D.A.5
  • 13
    • 0035797334 scopus 로고    scopus 로고
    • Integrin alphavbeta3 promotes anchorage-dependent apoptosis in human intestinal carcinoma cells
    • Kozlova N.I., Morozevich G.E., Chubukina A.N., Berman A.E. Integrin alphavbeta3 promotes anchorage-dependent apoptosis in human intestinal carcinoma cells. Oncogene. 20:2001;4710-4717.
    • (2001) Oncogene , vol.20 , pp. 4710-4717
    • Kozlova, N.I.1    Morozevich, G.E.2    Chubukina, A.N.3    Berman, A.E.4
  • 15
    • 0034787873 scopus 로고    scopus 로고
    • Induction of apoptosis of integrin-expressing human prostate cancer cells by cyclic Arg-Gly-Asp peptides
    • Chatterjee S., Brite K.H., Matsumura A. Induction of apoptosis of integrin-expressing human prostate cancer cells by cyclic Arg-Gly-Asp peptides. Clin. Cancer Res. 7:2001;3006-3011.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 3006-3011
    • Chatterjee, S.1    Brite, K.H.2    Matsumura, A.3
  • 17
    • 0031862889 scopus 로고    scopus 로고
    • Detection of tumor angiogenesis in vivo by alphaVbeta3-targeted magnetic resonance imaging
    • Sipkins D.A., Cheresh D.A., Kazemi M.R., Nevin L.M., Bednarski M.D., Li K.C. Detection of tumor angiogenesis in vivo by alphaVbeta3-targeted magnetic resonance imaging. Nature Med. 4:1998;623-626.
    • (1998) Nature Med. , vol.4 , pp. 623-626
    • Sipkins, D.A.1    Cheresh, D.A.2    Kazemi, M.R.3    Nevin, L.M.4    Bednarski, M.D.5    Li, K.C.6
  • 18
    • 0034705696 scopus 로고    scopus 로고
    • Development and application of cytotoxic T lymphocyte-associated antigen 4 as a protein scaffold for the generation of novel binding ligands
    • Hufton S.E., van Neer N., van den Beuken T., Desmet J., Sablon E., Hoogenboom H.R. Development and application of cytotoxic T lymphocyte-associated antigen 4 as a protein scaffold for the generation of novel binding ligands. FEBS Letters. 475:2000;225-231.
    • (2000) FEBS Letters , vol.475 , pp. 225-231
    • Hufton, S.E.1    Van Neer, N.2    Van den Beuken, T.3    Desmet, J.4    Sablon, E.5    Hoogenboom, H.R.6
  • 20
    • 0028171951 scopus 로고
    • Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1
    • Blystone S.D., Graham I.L., Lindberg F.P., Brown E.J. Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1. J. Cell. Biol. 127:1994;1129-1137.
    • (1994) J. Cell. Biol. , vol.127 , pp. 1129-1137
    • Blystone, S.D.1    Graham, I.L.2    Lindberg, F.P.3    Brown, E.J.4
  • 21
    • 0030570733 scopus 로고    scopus 로고
    • Importance of the structure of the RGD-containing loop in the disintegrins echistatin and eristostatin for recognition of alpha IIb beta 3 and alpha v beta 3 integrins
    • McLane M.A., Vijay-Kumar S., Marcinkiewicz C., Calvete J.J., Niewiarowski S. Importance of the structure of the RGD-containing loop in the disintegrins echistatin and eristostatin for recognition of alpha IIb beta 3 and alpha v beta 3 integrins. FEBS Letters. 391:1996;139-143.
    • (1996) FEBS Letters , vol.391 , pp. 139-143
    • McLane, M.A.1    Vijay-Kumar, S.2    Marcinkiewicz, C.3    Calvete, J.J.4    Niewiarowski, S.5
  • 22
    • 0026472751 scopus 로고
    • Inhibition of platelet adhesion to fibrin(ogen) in flowing whole blood by Arg-Gly-Asp and fibrinogen gamma-chain carboxy terminal peptides
    • Hantgan R.R., Endenburg S.C., Cavero I., Marguerie G., Uzan A., Sixma J.J., de Groot P.G. Inhibition of platelet adhesion to fibrin(ogen) in flowing whole blood by Arg-Gly-Asp and fibrinogen gamma-chain carboxy terminal peptides. Thromb. Haemost. 68:1992;694-700.
    • (1992) Thromb. Haemost. , vol.68 , pp. 694-700
    • Hantgan, R.R.1    Endenburg, S.C.2    Cavero, I.3    Marguerie, G.4    Uzan, A.5    Sixma, J.J.6    De Groot, P.G.7
  • 23
    • 0027508996 scopus 로고
    • Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms
    • Scarborough R.M., Rose J.W., Naughton M.A., Phillips D.R., Nannizzi L., Arfsten A., et al. Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms. J. Biol. Chem. 268:1993;1058-1065.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1058-1065
    • Scarborough, R.M.1    Rose, J.W.2    Naughton, M.A.3    Phillips, D.R.4    Nannizzi, L.5    Arfsten, A.6
  • 24
    • 0034644725 scopus 로고    scopus 로고
    • Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin alpha 9beta 1 with VCAM-1, tenascin-C, and osteopontin
    • Marcinkiewicz C., Taooka Y., Yokosaki Y., Calvete J.J., Marcinkiewicz M.M., Lobb R.R., et al. Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin alpha 9beta 1 with VCAM-1, tenascin-C, and osteopontin. J. Biol. Chem. 275:2000;31930-31937.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31930-31937
    • Marcinkiewicz, C.1    Taooka, Y.2    Yokosaki, Y.3    Calvete, J.J.4    Marcinkiewicz, M.M.5    Lobb, R.R.6
  • 25
    • 0027976103 scopus 로고
    • Isolation of a highly specific ligand for the alpha 5 beta 1 integrin from a phage display library
    • Koivunen E., Wang B., Ruoslahti E. Isolation of a highly specific ligand for the alpha 5 beta 1 integrin from a phage display library. J. Cell. Biol. 124:1994;373-380.
    • (1994) J. Cell. Biol. , vol.124 , pp. 373-380
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 27
    • 0029584214 scopus 로고
    • Protein loop grafting to construct a variant of tissue-type plasminogen activator that binds platelet integrin alpha IIb beta 3
    • Smith J.W., Tachias K., Madison E.L. Protein loop grafting to construct a variant of tissue-type plasminogen activator that binds platelet integrin alpha IIb beta 3. J. Biol. Chem. 270:1995;30486-30490.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30486-30490
    • Smith, J.W.1    Tachias, K.2    Madison, E.L.3
  • 28
    • 0036645674 scopus 로고    scopus 로고
    • In vitro selection of fibronectin gain-of-function mutations
    • Tani P.H., Loftus J.C., Bowditch R.D. In vitro selection of fibronectin gain-of-function mutations. Biochem. J. 365:2002;287-294.
    • (2002) Biochem. J. , vol.365 , pp. 287-294
    • Tani, P.H.1    Loftus, J.C.2    Bowditch, R.D.3
  • 29
    • 0035914421 scopus 로고    scopus 로고
    • The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain
    • Altroff H., van der Walle C.F., Asselin J., Fairless R., Campbell I.D., Mardon H.J. The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain. J. Biol. Chem. 276:2001;38885-38892.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38885-38892
    • Altroff, H.1    Van der Walle, C.F.2    Asselin, J.3    Fairless, R.4    Campbell, I.D.5    Mardon, H.J.6
  • 30
    • 0033618460 scopus 로고    scopus 로고
    • Mechanisms and consequences of affinity modulation of integrin alpha(V)beta(3) detected with a novel patch-engineered monovalent ligand
    • Pampori N., Hato T., Stupack D.G., Aidoudi S., Cheresh D.A., Nemerow G.R., Shattil S.J. Mechanisms and consequences of affinity modulation of integrin alpha(V)beta(3) detected with a novel patch-engineered monovalent ligand. J. Biol. Chem. 274:1999;21609-21616.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21609-21616
    • Pampori, N.1    Hato, T.2    Stupack, D.G.3    Aidoudi, S.4    Cheresh, D.A.5    Nemerow, G.R.6    Shattil, S.J.7
  • 32
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3
    • Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3. Science. 294:2001;339-345.
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1    Stehle, T.2    Diefenbach, B.3    Zhang, R.4    Dunker, R.5    Scott, D.L.6
  • 33
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • Xiong J.P., Stehle T., Zhang R., Joachimiak A., Frech M., Goodman S.L., Arnaout M.A. Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science. 296:2002;151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 34
    • 0024988364 scopus 로고
    • Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit
    • Suzuki S., Huang Z.S., Tanihara H. Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit. Proc. Natl Acad. Sci. USA. 87:1990;5354-5358.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5354-5358
    • Suzuki, S.1    Huang, Z.S.2    Tanihara, H.3
  • 36
    • 0030830511 scopus 로고    scopus 로고
    • Targeting endothelium for gene therapy via receptors up-regulated during angiogenesis and inflammation
    • Wickham T.J., Haskard D., Segal D., Kovesdi I. Targeting endothelium for gene therapy via receptors up-regulated during angiogenesis and inflammation. Cancer Immunol. Immunother. 45:1997;149-151.
    • (1997) Cancer Immunol. Immunother. , vol.45 , pp. 149-151
    • Wickham, T.J.1    Haskard, D.2    Segal, D.3    Kovesdi, I.4
  • 37
    • 0029794681 scopus 로고    scopus 로고
    • Targeted adenovirus gene transfer to endothelial and smooth muscle cells by using bispecific antibodies
    • Wickham T.J., Segal D.M., Roelvink P.W., Carrion M.E., Lizonova A., Lee G.M., Kovesdi I. Targeted adenovirus gene transfer to endothelial and smooth muscle cells by using bispecific antibodies. J. Virol. 70:1996;6831-6838.
    • (1996) J. Virol. , vol.70 , pp. 6831-6838
    • Wickham, T.J.1    Segal, D.M.2    Roelvink, P.W.3    Carrion, M.E.4    Lizonova, A.5    Lee, G.M.6    Kovesdi, I.7
  • 38
    • 0033042566 scopus 로고    scopus 로고
    • Integrin-mediated vectors for gene transfer and therapy
    • Hart S.L. Integrin-mediated vectors for gene transfer and therapy. Curr. Opin. Mol. Ther. 1:1999;197-203.
    • (1999) Curr. Opin. Mol. Ther. , vol.1 , pp. 197-203
    • Hart, S.L.1
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 40
    • 0032416098 scopus 로고    scopus 로고
    • Modulation of antibody display on M13 filamentous phage
    • Chappel J.A., He M., Kang A.S. Modulation of antibody display on M13 filamentous phage. J. Immunol. Methods. 221:1998;25-34.
    • (1998) J. Immunol. Methods , vol.221 , pp. 25-34
    • Chappel, J.A.1    He, M.2    Kang, A.S.3
  • 41
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA. 82:1985;488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.