메뉴 건너뛰기




Volumn 54, Issue 5, 1999, Pages 415-426

Grafting an RGD motif onto an epidermal growth factor-like module: Chemical synthesis and functional characterization of the chimeric molecule

Author keywords

Cell adhesion; EGF like module; Integrin; Peptide synthesis; Protein engineering; RGD

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; CHIMERIC PROTEIN; COMPLEMENT COMPONENT C1R; EPIDERMAL GROWTH FACTOR; FIBRONECTIN; GLUTATHIONE; INTEGRIN; INTEGRIN RECEPTOR; MONOCLONAL ANTIBODY; SYNTHETIC PEPTIDE; VITRONECTIN;

EID: 0032725858     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00137.x     Document Type: Article
Times cited : (7)

References (50)
  • 1
    • 0029584214 scopus 로고
    • Protein loop grafting to construct a variant of tissue-type plasminogen activator that binds platelet integrin αIIbβ3
    • Smith, J.W., Tachias, K. & Madison, E.L. (1995) Protein loop grafting to construct a variant of tissue-type plasminogen activator that binds platelet integrin αIIbβ3. J. Biol. Chem. 270, 30486-30490.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30486-30490
    • Smith, J.W.1    Tachias, K.2    Madison, E.L.3
  • 3
    • 0030753982 scopus 로고    scopus 로고
    • Engineering novel proteins by transfer of active sites to natural scaffolds
    • Vita, C. (1997) Engineering novel proteins by transfer of active sites to natural scaffolds. Curr. Opin. Biotech. 8, 429-434.
    • (1997) Curr. Opin. Biotech. , vol.8 , pp. 429-434
    • Vita, C.1
  • 4
    • 0028799070 scopus 로고
    • Synthesis of a metal binding protein designed on the α/β scaffold of charybdotoxin
    • Pierret, B., Virelizier, H. & Vita, C. (1995) Synthesis of a metal binding protein designed on the α/β scaffold of charybdotoxin. Int. J. Peptide Protein Res. 46, 471-479.
    • (1995) Int. J. Peptide Protein Res. , vol.46 , pp. 471-479
    • Pierret, B.1    Virelizier, H.2    Vita, C.3
  • 6
    • 0027423755 scopus 로고
    • Solution conformation of a synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: New structural alignment between the squash inhibitors and the potato carboxypeptidase inhibitor
    • Chiche, L., Heitz, A., Padilla, A., Le-Nguyen, D. & Castro, B. (1993) Solution conformation of a synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: new structural alignment between the squash inhibitors and the potato carboxypeptidase inhibitor. Protein Eng. 6, 675-682.
    • (1993) Protein Eng. , vol.6 , pp. 675-682
    • Chiche, L.1    Heitz, A.2    Padilla, A.3    Le-Nguyen, D.4    Castro, B.5
  • 7
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork, P., Downing, A.K., Kieffer, B. & Campbell, I.D. (1996) Structure and distribution of modules in extracellular proteins. Quart. Rev. Biophys. 19, 119-167.
    • (1996) Quart. Rev. Biophys. , vol.19 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 9
    • 0030975882 scopus 로고    scopus 로고
    • Chemical synthesis and characterization of the epidermal growth factor-like module of human complement protease
    • Hernandez, J.F., Bersch, R., Pétillot, Y., Gagnon, J. & Arlaud, G.J. (1997) Chemical synthesis and characterization of the Epidermal Growth Factor-like module of human complement protease Cir. J. Peptide Res. 49, 221-231.
    • (1997) Cir. J. Peptide Res. , vol.49 , pp. 221-231
    • Hernandez, J.F.1    Bersch, R.2    Pétillot, Y.3    Gagnon, J.4    Arlaud, G.J.5
  • 10
    • 0032477892 scopus 로고    scopus 로고
    • Solution structure of the epidermal growth factor (EGF) -like module of human complement protease Cir, an atypical member of the EGF family
    • Bersch, R., Hernandez, J.F., Marion, D. & Arlaud, G.J. (1998) Solution structure of the Epidermal Growth Factor (EGF) -like module of human complement protease Cir, an atypical member of the EGF family. Biochemistry 37, 1204-1214.
    • (1998) Biochemistry , vol.37 , pp. 1204-1214
    • Bersch, R.1    Hernandez, J.F.2    Marion, D.3    Arlaud, G.J.4
  • 13
    • 0028931325 scopus 로고
    • The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1
    • Handford, P., Downing, A.K., Rao, Z., Hewett, D.R., Sykes, B.C. & Kielty, C.M. (1995) The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1. J. Biol. Chem. 170, 6751-6756.
    • (1995) J. Biol. Chem. , vol.170 , pp. 6751-6756
    • Handford, P.1    Downing, A.K.2    Rao, Z.3    Hewett, D.R.4    Sykes, B.C.5    Kielty, C.M.6
  • 15
    • 0027191391 scopus 로고
    • Structural and functional analyses of the Arg-Gly-Asp sequence introduced into human lysozyme
    • Yamada, T., Matsushima, M., Inaka, K. et al. (1993) Structural and functional analyses of the Arg-Gly-Asp sequence introduced into human lysozyme. J. Biol. Chem. 268, 10588-10592.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10588-10592
    • Yamada, T.1    Matsushima, M.2    Inaka, K.3
  • 16
    • 0028947622 scopus 로고
    • Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme
    • Yamada, T., Song, H., Inaka, K., Shimada, Y., Kikuchi, M. & Matshushima, M. (1995) Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme. J. Biol. Chem. 270, 5687-5690.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5687-5690
    • Yamada, T.1    Song, H.2    Inaka, K.3    Shimada, Y.4    Kikuchi, M.5    Matshushima, M.6
  • 17
    • 0030581628 scopus 로고    scopus 로고
    • Integrin-specific tissue-type plasminogen activator engineered by introduction of the Arg-Gly-Asp sequence
    • Yamada, T., Shimada, Y. & Kikuchi, M. (1996) Integrin-specific tissue-type plasminogen activator engineered by introduction of the Arg-Gly-Asp sequence. Biochem. Biophys. Res. Commun. 228, 306-311.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 306-311
    • Yamada, T.1    Shimada, Y.2    Kikuchi, M.3
  • 18
    • 0031719841 scopus 로고    scopus 로고
    • Engineering of solvent-exposed loops in Escherichia coli β-galactosidase
    • Feliu, J.X. & Villaverde, A. (1998) Engineering of solvent-exposed loops in Escherichia coli β-galactosidase. FFBS Lett. 434, 23-27.
    • (1998) FFBS Lett. , vol.434 , pp. 23-27
    • Feliu, J.X.1    Villaverde, A.2
  • 19
    • 0343878382 scopus 로고
    • Partial primary structure of bovine plasma fibronectin: Three types of internal homology
    • Petersen, T., Thogersen, H.C., Skorstengaard, K. et al (1983) Partial primary structure of bovine plasma fibronectin: three types of internal homology. Proc. Natl. Acad. Sci. USA 80, 137-141.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 137-141
    • Petersen, T.1    Thogersen, H.C.2    Skorstengaard, K.3
  • 20
    • 0004043397 scopus 로고
    • Springer-Verlag, New York
    • Hynes, R.O., ed. (1990) Fibronectins, Springer-Verlag, New York.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 21
    • 0030907070 scopus 로고    scopus 로고
    • The molecular structure of cell adhesion molecules
    • Chothia, C. (1997) The molecular structure of cell adhesion molecules. Annu. Rev. Biochem. 66, 823-862.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 823-862
    • Chothia, C.1
  • 22
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota, S., Nomizu, M. & Yamada, K.D. (1994) The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J. Biol. Chem. 169, 24756-24761.
    • (1994) J. Biol. Chem. , vol.169 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.D.3
  • 23
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher, M.D. & Ruoslahti, E. [1987] Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262, 17294-17298.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 24
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti, E. & Pierschbacher, M.D. (1987) New perspectives in cell adhesion: RGD and integrins. Science 238, 491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 25
    • 0028791728 scopus 로고
    • Common molecular scaffold for two unrelated RGD molecules
    • Ely, K.R., Kunicki, T.J. & Kodandapani R. (1995) Common molecular scaffold for two unrelated RGD molecules. Protein Eng. 8, 823-827.
    • (1995) Protein Eng. , vol.8 , pp. 823-827
    • Ely, K.R.1    Kunicki, T.J.2    Kodandapani, R.3
  • 26
    • 0028216926 scopus 로고
    • Crystal structure of the tenth type III cell adhesion module of human fibronectin
    • Dickinson, C.D., Veerapandian, B., Dai, X.P. et al. (1994) Crystal structure of the tenth type III cell adhesion module of human fibronectin. J. Mol. Biol. 1079-1092.
    • (1994) J. Mol. Biol. , pp. 1079-1092
    • Dickinson, C.D.1    Veerapandian, B.2    Dai, X.P.3
  • 27
    • 0026350087 scopus 로고
    • Solution structure of kistrin, a potent platelet aggregation inhibitor and GPIIb-IIIa antagonist
    • Adler, M., Lazarus, R.A., Dennis, M.S. & Wagner, G. (1991) Solution structure of kistrin, a potent platelet aggregation inhibitor and GPIIb-IIIa antagonist. Science 253, 445-448.
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.A.2    Dennis, M.S.3    Wagner, G.4
  • 28
    • 0028222396 scopus 로고
    • Echistatin: The refined structure of a disintegrin in solution by 1H NMR and restrained molecular dynamics
    • Atkinson, R.A., Saudek, V. & Pelton, J.T. (1994) Echistatin: the refined structure of a disintegrin in solution by 1H NMR and restrained molecular dynamics. Int. J. Peptide Protein Res. 43, 563-572.
    • (1994) Int. J. Peptide Protein Res. , vol.43 , pp. 563-572
    • Atkinson, R.A.1    Saudek, V.2    Pelton, J.T.3
  • 29
    • 0028017504 scopus 로고
    • Structure of the RGD protein decorsin: Conserved motif und distinct function in leech proteins that affect blood clotting
    • Krezel, A.M., Wagner, G., Seymour-Ulmer, J. & Lazarus, R.A. (1994) Structure of the RGD protein decorsin: conserved motif und distinct function in leech proteins that affect blood clotting. Science 264, 1944-1947.
    • (1994) Science , vol.264 , pp. 1944-1947
    • Krezel, A.M.1    Wagner, G.2    Seymour-Ulmer, J.3    Lazarus, R.A.4
  • 30
    • 0019217766 scopus 로고
    • Elution of fibronectin from collagen with chaotropic agents
    • Klebe, R.J., Bentley, K.L., Sasser, P.J. & Schoen, R.C. (1980) Elution of fibronectin from collagen with chaotropic agents. Exp. Cell Res. 130, 111-117.
    • (1980) Exp. Cell Res. , vol.130 , pp. 111-117
    • Klebe, R.J.1    Bentley, K.L.2    Sasser, P.J.3    Schoen, R.C.4
  • 32
    • 13344276445 scopus 로고
    • N2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: Evidence and application in peptide synthesis
    • N2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: evidence and application in peptide synthesis. J. Am. Chem. Soc. 105, 6442-6455.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6442-6455
    • Tam, J.P.1    Heath, W.F.2    Merrifield, R.B.3
  • 33
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 34
    • 0029072783 scopus 로고
    • Two distinct cell attachment sites in entactin arc revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich Epidermal Growth Factor repeat 2
    • Dong, L.J., Hsieh, J.C. & Chung, A.E. (1995) Two distinct cell attachment sites in entactin arc revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich Epidermal Growth Factor repeat 2. J. Biol. Chem. 270, 15838-15843.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15838-15843
    • Dong, L.J.1    Hsieh, J.C.2    Chung, A.E.3
  • 35
    • 0028864654 scopus 로고
    • Selection of tumor-specific epitopes on target antigens for radioimmunotherapy of breast cancer
    • Peterson, J.A., Couto, J.R., Taylor, M.R. & Ceriani, R.L. (1995) Selection of tumor-specific epitopes on target antigens for radioimmunotherapy of breast cancer. Cancer Res. 55, 5847-5851.
    • (1995) Cancer Res. , vol.55 , pp. 5847-5851
    • Peterson, J.A.1    Couto, J.R.2    Taylor, M.R.3    Ceriani, R.L.4
  • 36
    • 0030993710 scopus 로고    scopus 로고
    • Bovine PAS-6/7 binds αvβ5 integrin and anionic phospholipids through two domains
    • Andersen, M.H., Berglund, L., Rasmussen, J.T. & Petersen, T.E. (1997) Bovine PAS-6/7 binds αvβ5 integrin and anionic phospholipids through two domains. Biochemistry 36, 5441-5446.
    • (1997) Biochemistry , vol.36 , pp. 5441-5446
    • Andersen, M.H.1    Berglund, L.2    Rasmussen, J.T.3    Petersen, T.E.4
  • 37
    • 15444354665 scopus 로고    scopus 로고
    • Cloning and characterization of developmental endothelial locus-1: An embryonic endothelial cell protein that binds the αvβ3 integrin receptor
    • Hidai, C., Zupancic, T., Penta, K. et al. (1998) Cloning and characterization of developmental endothelial locus-1: an embryonic endothelial cell protein that binds the αvβ3 integrin receptor. Genes and Dev. 12, 21-33.
    • (1998) Genes and Dev. , vol.12 , pp. 21-33
    • Hidai, C.1    Zupancic, T.2    Penta, K.3
  • 38
    • 0024292679 scopus 로고
    • Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
    • Obara, M., Kangs, M.S. & Yamada, K.M. (1988) Site-directed mutagenesis of the cell-binding domain of human fibronectin: separable, synergistic sites mediate adhesive function. Cell 53, 649-657.
    • (1988) Cell , vol.53 , pp. 649-657
    • Obara, M.1    Kangs, M.S.2    Yamada, K.M.3
  • 39
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond, M.S. & Springer, T.A. (1994) The dynamic regulation of integrin adhesiveness, Curr. Biol. 4, 506-517.
    • (1994) Curr. Biol. , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 40
    • 0021878620 scopus 로고
    • Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein
    • Brown, P.J. & Juliano, R.L. (1985) Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein. Science 228, 1448-1450.
    • (1985) Science , vol.228 , pp. 1448-1450
    • Brown, P.J.1    Juliano, R.L.2
  • 41
    • 0024280898 scopus 로고
    • Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor
    • D'souza, S.E., Ginsberg, M.H., Burke, T.A., Lam, S.C. & Plow, E.F. (1988) Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor. Science 142, 91-93.
    • (1988) Science , vol.142 , pp. 91-93
    • D'souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Lam, S.C.4    Plow, E.F.5
  • 42
    • 0028950139 scopus 로고
    • Possible involvement of the interaction of the alpha 5 subunit of alpha 5 beta 1 integrin with the synergistic region of the central cell-binding domain of fibronectin in cells to fibronectin binding
    • Obara, M. & Yoshizato, K. (1995) Possible involvement of the interaction of the alpha 5 subunit of alpha 5 beta 1 integrin with the synergistic region of the central cell-binding domain of fibronectin in cells to fibronectin binding. Exp. Cell Res. 216, 273-276.
    • (1995) Exp. Cell Res. , vol.216 , pp. 273-276
    • Obara, M.1    Yoshizato, K.2
  • 43
    • 0029120428 scopus 로고
    • A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
    • Pasqualini, R., Koivunen, E. & Ruoslahti, E. (1995) A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J. Cell Biol. 130, 1189-1196.
    • (1995) J. Cell Biol. , vol.130 , pp. 1189-1196
    • Pasqualini, R.1    Koivunen, E.2    Ruoslahti, E.3
  • 44
    • 0030798854 scopus 로고    scopus 로고
    • Defining the topology of integrins α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies
    • Mould, A.P., Askari, J.A., Aota, S. et al. (1997) Defining the topology of integrins α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies. J. Biol. Chem. 272, 17283-17292.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17283-17292
    • Mould, A.P.1    Askari, J.A.2    Aota, S.3
  • 45
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., Akiyama, S.K. & Yamada, K.M. (1995) Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267, 883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 46
    • 0028801218 scopus 로고
    • Integrin function: Molecular hierarchies of cytoskeletal and signaling molecules
    • Miyamoto, S., Teramoto, H., Coso, O.A. et al. (1995) Integrin function: molecular hierarchies of cytoskeletal and signaling molecules. J. Cell Biol. 131, 791-805.
    • (1995) J. Cell Biol. , vol.131 , pp. 791-805
    • Miyamoto, S.1    Teramoto, H.2    Coso, O.A.3
  • 47
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M. & Burridge, K. (1996) Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 48
    • 0029867570 scopus 로고    scopus 로고
    • Cell adhesion and integrin binding to recombinant human fibrillin-1
    • Pfaff, M., Reinhardt, D.P., Sakai, L.Y. & Timpl, R. (1996) Cell adhesion and integrin binding to recombinant human fibrillin-1. FEBS Lett. 384, 247-250.
    • (1996) FEBS Lett. , vol.384 , pp. 247-250
    • Pfaff, M.1    Reinhardt, D.P.2    Sakai, L.Y.3    Timpl, R.4
  • 49
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. (1996) RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12, 697-715.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 50
    • 0029004590 scopus 로고
    • Protein modeling by Email
    • Peitsch, M.C. (1995) Protein modeling by. Email. Bio/Technology 13, 658-660.
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.