메뉴 건너뛰기




Volumn 287, Issue 1, 2003, Pages 116-129

New cell attachment peptide sequences from conserved epitopes in the carboxy termini of fibrinogen

Author keywords

Cell uptake; Cell binding; Chemotaxis; Fibrin(ogen); Fibrinopeptides; Haptides; Haptotaxis

Indexed keywords

ANTIBODY; BETA1 INTEGRIN; EPITOPE; FIBRINOGEN; INTEGRIN; PROTEIN SUBUNIT; SEPHAROSE;

EID: 0038205329     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00120-4     Document Type: Article
Times cited : (35)

References (53)
  • 2
    • 0034743531 scopus 로고    scopus 로고
    • Contribution of the αE C domain to the structure and function of fibrinogen-420
    • Grieninger G. Contribution of the αE C domain to the structure and function of fibrinogen-420. Ann. N.Y. Acad. Sci. 936:2001;44-64.
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 44-64
    • Grieninger, G.1
  • 4
    • 0031903388 scopus 로고    scopus 로고
    • A three-dimensional consideration of variant human fibrinogens
    • Everse S.J., Spraggon G., Doolittle R.F. A three-dimensional consideration of variant human fibrinogens. Thromb. Haemost. 80:(1):1998;1-9.
    • (1998) Thromb. Haemost. , vol.80 , Issue.1 , pp. 1-9
    • Everse, S.J.1    Spraggon, G.2    Doolittle, R.F.3
  • 5
    • 0038736645 scopus 로고    scopus 로고
    • Modelling cation-driven (proto)fibrin coagulation
    • Marx G. Modelling cation-driven (proto)fibrin coagulation. Biopolymers. 27:1998;763-774.
    • (1998) Biopolymers , vol.27 , pp. 763-774
    • Marx, G.1
  • 6
    • 0034964447 scopus 로고    scopus 로고
    • The structure and biological features of fibrinogen and fibrin
    • Mosesson M.W., Siebenlist K., Meh D.A. The structure and biological features of fibrinogen and fibrin. Ann. N.Y. Acad. Sci. 936:2001;11-36.
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 11-36
    • Mosesson, M.W.1    Siebenlist, K.2    Meh, D.A.3
  • 7
    • 0027522533 scopus 로고
    • Diversity of primary structures of the carboxy-terminal regions of mammalian fibrinogen Aa-chains
    • Murakawa M., Okamura T., Kamura T., Shibuya T., Harada M., Niho Y. Diversity of primary structures of the carboxy-terminal regions of mammalian fibrinogen Aa-chains. Thromb. Haemost. 69:1993;351-360.
    • (1993) Thromb. Haemost. , vol.69 , pp. 351-360
    • Murakawa, M.1    Okamura, T.2    Kamura, T.3    Shibuya, T.4    Harada, M.5    Niho, Y.6
  • 8
    • 0019793525 scopus 로고
    • Localization of a fibrin polymerization site
    • Olexa S.A., Budzynski A.Z. Localization of a fibrin polymerization site. J. Biol. Chem. 256:1981;3544-3549.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3544-3549
    • Olexa, S.A.1    Budzynski, A.Z.2
  • 9
    • 0034719137 scopus 로고    scopus 로고
    • Role of the β-strand insert in the central domain of the fibrinogen γ-module
    • Yakovlev S., Litvinovich S., Loukinov D., Medved L. Role of the β-strand insert in the central domain of the fibrinogen γ-module. Biochemistry. 39:2000;15721-15729.
    • (2000) Biochemistry , vol.39 , pp. 15721-15729
    • Yakovlev, S.1    Litvinovich, S.2    Loukinov, D.3    Medved, L.4
  • 10
    • 0029822375 scopus 로고    scopus 로고
    • Degradation of cross-linked fibrin by metalloproteinase 3 (stromelysisn 1) by hydrolysis of the γ Gly-Ala 405 peptide bond
    • Bini A., Itoh Y., Kudryk B.J., Nagase H. Degradation of cross-linked fibrin by metalloproteinase 3 (stromelysisn 1) by hydrolysis of the γ Gly-Ala 405 peptide bond. Biochemistry. 35:1996;13056-13063.
    • (1996) Biochemistry , vol.35 , pp. 13056-13063
    • Bini, A.1    Itoh, Y.2    Kudryk, B.J.3    Nagase, H.4
  • 11
    • 0022534483 scopus 로고    scopus 로고
    • Effects of fibrinogen derivatives upon the inflammatory response: Studies with human fibrinopeptide
    • Senior R.M., Skogen W.F., Griffin G.L., Wilner G.D. Effects of fibrinogen derivatives upon the inflammatory response studies with human fibrinopeptide . Br. J. Clin. Invest. 77:1986;1014-1019.
    • (1986) Br. J. Clin. Invest. , vol.77 , pp. 1014-1019
    • Senior, R.M.1    Skogen, W.F.2    Griffin, G.L.3    Wilner, G.D.4
  • 13
    • 0027468975 scopus 로고
    • The structural motif glycine 190-valine 202 of fibrinogen γ chain interacts with the CD11b/CD18 integrin (aMb2, Mac-1) and promotes leukocyte adhesion
    • Altieri D.C., Plescia J., Plow E.F. The structural motif glycine 190-valine 202 of fibrinogen γ chain interacts with the CD11b/CD18 integrin (aMb2, Mac-1) and promotes leukocyte adhesion. J. Biol. Chem. 268:1993;1847-1853.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1847-1853
    • Altieri, D.C.1    Plescia, J.2    Plow, E.F.3
  • 14
    • 0017237180 scopus 로고
    • Chemotaxis for human monocytes by fibrinogen-derived peptides
    • Richardson D.L., Pepper B., Kay A.B. Chemotaxis for human monocytes by fibrinogen-derived peptides. Am. J. Hematol. 52:1976;507-513.
    • (1976) Am. J. Hematol. , vol.52 , pp. 507-513
    • Richardson, D.L.1    Pepper, B.2    Kay, A.B.3
  • 16
    • 0032504275 scopus 로고    scopus 로고
    • Role of β1 and β3 in human smooth muscle cell adhesion to and contraction of fibrin clots in-vitro
    • Yee K.O., Rooney M.M., Giacelli C.M., Lord S.T., Schwartz S.M. Role of β1 and β3 in human smooth muscle cell adhesion to and contraction of fibrin clots in-vitro. Circ. Res. 83:1998;241-251.
    • (1998) Circ. Res. , vol.83 , pp. 241-251
    • Yee, K.O.1    Rooney, M.M.2    Giacelli, C.M.3    Lord, S.T.4    Schwartz, S.M.5
  • 19
    • 0032033425 scopus 로고    scopus 로고
    • Chemotactic and growth stimulatory effects of fibrin(ogen) and thrombin on cultured fibroblasts
    • Gorodetsky R., Vexler A., An J., Mou X., Marx G. Chemotactic and growth stimulatory effects of fibrin(ogen) and thrombin on cultured fibroblasts. J. Lab. Clin. Med. 131:1998;269-280.
    • (1998) J. Lab. Clin. Med. , vol.131 , pp. 269-280
    • Gorodetsky, R.1    Vexler, A.2    An, J.3    Mou, X.4    Marx, G.5
  • 21
    • 0027419442 scopus 로고
    • Aα and Bβ chains of fibrinogen stimulate proliferation of human fibroblasts
    • Gray A.J., Bishop J.E., Reeves J.T., Laurent G.J. Aα and Bβ chains of fibrinogen stimulate proliferation of human fibroblasts. J. Cell. Sci. 104:1993;409-413.
    • (1993) J. Cell. Sci. , vol.104 , pp. 409-413
    • Gray, A.J.1    Bishop, J.E.2    Reeves, J.T.3    Laurent, G.J.4
  • 22
    • 0020972655 scopus 로고
    • Vasoactive peptides derived from degradation of fibrinogen and fibrin
    • Saldeen T. Vasoactive peptides derived from degradation of fibrinogen and fibrin. Ann. N.Y. Acad. Sci. USA. 408:1983;424-431.
    • (1983) Ann. N.Y. Acad. Sci. USA , vol.408 , pp. 424-431
    • Saldeen, T.1
  • 23
    • 0032535294 scopus 로고    scopus 로고
    • Structural studies of fibrinolysis by electron microscopy
    • Veklich Y., Francis C.W., White J., Weisel J.W. Structural studies of fibrinolysis by electron microscopy. Blood. 92:1998;4721-4729.
    • (1998) Blood , vol.92 , pp. 4721-4729
    • Veklich, Y.1    Francis, C.W.2    White, J.3    Weisel, J.W.4
  • 24
    • 0038398571 scopus 로고
    • Fibrinogen fragmentation by free radicals: Coagulation of fibrinogen with Cu(II) and ascorbate
    • E. Ricklis. Weinheim: Wiley-VCH
    • Marx G. Fibrinogen fragmentation by free radicals coagulation of fibrinogen with Cu(II) and ascorbate . Ricklis E. Radiation Biology. 1990;691-698 Wiley-VCH, Weinheim.
    • (1990) Radiation Biology , pp. 691-698
    • Marx, G.1
  • 25
    • 84907034627 scopus 로고
    • Immunological monitoring of Fenton fragmentation of fibrinogen
    • Marx G. Immunological monitoring of Fenton fragmentation of fibrinogen. Free Rad. Res. Commun. 12:1991;517-520.
    • (1991) Free Rad. Res. Commun. , vol.12 , pp. 517-520
    • Marx, G.1
  • 26
    • 0024428206 scopus 로고
    • Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells
    • Cheresh D.A., Berliner S.A., Vicente V., Ruggeri Z.M. Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells. Cell. 58:1989;945-953.
    • (1989) Cell , vol.58 , pp. 945-953
    • Cheresh, D.A.1    Berliner, S.A.2    Vicente, V.3    Ruggeri, Z.M.4
  • 28
    • 0026472751 scopus 로고
    • Inhibition of platelet adhesion to fibrin(ogen) in flowing whole blood by RGD and fibrinogen γ-chain carboxy terminal peptides
    • Hantgan R.R., Endenburg S., 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 RGD and fibrinogen γ-chain carboxy terminal peptides. Thromb. Haemost. 68:1992;694-700.
    • (1992) Thromb. Haemost. , vol.68 , pp. 694-700
    • Hantgan, R.R.1    Endenburg, S.2    Cavero, I.3    Marguerie, G.4    Uzan, A.5    Sixma, J.J.6    De Groot, P.G.7
  • 29
    • 0028973094 scopus 로고
    • Interaction of integrin alpha IIb beta with multiple fibrinogen domains during platelet adhesion
    • Savage B., Bottini E., Ruggeri Z.M. Interaction of integrin alpha IIb beta with multiple fibrinogen domains during platelet adhesion. J. Biol. Chem. 270:1995;28812-28817.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28812-28817
    • Savage, B.1    Bottini, E.2    Ruggeri, Z.M.3
  • 30
    • 0033522367 scopus 로고    scopus 로고
    • Specific binding of integrin αvβ3 to the fibrinogen α and αE chain C-terminal domains
    • Yokoyama K., Zhang X.P., Medved L., Takada Y. Specific binding of integrin αvβ3 to the fibrinogen α and αE chain C-terminal domains. Biochemistry. 38:1999;5872-5877.
    • (1999) Biochemistry , vol.38 , pp. 5872-5877
    • Yokoyama, K.1    Zhang, X.P.2    Medved, L.3    Takada, Y.4
  • 31
    • 0031057849 scopus 로고    scopus 로고
    • Fibrinogen is a ligand for integrin α5β1 in endothelial cells
    • Suehiro K., Gailit G., Plow E.F. Fibrinogen is a ligand for integrin α5β1 in endothelial cells. J. Biol. Chem. 272:1997;5360-5366.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5360-5366
    • Suehiro, K.1    Gailit, G.2    Plow, E.F.3
  • 32
    • 0031046237 scopus 로고    scopus 로고
    • Human fibroblast adhesion to fibrinogen
    • Farrell D.H., Al-Mondhiry H.A. Human fibroblast adhesion to fibrinogen. Biochemistry. 36:1997;1123-1128.
    • (1997) Biochemistry , vol.36 , pp. 1123-1128
    • Farrell, D.H.1    Al-Mondhiry, H.A.2
  • 34
    • 0029931068 scopus 로고    scopus 로고
    • Alternative adhesion sites in human fibrinogen for vascular endothelial cells
    • Thiagrajan P., Rippon A.J., Farrell D.H. Alternative adhesion sites in human fibrinogen for vascular endothelial cells. Biochemistry. 35:1996;4169-4175.
    • (1996) Biochemistry , vol.35 , pp. 4169-4175
    • Thiagrajan, P.1    Rippon, A.J.2    Farrell, D.H.3
  • 37
    • 0026729988 scopus 로고
    • Immuno-electrophoretic and immuno-histochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas
    • Valenuela R., Shainoff J.R., DiBello P.M., Urbanic D.A., Anderson J.M., Matsueda G.R., Kudryk B.J. Immuno-electrophoretic and immuno-histochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas. Am. J. Pathol. 141:1992;861-880.
    • (1992) Am. J. Pathol. , vol.141 , pp. 861-880
    • Valenuela, R.1    Shainoff, J.R.2    DiBello, P.M.3    Urbanic, D.A.4    Anderson, J.M.5    Matsueda, G.R.6    Kudryk, B.J.7
  • 38
    • 0001173793 scopus 로고    scopus 로고
    • Fibrinogen deficiency reduces vascular accumulation of apolipoprotein(a) and the development of atherosclerosis in apolipoprotein(a) transgenic mice
    • Horrigan F.T., Degen J.L., Lawn R.M. Fibrinogen deficiency reduces vascular accumulation of apolipoprotein(a) and the development of atherosclerosis in apolipoprotein(a) transgenic mice. Proc. Natl. Acad. Sci. USA. 95:1998;12591-12595.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12591-12595
    • Horrigan, F.T.1    Degen, J.L.2    Lawn, R.M.3
  • 39
    • 0028833860 scopus 로고
    • Pathogenesis of ascites tumor growth: Fibrinogen influx and fibrin accumulation in tissues lining the peritoneal cavity
    • Nagy J.A., Meyers M.S., Masse E.M., Herzberg K.T., Dvorak H.F. Pathogenesis of ascites tumor growth fibrinogen influx and fibrin accumulation in tissues lining the peritoneal cavity . Cancer Res. 55:1995;369-375.
    • (1995) Cancer Res. , vol.55 , pp. 369-375
    • Nagy, J.A.1    Meyers, M.S.2    Masse, E.M.3    Herzberg, K.T.4    Dvorak, H.F.5
  • 40
  • 44
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze S.R., Ho A., Vocero-Akbani A., Dowdy S.F. In vivo protein transduction delivery of a biologically active protein into the mouse . Science. 285:1999;1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 45
    • 0030904245 scopus 로고    scopus 로고
    • Truncated HIV-1 tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives E., Brodin P., Lebleu B. Truncated HIV-1 tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272:1997;16010-16017.
    • (1997) J. Biol. Chem , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 46
    • 0028113997 scopus 로고
    • Reversed-phase chromatography of synthetic amphiphilic alpha-helical peptides as a model for ligand/receptor interactions: Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains
    • Sereda T.J., Mant C.T., Sonnichsen F.D., Hodges R.S. Reversed-phase chromatography of synthetic amphiphilic alpha-helical peptides as a model for ligand/receptor interactions effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains . J. Chromatogy. 676:1994;139-153.
    • (1994) J. Chromatogy. , vol.676 , pp. 139-153
    • Sereda, T.J.1    Mant, C.T.2    Sonnichsen, F.D.3    Hodges, R.S.4
  • 47
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris, M.C., Vidal, P.L., Chaloin, Heitz, F., Divita, G. A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res. 25 (1997) 2730-2736.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.L.2    Chaloin Heitz, F.3    Divita, G.4
  • 48
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D., Joliot A.H., Chassaing G., Prochiantz A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269:1994;10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 49
    • 0031443422 scopus 로고    scopus 로고
    • Mode matches and their locations in the hydrophobic free energy sequences of peptide ligands and their receptor functions
    • Mandell A.J., Selz K.A., Shlesinger M.F. Mode matches and their locations in the hydrophobic free energy sequences of peptide ligands and their receptor functions. Proc. Natl. Acad. Sci. USA. 94:1997;13576-13581.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13576-13581
    • Mandell, A.J.1    Selz, K.A.2    Shlesinger, M.F.3
  • 50
    • 0031771874 scopus 로고    scopus 로고
    • Fibrin deposition in squamous cell carcinomas of the larynx and hypopharynx
    • Bardos H., Juhasz A., Repassy G., Adany R. Fibrin deposition in squamous cell carcinomas of the larynx and hypopharynx. Thromb. Haemost. 80:1998;767-772.
    • (1998) Thromb. Haemost. , vol.80 , pp. 767-772
    • Bardos, H.1    Juhasz, A.2    Repassy, G.3    Adany, R.4
  • 51
    • 0030906999 scopus 로고    scopus 로고
    • The fibrinogen like globe of tenascin-C mediates its interactions with neurocan and phophacan/protein-tyrosine phosphatase-ξβ
    • Milev P., Fischer D., Harig M., Schulthess T., Margolis R.K., Chicket-Ehrismann R., Margolis R.U. The fibrinogen like globe of tenascin-C mediates its interactions with neurocan and phophacan/protein-tyrosine phosphatase-ξβ J. Biol. Chem. 272:1997;15501-15509.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15501-15509
    • Milev, P.1    Fischer, D.2    Harig, M.3    Schulthess, T.4    Margolis, R.K.5    Chicket-Ehrismann, R.6    Margolis, R.U.7
  • 52
    • 0032844899 scopus 로고    scopus 로고
    • The fibrinogen-globe of tenascin-C promotes basic-FGF-induced endothelial cell elongation
    • Schenk S., Chiquet-Ehrismann R., Battegy E.J. The fibrinogen-globe of tenascin-C promotes basic-FGF-induced endothelial cell elongation. Mol. Biol Cell. 10:1999;2933-2943.
    • (1999) Mol. Biol Cell , vol.10 , pp. 2933-2943
    • Schenk, S.1    Chiquet-Ehrismann, R.2    Battegy, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.