메뉴 건너뛰기




Volumn 24, Issue 10, 2003, Pages 1759-1770

Engineering cell adhesive surfaces that direct integrin α5β1 binding using a recombinant fragment of fibronectin

Author keywords

Biomimetic; Cell adhesion; Fibronectin; Integrins; RGD

Indexed keywords

ADHESIVES; BIOMIMETIC MATERIALS; CONCENTRATION (PROCESS); PROTEINS;

EID: 0037404371     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0142-9612(02)00570-7     Document Type: Article
Times cited : (176)

References (65)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins. versatility, modulation, and signaling in cell adhesion Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 2
    • 0033036136 scopus 로고    scopus 로고
    • Extracellular matrix-integrin interactions in osteoblast function and tissue remodeling
    • Damsky C.H. Extracellular matrix-integrin interactions in osteoblast function and tissue remodeling. Bone. 25:1999;95-96.
    • (1999) Bone , vol.25 , pp. 95-96
    • Damsky, C.H.1
  • 3
    • 0034283814 scopus 로고    scopus 로고
    • Integrin and ECM functions: Roles in vertebrate development
    • De Arcangelis A., Georges-Labouesse E. Integrin and ECM functions. roles in vertebrate development Trends Genet. 16:2000;389-395.
    • (2000) Trends Genet , vol.16 , pp. 389-395
    • De Arcangelis, A.1    Georges-Labouesse, E.2
  • 4
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George E.L., Georges-Labouesse E.N., Patel-King R.S., Rayburn H., Hynes R.O. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 119:1993;1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 6
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta Y., Ilic D., Kanazawa S., Takeda N., Yamamoto T., Aizawa S. Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene. 11:1995;1989-1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 7
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development. 125:1998;327-337.
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 8
    • 0023848647 scopus 로고
    • In vitro and in vivo interactions of cells with biomaterials
    • Ziats N.P., Miller K.M., Anderson J.M. In vitro and in vivo interactions of cells with biomaterials. Biomaterials. 9:1988;5-13.
    • (1988) Biomaterials , vol.9 , pp. 5-13
    • Ziats, N.P.1    Miller, K.M.2    Anderson, J.M.3
  • 9
    • 0029203378 scopus 로고
    • Cell adhesion in animal cell culture: Physiological and fluid-mechanical implications
    • Koller M.R., Papoutsakis E.T. Cell adhesion in animal cell culture. physiological and fluid-mechanical implications Bioprocess Technol. 20:1995;61-110.
    • (1995) Bioprocess Technol , vol.20 , pp. 61-110
    • Koller, M.R.1    Papoutsakis, E.T.2
  • 10
    • 0027595948 scopus 로고
    • Tissue engineering
    • Langer R., Vacanti J.P. Tissue engineering. Science. 260:1993;920-926.
    • (1993) Science , vol.260 , pp. 920-926
    • Langer, R.1    Vacanti, J.P.2
  • 11
    • 0023649186 scopus 로고
    • Occupation of the extracellular matrix receptor integrin is a control point for myogenic differentiation
    • Menko A.S., Boettiger D. Occupation of the extracellular matrix receptor integrin is a control point for myogenic differentiation. Cell. 51:1987;51-57.
    • (1987) Cell , vol.51 , pp. 51-57
    • Menko, A.S.1    Boettiger, D.2
  • 12
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb Z., Tremble P.M., Behrendtsen O., Crowley E., Damsky C.H. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J Cell Biol. 109:1989;877-889.
    • (1989) J Cell Biol , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 14
    • 0029876639 scopus 로고    scopus 로고
    • Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein
    • Zhu X., Ohtsubo M., Bohmer R.M., Roberts J.M., Assoian R.K. Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein. J Cell Biol. 133:1996;391-403.
    • (1996) J Cell Biol , vol.133 , pp. 391-403
    • Zhu, X.1    Ohtsubo, M.2    Bohmer, R.M.3    Roberts, J.M.4    Assoian, R.K.5
  • 15
    • 0032935413 scopus 로고    scopus 로고
    • Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation
    • García A.J., Vega M.D., Boettiger D. Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation. Mol Biol Cell. 10:1999;785-798.
    • (1999) Mol Biol Cell , vol.10 , pp. 785-798
    • García, A.J.1    Vega, M.D.2    Boettiger, D.3
  • 22
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: A versatile cell recognition signal
    • Ruoslahti E., Pierschbacher M.D. Arg-Gly-Asp. a versatile cell recognition signal Cell. 44:1986;517-517.
    • (1986) Cell , vol.44 , pp. 517-517
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 23
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier A., Sonnenberg A. Function and interactions of integrins. Cell Tissue Res. 305:2001;285-298.
    • (2001) Cell Tissue Res , vol.305 , pp. 285-298
    • Van der Flier, A.1    Sonnenberg, A.2
  • 24
    • 0024292679 scopus 로고
    • Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
    • Obara M., Kang M.S., Yamada K.M. Site-directed mutagenesis of the cell-binding domain of human fibronectin. separable, synergistic sites mediate adhesive function Cell. 53(4):1988;649-657.
    • (1988) Cell , vol.53 , Issue.4 , pp. 649-657
    • Obara, M.1    Kang, M.S.2    Yamada, K.M.3
  • 25
  • 26
    • 0030880903 scopus 로고    scopus 로고
    • Interactions between integrin receptors and fibronectin are required for calvarial osteoblast differentiation in vitro
    • Moursi A.M., Globus R.K., Damsky C.H. Interactions between integrin receptors and fibronectin are required for calvarial osteoblast differentiation in vitro. J Cell Sci. 110:1997;2187-2196.
    • (1997) J Cell Sci , vol.110 , pp. 2187-2196
    • Moursi, A.M.1    Globus, R.K.2    Damsky, C.H.3
  • 27
    • 0032589393 scopus 로고    scopus 로고
    • Alpha5beta1 integrin controls cyclin D1 expression by sustaining mitogen-activated protein kinase activity in growth factor-treated cells
    • Roovers K., Davey G., Zhu X., Bottazzi M.E., Assoian R.K. Alpha5beta1 integrin controls cyclin D1 expression by sustaining mitogen-activated protein kinase activity in growth factor-treated cells. Mol Biol Cell. 10:1999;3197-3204.
    • (1999) Mol Biol Cell , vol.10 , pp. 3197-3204
    • Roovers, K.1    Davey, G.2    Zhu, X.3    Bottazzi, M.E.4    Assoian, R.K.5
  • 28
    • 0027422170 scopus 로고
    • The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly
    • Wu C., Bauer J.S., Juliano R.L., McDonald J.A. The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly. J Biol Chem. 268:1993;21883-21888.
    • (1993) J Biol Chem , vol.268 , pp. 21883-21888
    • Wu, C.1    Bauer, J.S.2    Juliano, R.L.3    McDonald, J.A.4
  • 29
    • 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.M. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J Biol Chem. 269:1994;24756-24761.
    • (1994) J Biol Chem , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 30
    • 0034678405 scopus 로고    scopus 로고
    • Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis
    • Redick S.D., Settles D.L., Briscoe G., Erickson H.P. Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis. J Cell Biol. 149:2000;521-527.
    • (2000) J Cell Biol , vol.149 , pp. 521-527
    • Redick, S.D.1    Settles, D.L.2    Briscoe, G.3    Erickson, H.P.4
  • 31
    • 0037162412 scopus 로고    scopus 로고
    • Distinct activation states of alpha5beta1 integrin show differential binding to RGD and synergy domains of fibronectin
    • García A.J., Schwarzbauer J.E., Boettiger D. Distinct activation states of alpha5beta1 integrin show differential binding to RGD and synergy domains of fibronectin. Biochemistry. 41:2002;9063-9069.
    • (2002) Biochemistry , vol.41 , pp. 9063-9069
    • García, A.J.1    Schwarzbauer, J.E.2    Boettiger, D.3
  • 32
    • 0030993915 scopus 로고    scopus 로고
    • Structural requirements for biological activity of the ninth and tenth FIII domains of human fibronectin
    • Grant R.P., Spitzfaden C., Altroff H., Campbell I.D., Mardon H.J. Structural requirements for biological activity of the ninth and tenth FIII domains of human fibronectin. J Biol Chem. 272:1997;6159-6166.
    • (1997) J Biol Chem , vol.272 , pp. 6159-6166
    • Grant, R.P.1    Spitzfaden, C.2    Altroff, H.3    Campbell, I.D.4    Mardon, H.J.5
  • 33
    • 0032994943 scopus 로고    scopus 로고
    • Bioactive biomaterials
    • Hubbell J.A. Bioactive biomaterials. Curr Opin Biotechnol. 10:1999;123-129.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 123-129
    • Hubbell, J.A.1
  • 34
    • 0031862030 scopus 로고    scopus 로고
    • Creating biomimetic micro-environments with synthetic polymer-peptide hybrid molecules
    • Shakesheff K., Cannizzaro S., Langer R. Creating biomimetic micro-environments with synthetic polymer-peptide hybrid molecules. J Biomater Sci Polym Ed. 9:1998;507-518.
    • (1998) J Biomater Sci Polym Ed , vol.9 , pp. 507-518
    • Shakesheff, K.1    Cannizzaro, S.2    Langer, R.3
  • 35
    • 0024704946 scopus 로고
    • Development of a novel artificial matrix with cell adhesion peptides for cell culture and artificial and hybrid organs
    • Matsuda T., Kondo A., Makino K., Akutsu T. Development of a novel artificial matrix with cell adhesion peptides for cell culture and artificial and hybrid organs. ASAIO Trans. 35:1989;677-679.
    • (1989) ASAIO Trans , vol.35 , pp. 677-679
    • Matsuda, T.1    Kondo, A.2    Makino, K.3    Akutsu, T.4
  • 36
    • 0025300277 scopus 로고
    • Covalent surface immobilization of Arg-Gly-Asp- and Tyr-Ile-Gly-Ser-Arg- containing peptides to obtain well-defined cell-adhesive substrates
    • Massia S.P., Hubbell J.A. Covalent surface immobilization of Arg-Gly-Asp- and Tyr-Ile-Gly-Ser-Arg- containing peptides to obtain well-defined cell-adhesive substrates. Anal Biochem. 187:1990;292-301.
    • (1990) Anal Biochem , vol.187 , pp. 292-301
    • Massia, S.P.1    Hubbell, J.A.2
  • 37
    • 0028116664 scopus 로고
    • Polymer networks with grafted cell adhesion peptides for highly biospecific cell adhesive substrates
    • Drumheller P.D., Hubbell J.A. Polymer networks with grafted cell adhesion peptides for highly biospecific cell adhesive substrates. Anal Biochem. 222:1994;380-388.
    • (1994) Anal Biochem , vol.222 , pp. 380-388
    • Drumheller, P.D.1    Hubbell, J.A.2
  • 38
    • 0030033721 scopus 로고    scopus 로고
    • Conditions which promote mineralization at the bone-implant interface: A model in vitro study
    • Dee K.C., Rueger D.C., Andersen T.T., Bizios R. Conditions which promote mineralization at the bone-implant interface. a model in vitro study Biomaterials. 17:1996;209-215.
    • (1996) Biomaterials , vol.17 , pp. 209-215
    • Dee, K.C.1    Rueger, D.C.2    Andersen, T.T.3    Bizios, R.4
  • 39
    • 0031824097 scopus 로고    scopus 로고
    • Biomolecular modification of p(AAm-co-EG/AA) IPNs supports osteoblast adhesion and phenotypic expression
    • Bearinger J.P., Castner D.G., Healy K.E. Biomolecular modification of p(AAm-co-EG/AA) IPNs supports osteoblast adhesion and phenotypic expression. J Biomater Sci Polym Ed. 9:1998;629-652.
    • (1998) J Biomater Sci Polym Ed , vol.9 , pp. 629-652
    • Bearinger, J.P.1    Castner, D.G.2    Healy, K.E.3
  • 40
    • 0032007690 scopus 로고    scopus 로고
    • Incorporation of adhesion peptides into nonadhesive hydrogels useful for tissue resurfacing
    • Hern D.L., Hubbell J.A. Incorporation of adhesion peptides into nonadhesive hydrogels useful for tissue resurfacing. J Biomed Mater Res. 39:1998;266-276.
    • (1998) J Biomed Mater Res , vol.39 , pp. 266-276
    • Hern, D.L.1    Hubbell, J.A.2
  • 41
    • 0032527082 scopus 로고    scopus 로고
    • A novel method for surface modification to promote cell attachment to hydrophobic substrates
    • Neff J.A., Caldwell K.D., Tresco P.A. A novel method for surface modification to promote cell attachment to hydrophobic substrates. J Biomed Mater Res. 40:1998;511-519.
    • (1998) J Biomed Mater Res , vol.40 , pp. 511-519
    • Neff, J.A.1    Caldwell, K.D.2    Tresco, P.A.3
  • 42
    • 0033054299 scopus 로고    scopus 로고
    • Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells
    • Rezania A., Healy K.E. Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells. Biotechnol Prog. 15:1999;19-32.
    • (1999) Biotechnol Prog , vol.15 , pp. 19-32
    • Rezania, A.1    Healy, K.E.2
  • 43
    • 0035889827 scopus 로고    scopus 로고
    • Smooth muscle cell growth in photopolymerized hydrogels with cell adhesive and proteolytically degradable domains: Synthetic ECM analogs for tissue engineering
    • Mann B.K., Gobin A.S., Tsai A.T., Schmedlen R.H., West J.L. Smooth muscle cell growth in photopolymerized hydrogels with cell adhesive and proteolytically degradable domains. synthetic ECM analogs for tissue engineering Biomaterials. 22:2001;3045-3051.
    • (2001) Biomaterials , vol.22 , pp. 3045-3051
    • Mann, B.K.1    Gobin, A.S.2    Tsai, A.T.3    Schmedlen, R.H.4    West, J.L.5
  • 46
    • 0035812487 scopus 로고    scopus 로고
    • Immobilized RGD peptides on surface-grafted dextran promote biospecific cell attachment
    • Massia S.P., Stark J. Immobilized RGD peptides on surface-grafted dextran promote biospecific cell attachment. J Biomed Mater Res. 56:2001;390-399.
    • (2001) J Biomed Mater Res , vol.56 , pp. 390-399
    • Massia, S.P.1    Stark, J.2
  • 47
    • 0035205503 scopus 로고    scopus 로고
    • Human osteoprogenitor growth and differentiation on synthetic biodegradable structures after surface modification
    • Yang X.B., Roach H.I., Clarke N.M., Howdle S.M., Quirk R., Shakesheff K.M., Oreffo R.O. Human osteoprogenitor growth and differentiation on synthetic biodegradable structures after surface modification. Bone. 29:2001;523-531.
    • (2001) Bone , vol.29 , pp. 523-531
    • Yang, X.B.1    Roach, H.I.2    Clarke, N.M.3    Howdle, S.M.4    Quirk, R.5    Shakesheff, K.M.6    Oreffo, R.O.7
  • 49
    • 0028925423 scopus 로고
    • Function and receptor specificity of a minimal 20 kilodalton cell adhesive fragment of fibronectin
    • Akiyama S.K., Aota S., Yamada K.M. Function and receptor specificity of a minimal 20 kilodalton cell adhesive fragment of fibronectin. Cell Adhes Commun. 3:1995;13-25.
    • (1995) Cell Adhes Commun , vol.3 , pp. 13-25
    • Akiyama, S.K.1    Aota, S.2    Yamada, K.M.3
  • 50
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins
    • Aukhil I., Joshi P., Yan Y., Erickson H.P. Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J Biol Chem. 268:1993;2542-2553.
    • (1993) J Biol Chem , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 51
    • 0036010014 scopus 로고    scopus 로고
    • Enhanced expression of the osteoblastic phenotype on substrates that modulate fibronectin conformation and integrin receptor binding
    • Stephansson S.N., Byers B.A., García A.J. Enhanced expression of the osteoblastic phenotype on substrates that modulate fibronectin conformation and integrin receptor binding. Biomaterials. 23:2002;2527-2534.
    • (2002) Biomaterials , vol.23 , pp. 2527-2534
    • Stephansson, S.N.1    Byers, B.A.2    García, A.J.3
  • 52
    • 0020414913 scopus 로고
    • Monoclonal antibody against human fibronectin inhibits cell attachment
    • Schoen R.C., Bentley K.L., Klebe R.J. Monoclonal antibody against human fibronectin inhibits cell attachment. Hybridoma. 1:1982;99-108.
    • (1982) Hybridoma , vol.1 , pp. 99-108
    • Schoen, R.C.1    Bentley, K.L.2    Klebe, R.J.3
  • 53
    • 0141724203 scopus 로고    scopus 로고
    • Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion
    • in press
    • Keselowsky BG, Collard DM, García AJ. Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion. J Biomed Mater Res, in press.
    • J Biomed Mater Res
    • Keselowsky, B.G.1    Collard, D.M.2    García, A.J.3
  • 54
    • 0028897148 scopus 로고
    • A genetic variant of albumin (albumin Asola; Tyr140→Cys) with no free -SH group but with an additional disulfide bridge
    • Minchiotti L., Galliano M., Kragh-Hansen U., Watkins S., Madison J., Putnam F.W. A genetic variant of albumin (albumin Asola; Tyr140→Cys) with no free -SH group but with an additional disulfide bridge. Eur J Biochem. 228:1995;155-159.
    • (1995) Eur J Biochem , vol.228 , pp. 155-159
    • Minchiotti, L.1    Galliano, M.2    Kragh-Hansen, U.3    Watkins, S.4    Madison, J.5    Putnam, F.W.6
  • 56
    • 0035135284 scopus 로고    scopus 로고
    • Surfactant-immobilized fibronectin enhances bioactivity and regulates sensory neurite outgrowth
    • Biran R., Webb K., Noble M.D., Tresco P.A. Surfactant-immobilized fibronectin enhances bioactivity and regulates sensory neurite outgrowth. J Biomed Mater Res. 55:2001;1-12.
    • (2001) J Biomed Mater Res , vol.55 , pp. 1-12
    • Biran, R.1    Webb, K.2    Noble, M.D.3    Tresco, P.A.4
  • 57
    • 85031216645 scopus 로고    scopus 로고
    • Engineering integrin-specific surfaces with a triple-helical collagen-mimetic peptide
    • in press
    • Reyes CD, García AJ. Engineering integrin-specific surfaces with a triple-helical collagen-mimetic peptide. J Biomed Mater Res, in press.
    • J Biomed Mater Res
    • Reyes, C.D.1    García, A.J.2
  • 58
    • 0032496959 scopus 로고    scopus 로고
    • Using mixed self-assembled monolayers presenting RGD and (EG)3OH groups to characterize long-term attachment of bovine capillary endothelial cells to surfaces
    • Roberts C., Chen C.S., Mrksich M., Martichonok V., Ingber D.E., Whitesides G.M. Using mixed self-assembled monolayers presenting RGD and (EG)3OH groups to characterize long-term attachment of bovine capillary endothelial cells to surfaces. J Am Chem Soc. 120:1998;6548-6555.
    • (1998) J Am Chem Soc , vol.120 , pp. 6548-6555
    • Roberts, C.1    Chen, C.S.2    Mrksich, M.3    Martichonok, V.4    Ingber, D.E.5    Whitesides, G.M.6
  • 59
    • 0035135285 scopus 로고    scopus 로고
    • Fibronectin modulates macrophage adhesion and FBGC formation: The role of RGD, PHSRN, and PRRARV domains
    • Kao W.J., Lee D., Schense J.C., Hubbell J.A. Fibronectin modulates macrophage adhesion and FBGC formation. the role of RGD, PHSRN, and PRRARV domains J Biomed Mater Res. 55:2001;79-88.
    • (2001) J Biomed Mater Res , vol.55 , pp. 79-88
    • Kao, W.J.1    Lee, D.2    Schense, J.C.3    Hubbell, J.A.4
  • 60
    • 0032486492 scopus 로고    scopus 로고
    • Design and function of novel osteoblast-adhesive peptides for chemical modification of biomaterials
    • Dee K.C., Andersen T.T., Bizios R. Design and function of novel osteoblast-adhesive peptides for chemical modification of biomaterials. J Biomed Mater Res. 40:1998;371-377.
    • (1998) J Biomed Mater Res , vol.40 , pp. 371-377
    • Dee, K.C.1    Andersen, T.T.2    Bizios, R.3
  • 61
  • 62
    • 0018838451 scopus 로고
    • Fibroblast adhesion to fibrinogen and fibrin substrata: Requirement for cold-insoluble globulin (plasma fibronectin)
    • Grinnell F., Feld M., Minter D. Fibroblast adhesion to fibrinogen and fibrin substrata. requirement for cold-insoluble globulin (plasma fibronectin) Cell. 19:1980;517-525.
    • (1980) Cell , vol.19 , pp. 517-525
    • Grinnell, F.1    Feld, M.2    Minter, D.3
  • 63
    • 0019766751 scopus 로고
    • Involvement of fibronectin, Von Willebrand factor, and fibrinogen in platelet interaction with solid substrata
    • Lahav J., Hynes R.O. Involvement of fibronectin, Von Willebrand factor, and fibrinogen in platelet interaction with solid substrata. J Supramol Struct Cell Biochem. 17:1981;299-311.
    • (1981) J Supramol Struct Cell Biochem , vol.17 , pp. 299-311
    • Lahav, J.1    Hynes, R.O.2
  • 64
    • 0037093523 scopus 로고    scopus 로고
    • The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases
    • Stanton H., Ung L., Fosang A.J. The 45. kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases Biochem J. 364:2002;181-190.
    • (2002) Biochem J , vol.364 , pp. 181-190
    • Stanton, H.1    Ung, L.2    Fosang, A.J.3
  • 65
    • 0036161629 scopus 로고    scopus 로고
    • A fibronectin fragment induces type II collagen degradation by collagenase through an interleukin-1-mediated pathway
    • Yasuda T., Poole A.R. A fibronectin fragment induces type II collagen degradation by collagenase through an interleukin-1-mediated pathway. Arthritis Rheum. 46:2002;138-148.
    • (2002) Arthritis Rheum , vol.46 , pp. 138-148
    • Yasuda, T.1    Poole, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.