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Volumn 6, Issue 5, 2011, Pages

Role of surface chemistry in protein remodeling at the cell-material interface

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; FOCAL ADHESION KINASE; GELATINASE A; GELATINASE B; INTEGRIN; SCLEROPROTEIN; TRANSCRIPTION FACTOR RUNX2; PHOSPHOTYROSINE;

EID: 79955853234     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019610     Document Type: Article
Times cited : (76)

References (77)
  • 1
    • 0022896245 scopus 로고
    • Focal adhesion sites and the removal of substratum-bound fibronectin
    • Grinnell F, (1986) Focal adhesion sites and the removal of substratum-bound fibronectin. J Cell Biol 103: 2697-2706.
    • (1986) J Cell Biol , vol.103 , pp. 2697-2706
    • Grinnell, F.1
  • 2
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes RO, (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110: 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 3
    • 23944456131 scopus 로고    scopus 로고
    • Get a grip: integrins in cell-biomaterial interactions
    • García AJ, (2005) Get a grip: integrins in cell-biomaterial interactions. Biomaterials 26: 7525-7529.
    • (2005) Biomaterials , vol.26 , pp. 7525-7529
    • García, A.J.1
  • 5
    • 0036299093 scopus 로고    scopus 로고
    • Tissue engineering and reparative medicine
    • Spie J, (2002) Tissue engineering and reparative medicine. Ann NY Acad Sci 961: 1-9.
    • (2002) Ann NY Acad Sci , vol.961 , pp. 1-9
    • Spie, J.1
  • 6
    • 18244366662 scopus 로고    scopus 로고
    • Tissue engineering - Current challenges and expanding opportunities
    • Griffin L, Naughton G, (2002) Tissue engineering - Current challenges and expanding opportunities. Science 259: 1009-1014.
    • (2002) Science , vol.259 , pp. 1009-1014
    • Griffin, L.1    Naughton, G.2
  • 7
    • 0028500114 scopus 로고
    • Reorganization of substratum-bound fibronectin on hydrophilic and hydrophobic materials is related to biocompatibility
    • Altankov G, Groth T, (1994) Reorganization of substratum-bound fibronectin on hydrophilic and hydrophobic materials is related to biocompatibility. J Mater Sci Mater M 5: 732-737.
    • (1994) J Mater Sci Mater M , vol.5 , pp. 732-737
    • Altankov, G.1    Groth, T.2
  • 8
    • 0019467882 scopus 로고
    • The removal of extracellular fibronectin from areas of cell-substrate contact
    • Avnur Z, Geiger B, (1981) The removal of extracellular fibronectin from areas of cell-substrate contact. Cell 25: 121-132.
    • (1981) Cell , vol.25 , pp. 121-132
    • Avnur, Z.1    Geiger, B.2
  • 9
    • 0030665379 scopus 로고    scopus 로고
    • Morphological evidence for different fibronectin receptor organization and function during fibroblast adhesion on hydrophilic and hydrophobic glass substrata
    • Altankov G, Groth T, Krasteva N, Albrecht W, Paul D, (1997) Morphological evidence for different fibronectin receptor organization and function during fibroblast adhesion on hydrophilic and hydrophobic glass substrata. J Biomat Sci Polym E 8: 721-740.
    • (1997) J Biomat Sci Polym E , vol.8 , pp. 721-740
    • Altankov, G.1    Groth, T.2    Krasteva, N.3    Albrecht, W.4    Paul, D.5
  • 10
    • 0036978457 scopus 로고    scopus 로고
    • Remodeling of fibrinogen by endothelial cells in dependence of fibronectin matrix assembly. Effect of substratum wettability
    • Tzoneva R, Groth T, Altankov G, Paul D, (2002) Remodeling of fibrinogen by endothelial cells in dependence of fibronectin matrix assembly. Effect of substratum wettability. J Mater Sci Mater M 13: 1235-1244.
    • (2002) J Mater Sci Mater M , vol.13 , pp. 1235-1244
    • Tzoneva, R.1    Groth, T.2    Altankov, G.3    Paul, D.4
  • 11
    • 0030199743 scopus 로고    scopus 로고
    • Fibronectin matrix formation and the biocompatibility of materials
    • Altankov G, Groth T, (2006) Fibronectin matrix formation and the biocompatibility of materials. J Mater Sci Mater M 7: 425-429.
    • (2006) J Mater Sci Mater M , vol.7 , pp. 425-429
    • Altankov, G.1    Groth, T.2
  • 12
    • 27744560439 scopus 로고    scopus 로고
    • Fibronectin fibril pattern displays the force balance of cell-matrix adhesion
    • Pompe T, Keller K, Mitdank C, Werner C, (2005) Fibronectin fibril pattern displays the force balance of cell-matrix adhesion. Eur Biophys J 34: 1049-1056.
    • (2005) Eur Biophys J , vol.34 , pp. 1049-1056
    • Pompe, T.1    Keller, K.2    Mitdank, C.3    Werner, C.4
  • 13
    • 33746902380 scopus 로고    scopus 로고
    • Inhibition of urokinase type plasminogen activator or matrix metalloproteinases prevents cardiac injury and dysfunction during viral myocarditis
    • Heyman S, Pauschinger M, De Plama A, Kollwellis-Opara A, Rutschow S, et al. (2006) Inhibition of urokinase type plasminogen activator or matrix metalloproteinases prevents cardiac injury and dysfunction during viral myocarditis. Circulation 114: 565-573.
    • (2006) Circulation , vol.114 , pp. 565-573
    • Heyman, S.1    Pauschinger, M.2    De Plama, A.3    Kollwellis-Opara, A.4    Rutschow, S.5
  • 14
    • 2142784516 scopus 로고    scopus 로고
    • MT1 MMP deficient mice develop dwarfism, osteopenia, arthritis and connective tissue disease due to unadequate collagen turnover
    • Holmbeck K, Bianco P, Caterina S, et al. (1999) MT1 MMP deficient mice develop dwarfism, osteopenia, arthritis and connective tissue disease due to unadequate collagen turnover. Cell 99: 81-92.
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1    Bianco, P.2    Caterina, S.3
  • 15
    • 34249987617 scopus 로고    scopus 로고
    • Increased carcinogenic potential of myeloid tumor cells induced by aberrant TGF-beta-signaling of cathepsin B
    • Reisenawer A, Eickelberg O, Wille A, Heimburg A, Reinhold A, et al. (2007) Increased carcinogenic potential of myeloid tumor cells induced by aberrant TGF-beta-signaling of cathepsin B. Biol Chem 288: 639-650.
    • (2007) Biol Chem , vol.288 , pp. 639-650
    • Reisenawer, A.1    Eickelberg, O.2    Wille, A.3    Heimburg, A.4    Reinhold, A.5
  • 16
    • 22344436842 scopus 로고    scopus 로고
    • Intracellular collagen degradation mediated ny uPAR/Endo 180 is a major pathway of extracellular matrix turnover during malignancy
    • Carino AC, Engelholm LH, Yamada SS, Holmbeck K, Lund LR, et al. (2005) Intracellular collagen degradation mediated ny uPAR/Endo 180 is a major pathway of extracellular matrix turnover during malignancy. J Cell Biol 169: 977-985.
    • (2005) J Cell Biol , vol.169 , pp. 977-985
    • Carino, A.C.1    Engelholm, L.H.2    Yamada, S.S.3    Holmbeck, K.4    Lund, L.R.5
  • 17
    • 0034651996 scopus 로고    scopus 로고
    • Unraveling the role of proteases in cancer
    • Koblinski J, Ahram M, Sloane BF, (2000) Unraveling the role of proteases in cancer. Clin Chem Acta 291: 113-135.
    • (2000) Clin Chem Acta , vol.291 , pp. 113-135
    • Koblinski, J.1    Ahram, M.2    Sloane, B.F.3
  • 18
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: multifunctional enzymes in cancer
    • Mohamed M, Sloane BF, (2006) Cysteine cathepsins: multifunctional enzymes in cancer. Nat Rev Cancer 6: 764-775.
    • (2006) Nat Rev Cancer , vol.6 , pp. 764-775
    • Mohamed, M.1    Sloane, B.F.2
  • 19
    • 0026575258 scopus 로고
    • Degradation of extracellular matrix proteins by human cathepsin B from normal and tumour tissues
    • Buck MR, Karustic DG, Day NA, Honn KV, Sloane BF, (1992) Degradation of extracellular matrix proteins by human cathepsin B from normal and tumour tissues. Biochem J 282: 273-278.
    • (1992) Biochem J , vol.282 , pp. 273-278
    • Buck, M.R.1    Karustic, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 20
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metaloproteinases and the regulation of tissue remodeling
    • Page-McCaw A, Ewald AJ, Werb Z, (2007) Matrix metaloproteinases and the regulation of tissue remodeling. Nat Rev Mol Cell Biol 8: 221-233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 21
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics
    • Rodríguez D, Morrison C, Over CM, (2010) Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics. Biochimica et Biophysica Acta 1803: 39-54.
    • (2010) Biochimica Et Biophysica Acta , vol.1803 , pp. 39-54
    • Rodríguez, D.1    Morrison, C.2    Over, C.M.3
  • 22
    • 70249120017 scopus 로고    scopus 로고
    • Polymer brushes and self-assembled monolayers: Versatile platforms to control cell adhesion to biomaterials
    • Raynor JE, Capadona JR, Collard DM, Petrie TA, García AJ, (2009) Polymer brushes and self-assembled monolayers: Versatile platforms to control cell adhesion to biomaterials. Biointerphases 4: FA3-16.
    • (2009) Biointerphases , vol.4 , pp. 3-16
    • Raynor, J.E.1    Capadona, J.R.2    Collard, D.M.3    Petrie, T.A.4    García, A.J.5
  • 23
    • 0141690719 scopus 로고    scopus 로고
    • Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion
    • Keselowsky BG, Collard DM, Garcia AJ, (2003) Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion. J Biomed Mater Res 66: 247-259.
    • (2003) J Biomed Mater Res , vol.66 , pp. 247-259
    • Keselowsky, B.G.1    Collard, D.M.2    Garcia, A.J.3
  • 24
    • 0344306504 scopus 로고    scopus 로고
    • Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers
    • Martins MC, Ratner BD, Barbosa MA, (2003) Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers. J Biomed Mater Res A 67: 158-71.
    • (2003) J Biomed Mater Res A , vol.67 , pp. 158-171
    • Martins, M.C.1    Ratner, B.D.2    Barbosa, M.A.3
  • 25
    • 33746216936 scopus 로고    scopus 로고
    • Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl/methyl terminated self-assembled monolayers
    • Rodrigues SN, Gonçalves IC, Martins MC, Barbosa MA, Ratner BD, (2006) Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl/methyl terminated self-assembled monolayers. Biomaterials 27: 5357-5367.
    • (2006) Biomaterials , vol.27 , pp. 5357-5367
    • Rodrigues, S.N.1    Gonçalves, I.C.2    Martins, M.C.3    Barbosa, M.A.4    Ratner, B.D.5
  • 26
    • 72649084943 scopus 로고    scopus 로고
    • Substrate-induced assembly of fibronectin into networks: influence of surface chemistry and effect on osteoblast adhesion
    • Rico P, Rodríguez Hernández JC, Moratal D, Altankov G, Monleón Pradas M, et al. (2009) Substrate-induced assembly of fibronectin into networks: influence of surface chemistry and effect on osteoblast adhesion. Tiss Eng Part A 15: 3271-3281.
    • (2009) Tiss Eng Part A , vol.15 , pp. 3271-3281
    • Rico, P.1    Rodríguez Hernández, J.C.2    Moratal, D.3    Altankov, G.4    Monleón Pradas, M.5
  • 28
    • 0034082752 scopus 로고    scopus 로고
    • Modulating fibroblast adhesion, spreading, and proliferation using self-assembled monolayer films of alkylthiolates on gold
    • McClary, Ugarova T, Grainger DW, (2000) Modulating fibroblast adhesion, spreading, and proliferation using self-assembled monolayer films of alkylthiolates on gold. J Biomed Mater Res 50A: 428-439.
    • (2000) J Biomed Mater Res , vol.50 A , pp. 428-439
    • McClary1    Ugarova, T.2    Grainger, D.W.3
  • 29
    • 0020414913 scopus 로고
    • Monoclonal antibody against human fibronectin which inhibits cell attachment
    • Schoen RC, Bentley KL, Klebe RJ, (1982) Monoclonal antibody against human fibronectin which inhibits cell attachment. Hybridoma 1: 99-108.
    • (1982) Hybridoma , vol.1 , pp. 99-108
    • Schoen, R.C.1    Bentley, K.L.2    Klebe, R.J.3
  • 30
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic D, Furuta Y, Kanazawa S, Takeda N, Sobue K, et al. (1995) Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377: 539-544.
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1    Furuta, Y.2    Kanazawa, S.3    Takeda, N.4    Sobue, K.5
  • 31
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary LA, Chang JF, Guan JL, (1996) Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J Cell Sci 109: 1787-1794.
    • (1996) J Cell Sci , vol.109 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.L.3
  • 32
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch SM, Vuori K, Ruoslahti E, Chan-Hui PY, (1996) Control of adhesion-dependent cell survival by focal adhesion kinase. J Cell Biol 134: 793-799.
    • (1996) J Cell Biol , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.Y.4
  • 33
    • 0032576547 scopus 로고    scopus 로고
    • Regulation of the cell cycle by focal adhesion kinase
    • Zhao JH, Reiske H, Guan JL, (1998) Regulation of the cell cycle by focal adhesion kinase. J Cell Biol 143: 1997-2008.
    • (1998) J Cell Biol , vol.143 , pp. 1997-2008
    • Zhao, J.H.1    Reiske, H.2    Guan, J.L.3
  • 34
    • 0038823614 scopus 로고    scopus 로고
    • Myofibroblast differentiation by transforming growth factor-beta1 is dependent on cell adhesion and integrin signaling via focal adhesion kinase
    • Thannickal VJ, Lee DY, White ES, Cui Z, Larios JM, et al. (2003) Myofibroblast differentiation by transforming growth factor-beta1 is dependent on cell adhesion and integrin signaling via focal adhesion kinase. J Biol Chem 278: 12384-12389.
    • (2003) J Biol Chem , vol.278 , pp. 12384-12389
    • Thannickal, V.J.1    Lee, D.Y.2    White, E.S.3    Cui, Z.4    Larios, J.M.5
  • 35
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, et al. (1994) Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14: 1680-1688.
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5
  • 36
    • 0033617357 scopus 로고    scopus 로고
    • Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration
    • Reiske HR, Kao SC, Cary LA, Guan JL, Lai JF, et al. (1999) Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration. J Biol Chem 274: 12361-12366.
    • (1999) J Biol Chem , vol.274 , pp. 12361-12366
    • Reiske, H.R.1    Kao, S.C.2    Cary, L.A.3    Guan, J.L.4    Lai, J.F.5
  • 37
    • 33749552179 scopus 로고    scopus 로고
    • Fabrication methods of an engineered microenvironment for analysis of cell-biomaterial interactions
    • Shin H, (2007) Fabrication methods of an engineered microenvironment for analysis of cell-biomaterial interactions. Biomaterials 28: 126-133.
    • (2007) Biomaterials , vol.28 , pp. 126-133
    • Shin, H.1
  • 38
    • 77955057133 scopus 로고    scopus 로고
    • Effects of surface properties and bioactivation of biomaterials on endothelial cells
    • Monchaux E, Vermette P, (2010) Effects of surface properties and bioactivation of biomaterials on endothelial cells. Front Biosci (Schol Ed) 2: 239-255.
    • (2010) Front Biosci (Schol Ed) , vol.2 , pp. 239-255
    • Monchaux, E.1    Vermette, P.2
  • 39
    • 17144422105 scopus 로고    scopus 로고
    • Mediation of biomaterial-cell interactions by adsorbed proteins: a review
    • Wilson CJ, Clegg RE, Leavesley DI, Pearcy MJ, (2005) Mediation of biomaterial-cell interactions by adsorbed proteins: a review. Tissue Eng 11 (1-2): 1-18.
    • (2005) Tissue Eng , vol.11 , Issue.1-2 , pp. 1-18
    • Wilson, C.J.1    Clegg, R.E.2    Leavesley, D.I.3    Pearcy, M.J.4
  • 40
    • 79953234254 scopus 로고    scopus 로고
    • Bioadhesion of various proteins on random, diblock and triblock copolymer surfaces and the effect of pH conditions
    • Palacio ML, Schricker SR, Bhushan B, (2011) Bioadhesion of various proteins on random, diblock and triblock copolymer surfaces and the effect of pH conditions. J R Soc Interface 8: 630-640.
    • (2011) J R Soc Interface , vol.8 , pp. 630-640
    • Palacio, M.L.1    Schricker, S.R.2    Bhushan, B.3
  • 41
    • 55249093830 scopus 로고    scopus 로고
    • The correlation between the adsorption of adhesive proteins and cell behaviour on hidroxi-methyl mixed self-assembled monolayer
    • Barrias CC, Martins MCL, Almeida-Porada G, Barbosa M, Granja PL, (2009) The correlation between the adsorption of adhesive proteins and cell behaviour on hidroxi-methyl mixed self-assembled monolayer. Biomaterials 30: 307-316.
    • (2009) Biomaterials , vol.30 , pp. 307-316
    • Barrias, C.C.1    Martins, M.C.L.2    Almeida-Porada, G.3    Barbosa, M.4    Granja, P.L.5
  • 42
    • 0141843475 scopus 로고    scopus 로고
    • Adsorption-Induced Conformational Changes in Fibronectin Due to Interactions with Well-Defined Surface Chemistries
    • Michael KE, Vernekar VN, Keselowsky BG, Meredith JC, Latour RA, et al. (2003) Adsorption-Induced Conformational Changes in Fibronectin Due to Interactions with Well-Defined Surface Chemistries. Langmuir 19: 8033-8040.
    • (2003) Langmuir , vol.19 , pp. 8033-8040
    • Michael, K.E.1    Vernekar, V.N.2    Keselowsky, B.G.3    Meredith, J.C.4    Latour, R.A.5
  • 43
    • 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 KM, (1994) The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J Biol Chem2 69: 24756-24761.
    • (1994) J Biol Chem2 , vol.69 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 44
    • 70349923746 scopus 로고    scopus 로고
    • Biological Activity of the Substrate-Induced Fibronectin Network: Insight into the Third Dimension through Electrospun Fibers
    • Gugutkov D, Hernandez JCR, González-García C, Altankov G, Salmerón-Sánchez M, (2009) Biological Activity of the Substrate-Induced Fibronectin Network: Insight into the Third Dimension through Electrospun Fibers. Langmuir 25 (18): 10893-10900.
    • (2009) Langmuir , vol.25 , Issue.18 , pp. 10893-10900
    • Gugutkov, D.1    Hernandez, J.C.R.2    González-García, C.3    Altankov, G.4    Salmerón-Sánchez, M.5
  • 45
    • 2942514778 scopus 로고    scopus 로고
    • Surface chemistry modulates focal adhesion composition and signaling through changes in integrin
    • Keselowsky BG, Collard DM, García AJ, (2004) Surface chemistry modulates focal adhesion composition and signaling through changes in integrin. Biomaterials 25: 5947-5954.
    • (2004) Biomaterials , vol.25 , pp. 5947-5954
    • Keselowsky, B.G.1    Collard, D.M.2    García, A.J.3
  • 46
    • 34247131744 scopus 로고    scopus 로고
    • Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers
    • Arima Y, Iwata H, (2007) Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers. Biomaterials 28: 3074-3082.
    • (2007) Biomaterials , vol.28 , pp. 3074-3082
    • Arima, Y.1    Iwata, H.2
  • 47
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, et al. (1994) Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14: 1680-1688.
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5
  • 49
    • 0033772308 scopus 로고    scopus 로고
    • FAK integrates growth-factor and integrin signals to promote cell migration
    • Sieg DJ, Hauck CR, Ilic D, Klingbeil CK, Schaefer E, et al. (2000) FAK integrates growth-factor and integrin signals to promote cell migration. Nat Cell Biol 2: 249-256.
    • (2000) Nat Cell Biol , vol.2 , pp. 249-256
    • Sieg, D.J.1    Hauck, C.R.2    Ilic, D.3    Klingbeil, C.K.4    Schaefer, E.5
  • 50
    • 0035949694 scopus 로고    scopus 로고
    • Focal adhesion kinase is involved in mechanosensing during fibroblast migration
    • Wang HB, Dembo M, Hanks SK, Wang YY, (2001) Focal adhesion kinase is involved in mechanosensing during fibroblast migration. Proc Natl Acad Sci USA 98: 11295-11300.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11295-11300
    • Wang, H.B.1    Dembo, M.2    Hanks, S.K.3    Wang, Y.Y.4
  • 51
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
    • Webb DJ, Donais K, Whitmore LA, Thomas SM, Turner CE, et al. (2004) FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat Cell Biol 6: 154-161.
    • (2004) Nat Cell Biol , vol.6 , pp. 154-161
    • Webb, D.J.1    Donais, K.2    Whitmore, L.A.3    Thomas, S.M.4    Turner, C.E.5
  • 52
    • 0028500114 scopus 로고
    • Reorganization of substratum-bound fibronectin on hydrophilic and hydrophobic materials is related to biocompatibility
    • Altankov G, Groth T, (1994) Reorganization of substratum-bound fibronectin on hydrophilic and hydrophobic materials is related to biocompatibility. J Mater Sci Mater Med 5: 732-737.
    • (1994) J Mater Sci Mater Med , vol.5 , pp. 732-737
    • Altankov, G.1    Groth, T.2
  • 53
    • 0030199743 scopus 로고    scopus 로고
    • Fibronectin matrix formation and the biocompatibility of materials
    • Altankov G, Groth T, (1996) Fibronectin matrix formation and the biocompatibility of materials. J Mater Sci Mater Med 7: 425-429.
    • (1996) J Mater Sci Mater Med , vol.7 , pp. 425-429
    • Altankov, G.1    Groth, T.2
  • 54
    • 0030665379 scopus 로고    scopus 로고
    • Morphological evidence for different fibronectin receptor organization and function during fibroblast adhesion on hydrophilic and hydrophobic glass substrata
    • Altankov G, Groth T, Krasteva N, Albrecht W, Paul D, (1997) Morphological evidence for different fibronectin receptor organization and function during fibroblast adhesion on hydrophilic and hydrophobic glass substrata. J Biomat Sci Polym E 8: 721-740.
    • (1997) J Biomat Sci Polym E , vol.8 , pp. 721-740
    • Altankov, G.1    Groth, T.2    Krasteva, N.3    Albrecht, W.4    Paul, D.5
  • 55
    • 0036978457 scopus 로고    scopus 로고
    • Remodeling of fibrinogen by endothelial cells in dependence of fibronectin matrix assembly. Effect of substratum wettability
    • Tzoneva R, Groth T, Altankov G, Paul D, (2002) Remodeling of fibrinogen by endothelial cells in dependence of fibronectin matrix assembly. Effect of substratum wettability. J Mater Sci Mater M 13: 1235-1244.
    • (2002) J Mater Sci Mater M , vol.13 , pp. 1235-1244
    • Tzoneva, R.1    Groth, T.2    Altankov, G.3    Paul, D.4
  • 56
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • Kaibuchi K, Kuroda S, Amano M, (1999) Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu Rev Biochem 68: 459-486.
    • (1999) Annu Rev Biochem , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 57
    • 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
  • 59
    • 0242509224 scopus 로고    scopus 로고
    • ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix
    • Wozniak MA, Desai R, Solski PA, Der CJ, Keely PJ, (2003) ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix. J Cell Biol 163: 583-595.
    • (2003) J Cell Biol , vol.163 , pp. 583-595
    • Wozniak, M.A.1    Desai, R.2    Solski, P.A.3    Der, C.J.4    Keely, P.J.5
  • 60
    • 77951246518 scopus 로고    scopus 로고
    • Contractility Modulates Cell Adhesion Strengthening Through Focal Adhesion Kinase and Assembly of Vinculin-Containing Focal Adhesions
    • Dumbauld DW, Shin H, Gallant N, Michael K, Radhakrishna H, et al. (2010) Contractility Modulates Cell Adhesion Strengthening Through Focal Adhesion Kinase and Assembly of Vinculin-Containing Focal Adhesions. J Cell Physiol 223: 746-756.
    • (2010) J Cell Physiol , vol.223 , pp. 746-756
    • Dumbauld, D.W.1    Shin, H.2    Gallant, N.3    Michael, K.4    Radhakrishna, H.5
  • 61
    • 77950863692 scopus 로고    scopus 로고
    • Effect of nanoscale topography on fibronectin adsorption, focal adhesion size and matrix organisation
    • González-García C, Sousa S, Moratal D, Rico P, Salmerón-Sánchez M, (2010) Effect of nanoscale topography on fibronectin adsorption, focal adhesion size and matrix organisation. Col Surf B 77: 181-190.
    • (2010) Col Surf B , vol.77 , pp. 181-190
    • González-García, C.1    Sousa, S.2    Moratal, D.3    Rico, P.4    Salmerón-Sánchez, M.5
  • 62
    • 77956181531 scopus 로고    scopus 로고
    • The effect of matrix characteristics on fibroblasts proliferation in 3D gels
    • Bott K, Upton Z, Schrobback K, Ehrbar M, Hubbell JA, et al. (2010) The effect of matrix characteristics on fibroblasts proliferation in 3D gels. Biomaterials 31: 8454-8464.
    • (2010) Biomaterials , vol.31 , pp. 8454-8464
    • Bott, K.1    Upton, Z.2    Schrobback, K.3    Ehrbar, M.4    Hubbell, J.A.5
  • 64
    • 0037965624 scopus 로고    scopus 로고
    • Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics
    • Lutolf MP, Lauer-Fields JL, Schmoekel HG, Metters AT, Weber FE, et al. (2003) Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics. Proc Nat Acad Sci 100: 5413-5418.
    • (2003) Proc Nat Acad Sci , vol.100 , pp. 5413-5418
    • Lutolf, M.P.1    Lauer-Fields, J.L.2    Schmoekel, H.G.3    Metters, A.T.4    Weber, F.E.5
  • 65
    • 70449084690 scopus 로고    scopus 로고
    • The osteogenic differentiation of adult bone marrow and perinatal umbilical mesenchymal stem cells and matrix remodelling in three-dimensional collagen scaffolds
    • Schneider R, Puellen A, Kramann R, Raupach K, Bornemann I, et al. (2010) The osteogenic differentiation of adult bone marrow and perinatal umbilical mesenchymal stem cells and matrix remodelling in three-dimensional collagen scaffolds. Biomaterials 31: 467-480.
    • (2010) Biomaterials , vol.31 , pp. 467-480
    • Schneider, R.1    Puellen, A.2    Kramann, R.3    Raupach, K.4    Bornemann, I.5
  • 66
    • 0033795706 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) by bone resorptive factors in osteoblastic cells
    • Uchida M, Shima M, Shimoaka T, Fujieda A, Obara K, et al. (2000) Regulation of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) by bone resorptive factors in osteoblastic cells. J Cell Physiol 185: 207-214.
    • (2000) J Cell Physiol , vol.185 , pp. 207-214
    • Uchida, M.1    Shima, M.2    Shimoaka, T.3    Fujieda, A.4    Obara, K.5
  • 67
    • 33847195428 scopus 로고    scopus 로고
    • Matriz metalloproteinases and the regulation of tissue remodelling
    • Page-MacCaw A, Ewald AJ, Werb Z, (2007) Matriz metalloproteinases and the regulation of tissue remodelling. Nat Mol Cell Biol 8: 221-233.
    • (2007) Nat Mol Cell Biol , vol.8 , pp. 221-233
    • Page-MacCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 68
    • 41849105806 scopus 로고    scopus 로고
    • The inicial stops of ovarian cancer cell metastasis are mediated by MMP-2 cleavage of vitronectin and fibronectin
    • Kenny HA, Kaur S, Coussens LM, Lengyel E, (2008) The inicial stops of ovarian cancer cell metastasis are mediated by MMP-2 cleavage of vitronectin and fibronectin. J Clin Invest 118: 1367-1379.
    • (2008) J Clin Invest , vol.118 , pp. 1367-1379
    • Kenny, H.A.1    Kaur, S.2    Coussens, L.M.3    Lengyel, E.4
  • 69
    • 2542442353 scopus 로고    scopus 로고
    • Mechanical strain induces collagenase-3 (MMP-13) expresión in MC3T3-E1 osteoblastic cells
    • Yang CM, Chien CS, Yao CC, Hsiao LD, Huang YC, et al. (2004) Mechanical strain induces collagenase-3 (MMP-13) expresión in MC3T3-E1 osteoblastic cells. J Biol Chem 279: 22158-22165.
    • (2004) J Biol Chem , vol.279 , pp. 22158-22165
    • Yang, C.M.1    Chien, C.S.2    Yao, C.C.3    Hsiao, L.D.4    Huang, Y.C.5
  • 70
    • 56049124072 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and -9 are induced differently by metal nanoparticles in human monocytes: The role of oxidative stress and protein tyrosine kinase activation
    • Wan R, Mo Y, Zhang X, Chien S, Tollerud DJ, et al. (2009) Matrix metalloproteinase-2 and-9 are induced differently by metal nanoparticles in human monocytes: The role of oxidative stress and protein tyrosine kinase activation. Toxicology and Applied Pharmacology 233: 276-285.
    • (2009) Toxicology and Applied Pharmacology , vol.233 , pp. 276-285
    • Wan, R.1    Mo, Y.2    Zhang, X.3    Chien, S.4    Tollerud, D.J.5
  • 71
    • 72349091680 scopus 로고    scopus 로고
    • MMP-9 and CD68+ cells are required for tissue remodeling in response to natural hydroxyapatite
    • Zambuzzi W, Paiva KB, Menezes R, Oliveira RC, Taga R, et al. (2009) MMP-9 and CD68+ cells are required for tissue remodeling in response to natural hydroxyapatite. J Mol Hist 40: 301-309.
    • (2009) J Mol Hist , vol.40 , pp. 301-309
    • Zambuzzi, W.1    Paiva, K.B.2    Menezes, R.3    Oliveira, R.C.4    Taga, R.5
  • 72
    • 70350337951 scopus 로고    scopus 로고
    • Monocyte inflammatory and matrix remodeling response modulated by grafted ECM-derived ligand concentration
    • Chung AS, Waldeck H, Schmidt DR, Kao WJ, (2009) Monocyte inflammatory and matrix remodeling response modulated by grafted ECM-derived ligand concentration. J Biomed Mater Res 91A: 742-752.
    • (2009) J Biomed Mater Res , vol.91 A , pp. 742-752
    • Chung, A.S.1    Waldeck, H.2    Schmidt, D.R.3    Kao, W.J.4
  • 73
    • 0030678549 scopus 로고    scopus 로고
    • Osf/Cbfa1: a transcripcional activator of osteoblast differentiation
    • Ducy P, Zhang R, Geoffroy V, Ridall AL, Karsenty G, (1997) Osf/Cbfa1: a transcripcional activator of osteoblast differentiation. Cell 89: 747-754.
    • (1997) Cell , vol.89 , pp. 747-754
    • Ducy, P.1    Zhang, R.2    Geoffroy, V.3    Ridall, A.L.4    Karsenty, G.5
  • 74
    • 56649088162 scopus 로고    scopus 로고
    • MMP-1 (collagenase-1) and MMP-13 (collagenase-3) differentially regulate markers of osteoblastic differentiation in osteogenic cells
    • Hayami T, Kapila YL, Kapila S, (2008) MMP-1 (collagenase-1) and MMP-13 (collagenase-3) differentially regulate markers of osteoblastic differentiation in osteogenic cells. Matrix Biol 27: 682-692.
    • (2008) Matrix Biol , vol.27 , pp. 682-692
    • Hayami, T.1    Kapila, Y.L.2    Kapila, S.3
  • 75
    • 25444473106 scopus 로고    scopus 로고
    • The Runx2 osteogenic transcription factor regulates matrix metalloproteinase 9 in bone metastático cancer cells and controls cell invasión
    • Pratap J, Javed A, Languino LR, van Wijnen AJ, Stein JL, et al. (2005) The Runx2 osteogenic transcription factor regulates matrix metalloproteinase 9 in bone metastático cancer cells and controls cell invasión. Mol Cell Biol 25: 8581-8591.
    • (2005) Mol Cell Biol , vol.25 , pp. 8581-8591
    • Pratap, J.1    Javed, A.2    Languino, L.R.3    van Wijnen, A.J.4    Stein, J.L.5
  • 76
    • 0035827689 scopus 로고    scopus 로고
    • AP-1 and Cbfa/Runt physically interact and regulate PTH-dependent MMP13 expression in osteoblasts through a new OSE2/AP-1 composite element
    • Hess J, Porte D, Munz C, Angel P, (2001) AP-1 and Cbfa/Runt physically interact and regulate PTH-dependent MMP13 expression in osteoblasts through a new OSE2/AP-1 composite element. J Biol Chem 276: 20029-20038.
    • (2001) J Biol Chem , vol.276 , pp. 20029-20038
    • Hess, J.1    Porte, D.2    Munz, C.3    Angel, P.4
  • 77
    • 31544472330 scopus 로고    scopus 로고
    • Quantitative kinetic analysis of gene expression during human osteoblastic adhesion on orthopaedic materials
    • Rouahi M, Champion E, Hardouin P, Anselme K, (2006) Quantitative kinetic analysis of gene expression during human osteoblastic adhesion on orthopaedic materials. Biomaterials 27: 2829-2844.
    • (2006) Biomaterials , vol.27 , pp. 2829-2844
    • Rouahi, M.1    Champion, E.2    Hardouin, P.3    Anselme, K.4


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