메뉴 건너뛰기




Volumn 34, Issue 8, 2005, Pages 1049-1056

Fibronectin fibril pattern displays the force balance of cell-matrix adhesion

Author keywords

[No Author keywords available]

Indexed keywords

COPOLYMER; FIBRONECTIN; MALEIC ANHYDRIDE;

EID: 27744560439     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-005-0490-z     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 0030111469 scopus 로고    scopus 로고
    • Studies on the biocompatibility of materials: Fibroblast reorganization of substratum bound fibronectin on surfaces varying in wettability
    • Altankov G, Grinnell F, Groth T (1996) Studies on the biocompatibility of materials: fibroblast reorganization of substratum bound fibronectin on surfaces varying in wettability. J Biomed Mater Res 30:385-391
    • (1996) J Biomed Mater Res , vol.30 , pp. 385-391
    • Altankov, G.1    Grinnell, F.2    Groth, T.3
  • 3
    • 0000468622 scopus 로고    scopus 로고
    • Mechanism of interfacial exchange phenomena for proteins adsorbed on solid-liquid interfaces
    • Malmsten M (ed). Marcel Dekker, New York
    • Ball V, Schaaf P, Voegel JC (1998) Mechanism of interfacial exchange phenomena for proteins adsorbed on solid-liquid interfaces. In: Malmsten M (ed) Biopolymers at interfaces. Marcel Dekker, New York
    • (1998) Biopolymers at Interfaces
    • Ball, V.1    Schaaf, P.2    Voegel, J.C.3
  • 4
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo KA, Dembo M, Kaverina I, Small JV, Wang I (2001) Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J Cell Biol 153:881-887
    • (2001) J Cell Biol , vol.153 , pp. 881-887
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, I.5
  • 6
    • 0035826819 scopus 로고    scopus 로고
    • Comparison of the early stages of forced unfolding for fibronectin type III modules
    • USA
    • Craig D, Krammer A, Schulten K, Vogel V (2001) Comparison of the early stages of forced unfolding for fibronectin type III modules. Proc Natl Acad Sci USA 98:5590-5595
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 5590-5595
    • Craig, D.1    Krammer, A.2    Schulten, K.3    Vogel, V.4
  • 7
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • Cukierman E, Pankov R, Stevens DR, Yamada KM (2001) Taking cell-matrix adhesions to the third dimension. Science 294:1708-1712
    • (2001) Science , vol.294 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 9
    • 1042263321 scopus 로고    scopus 로고
    • Self-assembled monolayers with different terminating groups as model substrates for cell adhesion studies
    • Faucheux N, Schweiss R, Lützow K, Werner C, Groth T (2004) Self-assembled monolayers with different terminating groups as model substrates for cell adhesion studies. Biomaterials 25:2721-2730
    • (2004) Biomaterials , vol.25 , pp. 2721-2730
    • Faucheux, N.1    Schweiss, R.2    Lützow, K.3    Werner, C.4    Groth, T.5
  • 10
    • 0032935413 scopus 로고    scopus 로고
    • Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation
    • Garcia AJ, Vega MD, Boettiger D (1999) Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation. Mol Biol Cell 10:785-798
    • (1999) Mol Biol Cell , vol.10 , pp. 785-798
    • Garcia, A.J.1    Vega, M.D.2    Boettiger, D.3
  • 12
    • 33746200227 scopus 로고
    • Globular proteins at solid/liquid interfaces
    • Haynes A, Norde W (1994) Globular proteins at solid/liquid interfaces. Colloids Surf B 2:517-566
    • (1994) Colloids Surf B , vol.2 , pp. 517-566
    • Haynes, A.1    Norde, W.2
  • 13
    • 0033017948 scopus 로고    scopus 로고
    • The dynamic dialogue between cells and matrices: Implications of fibronectin's elasticity
    • USA
    • Hynes RO (1999) The dynamic dialogue between cells and matrices: implications of fibronectin's elasticity. Proc Natl Acad Sci USA 96:2588-2590
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 2588-2590
    • Hynes, R.O.1
  • 14
    • 0018036788 scopus 로고
    • Relationships between fibronectin (LETS protein) and actin
    • Hynes RO, Destree AT (1978) Relationships between fibronectin (LETS protein) and actin. Cell 15:875-886
    • (1978) Cell , vol.15 , pp. 875-886
    • Hynes, R.O.1    Destree, A.T.2
  • 15
    • 0037112468 scopus 로고    scopus 로고
    • Mechanical signaling and the cellular response to extracellular matrix in angiogenesis and cardiovascular physiology
    • Ingber DE (2002) Mechanical signaling and the cellular response to extracellular matrix in angiogenesis and cardiovascular physiology. Circ Res 91:877-887
    • (2002) Circ Res , vol.91 , pp. 877-887
    • Ingber, D.E.1
  • 16
    • 0034114114 scopus 로고    scopus 로고
    • Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions
    • Katz Z, Zamir E, Bershadsky A, Kam Z, Yamada KM, Geiger B (2000) Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions. Mol Biol Cell 11:1047-1060
    • (2000) Mol Biol Cell , vol.11 , pp. 1047-1060
    • Katz, Z.1    Zamir, E.2    Bershadsky, A.3    Kam, Z.4    Yamada, K.M.5    Geiger, B.6
  • 17
    • 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 66A:247-259
    • (2003) J Biomed Mater Res , vol.66 A , pp. 247-259
    • Keselowsky, B.G.1    Collard, D.M.2    Garcia, A.J.3
  • 19
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti CK, Brugge, JS (2002) Sensing the environment: a historical perspective on integrin signal transduction. Nat Cell Biol 4:E83-E90
    • (2002) Nat Cell Biol , vol.4
    • Miranti, C.K.1    Brugge, J.S.2
  • 20
    • 0036305982 scopus 로고    scopus 로고
    • The mechanical hierarchies of fibronectin observed with single-molecule AFM
    • Oberhauser AF, Fernandez CB, Vazquez MC, Fernandez JM (2002) The mechanical hierarchies of fibronectin observed with single-molecule AFM. J Mol Biol 319:433-447
    • (2002) J Mol Biol , vol.319 , pp. 433-447
    • Oberhauser, A.F.1    Fernandez, C.B.2    Vazquez, M.C.3    Fernandez, J.M.4
  • 21
    • 0037087773 scopus 로고    scopus 로고
    • Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
    • Ohashi T, Kiehart DP, Erickson HP (2002) Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants. J Cell Sci 115:1221-1229
    • (2002) J Cell Sci , vol.115 , pp. 1221-1229
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 22
    • 0038041111 scopus 로고    scopus 로고
    • Ionization characteristics and structural transitions of alternating maleic acid copolymer films
    • Osaki T, Werner C (2003) Ionization characteristics and structural transitions of alternating maleic acid copolymer films. Langmuir 19:5787-5793
    • (2003) Langmuir , vol.19 , pp. 5787-5793
    • Osaki, T.1    Werner, C.2
  • 24
    • 0347384100 scopus 로고    scopus 로고
    • Fibronectin anchorage to polymer substrates controls the initial phase of endothelial cell adhesion
    • Pompe T, Kobe F, Salchert K, Jørgensen B, Oswald J, Werner C (2003a) Fibronectin anchorage to polymer substrates controls the initial phase of endothelial cell adhesion. J Biomed Mater Res 67A:647-657
    • (2003) J Biomed Mater Res , vol.67 A , pp. 647-657
    • Pompe, T.1    Kobe, F.2    Salchert, K.3    Jørgensen, B.4    Oswald, J.5    Werner, C.6
  • 26
    • 3042735324 scopus 로고    scopus 로고
    • Modulated fibronectin anchorage at polymer substrates controls angiogenesis
    • Pompe T, Markowski M, Werner C (2004a) Modulated fibronectin anchorage at polymer substrates controls angiogenesis. Tissue Eng 10:841-848
    • (2004) Tissue Eng , vol.10 , pp. 841-848
    • Pompe, T.1    Markowski, M.2    Werner, C.3
  • 27
    • 3142725746 scopus 로고    scopus 로고
    • Quantitative analysis of fibronectin fibrillogenesis by endothelial cells on biomaterials
    • Pompe T, Mitdank C, Werner C (2004b) Quantitative analysis of fibronectin fibrillogenesis by endothelial cells on biomaterials. J Phys: Condens Matter 16:S2421-S2426
    • (2004) J Phys: Condens Matter , vol.16
    • Pompe, T.1    Mitdank, C.2    Werner, C.3
  • 28
    • 11244279569 scopus 로고    scopus 로고
    • Nanoscale features of fibronectin fibrillogenesis depend on protein-substrate interaction and cytoskeleton structure
    • Pompe T, Renner L, Werner C (2005) Nanoscale features of fibronectin fibrillogenesis depend on protein-substrate interaction and cytoskeleton structure. Biophys J 88:527-534
    • (2005) Biophys J , vol.88 , pp. 527-534
    • Pompe, T.1    Renner, L.2    Werner, C.3
  • 29
    • 1842640370 scopus 로고    scopus 로고
    • Protein exchange on copolymer substrates with graded physicochemical characteristics
    • Renner L, Pompe T, Salchert K, Werner C (2004) Protein exchange on copolymer substrates with graded physicochemical characteristics. Langmuir 20:2928-2933
    • (2004) Langmuir , vol.20 , pp. 2928-2933
    • Renner, L.1    Pompe, T.2    Salchert, K.3    Werner, C.4
  • 30
    • 0037066260 scopus 로고    scopus 로고
    • Cell adhesion as wetting transition?
    • Sackmann E, Bruinsma RF (2002) Cell adhesion as wetting transition? Chem Phys Chem 3:262-269
    • (2002) Chem Phys Chem , vol.3 , pp. 262-269
    • Sackmann, E.1    Bruinsma, R.F.2
  • 31
    • 0037629568 scopus 로고    scopus 로고
    • Quantitative analysis of immobilized proteins and protein mixtures by amino acid analysis
    • Salchert K, Pompe T, Sperling C, Werner C (2003) Quantitative analysis of immobilized proteins and protein mixtures by amino acid analysis. J Chromatogr A 1005:113-122
    • (2003) J Chromatogr A , vol.1005 , pp. 113-122
    • Salchert, K.1    Pompe, T.2    Sperling, C.3    Werner, C.4
  • 32
    • 0018436046 scopus 로고
    • Quantitative electron spectroscopy of surfaces
    • Seah MP, Dench WA (1979) Quantitative electron spectroscopy of surfaces. Surf Interface Anal 1:2-11
    • (1979) Surf Interface Anal , vol.1 , pp. 2-11
    • Seah, M.P.1    Dench, W.A.2
  • 33
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • Sottile JJ, Hocking DC (2002) Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol Biol Cell 13:3546-3559
    • (2002) Mol Biol Cell , vol.13 , pp. 3546-3559
    • Sottile, J.J.1    Hocking, D.C.2
  • 34
    • 0036796781 scopus 로고    scopus 로고
    • Get a ligand, get a life: Integrins, signaling and cell survival
    • Stupack DG, Cheresh DA (2002) Get a ligand, get a life: integrins, signaling and cell survival. J Cell Sci 115:3729-3738
    • (2002) J Cell Sci , vol.115 , pp. 3729-3738
    • Stupack, D.G.1    Cheresh, D.A.2
  • 36
    • 0035478536 scopus 로고    scopus 로고
    • Structural insights into the mechanical regulation of molecular recognition sites
    • Vogel V, Thomas WE, Craig WW, Krammer A, Baneyx G (2001) Structural insights into the mechanical regulation of molecular recognition sites. Trends Biotechnol 19:416-423
    • (2001) Trends Biotechnol , vol.19 , pp. 416-423
    • Vogel, V.1    Thomas, W.E.2    Craig, W.W.3    Krammer, A.4    Baneyx, G.5
  • 37


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.