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Volumn 319, Issue 10, 2013, Pages 1553-1561

The selective role of ECM components on cell adhesion, morphology, proliferation and communication in vitro

Author keywords

Cell adhesion; Cell cell and cell matrix interaction; Extracellular matrix; Selective cell control

Indexed keywords

COLLAGEN TYPE 1; FIBRONECTIN; FOCAL ADHESION KINASE; LAMININ; LIGAND;

EID: 84877924729     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2013.03.016     Document Type: Article
Times cited : (97)

References (43)
  • 1
    • 78649737455 scopus 로고    scopus 로고
    • The extracellular matrix at a glance
    • Frantz C., Stewart K.M., Weaver V.M. The extracellular matrix at a glance. J. Cell Sci. 2011, 123:4195-4200.
    • (2011) J. Cell Sci. , vol.123 , pp. 4195-4200
    • Frantz, C.1    Stewart, K.M.2    Weaver, V.M.3
  • 2
    • 0033961642 scopus 로고    scopus 로고
    • Osteoblast adhesion on biomaterials
    • Anselme K. Osteoblast adhesion on biomaterials. Biomaterials 2000, 21:667-681.
    • (2000) Biomaterials , vol.21 , pp. 667-681
    • Anselme, K.1
  • 3
    • 78649603643 scopus 로고    scopus 로고
    • Extracellular matrix-mimetic adhesive biomaterials for bone repair
    • Shekeran A., García A.J. Extracellular matrix-mimetic adhesive biomaterials for bone repair. J. Biomed. Mater. Res. Part A 2011, 96A:261-272.
    • (2011) J. Biomed. Mater. Res. Part A , vol.96 A , pp. 261-272
    • Shekeran, A.1    García, A.J.2
  • 4
    • 0030582716 scopus 로고    scopus 로고
    • Fibrillar collagens inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors
    • Koyama H., Raines E.W., Bornfeldt K.E., Roberts J.M., Ross R. Fibrillar collagens inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors. Cell 1996, 87:1069-1078.
    • (1996) Cell , vol.87 , pp. 1069-1078
    • Koyama, H.1    Raines, E.W.2    Bornfeldt, K.E.3    Roberts, J.M.4    Ross, R.5
  • 5
    • 19444384572 scopus 로고    scopus 로고
    • Mechanical, biochemical, and extracellular matrix effects on vascular smooth muscle cell phenotype
    • Stegemann J.P., Hong H., Nerem R.M. Mechanical, biochemical, and extracellular matrix effects on vascular smooth muscle cell phenotype. J. Appl. Physiol. 2005, 98:2321-2327.
    • (2005) J. Appl. Physiol. , vol.98 , pp. 2321-2327
    • Stegemann, J.P.1    Hong, H.2    Nerem, R.M.3
  • 7
    • 0034064619 scopus 로고    scopus 로고
    • Integrin expression by primary and immortalized human chondrocytes: evidence of a differential role for α1β1 and α2β1 integrins in mediating chondrocyte adhesion to types II and VI collagen
    • Loeser R.F., Sadiev S., Tan L., Goldring M.B. Integrin expression by primary and immortalized human chondrocytes: evidence of a differential role for α1β1 and α2β1 integrins in mediating chondrocyte adhesion to types II and VI collagen. Osteoarthr. Cartilage 2000, 8:96-105.
    • (2000) Osteoarthr. Cartilage , vol.8 , pp. 96-105
    • Loeser, R.F.1    Sadiev, S.2    Tan, L.3    Goldring, M.B.4
  • 8
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signalling
    • Giancotti F.G., Ruoslahti E. Integrin signalling. Science 1999, 285:1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 9
    • 36249022091 scopus 로고    scopus 로고
    • Bridging structure with function: structural, regulatory, and developmental role of laminins
    • Tzu J., Marinkovich M.P. Bridging structure with function: structural, regulatory, and developmental role of laminins. Int. J. Biochem. Cell Biol. 2008, 40:199-214.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 199-214
    • Tzu, J.1    Marinkovich, M.P.2
  • 11
    • 0030298383 scopus 로고    scopus 로고
    • Structure and function of fibronectin modules
    • Potts J.R., Campbell I.D. Structure and function of fibronectin modules. Matrix Biol. 1996, 15:313-320.
    • (1996) Matrix Biol. , vol.15 , pp. 313-320
    • Potts, J.R.1    Campbell, I.D.2
  • 13
    • 35548939067 scopus 로고    scopus 로고
    • Structural basis for ligand recognition by integrins
    • Tagaki J. Structural basis for ligand recognition by integrins. Curr. Opin. Cell Biol. 2007, 19:557-564.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 557-564
    • Tagaki, J.1
  • 14
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 15
  • 16
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout M.A., Goodman D., Xiong J.P. Structure and mechanics of integrin-based cell adhesion. Curr. Opin. Cell Biol. 2007, 19(5):495-507.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, D.2    Xiong, J.P.3
  • 17
    • 0025376296 scopus 로고
    • Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that α6β1 but not α6β4 functions as a major receptor for fragment E8
    • Sonnenberg A., Linders C.J.T., Modderman P.W., Damsky C.H., Aumailley M., Timpl R. Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that α6β1 but not α6β4 functions as a major receptor for fragment E8. J. Cell Biol. 1990, 110:2145-2155.
    • (1990) J. Cell Biol. , vol.110 , pp. 2145-2155
    • Sonnenberg, A.1    Linders, C.J.T.2    Modderman, P.W.3    Damsky, C.H.4    Aumailley, M.5    Timpl, R.6
  • 18
  • 19
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B., Bershadsky A. Assembly and mechanosensory function of focal contacts. Curr. Opin. Cell Biol. 2001, 13:584-592.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 21
    • 33746800269 scopus 로고    scopus 로고
    • Focal adhesions: what's new inside
    • Lo S.H. Focal adhesions: what's new inside. Dev. Biol. 2006, 294:280-291.
    • (2006) Dev. Biol. , vol.294 , pp. 280-291
    • Lo, S.H.1
  • 22
    • 77955081211 scopus 로고    scopus 로고
    • Mesenchymal stem cells, osteoblasts and extracellular matrix proteins: enhancing cell adhesion and differentiation for bone tissue engineering
    • Hidalgo-Bastida L.A., Cartmell S.H. Mesenchymal stem cells, osteoblasts and extracellular matrix proteins: enhancing cell adhesion and differentiation for bone tissue engineering. Tissue Eng. Part B 2010, 16(4):405-412.
    • (2010) Tissue Eng. Part B , vol.16 , Issue.4 , pp. 405-412
    • Hidalgo-Bastida, L.A.1    Cartmell, S.H.2
  • 24
    • 84866983791 scopus 로고    scopus 로고
    • Dynamics of cell attachment: adhesion time and force
    • Schlie S., Gruene M., Dittmar H., Chichkov B. Dynamics of cell attachment: adhesion time and force. Tissue Eng. Part C 2012, 18(9):688-696.
    • (2012) Tissue Eng. Part C , vol.18 , Issue.9 , pp. 688-696
    • Schlie, S.1    Gruene, M.2    Dittmar, H.3    Chichkov, B.4
  • 25
    • 77956327716 scopus 로고    scopus 로고
    • Femtosecond laser fabricated spike structures for selective control of cellular behavior
    • Schlie S., Fadeeva E., Koch J., Ngezahayo A., Chichkov B.N. Femtosecond laser fabricated spike structures for selective control of cellular behavior. J. Biomater. Appl. 2010, 25:217-233.
    • (2010) J. Biomater. Appl. , vol.25 , pp. 217-233
    • Schlie, S.1    Fadeeva, E.2    Koch, J.3    Ngezahayo, A.4    Chichkov, B.N.5
  • 26
    • 77950021111 scopus 로고    scopus 로고
    • Dipyridamole increases gap junction coupling in bovine GM-7373 aortic endothelial cells by a cAMP-protein kinase A dependent pathway
    • Begandt D., Bintig W., Oberheide K., Schlie S., Ngezahayo A. Dipyridamole increases gap junction coupling in bovine GM-7373 aortic endothelial cells by a cAMP-protein kinase A dependent pathway. J. Bioenerg. Biomembr. 2010, 42(1):79-84.
    • (2010) J. Bioenerg. Biomembr. , vol.42 , Issue.1 , pp. 79-84
    • Begandt, D.1    Bintig, W.2    Oberheide, K.3    Schlie, S.4    Ngezahayo, A.5
  • 27
    • 0037383404 scopus 로고    scopus 로고
    • Cell structure and hierarchical systems biology
    • Ingber D.E., Tensegrity I. Cell structure and hierarchical systems biology. J. Cell Sci. 2003, 116:1157-1173.
    • (2003) J. Cell Sci. , vol.116 , pp. 1157-1173
    • Ingber, D.E.1    Tensegrity, I.2
  • 29
    • 17544364168 scopus 로고    scopus 로고
    • Ras activation is necessary for integrin-mediated activation of extracellular signal-regulated kinase 2 and cytosolic phospholipase A but not for cytoskeletal organization
    • Clark E.A., Hynes R.O. Ras activation is necessary for integrin-mediated activation of extracellular signal-regulated kinase 2 and cytosolic phospholipase A but not for cytoskeletal organization. Int. J. Biol. Chem. 1996, 271(25):14814-14818.
    • (1996) Int. J. Biol. Chem. , vol.271 , Issue.25 , pp. 14814-14818
    • Clark, E.A.1    Hynes, R.O.2
  • 30
    • 0035085628 scopus 로고    scopus 로고
    • Cell-matrix contact structures
    • Adams J.C. Cell-matrix contact structures. Cell. Mol. Life Sci. 2001, 58:371-392.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 371-392
    • Adams, J.C.1
  • 31
    • 0034902905 scopus 로고    scopus 로고
    • Integrins and cell proliferation: regulation of cyclin-dependent kinases via cytoplasmic signaling pathways
    • Schwartz M.A., Assoian R.K. Integrins and cell proliferation: regulation of cyclin-dependent kinases via cytoplasmic signaling pathways. J. Cell Sci. 2001, 114:2553-2560.
    • (2001) J. Cell Sci. , vol.114 , pp. 2553-2560
    • Schwartz, M.A.1    Assoian, R.K.2
  • 33
    • 33747882103 scopus 로고    scopus 로고
    • Activation of the integrin-linked kinase pathway downregulates hepatic connexin32 via nuclear Akt
    • Plante I., Charbonneau M., Cyr D.G. Activation of the integrin-linked kinase pathway downregulates hepatic connexin32 via nuclear Akt. Carcinogenesis 2006, 27(9):1923-1929.
    • (2006) Carcinogenesis , vol.27 , Issue.9 , pp. 1923-1929
    • Plante, I.1    Charbonneau, M.2    Cyr, D.G.3
  • 34
    • 16244373677 scopus 로고    scopus 로고
    • Matrix-protein-specific regulation of CX43 expression in cardiac myocytes subjected to mechanical load
    • Shanker A.J., Yamada K., Green K.G., Yamada K.A., Saffitz J.E. Matrix-protein-specific regulation of CX43 expression in cardiac myocytes subjected to mechanical load. Circ. Res. 2009, 96:559-566.
    • (2009) Circ. Res. , vol.96 , pp. 559-566
    • Shanker, A.J.1    Yamada, K.2    Green, K.G.3    Yamada, K.A.4    Saffitz, J.E.5
  • 35
    • 34547592530 scopus 로고    scopus 로고
    • Extracellular matrix, mechanotransduction and structural hierarchies in heart tissue engineering
    • Parker K.K., Ingber D.E. Extracellular matrix, mechanotransduction and structural hierarchies in heart tissue engineering. Philos. Trans. R. Soc. London, Ser. B 2007, 362:1267-1279.
    • (2007) Philos. Trans. R. Soc. London, Ser. B , vol.362 , pp. 1267-1279
    • Parker, K.K.1    Ingber, D.E.2
  • 36
    • 0030665379 scopus 로고    scopus 로고
    • Morphological evidence for a 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. Morphological evidence for a different fibronectin receptor organization and function during fibroblast adhesion on hydrophilic and hydrophobic glass substrata. J. Biomater. Sci., Polym. Ed. 1997, 8(9):721-740.
    • (1997) J. Biomater. Sci., Polym. Ed. , vol.8 , Issue.9 , pp. 721-740
    • Altankov, G.1    Groth, T.2    Krasteva, N.3    Albrecht, W.4    Paul, D.5
  • 38
    • 34249682108 scopus 로고    scopus 로고
    • Novel functions of vimentin in cell adhesion, migration, and signaling
    • Ivaska J., Pallari H.M., Nevo J., Eriksson J.E. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp. Cell. Res. 2007, 313:2050-2620.
    • (2007) Exp. Cell. Res. , vol.313 , pp. 2050-2620
    • Ivaska, J.1    Pallari, H.M.2    Nevo, J.3    Eriksson, J.E.4
  • 39
    • 52749086084 scopus 로고    scopus 로고
    • Extracellular matrix-specific focal adhesions in vascular smooth muscle produce mechanically active adhesion sites
    • Sun Z., Martinez-Lemus L.A., Hill M.A., Meininger G.A. Extracellular matrix-specific focal adhesions in vascular smooth muscle produce mechanically active adhesion sites. Am. J. Phyiol. Cell Physiol. 2008, 295:C268-C278.
    • (2008) Am. J. Phyiol. Cell Physiol. , vol.295
    • Sun, Z.1    Martinez-Lemus, L.A.2    Hill, M.A.3    Meininger, G.A.4
  • 42
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • Cukiermann E., Pankov R., Stevens D.R., Yamada K.M. Taking cell-matrix adhesions to the third dimension. Science 2001, 294:1708-1712.
    • (2001) Science , vol.294 , pp. 1708-1712
    • Cukiermann, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.