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Volumn 6, Issue , 2006, Pages

Thin films of Type 1 collagen for cell by cell analysis of morphology and tenascin-C promoter activity

Author keywords

[No Author keywords available]

Indexed keywords

CELL-BY-CELL ANALYSIS; EXTRACELLULAR MATRIX PROTEINS; FIBROBLAST MORPHOLOGY; PROMOTER ACTIVITY; TENASCIN-C;

EID: 33746624303     PISSN: 14726750     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-6-14     Document Type: Article
Times cited : (27)

References (47)
  • 1
    • 0034987580 scopus 로고    scopus 로고
    • Twisting integrin receptors increases endothelin-1 gene expression in endothelial cells
    • Chen JX, Fabry B, Schiffrin EL, Wang N: Twisting integrin receptors increases endothelin-1 gene expression in endothelial cells. Am J Physiol Cell Physiol 2001, 280:C1475-C1484.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Chen, J.X.1    Fabry, B.2    Schiffrin, E.L.3    Wang, N.4
  • 3
    • 0021627544 scopus 로고
    • Collagen-dependent growth suppression and changes in the shape of human dermal fibroblasts
    • Yoshizato K, Taira T, Shioya N: Collagen-dependent growth suppression and changes in the shape of human dermal fibroblasts. Ann Plast Surg 1984, 13:9-14.
    • (1984) Ann Plast Surg , vol.13 , pp. 9-14
    • Yoshizato, K.1    Taira, T.2    Shioya, N.3
  • 4
    • 0028557342 scopus 로고
    • Extracellular Matrix-Dependent Tissue-Specific Gene-Expression in Mammary Epithelial-Cells Requires Both Physical and Biochemical Signal-Transduction
    • Roskelley CD, Desprez PY, Bissell MJ: Extracellular Matrix-Dependent Tissue-Specific Gene-Expression in Mammary Epithelial-Cells Requires Both Physical and Biochemical Signal-Transduction. Proceedings of the National Academy of Sciences of the United States of America 1994, 91:12378-12382.
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , pp. 12378-12382
    • Roskelley, C.D.1    Desprez, P.Y.2    Bissell, M.J.3
  • 5
    • 0033731472 scopus 로고    scopus 로고
    • Tenascin-C in development and disease: Gene regulation and cell function
    • Jones PL, Jones FS: Tenascin-C in development and disease: gene regulation and cell function. Matrix Biol 2000, 19:581-596.
    • (2000) Matrix Biol , vol.19 , pp. 581-596
    • Jones, P.L.1    Jones, F.S.2
  • 6
    • 0034117025 scopus 로고    scopus 로고
    • The tenascin family of ECM glycoproteins: Structure, function, and regulation during embryonic development and tissue remodeling
    • Jones FS, Jones PL: The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev Dyn 2000, 218:235-259.
    • (2000) Dev Dyn , vol.218 , pp. 235-259
    • Jones, F.S.1    Jones, P.L.2
  • 7
    • 0037360165 scopus 로고    scopus 로고
    • How do fibroblasts translate mechanical signals into changes in extracellular matrix production?
    • Chiquet M, Renedo AS, Huber F, Fluck M: How do fibroblasts translate mechanical signals into changes in extracellular matrix production? Matrix Biol 2003, 22:73-80.
    • (2003) Matrix Biol , vol.22 , pp. 73-80
    • Chiquet, M.1    Renedo, A.S.2    Huber, F.3    Fluck, M.4
  • 11
    • 0035896242 scopus 로고    scopus 로고
    • Fibrillar collagen specifically regulates human vascular smooth muscle cell genes involved in cellular responses and the pericellular matrix environment
    • Ichii T, Koyama H, Tanaka S, Kim S, Shioi A, Okuno Y, Raines EW, Iwao H, Otani S, Nishizawa Y: Fibrillar collagen specifically regulates human vascular smooth muscle cell genes involved in cellular responses and the pericellular matrix environment. Circ Res 2001, 88:460-467.
    • (2001) Circ Res , vol.88 , pp. 460-467
    • Ichii, T.1    Koyama, H.2    Tanaka, S.3    Kim, S.4    Shioi, A.5    Okuno, Y.6    Raines, E.W.7    Iwao, H.8    Otani, S.9    Nishizawa, Y.10
  • 13
    • 0033657701 scopus 로고    scopus 로고
    • Using self-assembled monolayers to pattern ECM proteins and cells on substrates
    • Chen CS, Ostuni E, Whitesides GM, Ingber DE: Using self-assembled monolayers to pattern ECM proteins and cells on substrates. Methods Mol Biol 2000, 139:209-219.
    • (2000) Methods Mol Biol , vol.139 , pp. 209-219
    • Chen, C.S.1    Ostuni, E.2    Whitesides, G.M.3    Ingber, D.E.4
  • 14
    • 0029784468 scopus 로고    scopus 로고
    • Controlling cell attachment on contoured surfaces with self-assembled monolayers of alkanethiolates on gold
    • Mrksich M, Chen CS, Xia Y, Dike LE, Ingber DE, Whitesides GM: Controlling cell attachment on contoured surfaces with self-assembled monolayers of alkanethiolates on gold. Proc Natl Acad Sci U S A 1996, 93:10775-10778.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10775-10778
    • Mrksich, M.1    Chen, C.S.2    Xia, Y.3    Dike, L.E.4    Ingber, D.E.5    Whitesides, G.M.6
  • 16
    • 0037047193 scopus 로고    scopus 로고
    • Micropatterned surfaces to engineer focal adhesions for analysis of cell adhesion strengthening
    • Gallant ND, Capadona JR, Frazier AB, Collard DM, Garcia AJ: Micropatterned surfaces to engineer focal adhesions for analysis of cell adhesion strengthening. Langmuir 2002, 18:5579-5584.
    • (2002) Langmuir , vol.18 , pp. 5579-5584
    • Gallant, N.D.1    Capadona, J.R.2    Frazier, A.B.3    Collard, D.M.4    Garcia, A.J.5
  • 17
    • 0031572307 scopus 로고    scopus 로고
    • Using microcontact printing to pattern the attachment of mammalian cells to self-assembled monolayers of alkanethiolates on transparent films of gold and silver
    • Mrksich M, Dike LE, Tien J, Ingber DE, Whitesides GM: Using microcontact printing to pattern the attachment of mammalian cells to self-assembled monolayers of alkanethiolates on transparent films of gold and silver. Exp Cell Res 1997, 235:305-313.
    • (1997) Exp Cell Res , vol.235 , pp. 305-313
    • Mrksich, M.1    Dike, L.E.2    Tien, J.3    Ingber, D.E.4    Whitesides, G.M.5
  • 19
    • 0018079235 scopus 로고
    • Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results
    • Williams BR, Gelman RA, Poppke DC, Piez KA: Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results. Journal of Biological Chemistry 1978, 253:6578-6585.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 6578-6585
    • Williams, B.R.1    Gelman, R.A.2    Poppke, D.C.3    Piez, K.A.4
  • 20
    • 0027463517 scopus 로고
    • A new type of biomaterial for artificial skin: Dehydrothermally cross-linked composites of fibrillar and denatured collagens
    • Koide M, Osaki K, Konishi J, Oyamada K, Katakura T, Takahashi A, Yoshizato K: A new type of biomaterial for artificial skin: dehydrothermally cross-linked composites of fibrillar and denatured collagens. J Biomed Mater Res 1993, 27:79-87.
    • (1993) J Biomed Mater Res , vol.27 , pp. 79-87
    • Koide, M.1    Osaki, K.2    Konishi, J.3    Oyamada, K.4    Katakura, T.5    Takahashi, A.6    Yoshizato, K.7
  • 21
    • 0015402532 scopus 로고
    • Collagen substrata for studies on cell behavior
    • Elsdale T, Bard J: Collagen substrata for studies on cell behavior. J Cell Biol 1972, 54:626-637.
    • (1972) J Cell Biol , vol.54 , pp. 626-637
    • Elsdale, T.1    Bard, J.2
  • 22
    • 0031824197 scopus 로고    scopus 로고
    • Tailored substrates for studies of attached cell culture
    • Mrksich M: Tailored substrates for studies of attached cell culture. Cell Mol Life Sci 1998, 54:653-662.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 653-662
    • Mrksich, M.1
  • 23
    • 0024309946 scopus 로고
    • Extracellular matrix organization modulates fibroblast growth and growth factor responsiveness
    • Nakagawa S, Pawelek P, Grinnell F: Extracellular matrix organization modulates fibroblast growth and growth factor responsiveness. Exp Cell Res 1989, 182:572-582.
    • (1989) Exp Cell Res , vol.182 , pp. 572-582
    • Nakagawa, S.1    Pawelek, P.2    Grinnell, F.3
  • 24
    • 0029954059 scopus 로고    scopus 로고
    • Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organization of the cytoskeleton
    • Mercier I, Lechaire JP, Desmouliere A, Gaill F, Aumailley M: Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organization of the cytoskeleton. Exp Cell Res 1996, 225:245-256.
    • (1996) Exp Cell Res , vol.225 , pp. 245-256
    • Mercier, I.1    Lechaire, J.P.2    Desmouliere, A.3    Gaill, F.4    Aumailley, M.5
  • 25
    • 0242693917 scopus 로고    scopus 로고
    • Spike formation by fibroblasts adhering to fibrillar collagen 1 gel
    • Sato K, Hattori S, Irie S, Kawashima S: Spike formation by fibroblasts adhering to fibrillar collagen 1 gel. Cell Struct Funct 2003, 28:229-241.
    • (2003) Cell Struct Funct , vol.28 , pp. 229-241
    • Sato, K.1    Hattori, S.2    Irie, S.3    Kawashima, S.4
  • 26
    • 0036855955 scopus 로고    scopus 로고
    • Modulation of fibroblast morphology and adhesion during collagen matrix remodeling
    • Tamariz E, Grinnell F: Modulation of fibroblast morphology and adhesion during collagen matrix remodeling. Molecular Biology Cell 2002, 13:3915-3929.
    • (2002) Molecular Biology Cell , vol.13 , pp. 3915-3929
    • Tamariz, E.1    Grinnell, F.2
  • 27
    • 0347505006 scopus 로고    scopus 로고
    • Comparison of reagents for shape analysis of fixed cells by automated fluorescence microscopy
    • Elliott JT, Tona A, Plant AL: Comparison of reagents for shape analysis of fixed cells by automated fluorescence microscopy. Cytometry Part A 2003, 52A:90-100.
    • (2003) Cytometry , vol.52 A , Issue.PART A , pp. 90-100
    • Elliott, J.T.1    Tona, A.2    Plant, A.L.3
  • 28
    • 0024322562 scopus 로고
    • The collagen recognition sequence for fibroblasts depends on collagen topography
    • Grinnell F, Nakagawa S, Ho CH: The collagen recognition sequence for fibroblasts depends on collagen topography. Exp Cell Res 1989, 182:668-672.
    • (1989) Exp Cell Res , vol.182 , pp. 668-672
    • Grinnell, F.1    Nakagawa, S.2    Ho, C.H.3
  • 29
    • 0034254009 scopus 로고    scopus 로고
    • The collagen receptor integrins have distinct ligand recognition and signaling functions
    • Heino J: The collagen receptor integrins have distinct ligand recognition and signaling functions. Matrix Biology 2000, 19:319-323.
    • (2000) Matrix Biology , vol.19 , pp. 319-323
    • Heino, J.1
  • 30
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Danen EH, Yamada KM: Fibronectin, integrins, and growth control. J Cell Physiol 2001, 189:1-13.
    • (2001) J Cell Physiol , vol.189 , pp. 1-13
    • Danen, E.H.1    Yamada, K.M.2
  • 32
    • 0030031228 scopus 로고    scopus 로고
    • Studies in vitro on the role of alpha v and beta 1 integrins in the adhesion of human dermal fibroblasts to provisional matrix proteins fibronectin, vitronectin, and fibrinogen
    • Gailit J, Clark RA: Studies in vitro on the role of alpha v and beta 1 integrins in the adhesion of human dermal fibroblasts to provisional matrix proteins fibronectin, vitronectin, and fibrinogen. J Invest Dermatol 1996, 106:102-108.
    • (1996) J Invest Dermatol , vol.106 , pp. 102-108
    • Gailit, J.1    Clark, R.A.2
  • 33
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO: Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 1992, 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 34
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto S, Teramoto H, Gutkind JS, Yamada KM: Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors. J Cell Biol 1996, 135:1633-1642.
    • (1996) J Cell Biol , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 35
    • 0036775137 scopus 로고    scopus 로고
    • Integrin signaling: It's where the action is
    • Damsky CH, Ilic D: Integrin signaling: it's where the action is. Curr Opin Cell Biol 2002, 14:594-602.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 594-602
    • Damsky, C.H.1    Ilic, D.2
  • 36
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper GE, McNamee HP, Dike LE, Bojanowski K, Ingber DE: Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Molecular Biology Cell 1995, 6:1349-1365.
    • (1995) Molecular Biology Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 37
    • 0035920254 scopus 로고    scopus 로고
    • Prx1 controls vascular smooth muscle cell proliferation and tenascin-C expression and is upregulated with Prx2 in pulmonary vascular disease
    • Jones FS, Meech R, Edelman DB, Oakey RJ, Jones PL: Prx1 controls vascular smooth muscle cell proliferation and tenascin-C expression and is upregulated with Prx2 in pulmonary vascular disease. Circ Res 2001, 20;89:131-138.
    • (2001) Circ Res , vol.20 , Issue.89 , pp. 131-138
    • Jones, F.S.1    Meech, R.2    Edelman, D.B.3    Oakey, R.J.4    Jones, P.L.5
  • 38
    • 0035920222 scopus 로고    scopus 로고
    • The identification of Prx1 transcription regulatory domains provides a mechanism for unequal compensation by the Prx1 and Prx2 loci
    • Norris RA, Kern MJ: The identification of Prx1 transcription regulatory domains provides a mechanism for unequal compensation by the Prx1 and Prx2 loci. Journal of Biological Chemistry 2001, 276:26829-26837.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 26829-26837
    • Norris, R.A.1    Kern, M.J.2
  • 39
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix - Cytoskeleton crosstalk
    • Geiger B, Bershadsky A, Pankov R, Yamada KM: Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat Rev Mol Cell Biol 2001, 2:793-805.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 40
    • 2542467721 scopus 로고    scopus 로고
    • Vascular endothelial-cadherin regulates cytoskeletal tension, cell spreading, and focal adhesions stimulating RhoA
    • Nelson CM, Pirone DM, Tan JL, Chen CS: Vascular endothelial-cadherin regulates cytoskeletal tension, cell spreading, and focal adhesions stimulating RhoA. Molecular Biology of the Cell 2004, 15:2943-2953.
    • (2004) Molecular Biology of the Cell , vol.15 , pp. 2943-2953
    • Nelson, C.M.1    Pirone, D.M.2    Tan, J.L.3    Chen, C.S.4
  • 42
    • 0028342810 scopus 로고
    • Control of cytoskeletal mechanics by extracellular matrix, cell shape, and mechanical tension
    • Wang N, Ingber DE: Control of cytoskeletal mechanics by extracellular matrix, cell shape, and mechanical tension. Biophys J 1994, 66:2181-2189.
    • (1994) Biophys J , vol.66 , pp. 2181-2189
    • Wang, N.1    Ingber, D.E.2
  • 43
    • 0033036061 scopus 로고    scopus 로고
    • Tensegrity and mechanoregulation: From skeleton to cytoskeleton
    • Chen CS, Ingber DE: Tensegrity and mechanoregulation: from skeleton to cytoskeleton. Osteoarthritis Cartilage 1999, 7:81-94.
    • (1999) Osteoarthritis Cartilage , vol.7 , pp. 81-94
    • Chen, C.S.1    Ingber, D.E.2
  • 45
    • 15544388848 scopus 로고    scopus 로고
    • Noise propagation in gene networks
    • Pedraza JM, van Oudenaarden A: Noise propagation in gene networks. Science 2005, 307:1965-1969.
    • (2005) Science , vol.307 , pp. 1965-1969
    • Pedraza, J.M.1    van Oudenaarden, A.2
  • 46
    • 0029884907 scopus 로고    scopus 로고
    • Bifunctional protein cross-linking reagents improve labeling of cytoskeletal proteins for qualitative and quantitative fluorescence microscopy
    • Safiejko-Mroczka B, Bell PBJ: Bifunctional protein cross-linking reagents improve labeling of cytoskeletal proteins for qualitative and quantitative fluorescence microscopy. J Histochem Cytochem 1996, 44:641-656.
    • (1996) J Histochem Cytochem , vol.44 , pp. 641-656
    • Safiejko-Mroczka, B.1    Bell, P.B.J.2
  • 47
    • 0030049459 scopus 로고    scopus 로고
    • Maleimidobenzoyl actin: Its biochemical properties and in vitro motility
    • Hozumi T, Miki M, Higashi-Fujime S: Maleimidobenzoyl actin: its biochemical properties and in vitro motility. J Biochem (Tokyo) 1996, 119:151-156.
    • (1996) J Biochem (Tokyo) , vol.119 , pp. 151-156
    • Hozumi, T.1    Miki, M.2    Higashi-Fujime, S.3


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