메뉴 건너뛰기




Volumn 44, Issue 1, 1999, Pages 44-52

Signal transduction and cytoskeletal reorganization are required for cell detachment from cell culture surfaces grafted with a temperature-responsive polymer

Author keywords

Actin filament; Cell detachment; Endothelial cell; Isopropylacrylamide; Tyrosine phosphorylation

Indexed keywords

ANIMAL CELL CULTURE; CELL MEMBRANES; DENSITY (SPECIFIC GRAVITY); ELECTRON IRRADIATION; ENZYME IMMOBILIZATION; GRAFTING (CHEMICAL); HYDROPHOBICITY; MOLECULAR DYNAMICS; MORPHOLOGY; POLYAMIDES; SURFACE PROPERTIES; THERMAL EFFECTS;

EID: 0031724083     PISSN: 00219304     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-4636(199901)44:1<44::aid-jbm5>3.0.co;2-x     Document Type: Article
Times cited : (134)

References (53)
  • 1
    • 0029361095 scopus 로고
    • Photochemical surface derivatization of a peptide containing Arg-Gly-Asp (RGD)
    • Sugawara T, Matsuda T. Photochemical surface derivatization of a peptide containing Arg-Gly-Asp (RGD). J Biomed Mater Res 1995;29:1047-1052.
    • (1995) J Biomed Mater Res , vol.29 , pp. 1047-1052
    • Sugawara, T.1    Matsuda, T.2
  • 2
    • 0026114629 scopus 로고
    • Human endothelial cell interactions with surface-coupled adhesion peptides on a nonadhesive glass substrate and two polymeric biomaterials
    • Massia SP, Hubbell JA. Human endothelial cell interactions with surface-coupled adhesion peptides on a nonadhesive glass substrate and two polymeric biomaterials. J Biomed Mater Res 1991;25:223-242.
    • (1991) J Biomed Mater Res , vol.25 , pp. 223-242
    • Massia, S.P.1    Hubbell, J.A.2
  • 3
    • 0018140371 scopus 로고
    • Role of cell shape in growth control
    • Folkman J, Moscona A. Role of cell shape in growth control. Nature 1978;273:345-347.
    • (1978) Nature , vol.273 , pp. 345-347
    • Folkman, J.1    Moscona, A.2
  • 4
    • 0026832927 scopus 로고
    • Synthesis of photoreactive poly(ethylene glycol) and its application to the prevention of surface-induced platelet activation
    • Tseng YC, Park K. Synthesis of photoreactive poly(ethylene glycol) and its application to the prevention of surface-induced platelet activation. J Biomed Mater Res 1992;26:373-391.
    • (1992) J Biomed Mater Res , vol.26 , pp. 373-391
    • Tseng, Y.C.1    Park, K.2
  • 6
    • 0027686384 scopus 로고
    • A novel recovery system for cultured cells using plasma-treated polystyrene dishes grafted with poly (N-isopropylacrylamide)
    • Okano T, Yamada N, Sakai H, Sakurai Y. A novel recovery system for cultured cells using plasma-treated polystyrene dishes grafted with poly (N-isopropylacrylamide). J Biomed Mater Res 1993;27:1243-1251.
    • (1993) J Biomed Mater Res , vol.27 , pp. 1243-1251
    • Okano, T.1    Yamada, N.2    Sakai, H.3    Sakurai, Y.4
  • 7
    • 0029256680 scopus 로고
    • Mechanism of cell detachment from temperature-modulated, hydrophilic-hydrophobic polymer surfaces
    • Okano T, Yamada N, Okuhara M, Sakai H, Sakurai Y. Mechanism of cell detachment from temperature-modulated, hydrophilic-hydrophobic polymer surfaces. Biomaterials 1995;16: 297-303.
    • (1995) Biomaterials , vol.16 , pp. 297-303
    • Okano, T.1    Yamada, N.2    Okuhara, M.3    Sakai, H.4    Sakurai, Y.5
  • 8
    • 0025432734 scopus 로고
    • Temperature dependence on swelling of crosslinked poly(N,N′-alkyl substituted acrylamide) in water
    • Bae YH, Okano T, Kim SW. Temperature dependence on swelling of crosslinked poly(N,N′-alkyl substituted acrylamide) in water. J Polym Sci, Polym Phys 1990;28:923-936.
    • (1990) J Polym Sci, Polym Phys , vol.28 , pp. 923-936
    • Bae, Y.H.1    Okano, T.2    Kim, S.W.3
  • 9
    • 84924991730 scopus 로고
    • Solution properties of poly (N-isopropylacrylamide)
    • Heskins M, Guillent JE, James E. Solution properties of poly (N-isopropylacrylamide). J Macromol Sci Chem 1968;A2:1441-1455.
    • (1968) J Macromol Sci Chem , vol.A2 , pp. 1441-1455
    • Heskins, M.1    Guillent, J.E.2    James, E.3
  • 10
    • 0021813717 scopus 로고
    • Detachment of cells from culture substrate by soluble fibronectin peptides
    • Hayman EG, Pierschbacher MD, Ruoslahti E. Detachment of cells from culture substrate by soluble fibronectin peptides. J Cell Biol 1985;100:1948-1954.
    • (1985) J Cell Biol , vol.100 , pp. 1948-1954
    • Hayman, E.G.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 11
    • 0025248510 scopus 로고
    • The role of integrins α2β1 and α3α1 in cell-cell and cell-substrate adhesion of human epidermal cells
    • Carter WG, Wayner EA, Bouchard TS, Kaur P. The role of integrins α2β1 and α3α1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 1990;110:1387-1404.
    • (1990) J Cell Biol , vol.110 , pp. 1387-1404
    • Carter, W.G.1    Wayner, E.A.2    Bouchard, T.S.3    Kaur, P.4
  • 12
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane TF, Sage EH. The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J 1994;8:163-173.
    • (1994) FASEB J , vol.8 , pp. 163-173
    • Lane, T.F.1    Sage, E.H.2
  • 14
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions: SPARC, tenascin, and thrombospondin
    • Sage EH, Bornstein P. Extracellular proteins that modulate cell-matrix interactions: SPARC, tenascin, and thrombospondin. J Biol Chem 1991;266:14831-14834.
    • (1991) J Biol Chem , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 15
    • 0027415981 scopus 로고
    • Inhibition of fibronectin binding and fibronectin-mediated cell adhesion to collagen by a peptide from the second type I repeat of thrombospondin
    • Sipes JM, Guo N-H, Nègre E, Vogel T, Krutzsch HC, Roberts DD. Inhibition of fibronectin binding and fibronectin-mediated cell adhesion to collagen by a peptide from the second type I repeat of thrombospondin. J Cell Biol 1993;121:469-477.
    • (1993) J Cell Biol , vol.121 , pp. 469-477
    • Sipes, J.M.1    Guo, N.-H.2    Nègre, E.3    Vogel, T.4    Krutzsch, H.C.5    Roberts, D.D.6
  • 17
    • 0028307404 scopus 로고
    • Interactions between cells and collagen V molecules or single chains
    • Ruggiero F, Champliaud M-F, Garrone R, Aumailley M. Interactions between cells and collagen V molecules or single chains. Exp Cell Res 1993;210:215-223.
    • (1993) Exp Cell Res , vol.210 , pp. 215-223
    • Ruggiero, F.1    Champliaud, M.-F.2    Garrone, R.3    Aumailley, M.4
  • 19
    • 0026077754 scopus 로고
    • Inhibition of cell adhesion by type V collagen
    • Hashimoto K, Hatai M, Yaoi Y. Inhibition of cell adhesion by type V collagen. Cell Struc Func 1991;16:391-397.
    • (1991) Cell Struc Func , vol.16 , pp. 391-397
    • Hashimoto, K.1    Hatai, M.2    Yaoi, Y.3
  • 20
    • 0027215624 scopus 로고
    • Inhibition of cell adhesion by proteolytic fragments of type V collagen
    • Hatai M, Hashi H, Kato I, Yaoi Y. Inhibition of cell adhesion by proteolytic fragments of type V collagen. Cell Struc Func 1993; 18:53-60.
    • (1993) Cell Struc Func , vol.18 , pp. 53-60
    • Hatai, M.1    Hashi, H.2    Kato, I.3    Yaoi, Y.4
  • 21
    • 0026688923 scopus 로고
    • Disassembly of F-actin filaments in human endothelial cells cultured on type V collagen
    • Yamamoto K, Yamamoto M, Noumura T. Disassembly of F-actin filaments in human endothelial cells cultured on type V collagen. Exp Cell Res 1992;201:55-63.
    • (1992) Exp Cell Res , vol.201 , pp. 55-63
    • Yamamoto, K.1    Yamamoto, M.2    Noumura, T.3
  • 22
    • 0028641175 scopus 로고
    • The failure to reconstitute the second extracellular matrix-integrin-cytoskeleton system in human endothelial cells on type V collagen
    • Yamamoto K, Yamamoto M. The failure to reconstitute the second extracellular matrix-integrin-cytoskeleton system in human endothelial cells on type V collagen. Artery 1994;21:76-93.
    • (1994) Artery , vol.21 , pp. 76-93
    • Yamamoto, K.1    Yamamoto, M.2
  • 23
    • 0022388911 scopus 로고
    • Cellular interactions with synthetic polymer surfaces in culture
    • Lydon MJ, Minett TW, Tighe BJ. Cellular interactions with synthetic polymer surfaces in culture. Biomaterials 1985;6:396-402.
    • (1985) Biomaterials , vol.6 , pp. 396-402
    • Lydon, M.J.1    Minett, T.W.2    Tighe, B.J.3
  • 25
    • 0022757735 scopus 로고
    • The influence of substratum surface free energy on growth and spreading of human fibroblasts in the presence and absence of serum proteins
    • Schakenraad JM, Busscher HJ, Wildevuur CRH, Arends J. The influence of substratum surface free energy on growth and spreading of human fibroblasts in the presence and absence of serum proteins. J Biomed Mater Res 1986;20:773-784.
    • (1986) J Biomed Mater Res , vol.20 , pp. 773-784
    • Schakenraad, J.M.1    Busscher, H.J.2    Wildevuur, C.R.H.3    Arends, J.4
  • 27
    • 0019534204 scopus 로고
    • Hydrophilic-hydrophobic copolymers as cell substrates: Effects on 3T3 cell growth rates
    • Horbett TA, Schway MB, Ratner BD. Hydrophilic-hydrophobic copolymers as cell substrates: Effects on 3T3 cell growth rates. J Colloid Interface Sci 1985;104:28-39.
    • (1985) J Colloid Interface Sci , vol.104 , pp. 28-39
    • Horbett, T.A.1    Schway, M.B.2    Ratner, B.D.3
  • 28
    • 0024017405 scopus 로고
    • Cell adhesion to a series of hydrophilic-hydrophobic copolymers studied with a spinning disc apparatus
    • Horbett TA, Waldburger JJ, Ratner BD, Hoffman AS. Cell adhesion to a series of hydrophilic-hydrophobic copolymers studied with a spinning disc apparatus. J Biomed Mater Res 1988;22:383-404.
    • (1988) J Biomed Mater Res , vol.22 , pp. 383-404
    • Horbett, T.A.1    Waldburger, J.J.2    Ratner, B.D.3    Hoffman, A.S.4
  • 29
    • 0026941772 scopus 로고
    • Influence of the substrate binding characteristics of fibronectin on corneal epithelial cell growth
    • Pettit DK, Horbett TA, Hoffman AS. Influence of the substrate binding characteristics of fibronectin on corneal epithelial cell growth. J Biomed Mater Res 1992;26:1259-1275.
    • (1992) J Biomed Mater Res , vol.26 , pp. 1259-1275
    • Pettit, D.K.1    Horbett, T.A.2    Hoffman, A.S.3
  • 30
    • 0025775426 scopus 로고
    • Adhesion of L1210 cells to modified styrene copolymer surfaces in the presence of serum
    • Kowalczynska HM, Kaminski J. Adhesion of L1210 cells to modified styrene copolymer surfaces in the presence of serum. J Cell Sci 1991;99:587-593.
    • (1991) J Cell Sci , vol.99 , pp. 587-593
    • Kowalczynska, H.M.1    Kaminski, J.2
  • 31
    • 0017195892 scopus 로고
    • Synthesis of basement membrane collagen by cultured human endothelial cells
    • Jaffe EA, Minick CR, Adelman B, Becker CG. Synthesis of basement membrane collagen by cultured human endothelial cells. J Exp Med 1976;144:209-225.
    • (1976) J Exp Med , vol.144 , pp. 209-225
    • Jaffe, E.A.1    Minick, C.R.2    Adelman, B.3    Becker, C.G.4
  • 32
    • 0018879730 scopus 로고
    • Extracellular matrix and control of proliferation of vascular endothelial cells
    • Gospodarowitcz D, Ill C. Extracellular matrix and control of proliferation of vascular endothelial cells. J Clin Invest 1980; 65:1351-1364.
    • (1980) J Clin Invest , vol.65 , pp. 1351-1364
    • Gospodarowitcz, D.1    Ill, C.2
  • 33
    • 0040586197 scopus 로고
    • Binding of soluble plasma fibronectin to baby hamster kidney cells occurs at 4°C
    • Grinnell F, Lang BS. Binding of soluble plasma fibronectin to baby hamster kidney cells occurs at 4°C. J Cell Biol 1981;87: 127a.
    • (1981) J Cell Biol , vol.87
    • Grinnell, F.1    Lang, B.S.2
  • 34
    • 0018835908 scopus 로고
    • The modulation of cellular contractility and adhesion by trypsin and EDTA
    • Britch M, Allen TD. The modulation of cellular contractility and adhesion by trypsin and EDTA. Exp Cell Res 1980;125: 221-231.
    • (1980) Exp Cell Res , vol.125 , pp. 221-231
    • Britch, M.1    Allen, T.D.2
  • 35
    • 0017386479 scopus 로고
    • Control of grip and stick in cell adhesion through lateral relationship of membrane glycoproteins
    • Rees DA, Lloyd CW, Thom D. Control of grip and stick in cell adhesion through lateral relationship of membrane glycoproteins. Nature 1977;267:124-128.
    • (1977) Nature , vol.267 , pp. 124-128
    • Rees, D.A.1    Lloyd, C.W.2    Thom, D.3
  • 36
    • 0020465828 scopus 로고
    • Inhibition of fibronectin receptor function by antibodies against baby hamster kidney cell wheat germ agglutinin receptors
    • Oppenheimer-Marks N, Grinnell F. Inhibition of fibronectin receptor function by antibodies against baby hamster kidney cell wheat germ agglutinin receptors. J Cell Biol 1982;95:876-884.
    • (1982) J Cell Biol , vol.95 , pp. 876-884
    • Oppenheimer-Marks, N.1    Grinnell, F.2
  • 37
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan JL, Shalloway D. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 1992;358:690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 38
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of ßl integrins
    • Kornberg L, Earp HS, Turner CE, Prockop C, Juliano RL. Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of ßl integrins. Proc Natl Acad Sci USA 1991;88:8392-8396.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8392-8396
    • Kornberg, L.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 39
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg L, Earp HS, Parsons JT, Schaller M, Juliano RL. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 1992; 267:23439-23442.
    • (1992) J Biol Chem , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 40
    • 0031044781 scopus 로고    scopus 로고
    • Focal adhesion kinase: At the crossroads of signal transduction
    • Ilic D, Damsky CH, Yamamoto T. Focal adhesion kinase: At the crossroads of signal transduction. J Cell Sci 1997;110:401-407.
    • (1997) J Cell Sci , vol.110 , pp. 401-407
    • Ilic, D.1    Damsky, C.H.2    Yamamoto, T.3
  • 41
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly. J Cell Biol 1992; 119:893-903.
    • (1992) J Cell Biol , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 42
    • 0028278005 scopus 로고
    • Three-dimensional contact with type I collagen mediates tyrosine phosphorylation in primary human fibroblasts
    • Roeckel D, Krieg T. Three-dimensional contact with type I collagen mediates tyrosine phosphorylation in primary human fibroblasts. Exp Cell Res 1994;211:42-48.
    • (1994) Exp Cell Res , vol.211 , pp. 42-48
    • Roeckel, D.1    Krieg, T.2
  • 43
    • 0026529501 scopus 로고
    • The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions
    • Volberg T, Zick Y, Dror R, Sabanay I, Gilon C, Levitzki A, Geiger B. The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions. EMBO J 1992; 11:1733-1742.
    • (1992) EMBO J , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3    Sabanay, I.4    Gilon, C.5    Levitzki, A.6    Geiger, B.7
  • 44
    • 0028853550 scopus 로고
    • Differential role of protein tyrosine phosphorylation/dephosphorylation in affinity regulation of β1 and β3 integrin in human fibroblasts
    • Takagi J, Saito Y. Differential role of protein tyrosine phosphorylation/dephosphorylation in affinity regulation of β1 and β3 integrin in human fibroblasts. Cell Struc Func 1995;20: 403-413.
    • (1995) Cell Struc Func , vol.20 , pp. 403-413
    • Takagi, J.1    Saito, Y.2
  • 45
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Ann Rev Biochem 1986;55:987-1035.
    • (1986) Ann Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 46
    • 0022160737 scopus 로고
    • Human platelet spreading on substrata of known surface chemistry
    • Baier RE, DePalma VA, Goupil DW, Cohen E. Human platelet spreading on substrata of known surface chemistry. J Biomed Mater Res 1985;19:1157-1167.
    • (1985) J Biomed Mater Res , vol.19 , pp. 1157-1167
    • Baier, R.E.1    DePalma, V.A.2    Goupil, D.W.3    Cohen, E.4
  • 47
    • 0025267402 scopus 로고
    • Spreading of trypsinized cells: Cytoskeletal dynamics and energy requirements
    • Bereiter-Hahn J, Lück M, Miebach T, Stelzer HK, Vöth M. Spreading of trypsinized cells: Cytoskeletal dynamics and energy requirements. J Cell Sci 1990;96:171-188.
    • (1990) J Cell Sci , vol.96 , pp. 171-188
    • Bereiter-Hahn, J.1    Lück, M.2    Miebach, T.3    Stelzer, H.K.4    Vöth, M.5
  • 48
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrins transmembrane function
    • Miyamoto S, Akiyama SK, Yamada KM. Synergistic roles for receptor occupancy and aggregation in integrins transmembrane function. Science 1995;267:883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 49
    • 0018838995 scopus 로고
    • Silicon rubber substrate: A new wrinkle in the study of cell locomotion
    • Harris AK, Wild P, Stopak D. Silicon rubber substrate: A new wrinkle in the study of cell locomotion. Science 1980;280:179.
    • (1980) Science , vol.280 , pp. 179
    • Harris, A.K.1    Wild, P.2    Stopak, D.3
  • 50
    • 0029013320 scopus 로고
    • Condensation of collagen fibrils to the direct vicinity of fibroblasts as a cause of gel contraction
    • Yamato M, Adachi E, Yamamoto K, Hayashi T. Condensation of collagen fibrils to the direct vicinity of fibroblasts as a cause of gel contraction. J Biochem 1995;117:940-946.
    • (1995) J Biochem , vol.117 , pp. 940-946
    • Yamato, M.1    Adachi, E.2    Yamamoto, K.3    Hayashi, T.4
  • 51
    • 0028282547 scopus 로고
    • Cellular tensegrity: Exploring how mechanical changes in the cytoskeleton regulate cell growth, migration, and tissue pattern during morphogenesis
    • Ingber DE, Dike L, Hansen L, Karp S, Liley H, Maniotis A, McNamee H, Mooney D, Plopper G, Sims J, Wang N. Cellular tensegrity: Exploring how mechanical changes in the cytoskeleton regulate cell growth, migration, and tissue pattern during morphogenesis. Int Rev Cytol 1994;150:173-224.
    • (1994) Int Rev Cytol , vol.150 , pp. 173-224
    • Ingber, D.E.1    Dike, L.2    Hansen, L.3    Karp, S.4    Liley, H.5    Maniotis, A.6    McNamee, H.7    Mooney, D.8    Plopper, G.9    Sims, J.10    Wang, N.11
  • 52
    • 0017621895 scopus 로고
    • The adhesion of Chinese hamster cells. I. Effects of temperature, metabolic inhibitors, and proteolytic dissection of cell surface macromolecules
    • Juliano RL, Gagalang E. The adhesion of Chinese hamster cells. I. Effects of temperature, metabolic inhibitors, and proteolytic dissection of cell surface macromolecules. J Cell Physiol 1977; 92:209-220.
    • (1977) J Cell Physiol , vol.92 , pp. 209-220
    • Juliano, R.L.1    Gagalang, E.2
  • 53
    • 0021269999 scopus 로고
    • Calcium ions protect cell-substratum adhesion receptors against proteolysis
    • Oppenheimer-Marks N, Grinnell F. Calcium ions protect cell-substratum adhesion receptors against proteolysis. Exp Cell Res 1984;152:467-175.
    • (1984) Exp Cell Res , vol.152 , pp. 467-1175
    • Oppenheimer-Marks, N.1    Grinnell, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.