메뉴 건너뛰기




Volumn 8, Issue 12, 1997, Pages 2563-2573

Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; INTEGRIN;

EID: 0030659845     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.12.2563     Document Type: Article
Times cited : (130)

References (52)
  • 1
    • 0028043949 scopus 로고
    • Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule
    • Aguirre, K.M., McCormick, R.J., and Schwarzbauer, J.E. (1994). Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule. J. Biol. Chem. 269, 27863-27868.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27863-27868
    • Aguirre, K.M.1    McCormick, R.J.2    Schwarzbauer, J.E.3
  • 2
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama, S.K., Yamada, S.S., Chen, W.-T., and Yamada, K.M. (1989). Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J. Cell Biol. 109, 863-875.
    • (1989) J. Cell Biol. , vol.109 , pp. 863-875
    • Akiyama, S.K.1    Yamada, S.S.2    Chen, W.-T.3    Yamada, K.M.4
  • 3
    • 0017646305 scopus 로고
    • Restoration of a normal morphology, adhesion, and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein
    • Ali, I.U., Mautner, V.M., Lanza, R.P., and Hynes, R.O. (1977). Restoration of a normal morphology, adhesion, and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell 11, 115-126.
    • (1977) Cell , vol.11 , pp. 115-126
    • Ali, I.U.1    Mautner, V.M.2    Lanza, R.P.3    Hynes, R.O.4
  • 4
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota, S., Nomiau, M., and Yamada, K.M. (1994). The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J. Biol. Chem. 269, 24756-24761.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomiau, M.2    Yamada, K.M.3
  • 5
    • 0026040206 scopus 로고
    • Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis
    • Aota, S., Toshihiko, T., and Yamada, K.M. (1991). Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J. Biol. Chem. 266, 15938-15943.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15938-15943
    • Aota, S.1    Toshihiko, T.2    Yamada, K.M.3
  • 7
    • 0031022256 scopus 로고    scopus 로고
    • Anchorage-dependent cell cycle progression
    • Assoian, R.K. (1997). Anchorage-dependent cell cycle progression. J. Cell Biol. 136, 1-4.
    • (1997) J. Cell Biol. , vol.136 , pp. 1-4
    • Assoian, R.K.1
  • 8
    • 0028858576 scopus 로고
    • Mono-clonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni, G., Shih, D.-T., Buck, C.A., and Hemler, M.E. (1995). Mono-clonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270, 25570-25577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.-T.2    Buck, C.A.3    Hemler, M.E.4
  • 10
  • 11
    • 0021878620 scopus 로고
    • Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein
    • Brown, P.J., and Juliano, R.L. (1985). Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein. Science 228, 1448-1451.
    • (1985) Science , vol.228 , pp. 1448-1451
    • Brown, P.J.1    Juliano, R.L.2
  • 12
    • 0023714090 scopus 로고
    • Monoclonal antibodies to distinctive epitopes on the α and α subunits of the fibronectin receptor
    • Brown, P.J., and Juliano, R.L. (1988). Monoclonal antibodies to distinctive epitopes on the α and α subunits of the fibronectin receptor. Exp. Cell Res. 177, 303-318.
    • (1988) Exp. Cell Res. , vol.177 , pp. 303-318
    • Brown, P.J.1    Juliano, R.L.2
  • 13
    • 0029100101 scopus 로고
    • Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin α5β1
    • Danen, E.J., Aota, S., vanKraats, A.A., Yamada, K.M., Ruiter, D.J., and vanMuijen, G.N.P. (1995). Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin α5β1. J. Biol. Chem. 270, 21612-21618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21612-21618
    • Danen, E.J.1    Aota, S.2    VanKraats, A.A.3    Yamada, K.M.4    Ruiter, D.J.5    VanMuijen, G.N.P.6
  • 14
    • 0024506757 scopus 로고
    • Phorbol ester modulation of integrin-mediated cell adhesion: A postreceptor event
    • Danilov, Y.N., and Juliano, R.L. (1989). Phorbol ester modulation of integrin-mediated cell adhesion: a postreceptor event. J. Cell Biol. 108, 1925-1933.
    • (1989) J. Cell Biol. , vol.108 , pp. 1925-1933
    • Danilov, Y.N.1    Juliano, R.L.2
  • 16
    • 0027395041 scopus 로고
    • Affinity modulation of integrin α5β1: Regulation of the functional response by soluble fibronectin
    • Faull, R.J., Kovach, N.L., Harlan, J.M., and Ginsberg, M.H. (1993). Affinity modulation of integrin α5β1: regulation of the functional response by soluble fibronectin. J. Cell Biol. 222, 155-162.
    • (1993) J. Cell Biol. , vol.222 , pp. 155-162
    • Faull, R.J.1    Kovach, N.L.2    Harlan, J.M.3    Ginsberg, M.H.4
  • 17
    • 0028349012 scopus 로고
    • Stimulation of integrin-mediated adhesion of T-lymphocytes and monocytes: Two mechanisms with divergent biological consequences
    • Faull, R.J., Kovach, N.L., Harlan, J.M., and Ginsberg, M.H. (1994). Stimulation of integrin-mediated adhesion of T-lymphocytes and monocytes: two mechanisms with divergent biological consequences. J. Exp. Med. 179, 1307-1316.
    • (1994) J. Exp. Med. , vol.179 , pp. 1307-1316
    • Faull, R.J.1    Kovach, N.L.2    Harlan, J.M.3    Ginsberg, M.H.4
  • 18
    • 0025362679 scopus 로고
    • Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (alpha 5 beta 1) antibodies
    • Fogerty, F.J., Akiyama, S.K., Yamada, K.M., and Mosher, D.F. (1990). Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (alpha 5 beta 1) antibodies. J. Cell Biol. 111, 699-708.
    • (1990) J. Cell Biol. , vol.111 , pp. 699-708
    • Fogerty, F.J.1    Akiyama, S.K.2    Yamada, K.M.3    Mosher, D.F.4
  • 19
    • 0026063230 scopus 로고
    • Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger, A.L., III, Du, X., Plow, E.F., and Ginsberg, M.H. (1991). Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266, 17106-17111.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17106-17111
    • Frelinger III, A.L.1    Du, X.2    Plow, E.F.3    Ginsberg, M.H.4
  • 20
    • 0023730954 scopus 로고
    • Regulation of fibronectin receptor affinity by divalent cations
    • Gailit, J., and Ruoslahti, E. (1988). Regulation of fibronectin receptor affinity by divalent cations. J. Biol. Chem. 263, 12927-12932.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12927-12932
    • Gailit, J.1    Ruoslahti, E.2
  • 21
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George, E.L., Georges-Labouesse, E.N., Patel-King, R.S., Rayburn, H., and Hynes, R.O. (1993). Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 229, 1079-1091.
    • (1993) Development , vol.229 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 22
    • 0025214421 scopus 로고
    • Elevated levels of the α5βl fibronectin receptor suppress the transformed phenotype of the Chinese hamster ovary cells
    • Giancotti, F.G., and Ruoslahti, E. (1990). Elevated levels of the α5βl fibronectin receptor suppress the transformed phenotype of the Chinese hamster ovary cells. Cell 60, 849-859.
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 24
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin
    • Hocking, D.C., Sottile, J., and McKeown-Longo, P.J. (1994). Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J. Biol. Chem. 269, 19183-19191.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19183-19191
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 25
    • 0030272101 scopus 로고    scopus 로고
    • Integrin activation: The link between ligand binding and signal transduction
    • Humphries, M.J. (1996). Integrin activation: the link between ligand binding and signal transduction. Curr. Opin. Cell Biol. 8, 632-640.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 632-640
    • Humphries, M.J.1
  • 26
    • 0004043397 scopus 로고
    • New York: Springer-Verlag
    • Hynes, R.O. (1990). Fibronectins, New York: Springer-Verlag.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 27
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 28
    • 0030222341 scopus 로고    scopus 로고
    • Crosstalk between cell adhesion molecules: Vinculin as a paradigm for regulation by conformation
    • Jockusch, B.M., and Rudiger, M. (1996). Crosstalk between cell adhesion molecules: vinculin as a paradigm for regulation by conformation. Trends Cell Biol. 6, 311-315.
    • (1996) Trends Cell Biol. , vol.6 , pp. 311-315
    • Jockusch, B.M.1    Rudiger, M.2
  • 29
    • 0026512171 scopus 로고
    • A monoclonal antibody to beta 1 integrin (CD29) stimulates VLA-dependent adherence of leukocytes to human umbilical vein endothelial cells and matrix components
    • Kovach, N.L., Carlos, T.M., Yee, E., and Harlan, J.M. (1992). A monoclonal antibody to beta 1 integrin (CD29) stimulates VLA-dependent adherence of leukocytes to human umbilical vein endothelial cells and matrix components. J. Cell Biol. 326, 499-509.
    • (1992) J. Cell Biol. , vol.326 , pp. 499-509
    • Kovach, N.L.1    Carlos, T.M.2    Yee, E.3    Harlan, J.M.4
  • 30
    • 0024150414 scopus 로고
    • Extracellular matrix assembly
    • McDonald, J.A. (1988). Extracellular matrix assembly. Annu. Rev. Cell Biol. 4, 183-207.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 183-207
    • McDonald, J.A.1
  • 31
    • 0026652898 scopus 로고
    • A fibronectin self-assembly site involved in fibronectin matrix assembly: Reconstruction in a synthetic peptide
    • Morla, A., and Rouslahti, E. (1992). A fibronectin self-assembly site involved in fibronectin matrix assembly: reconstruction in a synthetic peptide. J. Cell Biol. 118, 421-429.
    • (1992) J. Cell Biol. , vol.118 , pp. 421-429
    • Morla, A.1    Rouslahti, E.2
  • 32
    • 0027483402 scopus 로고
    • Assembly of fibronectin into extracellular matrix
    • Mosher, D.F. (1993). Assembly of fibronectin into extracellular matrix. Curr. Opin. Struct. Biol. 3, 214-222.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 214-222
    • Mosher, D.F.1
  • 33
    • 0029969086 scopus 로고    scopus 로고
    • Getting integrins into shape: Recent insights into how integrin activity is regulated by conformational changes
    • Mould, A.P. (1996). Getting integrins into shape: recent insights into how integrin activity is regulated by conformational changes. J. Cell Sci. 209, 2613-2618.
    • (1996) J. Cell Sci. , vol.209 , pp. 2613-2618
    • Mould, A.P.1
  • 34
    • 0028970566 scopus 로고
    • Regulation of integrin α5β1-fibronectin interactions by divalent cations
    • Mould, A.P., Akiyama, S., and Humphries, M.J. (1995). Regulation of integrin α5β1-fibronectin interactions by divalent cations. J. Biol. Chem. 270, 26270-26277.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26270-26277
    • Mould, A.P.1    Akiyama, S.2    Humphries, M.J.3
  • 35
    • 0025948419 scopus 로고
    • Monoclonal antibody characterization of two distant sites required for function in cell adhesion, cell migration, and matrix assembly
    • Nagai, T., Yamakawa, N., Aota, S., Yamada, S.S., Akiyama, S.K., Olden, K., and Yamada, K.M. (1991). Monoclonal antibody characterization of two distant sites required for function in cell adhesion, cell migration, and matrix assembly. J. Cell Biol. 114, 1295-1305.
    • (1991) J. Cell Biol. , vol.114 , pp. 1295-1305
    • Nagai, T.1    Yamakawa, N.2    Aota, S.3    Yamada, S.S.4    Akiyama, S.K.5    Olden, K.6    Yamada, K.M.7
  • 36
    • 0025519981 scopus 로고
    • Affinity modulation of the alpha lib beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor
    • O'Toole, T.E., Loftus, J.C., Du, X., Glass, A.A., Ruggeri, Z.M., Shattil, S.J., Plow, E.P., and Ginsberg, M.H. (1990). Affinity modulation of the alpha lib beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor. Cell Regul. 1, 883-893.
    • (1990) Cell Regul. , vol.1 , pp. 883-893
    • O'Toole, T.E.1    Loftus, J.C.2    Du, X.3    Glass, A.A.4    Ruggeri, Z.M.5    Shattil, S.J.6    Plow, E.P.7    Ginsberg, M.H.8
  • 37
    • 0029903961 scopus 로고    scopus 로고
    • Xenopus embryonic cell adhesion to fibronectin: Position-specific activation of RGD/synergy site-dependent migratory behavior at gastrulation
    • Ramos, J.W., and DeSimone, D.W. (1996). Xenopus embryonic cell adhesion to fibronectin: position-specific activation of RGD/synergy site-dependent migratory behavior at gastrulation. J. Cell Biol. 234, 227-240.
    • (1996) J. Cell Biol. , vol.234 , pp. 227-240
    • Ramos, J.W.1    DeSimone, D.W.2
  • 38
    • 0024328167 scopus 로고
    • The fibronectin receptor is organized by extracellular matrix fibronectin: Implications for oncogenic transformation and for cell recognition of fibronectin matrices
    • Roman, J., R.M. LaChance, Broekelmann, T.J., Kennedy, C.J.R., Wagner, E.A., Carter, W.G., and McDonald, J.A. (1989). The fibronectin receptor is organized by extracellular matrix fibronectin: implications for oncogenic transformation and for cell recognition of fibronectin matrices. J. Cell Biol. 108, 2529-2543.
    • (1989) J. Cell Biol. , vol.108 , pp. 2529-2543
    • Roman, J.1    LaChance, R.M.2    Broekelmann, T.J.3    Kennedy, C.J.R.4    Wagner, E.A.5    Carter, W.G.6    McDonald, J.A.7
  • 40
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequences required for assembly of a fibrillar matrix
    • Schwarzbauer, J.E. (1991). Identification of the fibronectin sequences required for assembly of a fibrillar matrix. J. Cell Biol. 223, 1463-1473.
    • (1991) J. Cell Biol. , vol.223 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 41
    • 0030036963 scopus 로고    scopus 로고
    • Altered rate of fibronectin matrix assembly by deletion of the first type III repeats
    • Sechler, J.L., Takada, Y., and Schwarzbauer, J.E. (1996). Altered rate of fibronectin matrix assembly by deletion of the first type III repeats. J. Cell. Biol. 234, 575-585.
    • (1996) J. Cell. Biol. , vol.234 , pp. 575-585
    • Sechler, J.L.1    Takada, Y.2    Schwarzbauer, J.E.3
  • 42
    • 0030976429 scopus 로고    scopus 로고
    • Coordinate regulation of fibronectin fibril assembly and actin stress fiber formation
    • Sechler, J.L., and Schwarzbauer, J.E. (1997). Coordinate regulation of fibronectin fibril assembly and actin stress fiber formation. Cell Adhes. Commun. 4, 413-424.
    • (1997) Cell Adhes. Commun. , vol.4 , pp. 413-424
    • Sechler, J.L.1    Schwarzbauer, J.E.2
  • 43
    • 0027364276 scopus 로고
    • Protein kinase C modulation of fibronectin matrix assembly
    • Somers, C.E., and Mosher, D.E. (1993). Protein kinase C modulation of fibronectin matrix assembly. J. Biol. Chem. 268, 22277-22280.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22277-22280
    • Somers, C.E.1    Mosher, D.E.2
  • 45
    • 0027373782 scopus 로고
    • Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin
    • Vuori, K., and Ruoslahti, E. (1993). Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin. J. Biol. Chem. 265, 21459-21462.
    • (1993) J. Biol. Chem. , vol.265 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 47
    • 0029800576 scopus 로고    scopus 로고
    • Identification of a new biological function for the integrin avb3: Initiation of fibronectin matrix assembly
    • Wu, C., Hughes, P.E., Ginsberg, M.H., and McDonald, J.A. (1996). Identification of a new biological function for the integrin avb3: initiation of fibronectin matrix assembly. Cell Adhes. Commun. 4, 149-158.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 149-158
    • Wu, C.1    Hughes, P.E.2    Ginsberg, M.H.3    McDonald, J.A.4
  • 48
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are critical steps in the assembly of a fibronectin matrix
    • Wu, C., Kevins, V., O'Toole, T.E., McDonald, J.A., and Ginsberg, M.H. (1995). Integrin activation and cytoskeletal interaction are critical steps in the assembly of a fibronectin matrix. Cell 83, 715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Kevins, V.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 49
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada, K.M., and Miyamoto, S. (1995). Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7, 681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 50
    • 1842389885 scopus 로고
    • Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts
    • Yamada, K.M., Yamada, S.S., and Pastan, I. (1976). Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts. Proc. Natl. Acad. Sci. USA 73, 1271-1221.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1271-11221
    • Yamada, K.M.1    Yamada, S.S.2    Pastan, I.3
  • 51
    • 0027371908 scopus 로고
    • Embryonic mesodermal defects in α5 integrin-deficient mice
    • Yang, J.T., Rayburn, H., and Hynes, R.O. (1993). Embryonic mesodermal defects in α5 integrin-deficient mice. Development 119, 1093-1105.
    • (1993) Development , vol.119 , pp. 1093-1105
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 52
    • 0029957287 scopus 로고    scopus 로고
    • Fibronectin receptor functions in embryonic cells deficient in α5β1 integrin can be replaced by αv integrins
    • Yang, J.T., and Hynes, R.O. (1996). Fibronectin receptor functions in embryonic cells deficient in α5β1 integrin can be replaced by αv integrins. Mol. Biol. Cell 7, 1737-1748.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1737-1748
    • Yang, J.T.1    Hynes, R.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.