메뉴 건너뛰기




Volumn 5, Issue 4, 1994, Pages 439-453

The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; COLLAGENASE; FIBRONECTIN; FIBRONECTIN RECEPTOR; GELATINASE; MESSENGER RNA; MONOCLONAL ANTIBODY; PLASMA PROTEIN; STROMELYSIN; TENASCIN; VITRONECTIN;

EID: 0028339075     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.5.4.439     Document Type: Article
Times cited : (201)

References (66)
  • 1
    • 0021278562 scopus 로고
    • Collagenase is a major gene product of induced rabbit synovial fibroblasts
    • Aggeler, J.M., Frisch, S.M., and Werb, Z. (1984). Collagenase is a major gene product of induced rabbit synovial fibroblasts. J. Cell Biol. 98, 1656-1661.
    • (1984) J. Cell Biol. , vol.98 , pp. 1656-1661
    • Aggeler, J.M.1    Frisch, S.M.2    Werb, Z.3
  • 3
    • 0026769909 scopus 로고
    • Targeted disruption of the tissue inhibitor of metalloproteinases gene increases the invasive behavior of primitive mesenchymal cells derived from embryonic stem cells in vitro
    • Alexander, C.M., and Werb, Z. (1992). Targeted disruption of the tissue inhibitor of metalloproteinases gene increases the invasive behavior of primitive mesenchymal cells derived from embryonic stem cells in vitro. J. Cell Biol. 118, 727-739.
    • (1992) J. Cell Biol. , vol.118 , pp. 727-739
    • Alexander, C.M.1    Werb, Z.2
  • 4
    • 0027015773 scopus 로고
    • Specific members of the Jun protein family regulate collagenase expression in response to various extracellular stimuli
    • Angel, P., and Karin, M. (1992). Specific members of the Jun protein family regulate collagenase expression in response to various extracellular stimuli. Matrix Suppl. 1, 156-164.
    • (1992) Matrix Suppl. , vol.1 , pp. 156-164
    • Angel, P.1    Karin, M.2
  • 6
    • 0025896276 scopus 로고
    • The AP-1 sequence is necessary but not sufficient for phorbol induction of collagenase in fibroblasts
    • Auble, D.T., and Brinckerhoff, C.E. (1991). The AP-1 sequence is necessary but not sufficient for phorbol induction of collagenase in fibroblasts. Biochemistry 30, 4629-4635.
    • (1991) Biochemistry , vol.30 , pp. 4629-4635
    • Auble, D.T.1    Brinckerhoff, C.E.2
  • 7
    • 0024687481 scopus 로고
    • Genes for extracellular-matrix-degrading metalloproteinases and their inhibitor, TIMP, are expressed during early mammalian development
    • Brenner, C.A., Adler, R.R., Rappolee, D.A., and Werb, Z. (1989). Genes for extracellular-matrix-degrading metalloproteinases and their inhibitor, TIMP, are expressed during early mammalian development. Genes & Dev. 3, 848-859.
    • (1989) Genes & Dev. , vol.3 , pp. 848-859
    • Brenner, C.A.1    Adler, R.R.2    Rappolee, D.A.3    Werb, Z.4
  • 8
    • 0021270360 scopus 로고
    • Chick myotendinous antigen. I. A monoclonal antibody as a marker for tendon and muscle morphogenesis
    • Chiquet, M., and Fambrough, D.M. (1984). Chick myotendinous antigen. I. A monoclonal antibody as a marker for tendon and muscle morphogenesis. J. Cell Biol. 98, 1926-1936.
    • (1984) J. Cell Biol. , vol.98 , pp. 1926-1936
    • Chiquet, M.1    Fambrough, D.M.2
  • 9
    • 0025736963 scopus 로고
    • Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant
    • Chiquet, M., Vrucinic-Filipi, N., Schenk, S., Beck, K., and Chiquet-Ehrismann, R. (1991). Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant. Eur. J. Biochem. 199, 379-388.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 379-388
    • Chiquet, M.1    Vrucinic-Filipi, N.2    Schenk, S.3    Beck, K.4    Chiquet-Ehrismann, R.5
  • 10
    • 0026244872 scopus 로고
    • Anti-adhesive molecules of the extracellular matrix
    • Chiquet-Ehrismann, R. (1991). Anti-adhesive molecules of the extracellular matrix. Curr. Opin. Cell Biol. 3, 800-804.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 800-804
    • Chiquet-Ehrismann, R.1
  • 11
    • 0022972814 scopus 로고
    • Tenascin: An extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis
    • Chiquet-Ehrismann, R., Mackie, E.J., Pearson, C.A., and Sakakura, T. (1986). Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell 47, 131-139.
    • (1986) Cell , vol.47 , pp. 131-139
    • Chiquet-Ehrismann, R.1    Mackie, E.J.2    Pearson, C.A.3    Sakakura, T.4
  • 13
    • 0026252643 scopus 로고
    • Tenascin variants: Differential binding to fibronectin and distinct distribution in cell cultures and tissues
    • Chiquet-Ehrismann, R., Matsuoka, Y., Hofer, U., Spring, J., Bernasconi, C., and Chiquet, M. (1991). Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. Cell Regul. 2, 927-938.
    • (1991) Cell Regul. , vol.2 , pp. 927-938
    • Chiquet-Ehrismann, R.1    Matsuoka, Y.2    Hofer, U.3    Spring, J.4    Bernasconi, C.5    Chiquet, M.6
  • 14
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • Damsky, C.H., and Werb, Z. (1992). Signal transduction by integrin receptors for extracellular matrix: cooperative processing of extracellular information. Curr. Opin. Cell Biol. 4, 772-781.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 15
    • 0024454215 scopus 로고
    • Stimulation of tenascin expression in mesenchyme by epithelial-mesenchymal interactions
    • Ekblom, P., and Aufderheide, E. (1989). Stimulation of tenascin expression in mesenchyme by epithelial-mesenchymal interactions. Int. J. Dev. Biol. 33, 71-79.
    • (1989) Int. J. Dev. Biol. , vol.33 , pp. 71-79
    • Ekblom, P.1    Aufderheide, E.2
  • 16
    • 0025818844 scopus 로고
    • Domains in proteins and proteoglycans of the extracellular matrix with functions in assembly and cellular activities
    • Engel, J. (1991). Domains in proteins and proteoglycans of the extracellular matrix with functions in assembly and cellular activities. Int. J. Biol. Macromol. 13, 147-151.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 147-151
    • Engel, J.1
  • 17
    • 0024441046 scopus 로고
    • Tenascin: An extracellular matrix protein prominent in specialized embryonic tissues and tumors
    • Erickson, H.P., and Bourdon, M.A. (1989). Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol. 5, 71-92.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 71-92
    • Erickson, H.P.1    Bourdon, M.A.2
  • 18
    • 0024344620 scopus 로고
    • Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat
    • ffrench-Constant, C., Van de Water, L., Dvorak, H.F., and Hynes, R.O. (1989). Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat. J. Cell Biol. 109, 903-914.
    • (1989) J. Cell Biol. , vol.109 , pp. 903-914
    • Ffrench-Constant, C.1    Van De Water, L.2    Dvorak, H.F.3    Hynes, R.O.4
  • 19
    • 0024204115 scopus 로고
    • Functional mapping of cytotactin: Proteolytic fragments active in cell-substrate adhesion
    • Friedlander, D.R., Hoffman, S., and Edelman, G.M. (1988). Functional mapping of cytotactin: proteolytic fragments active in cell-substrate adhesion. J. Cell Biol. 107, 2329-2340.
    • (1988) J. Cell Biol. , vol.107 , pp. 2329-2340
    • Friedlander, D.R.1    Hoffman, S.2    Edelman, G.M.3
  • 20
    • 0011911911 scopus 로고
    • Molecular biology of collagen degradation
    • eds. B.R. Olsen and M.E. Nimni, Boca Raton, FL: CRC Press
    • Frisch, S.M., and Werb, Z. (1989). Molecular biology of collagen degradation. In: Collagen, vol. IV, eds. B.R. Olsen and M.E. Nimni, Boca Raton, FL: CRC Press.
    • (1989) Collagen , vol.4
    • Frisch, S.M.1    Werb, Z.2
  • 21
    • 0024515867 scopus 로고
    • Fibroblasts that proliferate near denervated synaptic sites in skeletal muscle synthesize the adhesive molecules tenascin (J1), N-CAM, fibronectin and a heparan sulfate proteoglycan
    • Gatchalian, C.L., Schachner, M., and Sanes, J.R. (1989). Fibroblasts that proliferate near denervated synaptic sites in skeletal muscle synthesize the adhesive molecules tenascin (J1), N-CAM, fibronectin and a heparan sulfate proteoglycan. J. Cell Biol. 108, 1873-1890.
    • (1989) J. Cell Biol. , vol.108 , pp. 1873-1890
    • Gatchalian, C.L.1    Schachner, M.2    Sanes, J.R.3
  • 22
    • 0021972086 scopus 로고
    • Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion
    • Ginsberg, M., Pierschbacher, M.D., Ruoslahti, E., and Plow, E. (1987). Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion. J. Biol. Chem. 260, 3931-3936.
    • (1987) J. Biol. Chem. , vol.260 , pp. 3931-3936
    • Ginsberg, M.1    Pierschbacher, M.D.2    Ruoslahti, E.3    Plow, E.4
  • 24
    • 0025346113 scopus 로고
    • The collagenase gene promoter contains a TPA and oncogens-responsive unit encompassing the PEA3 and AP-1 binding sites
    • Gutman, A., and Wasylyk, B. (1990). The collagenase gene promoter contains a TPA and oncogens-responsive unit encompassing the PEA3 and AP-1 binding sites. EMBO J. 9, 2241-2246.
    • (1990) EMBO J. , vol.9 , pp. 2241-2246
    • Gutman, A.1    Wasylyk, B.2
  • 25
    • 0024596971 scopus 로고
    • The effect of tenascin and embryonic basal lamina on the behavior and morphology of neural crest cells in vitro
    • Halfter, W., Chiquet-Ehrismann, R., and Tucker, R.P. (1989). The effect of tenascin and embryonic basal lamina on the behavior and morphology of neural crest cells in vitro. Dev. Biol. 132, 14-25.
    • (1989) Dev. Biol. , vol.132 , pp. 14-25
    • Halfter, W.1    Chiquet-Ehrismann, R.2    Tucker, R.P.3
  • 26
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (eds.) (1989). Antibodies: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1989) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 28
    • 0023905350 scopus 로고
    • Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules
    • Hoffman, S., Crossin, K.L., and Edelman, G.M. (1988). Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules. J. Cell Biol. 106, 519-532.
    • (1988) J. Cell Biol. , vol.106 , pp. 519-532
    • Hoffman, S.1    Crossin, K.L.2    Edelman, G.M.3
  • 29
    • 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
  • 30
    • 0022979093 scopus 로고
    • Fibronectin glycosylation modulates fibroblast adhesion and spreading
    • Jones, G.E., Arumugham, R.G., and Tanzer, M.L. (1986). Fibronectin glycosylation modulates fibroblast adhesion and spreading. J. Cell Biol. 103, 1663-1670.
    • (1986) J. Cell Biol. , vol.103 , pp. 1663-1670
    • Jones, G.E.1    Arumugham, R.G.2    Tanzer, M.L.3
  • 31
    • 0027497077 scopus 로고
    • Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin
    • Joshi, P., Chung, C-Y., Aukhil, I., and Erickson, H.P. (1993). Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin. J. Cell Sci. 106, 389-400.
    • (1993) J. Cell Sci. , vol.106 , pp. 389-400
    • Joshi, P.1    Chung, C.-Y.2    Aukhil, I.3    Erickson, H.P.4
  • 32
    • 0026012443 scopus 로고
    • Undulin is a novel member of the fibronectin-tenascin family of extracellular matrix glycoproteins
    • Just, M., Herbst, H., Hummel, M., Durkop, H., Tripier, D., Stein, H., and Schuppan, D. (1991). Undulin is a novel member of the fibronectin-tenascin family of extracellular matrix glycoproteins. J. Biol. Chem. 266, 17326-17332.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17326-17332
    • Just, M.1    Herbst, H.2    Hummel, M.3    Durkop, H.4    Tripier, D.5    Stein, H.6    Schuppan, D.7
  • 33
    • 0025098987 scopus 로고
    • Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion
    • Lightner, V., and Erickson, H.P. (1990). Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion. J. Cell Sci. 95, 263-277.
    • (1990) J. Cell Sci. , vol.95 , pp. 263-277
    • Lightner, V.1    Erickson, H.P.2
  • 34
    • 0025836594 scopus 로고
    • J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth
    • Lochter, A., Vaughn, L., Kaplony, A., Prochiantz, A., Schachner, M., and Faissner, A. (1991). J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. J. Cell Biol. 113, 1159-1171.
    • (1991) J. Cell Biol. , vol.113 , pp. 1159-1171
    • Lochter, A.1    Vaughn, L.2    Kaplony, A.3    Prochiantz, A.4    Schachner, M.5    Faissner, A.6
  • 35
    • 0024461009 scopus 로고
    • Cell adhesion to fibronectin and tenascin: Quantitative measurements of initial binding and subsequent strengthening response
    • Lotz, M.M., Burdsal, C.A., Erickson, H.P., and McClay, D.R. (1989). Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J. Cell Biol. 109, 1795-1805.
    • (1989) J. Cell Biol. , vol.109 , pp. 1795-1805
    • Lotz, M.M.1    Burdsal, C.A.2    Erickson, H.P.3    McClay, D.R.4
  • 36
    • 0024215607 scopus 로고
    • Induction of tenascin in healing wounds
    • Mackie, E.J., Halfter, W., and Liverani, D. (1988). Induction of tenascin in healing wounds. J. Cell Biol. 107, 2757-2767.
    • (1988) J. Cell Biol. , vol.107 , pp. 2757-2767
    • Mackie, E.J.1    Halfter, W.2    Liverani, D.3
  • 37
    • 0026606265 scopus 로고
    • Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin
    • Matsumoto, K., Arai, M., Ishihara, N., Ando, A., Inoko, H., and Ikemura, T. (1992). Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin. Genomics 12, 485-491.
    • (1992) Genomics , vol.12 , pp. 485-491
    • Matsumoto, K.1    Arai, M.2    Ishihara, N.3    Ando, A.4    Inoko, H.5    Ikemura, T.6
  • 38
    • 0026321941 scopus 로고
    • Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin
    • Murphy-Ullrich, J.E., Lightner, V.A., Aukhil, I., Yan, Y.Z., Erickson, H.P., and Hook, M. (1991). Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J. Cell Biol. 115, 1127-1136.
    • (1991) J. Cell Biol. , vol.115 , pp. 1127-1136
    • Murphy-Ullrich, J.E.1    Lightner, V.A.2    Aukhil, I.3    Yan, Y.Z.4    Erickson, H.P.5    Hook, M.6
  • 39
    • 0025828299 scopus 로고
    • The complete cDNA sequence of human hexabrachion (tenascin). A multidomain protein containing unique epidermal growth factor repeats
    • Nies, D.E., Hemesath, T.J., Kim, J.H., Gulcher, J.R., and Stefansson, K. (1991). The complete cDNA sequence of human hexabrachion (tenascin). A multidomain protein containing unique epidermal growth factor repeats. J. Biol. Chem. 266, 2818-2823.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2818-2823
    • Nies, D.E.1    Hemesath, T.J.2    Kim, J.H.3    Gulcher, J.R.4    Stefansson, K.5
  • 40
    • 0026039776 scopus 로고
    • Complete primary structure of porcine tenascin. Detection of tenascin transcripts in adult submaxillary glands
    • Nishi, T., Weinstein, J., Gillespie, W.M., and Paulson, J.C. (1991). Complete primary structure of porcine tenascin. Detection of tenascin transcripts in adult submaxillary glands. Eur. J. Biochem. 202, 643-648.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 643-648
    • Nishi, T.1    Weinstein, J.2    Gillespie, W.M.3    Paulson, J.C.4
  • 41
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Norenberg, U., Wille, H., Wolff, J.M., Frank, R., and Rathjen, F.G. (1992). The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron 8, 849-863.
    • (1992) Neuron , vol.8 , pp. 849-863
    • Norenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 42
    • 0024292679 scopus 로고
    • Site-directed mutagenesis of the cell binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
    • Obara, M., Kang, M.S., and Yamada, K.M. (1988). Site-directed mutagenesis of the cell binding domain of human fibronectin: separable, synergistic sites mediate adhesive function. Cell 53, 649-657.
    • (1988) Cell , vol.53 , pp. 649-657
    • Obara, M.1    Kang, M.S.2    Yamada, K.M.3
  • 43
    • 0025296045 scopus 로고
    • Localization during development of alternatively spliced forms of cytotactin mRNA by in situ hybridization
    • Prieto, A.L., Jones, F.S., Cunningham, B.A., Crossin, K.L., and Edelman, G.M. (1990). Localization during development of alternatively spliced forms of cytotactin mRNA by in situ hybridization. J. Cell Biol. 111, 685-698.
    • (1990) J. Cell Biol. , vol.111 , pp. 685-698
    • Prieto, A.L.1    Jones, F.S.2    Cunningham, B.A.3    Crossin, K.L.4    Edelman, G.M.5
  • 44
    • 0026732724 scopus 로고
    • Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin
    • Prieto, A.L., Andersson-Fisone, C., and Crossin, K.L. (1992). Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin. J. Cell Biol. 119, 663-678.
    • (1992) J. Cell Biol. , vol.119 , pp. 663-678
    • Prieto, A.L.1    Andersson-Fisone, C.2    Crossin, K.L.3
  • 45
    • 0024571529 scopus 로고
    • Novel method for studying mRNA phenotypes in single or small numbers of cells
    • Rappolee, D.A., Wang, A., Mark, D., and Werb, Z. (1989). Novel method for studying mRNA phenotypes in single or small numbers of cells. J. Cell. Biochem. 39, 1-11.
    • (1989) J. Cell. Biochem. , vol.39 , pp. 1-11
    • Rappolee, D.A.1    Wang, A.2    Mark, D.3    Werb, Z.4
  • 46
    • 0026710836 scopus 로고
    • Insulin-like growth factor II acts through an endogenous growth pathway regulated by imprinting in early mouse embryos
    • Rappolee, D.A., Sturm, K.S., Behrendtsen, O., Schultz, G.A., Pedersen, R.A., and Werb, Z. (1992). Insulin-like growth factor II acts through an endogenous growth pathway regulated by imprinting in early mouse embryos. Genes & Dev. 6, 939-952.
    • (1992) Genes & Dev. , vol.6 , pp. 939-952
    • Rappolee, D.A.1    Sturm, K.S.2    Behrendtsen, O.3    Schultz, G.A.4    Pedersen, R.A.5    Werb, Z.6
  • 47
    • 0025128560 scopus 로고
    • Exogenous tenascin inhibits mesodermal cell migration during amphibian gastrulation
    • Riou, J.F., Shi, D.L., Chiquet, M., and Boucaut, J.C. (1990). Exogenous tenascin inhibits mesodermal cell migration during amphibian gastrulation. Dev. Biol. 137, 305-317.
    • (1990) Dev. Biol. , vol.137 , pp. 305-317
    • Riou, J.F.1    Shi, D.L.2    Chiquet, M.3    Boucaut, J.C.4
  • 49
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin
    • Sage, E.H., and Bornstein, P. (1991). Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin. J. Biol. Chem. 266, 14831-14834.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 51
    • 0025975626 scopus 로고
    • Human tenascin: Primary structure, pre-mRNA splicing patterns and localization of the epitopes recognized by two monoclonal antibodies
    • Sin, A., Carnemolla, B., Saginati, M., Leprini, A., Casari, G., Baralle, F., and Zardi, L. (1991). Human tenascin: primary structure, pre-mRNA splicing patterns and localization of the epitopes recognized by two monoclonal antibodies. Nucleic Acids Res. 19, 525-531.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 525-531
    • Sin, A.1    Carnemolla, B.2    Saginati, M.3    Leprini, A.4    Casari, G.5    Baralle, F.6    Zardi, L.7
  • 52
    • 0024347096 scopus 로고
    • Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments
    • Spring, J., Beck, K., and Chiquet-Ehrismann, R. (1989). Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell 59, 325-334.
    • (1989) Cell , vol.59 , pp. 325-334
    • Spring, J.1    Beck, K.2    Chiquet-Ehrismann, R.3
  • 54
    • 0024535146 scopus 로고
    • Boundaries defined by adhesion molecules during development of the cerebral cortex: The J1/tenascin glycoprotein in the mouse somatosensory cortical barrel field
    • Steindler, D.A., Cooper, N.G., Faissner, A., and Schachner, M. (1989). Boundaries defined by adhesion molecules during development of the cerebral cortex: the J1/tenascin glycoprotein in the mouse somatosensory cortical barrel field. Dev. Biol. 131, 243-260.
    • (1989) Dev. Biol. , vol.131 , pp. 243-260
    • Steindler, D.A.1    Cooper, N.G.2    Faissner, A.3    Schachner, M.4
  • 55
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution
    • Talhouk, R.S., Bissell, M.J., and Werb, Z. (1992). Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution. J. Cell Biol. 118, 1271-1282.
    • (1992) J. Cell Biol. , vol.118 , pp. 1271-1282
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 56
    • 0027297962 scopus 로고
    • SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway
    • Tremble, P., Lane, T.F., Sage, E.H., and Werb, Z. (1993). SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway. J. Cell Biol. 121, 1433-1444.
    • (1993) J. Cell Biol. , vol.121 , pp. 1433-1444
    • Tremble, P.1    Lane, T.F.2    Sage, E.H.3    Werb, Z.4
  • 57
    • 0025776976 scopus 로고
    • The expression of tenascin by neural crest cells and glia
    • Tucker, R.P., and McKay, S.E. (1991). The expression of tenascin by neural crest cells and glia. Development 112, 1031-1039.
    • (1991) Development , vol.112 , pp. 1031-1039
    • Tucker, R.P.1    McKay, S.E.2
  • 58
    • 0022977704 scopus 로고
    • Reorganization of polymerized actin: A possible trigger for induction of procollagenase in fibroblasts cultured in and on collagen gels
    • Unemori, E.N., and Werb, Z. (1986). Reorganization of polymerized actin: a possible trigger for induction of procollagenase in fibroblasts cultured in and on collagen gels. J. Cell Biol. 103, 1021-1031.
    • (1986) J. Cell Biol. , vol.103 , pp. 1021-1031
    • Unemori, E.N.1    Werb, Z.2
  • 59
    • 0025186040 scopus 로고
    • Tenascin is accumulated along developing peripheral nerves and allows neurite outgrowth in vitro
    • Wehrle, B., and Chiquet, M. (1990). Tenascin is accumulated along developing peripheral nerves and allows neurite outgrowth in vitro. Development 110, 401-415.
    • (1990) Development , vol.110 , pp. 401-415
    • Wehrle, B.1    Chiquet, M.2
  • 60
    • 0025965905 scopus 로고
    • Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis
    • Weller, A., Beck, S., and Ekblom, P. (1991). Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis. J. Cell Biol. 112, 355-362.
    • (1991) J. Cell Biol. , vol.112 , pp. 355-362
    • Weller, A.1    Beck, S.2    Ekblom, P.3
  • 61
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., Tremble, P., Behrendtsen, O., Crowley, E., and Damsky, C.H. (1989). Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 109, 877-889.
    • (1989) J. Cell Biol. , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 62
    • 0025847137 scopus 로고
    • The extracellular matrix of lip wounds in fetal, neonatal and adult mice
    • Whitby, D.J., and Ferguson, M.W.J. (1991). The extracellular matrix of lip wounds in fetal, neonatal and adult mice. Development 112, 651-668.
    • (1991) Development , vol.112 , pp. 651-668
    • Whitby, D.J.1    Ferguson, M.W.J.2
  • 63
    • 0025813411 scopus 로고
    • Rapid epithelialisation of fetal wounds is associated with the early deposition of tenascin
    • Whitby, D.J., Longaker, M.T., Harrison, M.R., Adzick, N.S., and Ferguson, M.W.J. (1991). Rapid epithelialisation of fetal wounds is associated with the early deposition of tenascin. J. Cell Sci. 99, 583-586.
    • (1991) J. Cell Sci. , vol.99 , pp. 583-586
    • Whitby, D.J.1    Longaker, M.T.2    Harrison, M.R.3    Adzick, N.S.4    Ferguson, M.W.J.5
  • 64
    • 0027033197 scopus 로고
    • Primary structure and function of stromelysin/ transin in cartilage matrix turnover
    • Wilhelm, SM., Wunderlich, D., Maniglia, C.A., Eisen, A.Z., and Goldberg, G.I. (1992). Primary structure and function of stromelysin/ transin in cartilage matrix turnover. Matrix Suppl. 1, 37-44.
    • (1992) Matrix Suppl. , vol.1 , pp. 37-44
    • Wilhelm, S.M.1    Wunderlich, D.2    Maniglia, C.A.3    Eisen, A.Z.4    Goldberg, G.I.5
  • 65
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • Woods, A., and Couchman, J.R. (1992). Protein kinase C involvement in focal adhesion formation. J. Cell Sci. 101, 277-290.
    • (1992) J. Cell Sci. , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 66
    • 0026688638 scopus 로고
    • Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains
    • Zisch, A.H., D'Alessandri, L., Ranscht, B., Falchetto, R., Winterhalter, K.H., and Vaughan, L. (1992). Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains. J. Cell Biol. 119, 203-213.
    • (1992) J. Cell Biol. , vol.119 , pp. 203-213
    • Zisch, A.H.1    D'Alessandri, L.2    Ranscht, B.3    Falchetto, R.4    Winterhalter, K.H.5    Vaughan, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.