메뉴 건너뛰기




Volumn 129, Issue 3, 1995, Pages 867-879

Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; COLLAGENASE; GELATINASE; HEPARIN; INTEGRIN; METALLOPROTEINASE; STROMELYSIN;

EID: 0028987190     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.129.3.867     Document Type: Article
Times cited : (369)

References (74)
  • 1
    • 0027230170 scopus 로고
    • Regulation of development and differentiThe Journal of Cell Biology, Volume 129, 1995 ation by the extracellular matrix
    • Adams, J. C., and F. M. Watt. 1993. Regulation of development and differentiThe Journal of Cell Biology, Volume 129, 1995 ation by the extracellular matrix. Development. 117:1183-1198.
    • (1993) Development , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, F.M.2
  • 2
    • 0021278562 scopus 로고
    • Collagenase is a major gene product of induced rabbit synovial fibroblasts
    • Aggeler, J.. S. M. Frisch, and Z. Werb. 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.S.1    Frisch, M.2    Werb, Z.3
  • 4
    • 0000999998 scopus 로고
    • Extracellular matrix degradation
    • E. D. Hay, editor. Plenum Press, New York
    • Alexander, C. M., and Z. Werb. 1991. Extracellular matrix degradation. In Cell Biology of Extracellular Matrix, 2nd ed. E. D. Hay, editor. Plenum Press, New York. 255-302.
    • (1991) Cell Biology of Extracellular Matrix, 2nd Ed. , pp. 255-302
    • Alexander, C.M.1    Werb, Z.2
  • 5
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota, S., M. Nomizu, and K. M. Yamada. 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    Nomizu, M.2    Yamada, K.M.3
  • 7
    • 0026736007 scopus 로고
    • Expression and ligand-binding function of the integrin α4β1 (VLA-4) on neural-crest-derived tumor cell lines
    • Bednarczyk, J. L., and B. W. McIntyre. 1992. Expression and ligand-binding function of the integrin α4β1 (VLA-4) on neural-crest-derived tumor cell lines. Clin. Exp. Metastasis. 10:281-290.
    • (1992) Clin. Exp. Metastasis , vol.10 , pp. 281-290
    • Bednarczyk, J.L.1    McIntyre, B.W.2
  • 10
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidium thiocyanate phenol chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single step method of RNA isolation by acid guanidium thiocyanate phenol chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 12
    • 0023789470 scopus 로고
    • An adhesive defective BHK cell mutant has cell surface heparan sulfate proteoglycan of altered properties
    • Couchman, J. R., R. Austria, A. Woods, and R. C. Hughes. 1988. An adhesive defective BHK cell mutant has cell surface heparan sulfate proteoglycan of altered properties. J. Cell Physiol. 136:226-236.
    • (1988) J. Cell Physiol. , vol.136 , pp. 226-236
    • Couchman, J.R.1    Austria, R.2    Woods, A.3    Hughes, R.C.4
  • 13
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • Damsky, C. H., and Z. Werb. 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
  • 14
    • 0026762840 scopus 로고
    • Cell surface phosphatidylinositol-anchored heparan sulfate proteoglycan initiates mouse melanoma cell adhesion to a fibronectin-derived, heparin-binding synthetic peptide
    • Drake, S. L., D. J. Klein, D. J. Mickelson, T. R. Oegema, L. T. Furcht, and J. B. McCarthy. 1992. Cell surface phosphatidylinositol-anchored heparan sulfate proteoglycan initiates mouse melanoma cell adhesion to a fibronectin-derived, heparin-binding synthetic peptide. J. Cell Biol. 117:1331-1341.
    • (1992) J. Cell Biol. , vol.117 , pp. 1331-1341
    • Drake, S.L.1    Klein, D.J.2    Mickelson, D.J.3    Oegema, T.R.4    Furcht, L.T.5    McCarthy, J.B.6
  • 15
    • 0024075252 scopus 로고
    • Attachment, spreading and locomotion of avian neural crest cells are mediated by multiple adhesion sites on fibronectin molecules
    • Dufour, S., J.-L. Duband, M. J. Humphries, M. Obara, K. M. Yamada, and J. P. Thiery. 1988. Attachment, spreading and locomotion of avian neural crest cells are mediated by multiple adhesion sites on fibronectin molecules. EMBO (Eur. Mol. Biol. Organ.) J. 7:2661-2671.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 2661-2671
    • Dufour, S.1    Duband, J.-L.2    Humphries, M.J.3    Obara, M.4    Yamada, K.M.5    Thiery, J.P.6
  • 16
    • 0025772150 scopus 로고
    • Complete amino acid sequence of an integrin β subunit (β7) identified in leukocytes
    • Erle, D. J., C. Ruegg, D. Sheppard, and R. Pytela. 1991. Complete amino acid sequence of an integrin β subunit (β7) identified in leukocytes. J. Biol. Chem. 266:11009-11016.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11009-11016
    • Erle, D.J.1    Ruegg, C.2    Sheppard, D.3    Pytela, R.4
  • 17
    • 0025226540 scopus 로고
    • Positive and negative transcriptional elements of the human type IV collagenase gene
    • Frisch, S. M., and J. H. Morisaki. 1990. Positive and negative transcriptional elements of the human type IV collagenase gene. Mol. Cell. Biol. 10: 6524-6532.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6524-6532
    • Frisch, S.M.1    Morisaki, J.H.2
  • 18
    • 0342642931 scopus 로고
    • Coordinate regulation of stromelysin and collagenase genes determined with cDNA probes
    • Frisch, S. M., E. J. Clark, and Z. Werb. 1987. Coordinate regulation of stromelysin and collagenase genes determined with cDNA probes. Proc. Natl. Acad. Sci. USA. 84:2600-2604.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2600-2604
    • Frisch, S.M.1    Clark, E.J.2    Werb, Z.3
  • 19
    • 0027419098 scopus 로고
    • Expression of functional α4β1 integrin by human dermal fibroblasts
    • Gailit, J., M. Pierschbacher, and R. A. Clark. 1993. Expression of functional α4β1 integrin by human dermal fibroblasts. J. Invest. Dermatol. 100: 323-328.
    • (1993) J. Invest. Dermatol. , vol.100 , pp. 323-328
    • Gailit, J.1    Pierschbacher, M.2    Clark, R.A.3
  • 20
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George, E. L., E. N. Georges-Labouessa, R. S. Patel-King, H. Rayburn, and R. O. Hynes. 1994. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 119:1079-1091.
    • (1994) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labouessa, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 21
    • 0028351860 scopus 로고
    • Isolation and partial characterization of a cell-surface heparan sulfate proteoglycan from embryonic rat spinal cord
    • Giuseppetti, J. M., J. B. McCarthy, and P. C. Letourneau. 1994. Isolation and partial characterization of a cell-surface heparan sulfate proteoglycan from embryonic rat spinal cord. J. Neurosci. Res. 37:584-595.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 584-595
    • Giuseppetti, J.M.1    McCarthy, J.B.2    Letourneau, P.C.3
  • 22
    • 0026605281 scopus 로고
    • Degradation of fibronectin and vitronectin in chronic wound fluid: Analysis by cell blotting, immunoblotting, and cell adhesion assays
    • Grinnell, F., C-H. Ho, and A. Wysocki. 1992. Degradation of fibronectin and vitronectin in chronic wound fluid: analysis by cell blotting, immunoblotting, and cell adhesion assays. J. Invest. Dermatol. 98:410-416.
    • (1992) J. Invest. Dermatol. , vol.98 , pp. 410-416
    • Grinnell, F.1    Ho, C.-H.2    Wysocki, A.3
  • 23
    • 0025124607 scopus 로고
    • Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor α4β1
    • Guan, J-L., and R. O. Hynes. 1990. Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor α4β1. Cell. 60:53-61.
    • (1990) Cell , vol.60 , pp. 53-61
    • Guan, J.-L.1    Hynes, R.O.2
  • 24
    • 0026716204 scopus 로고
    • Biology of tumour metastasis
    • Hart, I. A., and A. Saini. 1992. Biology of tumour metastasis. Lancet. 339:1453-1457.
    • (1992) Lancet , vol.339 , pp. 1453-1457
    • Hart, I.A.1    Saini, A.2
  • 25
    • 0025605064 scopus 로고
    • Recognition of the a chain carboxy-terminal heparin binding region of fibronectin involves multiple sites: Two contiguous sequences act independently to promote neural cell adhesion
    • Huagen, P. K., J. B. McCarthy, A. P. Skubitz, L. T. Furcht, and P. C. Letourneau. 1990. Recognition of the A chain carboxy-terminal heparin binding region of fibronectin involves multiple sites: two contiguous sequences act independently to promote neural cell adhesion. J. Cell Biol. 111:2733-2745.
    • (1990) J. Cell Biol. , vol.111 , pp. 2733-2745
    • Huagen, P.K.1    McCarthy, J.B.2    Skubitz, A.P.3    Furcht, L.T.4    Letourneau, P.C.5
  • 27
    • 0022979424 scopus 로고
    • Secretion of metalloproteinases by stimulated capillary endothelial cells
    • Herron, G. S., M. J. Banda, E. J. Clark, and Z. Werb. 1986. Secretion of metalloproteinases by stimulated capillary endothelial cells. J. Biol. Chem. 261:2814-2818.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2814-2818
    • Herron, G.S.1    Banda, M.J.2    Clark, E.J.3    Werb, Z.4
  • 28
    • 0025138983 scopus 로고
    • Cell-type-specific expression of alternatively spliced human fibronectin IIICS mRNAs
    • Hershberger, R. P., and L. A. Culp. 1990. Cell-type-specific expression of alternatively spliced human fibronectin IIICS mRNAs. Mol. Cell. Biol. 10:662-671.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 662-671
    • Hershberger, R.P.1    Culp, L.A.2
  • 30
    • 0022870911 scopus 로고
    • Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion
    • Humphries, M. J., S. Akiyama, A. Komoriya, K. Olden, and K. M. Yamada. 1986 Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion. J. Cell Biol. 103:2637-2647.
    • (1986) J. Cell Biol. , vol.103 , pp. 2637-2647
    • Humphries, M.J.1    Akiyama, S.2    Komoriya, A.3    Olden, K.4    Yamada, K.M.5
  • 31
    • 0023223464 scopus 로고
    • Identification of two distinct regions of the type III connecting segment of human plasma fibronectin that promote cell type-specific adhesion
    • Humphries, M. J., S. Akiyama, A. Komoriya, K. Olden, and K. M. Yamada. 1987. Identification of two distinct regions of the type III connecting segment of human plasma fibronectin that promote cell type-specific adhesion. J. Biol. Chem. 262:6886-6892.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6886-6892
    • Humphries, M.J.1    Akiyama, S.2    Komoriya, A.3    Olden, K.4    Yamada, K.M.5
  • 33
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signal ing in cell adhesion
    • Hynes. R. O. 1992. Integrins: versatility, modulation and signal ing in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 34
    • 0026691731 scopus 로고
    • Coordinate role for cell surface chondroitin sulfate proteoglycan and α4β1 integrin in mediating melanoma cell adhesion to fibronection
    • Iida, J., A. P. Skubitz, L. T. Furcht, E. W. Wayner, and J. B. McCarthy. 1992. Coordinate role for cell surface chondroitin sulfate proteoglycan and α4β1 integrin in mediating melanoma cell adhesion to fibronection. J. Cell Biol. 118:431-444.
    • (1992) J. Cell Biol. , vol.118 , pp. 431-444
    • Iida, J.1    Skubitz, A.P.2    Furcht, L.T.3    Wayner, E.W.4    McCarthy, J.B.5
  • 35
    • 85007658919 scopus 로고
    • Role of cell surface proteoglycans in tumor cell recognition of fibronectin. Trends Glycosci
    • Iida, J., R. P. Milius, T. R. Oegema, L. T. Furcht, and J. B. McCarthy. 1994. Role of cell surface proteoglycans in tumor cell recognition of fibronectin. Trends Glycosci. Glycotechnol. 6:1-16.
    • (1994) Glycotechnol. , vol.6 , pp. 1-16
    • Iida, J.1    Milius, R.P.2    Oegema, T.R.3    Furcht, L.T.4    McCarthy, J.B.5
  • 36
    • 0022102304 scopus 로고
    • Primary structure of human plasma fibronectin: Differential splicing may generate at !east 10 polypeptides from a single gene
    • Kornblihtt, A. R., K. Umezawa, K. Vibe-Pedersen, and F. Baralle. 1985. Primary structure of human plasma fibronectin: differential splicing may generate at !east 10 polypeptides from a single gene. EMBO (Ear. Mol. Biol. Organ.) J. 4:1755-1759.
    • (1985) EMBO (Ear. Mol. Biol. Organ.) J. , vol.4 , pp. 1755-1759
    • Kornblihtt, A.R.1    Umezawa, K.2    Vibe-Pedersen, K.3    Baralle, F.4
  • 37
    • 0026535449 scopus 로고
    • Regulation of fibronectin receptor distribution
    • LaFlamme, S. E., S. K. Akiyama, and K. M. Yamada. 1992. Regulation of fibronectin receptor distribution. J. Cell Biol. 117:437-447.
    • (1992) J. Cell Biol. , vol.117 , pp. 437-447
    • Laflamme, S.E.1    Akiyama, S.K.2    Yamada, K.M.3
  • 38
    • 0023870741 scopus 로고
    • Adhesion of glycosaminoglycan-deficient Chinese hamster ovary cell mutants to fibronectin substrata
    • LeBaron, R G., J. D. Esko, A. Woods, S. Johansson, and M. Hook. 1988. Adhesion of glycosaminoglycan-deficient Chinese hamster ovary cell mutants to fibronectin substrata. J. Cell Biol. 106:945-952.
    • (1988) J. Cell Biol. , vol.106 , pp. 945-952
    • Lebaron, R.G.1    Esko, J.D.2    Woods, A.3    Johansson, S.4    Hook, M.5
  • 40
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta, L. A., P. Steeg, and W. Stetler-Stevenson. 1991. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell. 64. 327-336.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.2    Stetler-Stevenson, W.3
  • 41
    • 0026593295 scopus 로고
    • Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cell and fibroblasts
    • Lories, V., J. J Cassiman, H van der Berghe, and G. David. 1992. Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cell and fibroblasts. J. Biol. Chem. 267:1116-1122.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1116-1122
    • Lories, V.1    Cassiman, J.J.2    Van Der Berghe, H.3    David, G.4
  • 42
    • 0028095114 scopus 로고
    • Competitive binding of vascular cell adhesion molecule-1 and the HepII/IIICS domain of fibronectin to the integrin α4β1
    • Makarem, R., P. Newham, J. A. Askari, L. J. Green, J. Clements, M. Ed-wards, M. J. Humphries, and A. P. Mould. 1994. Competitive binding of vascular cell adhesion molecule-1 and the HepII/IIICS domain of fibronectin to the integrin α4β1. J. Biol. Chem. 269:4005-4011.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4005-4011
    • Makarem, R.1    Newham, P.2    Askari, J.A.3    Green, L.J.4    Clements, J.5    Ed-wards, M.6    Humphries, M.J.7    Mould, A.P.8
  • 43
    • 0023850707 scopus 로고
    • Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities
    • McCarthy, J. B., M. K. Chelberg, D. J. Mickelson, and L. T. Furcht. 1988. Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities. Biochemistry. 27:1380-1388.
    • (1988) Biochemistry , vol.27 , pp. 1380-1388
    • McCarthy, J.B.1    Chelberg, M.K.2    Mickelson, D.J.3    Furcht, L.T.4
  • 44
    • 0025317131 scopus 로고
    • RGD-independent cell adhesion to the carboxyl-terminal heparin-binding fragment of fibronectin involves heparin-dependent and independent activities
    • McCarthy, J. B., A. P. N. Skubitz, Q. Zhao, X-y. Yi, D. J. Mickelson, D. J. Klein, and L. T. Furcht. 1990. RGD-independent cell adhesion to the carboxyl-terminal heparin-binding fragment of fibronectin involves heparin-dependent and independent activities. J. Cell Biol. 110:777-787.
    • (1990) J. Cell Biol. , vol.110 , pp. 777-787
    • McCarthy, J.B.1    Skubitz, A.P.N.2    Zhao, Q.3    Yi, X.-Y.4    Mickelson, D.J.5    Klein, D.J.6    Furcht, L.T.7
  • 45
    • 0023178166 scopus 로고
    • Fibronectin's cell-adhesive domain and an aminoterminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix
    • McDonald, J. A., B. J. Quade, T. J. Broekelmann, R. LaChance, K. Forsman, E. Hasegawa, and S. Akiyama. 1987. Fibronectin's cell-adhesive domain and an aminoterminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix. J. Biol. Chem. 262:2957-2967.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    Lachance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 46
    • 0024312221 scopus 로고
    • Lymphocyte surface antigen L25 is a member of the integrin receptor superfamily
    • McIntyre, B. W., E. L. Evans, and J. L. Bednarczyk. 1989. Lymphocyte surface antigen L25 is a member of the integrin receptor superfamily. J. Biol. Chem. 264:13745-13750.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13745-13750
    • McIntyre, B.W.1    Evans, E.L.2    Bednarczyk, J.L.3
  • 47
    • 0028290661 scopus 로고
    • A candidate molecule for the matrix assembly receptor to the N-terminal 29-kD fragment of fibronectin in chick myoblasts
    • Moon, K-Y, K. S. Shin, W. K. Song, C. H. Chung, D. B. Ha, and M-S. Kang. 1994. A candidate molecule for the matrix assembly receptor to the N-terminal 29-kD fragment of fibronectin in chick myoblasts. J. Biol. Chem. 269:7651-7657.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7651-7657
    • Moon, K.-Y.1    Shin, K.S.2    Song, W.K.3    Chung, C.H.4    Ha, D.B.5    Kang, M.-S.6
  • 48
    • 0025932687 scopus 로고
    • Identification of a novel recognition sequence for the α4β1 in the COOH-terminal heparin-binding domain of fibronectin
    • Mould, A. P., and M. J. Humphries. 1991. Identification of a novel recognition sequence for the α4β1 in the COOH-terminal heparin-binding domain of fibronectin. EMBO (Eur. Mol. Biol. Organ.) J. 10:4089-4095.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 4089-4095
    • Mould, A.P.1    Humphries, M.J.2
  • 49
    • 0025219640 scopus 로고
    • Affinity Chromatographic isolation of the melanoma adhesion receptor for the IIICS region of fibronectin and its identification as the integrin α4β1
    • Mould, A. P., L. A. Wheldon, A. Koriyama, E. A. Wayner, K. M. Yamada, and M. J. Humphries. 1990. Affinity Chromatographic isolation of the melanoma adhesion receptor for the IIICS region of fibronectin and its identification as the integrin α4β1. J. Biol. Chem. 265:4020-4024.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4020-4024
    • Mould, A.P.1    Wheldon, L.A.2    Koriyama, A.3    Wayner, E.A.4    Yamada, K.M.5    Humphries, M.J.6
  • 50
    • 0025907474 scopus 로고
    • The CS5 peptide is a second site in the IIICS region of fibronectin recognized by the integrin α4β1
    • Mould, A. P., A. Komoriya, K. M. Yamada, and M. J. Humphries. 1991. The CS5 peptide is a second site in the IIICS region of fibronectin recognized by the integrin α4β1. J. Biol. Chem. 266:3579-3585.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3579-3585
    • Mould, A.P.1    Komoriya, A.2    Yamada, K.M.3    Humphries, M.J.4
  • 51
    • 0028172398 scopus 로고
    • Cell adhesion and migration mediated by the integrin α4β1 : Effect of fibronectin alternative splicing and the role of ligand affinity
    • Mould, A. P., J. A. Askari, S. E. Craig, A. N. Garratt, J. Clements, and M. J. Humphries. 1994. Cell adhesion and migration mediated by the integrin α4β1 : effect of fibronectin alternative splicing and the role of ligand affinity. J. Biol. Chem. 269:27224-27230.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27224-27230
    • Mould, A.P.1    Askari, J.A.2    Craig, S.E.3    Garratt, A.N.4    Clements, J.5    Humphries, M.J.6
  • 52
    • 0026535397 scopus 로고
    • Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein
    • Nojima, Y., D. M. Rothstein, K. Sugita, S. F. Schlossman, and C. Morimoto. 1992. Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein. J. Exp. Med. 175:1045-1053.
    • (1992) J. Exp. Med. , vol.175 , pp. 1045-1053
    • Nojima, Y.1    Rothstein, D.M.2    Sugita, K.3    Schlossman, S.F.4    Morimoto, C.5
  • 53
    • 0028175008 scopus 로고
    • Expression of the integrin α4β1 in melanoma cells can inhibit the invasive stage of metastasis formation
    • Qian, F., D. L. Vaux, and I. L. Weissman. 1994. Expression of the integrin α4β1 in melanoma cells can inhibit the invasive stage of metastasis formation. Cell. 77:335-347.
    • (1994) Cell , vol.77 , pp. 335-347
    • Qian, F.1    Vaux, D.L.2    Weissman, I.L.3
  • 54
    • 0026642556 scopus 로고
    • Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association
    • Reszka, A. A., Y. Hayashi, and A. F. Horwitz. 1992. Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association. J. Cell Biol. 117:1321-1330.
    • (1992) J. Cell Biol. , vol.117 , pp. 1321-1330
    • Reszka, A.A.1    Hayashi, Y.2    Horwitz, A.F.3
  • 55
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • Romanic, A.M., and J. A. Madri. 1994. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. J. Cell Biol. 125:1165-1178.
    • (1994) J. Cell Biol. , vol.125 , pp. 1165-1178
    • Romanic, A.M.1    Madri, J.A.2
  • 56
    • 0026574125 scopus 로고
    • Role of integrin α4β7/α4βP in lymphocyte adherence to fibronectin and VCAM-I and in homotypic cell clustering
    • Ruegg, C., A. A. Postigo, E. E. Sikorski. E. C. Butcher, R. Pytela, and D. J. Erle. 1992. Role of integrin α4β7/α4βP in lymphocyte adherence to fibronectin and VCAM-I and in homotypic cell clustering. J. Cell Biol. 117:179-189.
    • (1992) J. Cell Biol. , vol.117 , pp. 179-189
    • Ruegg, C.1    Postigo, A.A.2    Sikorski, E.E.3    Butcher, E.C.4    Pytela, R.5    Erle, D.J.6
  • 57
    • 0025064980 scopus 로고
    • Inhibition of lung metastasis by synthesis and recombinant fragments of human fibronectin with functional domains
    • Saiki, I., J. Murata, T. Mukabe, Y. Matsumoto, Y. Ohdate, Y. Kawase, Y. Taguchi, and I. Kato. 1990. Inhibition of lung metastasis by synthesis and recombinant fragments of human fibronectin with functional domains. Jap. J. Cancer Res. 81:1003-1011.
    • (1990) Jap. J. Cancer Res. , vol.81 , pp. 1003-1011
    • Saiki, I.1    Murata, J.2    Mukabe, T.3    Matsumoto, Y.4    Ohdate, Y.5    Kawase, Y.6    Taguchi, Y.7    Kato, I.8
  • 59
    • 0028180647 scopus 로고
    • Activation of the α4β1 integrin through the β1 subunit induces recognition of the RGDS sequence in fibronectin
    • Sanchez-Aparicio, P., C. Dominguez-Jimenez, and A. Garcia-Pardo. 1994. Activation of the α4β1 integrin through the β1 subunit induces recognition of the RGDS sequence in fibronectin. J. Cell Biol. 126:271-279.
    • (1994) J. Cell Biol. , vol.126 , pp. 271-279
    • Sanchez-Aparicio, P.1    Dominguez-Jimenez, C.2    Garcia-Pardo, A.3
  • 60
    • 0026233153 scopus 로고
    • Alternative splicing of fibronection: Three variants, three functions
    • Schwarzbauer, J. E. 1991. Alternative splicing of fibronection: three variants, three functions. Bio Essays. 13:527-533.
    • (1991) Bio Essays , vol.13 , pp. 527-533
    • Schwarzbauer, J.E.1
  • 61
    • 0027142391 scopus 로고
    • Targeted deletion of β1 integrins in F9 embryonal carcinoma cell affects morphological differentiation but not tissue-specific gene expression
    • Stephens, L. E., J. E. Sonne, M, L. Fitzgerald, and C. H. Damsky. 1993. Targeted deletion of β1 integrins in F9 embryonal carcinoma cell affects morphological differentiation but not tissue-specific gene expression. J. Cell Biol. 123:1607-1620.
    • (1993) J. Cell Biol. , vol.123 , pp. 1607-1620
    • Stephens, L.E.1    Sonne, J.E.2    Fitzgerald, M.L.3    Damsky, C.H.4
  • 62
    • 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. M., T. F. Lane, E. H. Sage, and Z. Werb. 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.M.1    Lane, T.F.2    Sage, E.H.3    Werb, Z.4
  • 63
    • 0028339075 scopus 로고
    • The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts
    • Tremble, P., R. Chiquet-Ehrismann, and Z. Werb. 1994. The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts. Mol. Biol. Cell. 5:439-453.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 439-453
    • Tremble, P.1    Chiquet-Ehrismann, R.2    Werb, Z.3
  • 64
    • 0027997899 scopus 로고
    • Using inhibitors of metalloproteinases to treat arthritis
    • Vincenti, M. P., I. M. Clark, and C. E. Brinckerhoff. 1994. Using inhibitors of metalloproteinases to treat arthritis. Arthr. Rheum. 37:1115-1126.
    • (1994) Arthr. Rheum. , vol.37 , pp. 1115-1126
    • Vincenti, M.P.1    Clark, I.M.2    Brinckerhoff, C.E.3
  • 65
    • 0024418764 scopus 로고
    • Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin
    • Wayner, E. A., A. Garcia-Pardo, M. J. Humphries, J. A. McDonald, and W. G. Carter. 1989. Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin. J. Cell Biol. 109:1321-1330.
    • (1989) J. Cell Biol. , vol.109 , pp. 1321-1330
    • Wayner, E.A.1    Garcia-Pardo, A.2    Humphries, M.J.3    McDonald, J.A.4    Carter, W.G.5
  • 66
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., P. M. Tremble, O. Behrendtsen, E. Crowley, and C. H. Damsky. 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.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 67
    • 0027033197 scopus 로고
    • Primary structure and function of stromelysin/transin in cartilage matrix turnover
    • Wilhelm, S. M., D. Wunderlich, C. A. Maniglia, A. Z. Eisen, and G. I. Goldberg. 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
  • 68
    • 0022707292 scopus 로고
    • Adhesion and cytoskeletal organization of fibroblasts in response to fibronectin fragments
    • Woods, A., J. R. Couchman, S. Johansson, and M. Hook. 1986. Adhesion and cytoskeletal organization of fibroblasts in response to fibronectin fragments EMBO (Eur. Mol. Biol. Organ.) J. 5:665-670.
    • (1986) EMBO (Eur. Mol. Biol. Organ.) J. , vol.5 , pp. 665-670
    • Woods, A.1    Couchman, J.R.2    Johansson, S.3    Hook, M.4
  • 69
    • 0027315260 scopus 로고
    • A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation
    • Woods, A., J. B. McCarthy, L. T. Furcht, and J. R. Couchman. 1993. A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation. Mol. Biol. Cell. 4:605-613.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 605-613
    • Woods, A.1    McCarthy, J.B.2    Furcht, L.T.3    Couchman, J.R.4
  • 70
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP 9
    • Wysocki, A., L. Staiano-Coico, and F. Grinnell. 1993. Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP 9. J. Invest. Dermatol. 101:64-68.
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 64-68
    • Wysocki, A.1    Staiano-Coico, L.2    Grinnell, F.3
  • 71
    • 0026699536 scopus 로고
    • Fibronectin fragments in osteoarthritic synovial fluid
    • Xie. D.-L,. R. Meyers, and G. A. Homandberg. 1992. Fibronectin fragments in osteoarthritic synovial fluid. J. Rheumatol 19:1448-1452.
    • (1992) J. Rheumatol , vol.19 , pp. 1448-1452
    • Xie, D.-L.1    Meyers, R.2    Homandberg, G.A.3
  • 72
    • 0025734184 scopus 로고
    • Adhesive recognition sequences
    • Yamada, K. M. 1991. Adhesive recognition sequences J Biol. Chem 266:12809-12812.
    • (1991) J Biol. Chem , vol.266 , pp. 12809-12812
    • Yamada, K.M.1
  • 73
    • 0027371908 scopus 로고
    • Embryonic mesodermal defects in α5 integrin-deficient mice
    • Yang, J. T., H. Rayburn, and R. O. Hynes. 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
  • 74
    • 0028955748 scopus 로고
    • Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development
    • Yang, J. T., H. Rayburn, and R. O. Hynes. 1995. Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development. Development. 121:549-560.
    • (1995) Development , vol.121 , pp. 549-560
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.