메뉴 건너뛰기




Volumn 43, Issue , 2015, Pages 122-128

Fibronectin remodelling: Cell-mediated regulation of the microenvironment

Author keywords

Extracellular matrix; Fibrillogenesis; Fibronectin; Integrin; MMP; Syndecan

Indexed keywords

FIBRONECTIN; GROWTH FACTOR RECEPTOR; HETERODIMER; INTEGRIN; SYNDECAN; MATRIX METALLOPROTEINASE;

EID: 84921822566     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140313     Document Type: Article
Times cited : (18)

References (75)
  • 1
    • 79952340427 scopus 로고    scopus 로고
    • Remodeling and homeostasis of the extracellular matrix: Implications for fibrotic diseases and cancer
    • CrossRef PubMed
    • Cox, T.R. and Erler, J.T. (2011) Remodeling and homeostasis of the extracellular matrix: implications for fibrotic diseases and cancer. Dis. Model. Mech. 4, 165-178 CrossRef PubMed
    • (2011) Dis. Model. Mech. , vol.4 , pp. 165-178
    • Cox, T.R.1    Erler, J.T.2
  • 3
    • 84555179609 scopus 로고    scopus 로고
    • Extracellular matrix degradation and remodeling in development and disease
    • CrossRef PubMed
    • Lu, P., Takai, K., Weaver, V.M. and Werb, Z. (2011) Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb. Perspect. Biol. 3, a005058 CrossRef PubMed
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a005058
    • Lu, P.1    Takai, K.2    Weaver, V.M.3    Werb, Z.4
  • 5
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • CrossRef PubMed
    • Hynes, R.O. (2009) The extracellular matrix: not just pretty fibrils. Science 326, 1216-1219 CrossRef PubMed
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 6
    • 50849143487 scopus 로고    scopus 로고
    • The role of integrin binding sites in fibronectin matrix assembly in vivo
    • CrossRef PubMed
    • Leiss, M., Beckmann, K., Giros, A., Costell, M. and Fassler, R. (2008) The role of integrin binding sites in fibronectin matrix assembly in vivo. Curr. Opin. Cell Biol 20, 502-507 CrossRef PubMed
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 502-507
    • Leiss, M.1    Beckmann, K.2    Giros, A.3    Costell, M.4    Fassler, R.5
  • 7
    • 36448970493 scopus 로고    scopus 로고
    • Synergistic control of cell adhesion by integrins and syndecans
    • CrossRef PubMed
    • Morgan, M.R., Humphries, M.J. and Bass, M.D. (2007) Synergistic control of cell adhesion by integrins and syndecans. Nat. Rev. Mol. Cell Biol. 8, 957-969 CrossRef PubMed
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 957-969
    • Morgan, M.R.1    Humphries, M.J.2    Bass, M.D.3
  • 8
    • 77951458501 scopus 로고    scopus 로고
    • Collagen i matrix turnover is regulated by fibronectin polymerization
    • CrossRef PubMed
    • Shi, F., Harman, J., Fujiwara, K. and Sottile, J. (2010) Collagen I matrix turnover is regulated by fibronectin polymerization. Am. J. Physiol. Cell Physiol. 298, C1265-C1275 CrossRef PubMed
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298 , pp. C1265-C1275
    • Shi, F.1    Harman, J.2    Fujiwara, K.3    Sottile, J.4
  • 9
    • 0037020239 scopus 로고    scopus 로고
    • Polymerization of type i and III collagens is dependent on fibronectin and enhanced by integrins α11β1 and α2β1
    • CrossRef PubMed
    • Velling, T., Risteli, J., Wennerberg, K., Mosher, D.F. and Johansson, S. (2002) Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins α11β1 and α2β1. J. Biol. Chem. 277, 37377-37381 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 37377-37381
    • Velling, T.1    Risteli, J.2    Wennerberg, K.3    Mosher, D.F.4    Johansson, S.5
  • 10
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequences required for assembly of a fibrillar matrix
    • CrossRef PubMed
    • Schwarzbauer, J.E. (1991) Identification of the fibronectin sequences required for assembly of a fibrillar matrix. J. Cell Biol. 113, 1463-1473 CrossRef PubMed
    • (1991) J. Cell Biol. , vol.113 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 11
    • 0033016468 scopus 로고    scopus 로고
    • The compact conformation of fibronectin is determined by intramolecular ionic interactions
    • CrossRef PubMed
    • Johnson, K.J., Sage, H., Briscoe, G. and Erickson, H.P. (1999) The compact conformation of fibronectin is determined by intramolecular ionic interactions. J. Biol. Chem. 274, 15473-15479 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 15473-15479
    • Johnson, K.J.1    Sage, H.2    Briscoe, G.3    Erickson, H.P.4
  • 12
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
    • CrossRef PubMed
    • Geiger, B., Bershadsky, A., Pankov, R. and Yamada, K.M. (2001) Transmembrane crosstalk between the extracellular matrix and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 2, 793-805 CrossRef PubMed
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 13
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of α5β1 integrins promotes early fibronectin fibrillogenesis
    • CrossRef PubMed
    • Pankov, R., Cukierman, E., Katz, B.Z., Matsumoto, K., Lin, D.C., Lin, S., Hahn, C. and Yamada, K.M. (2000) Integrin dynamics and matrix assembly: tensin-dependent translocation of α5β1 integrins promotes early fibronectin fibrillogenesis. J. Cell Biol. 148, 1075-1090 CrossRef PubMed
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5    Lin, S.6    Hahn, C.7    Yamada, K.M.8
  • 14
    • 0031036225 scopus 로고    scopus 로고
    • Cryptic self-association sites in type III modules of fibronectin
    • CrossRef PubMed
    • Ingham, K.C., Brew, S.A., Huff, S. and Litvinovich, S.V. (1997) Cryptic self-association sites in type III modules of fibronectin. J. Biol. Chem. 272, 1718-1724 CrossRef PubMed
    • (1997) J. Biol. Chem. , vol.272 , pp. 1718-1724
    • Ingham, K.C.1    Brew, S.A.2    Huff, S.3    Litvinovich, S.V.4
  • 15
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • CrossRef PubMed
    • Wu, C., Keivens, V.M., O'Toole, T.E., McDonald, J.A. and Ginsberg, M.H. (1995) Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 83, 715-724 CrossRef PubMed
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 16
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • CrossRef PubMed
    • Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A.M. and Burridge, K. (1998) Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551 CrossRef PubMed
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 17
    • 23944441761 scopus 로고    scopus 로고
    • Fibronectin fragmentation promotes α4β1 integrin-mediated contraction of a fibrin-fibronectin provisional matrix
    • CrossRef PubMed
    • Valenick, L.V., Hsia, H.C. and Schwarzbauer, J.E. (2005) Fibronectin fragmentation promotes α4β1 integrin-mediated contraction of a fibrin-fibronectin provisional matrix. Exp. Cell Res. 309, 48-55 CrossRef PubMed
    • (2005) Exp. Cell Res. , vol.309 , pp. 48-55
    • Valenick, L.V.1    Hsia, H.C.2    Schwarzbauer, J.E.3
  • 18
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs of fibronectin matrix assembly
    • CrossRef PubMed
    • Wierzbicka-Patynowski, I. and Schwarzbauer, J.E. (2003) The ins and outs of fibronectin matrix assembly. J. Cell Sci. 116, 3269-3276 CrossRef PubMed
    • (2003) J. Cell Sci. , vol.116 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 19
    • 0030907334 scopus 로고    scopus 로고
    • N-terminal type i modules required for fibronectin binding to fibroblasts and to fibronectin's III1 module
    • PubMed
    • Sottile, J. and Mosher, D.F. (1997) N-terminal type I modules required for fibronectin binding to fibroblasts and to fibronectin's III1 module. Biochem. J. 323, 51-60 PubMed
    • (1997) Biochem. J. , vol.323 , pp. 51-60
    • Sottile, J.1    Mosher, D.F.2
  • 20
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • CrossRef PubMed
    • Mao, Y. and Schwarzbauer, J.E. (2005) Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol. 24, 389-399 CrossRef PubMed
    • (2005) Matrix Biol. , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 21
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • CrossRef PubMed
    • Pierschbacher, M.D. and Ruoslahti, E. (1984) Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc. Natl. Acad. Sci. U.S.A. 81, 5985-5988 CrossRef PubMed
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 5985-5988
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 22
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • PubMed
    • Aota, S., Nomizu, 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 PubMed
    • (1994) J. Biol. Chem. , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 23
    • 0034092910 scopus 로고    scopus 로고
    • A novel RGD-independent fibronectin assembly pathway initiated by α4β1 integrin binding to the alternatively spliced v region
    • PubMed
    • Sechler, J.L., Cumiskey, A.M., Gazzola, D.M. and Schwarzbauer, J.E. (2000) A novel RGD-independent fibronectin assembly pathway initiated by α4β1 integrin binding to the alternatively spliced V region. J. Cell Sci. 113, 1491-1498 PubMed
    • (2000) J. Cell Sci. , vol.113 , pp. 1491-1498
    • Sechler, J.L.1    Cumiskey, A.M.2    Gazzola, D.M.3    Schwarzbauer, J.E.4
  • 26
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • PubMed
    • Zamir, E. and Geiger, B. (2001) Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114, 3583-3590 PubMed.
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 28
    • 70349496205 scopus 로고    scopus 로고
    • Clustering of α5β1 integrins determines adhesion strength whereas αvβ3 and talin enable mechanotransduction
    • CrossRef PubMed
    • Roca-Cusachs, P., Gauthier, N.C., Del Rio, A. and Sheetz, M.P. (2009) Clustering of α5β1 integrins determines adhesion strength whereas αvβ3 and talin enable mechanotransduction. Proc. Natl. Acad. Sci. U.S.A. 106, 16245-16250 CrossRef PubMed
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16245-16250
    • Roca-Cusachs, P.1    Gauthier, N.C.2    Del Rio, A.3    Sheetz, M.P.4
  • 30
    • 0037164867 scopus 로고    scopus 로고
    • The fibronectin-binding integrins α5β1 and αvβ3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis
    • CrossRef PubMed
    • Danen, E.H., Sonneveld, P., Brakebusch, C., Fassler, R. and Sonnenberg, A. (2002) The fibronectin-binding integrins α5β1 and αvβ3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis. J. Cell Biol. 159, 1071-1086 CrossRef PubMed
    • (2002) J. Cell Biol. , vol.159 , pp. 1071-1086
    • Danen, E.H.1    Sonneveld, P.2    Brakebusch, C.3    Fassler, R.4    Sonnenberg, A.5
  • 31
    • 69249235440 scopus 로고    scopus 로고
    • Giving off mixed signals: Distinct functions of α5β1 and αvβ3 integrins in regulating cell behaviour
    • CrossRef PubMed
    • Morgan, M.R., Byron, A., Humphries, M.J. and Bass, M.D. (2009) Giving off mixed signals: distinct functions of α5β1 and αvβ3 integrins in regulating cell behaviour. IUBMB Life 61, 731-738 CrossRef PubMed
    • (2009) IUBMB Life , vol.61 , pp. 731-738
    • Morgan, M.R.1    Byron, A.2    Humphries, M.J.3    Bass, M.D.4
  • 32
    • 3342906957 scopus 로고    scopus 로고
    • PKD1/PKCμ promotes αvβ3 integrin recycling and delivery to nascent focal adhesions
    • CrossRef PubMed
    • Woods, A.J., White, D.P., Caswell, P.T. and Norman, J.C. (2004) PKD1/PKCμ promotes αvβ3 integrin recycling and delivery to nascent focal adhesions. EMBO J. 23, 2531-2543 CrossRef PubMed
    • (2004) EMBO J. , vol.23 , pp. 2531-2543
    • Woods, A.J.1    White, D.P.2    Caswell, P.T.3    Norman, J.C.4
  • 33
    • 0035908956 scopus 로고    scopus 로고
    • PDGF-regulated rab4-dependent recycling of αvβ3 integrin from early endosomes is necessary for cell adhesion and spreading
    • CrossRef PubMed
    • Roberts, M., Barry, S., Woods, A., van der Sluijs, P. and Norman, J. (2001) PDGF-regulated rab4-dependent recycling of αvβ3 integrin from early endosomes is necessary for cell adhesion and spreading. Curr. Biol. 11, 1392-1402 CrossRef PubMed
    • (2001) Curr. Biol. , vol.11 , pp. 1392-1402
    • Roberts, M.1    Barry, S.2    Woods, A.3    Van Der Sluijs, P.4    Norman, J.5
  • 34
    • 34248226275 scopus 로고    scopus 로고
    • αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration
    • CrossRef PubMed
    • White, D.P., Caswell, P.T. and Norman, J.C. (2007) αvβ3 and α5β1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration. J. Cell Biol. 177, 515-525 CrossRef PubMed
    • (2007) J. Cell Biol. , vol.177 , pp. 515-525
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 35
    • 70549101138 scopus 로고    scopus 로고
    • Integrins: Masters and slaves of endocytic transport
    • CrossRef PubMed
    • Caswell, P.T., Vadrevu, S. and Norman, J.C. (2009) Integrins: masters and slaves of endocytic transport. Nat. Rev. Mol. Cell Biol. 10, 843-853 CrossRef PubMed
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 843-853
    • Caswell, P.T.1    Vadrevu, S.2    Norman, J.C.3
  • 36
    • 53749092962 scopus 로고    scopus 로고
    • Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments
    • CrossRef PubMed
    • Caswell, P.T., Chan, M., Lindsay, A.J., McCaffrey, M.W., Boettiger, D. and Norman, J.C. (2008) Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments. J. Cell Biol. 183, 143-155 CrossRef PubMed
    • (2008) J. Cell Biol. , vol.183 , pp. 143-155
    • Caswell, P.T.1    Chan, M.2    Lindsay, A.J.3    McCaffrey, M.W.4    Boettiger, D.5    Norman, J.C.6
  • 37
    • 84875259429 scopus 로고    scopus 로고
    • Syndecan-4 phosphorylation is a control point for integrin recycling
    • CrossRef PubMed
    • Morgan, M.R., Hamidi, H., Bass, M.D., Warwood, S., Ballestrem, C. and Humphries, M.J. (2013) Syndecan-4 phosphorylation is a control point for integrin recycling. Dev. Cell 24, 472-485 CrossRef PubMed
    • (2013) Dev. Cell , vol.24 , pp. 472-485
    • Morgan, M.R.1    Hamidi, H.2    Bass, M.D.3    Warwood, S.4    Ballestrem, C.5    Humphries, M.J.6
  • 38
    • 84866038353 scopus 로고    scopus 로고
    • PKD controls αvβ3 integrin recycling and tumor cell invasive migration through its substrate Rabaptin-5
    • CrossRef PubMed
    • Christoforides, C., Rainero, E., Brown, K.K., Norman, J.C. and Toker, A. (2012) PKD controls αvβ3 integrin recycling and tumor cell invasive migration through its substrate Rabaptin-5. Dev. Cell 23, 560-572 CrossRef PubMed
    • (2012) Dev. Cell , vol.23 , pp. 560-572
    • Christoforides, C.1    Rainero, E.2    Brown, K.K.3    Norman, J.C.4    Toker, A.5
  • 40
    • 65749084249 scopus 로고    scopus 로고
    • VEGFR1 (Flt1) regulates Rab4 recycling to control fibronectin polymerization and endothelial vessel branching
    • CrossRef PubMed
    • Jones, M.C., Caswell, P.T., Moran-Jones, K., Roberts, M., Barry, S., Gampel, A., Mellor, H. and Norman, J. (2009) VEGFR1 (Flt1) regulates Rab4 recycling to control fibronectin polymerization and endothelial vessel branching. Traffic 10, 754-766 CrossRef PubMed
    • (2009) Traffic , vol.10 , pp. 754-766
    • Jones, M.C.1    Caswell, P.T.2    Moran-Jones, K.3    Roberts, M.4    Barry, S.5    Gampel, A.6    Mellor, H.7    Norman, J.8
  • 42
    • 72449124139 scopus 로고    scopus 로고
    • Interplay between cell adhesion and growth factor receptors: From the plasma membrane to the endosomes
    • CrossRef PubMed
    • Ivaska, J. and Heino, J. (2009) Interplay between cell adhesion and growth factor receptors: from the plasma membrane to the endosomes. Cell Tissue Res. 339, 111-120 CrossRef PubMed
    • (2009) Cell Tissue Res. , vol.339 , pp. 111-120
    • Ivaska, J.1    Heino, J.2
  • 43
    • 33749676409 scopus 로고    scopus 로고
    • Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: Enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism
    • CrossRef PubMed
    • Wijelath, E.S., Rahman, S., Namekata, M., Murray, J., Nishimura, T., Mostafavi-Pour, Z., Patel, Y., Suda, Y., Humphries, M.J. and Sobel, M. (2006) Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism. Circ. Res. 99, 853-860 CrossRef PubMed
    • (2006) Circ. Res. , vol.99 , pp. 853-860
    • Wijelath, E.S.1    Rahman, S.2    Namekata, M.3    Murray, J.4    Nishimura, T.5    Mostafavi-Pour, Z.6    Patel, Y.7    Suda, Y.8    Humphries, M.J.9    Sobel, M.10
  • 44
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
    • CrossRef PubMed
    • Martino, M.M. and Hubbell, J.A. (2010) The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J. 24, 4711-4721 CrossRef PubMed
    • (2010) FASEB J. , vol.24 , pp. 4711-4721
    • Martino, M.M.1    Hubbell, J.A.2
  • 45
    • 49649095969 scopus 로고    scopus 로고
    • Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover
    • CrossRef PubMed
    • Shi, F. and Sottile, J. (2008) Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover. J. Cell Sci. 121, 2360-2371 CrossRef PubMed
    • (2008) J. Cell Sci. , vol.121 , pp. 2360-2371
    • Shi, F.1    Sottile, J.2
  • 46
    • 12844269776 scopus 로고    scopus 로고
    • Fibronectin matrix turnover occurs through a caveolin-1-dependent process
    • CrossRef PubMed
    • Sottile, J. and Chandler, J. (2005) Fibronectin matrix turnover occurs through a caveolin-1-dependent process. Mol. Biol. Cell 16, 757-768 CrossRef PubMed
    • (2005) Mol. Biol. Cell , vol.16 , pp. 757-768
    • Sottile, J.1    Chandler, J.2
  • 47
    • 77954902702 scopus 로고    scopus 로고
    • Ubiquitination of α5β1 integrin controls fibroblast migration through lysosomal degradation of fibronectin-integrin complexes
    • CrossRef PubMed
    • Lobert, V.H., Brech, A., Pedersen, N.M., Wesche, J., Oppelt, A., Malerød, L. and Stenmark, H. (2010) Ubiquitination of α5β1 integrin controls fibroblast migration through lysosomal degradation of fibronectin-integrin complexes. Dev. Cell 19, 148-159 CrossRef PubMed
    • (2010) Dev. Cell , vol.19 , pp. 148-159
    • Lobert, V.H.1    Brech, A.2    Pedersen, N.M.3    Wesche, J.4    Oppelt, A.5    Malerød, L.6    Stenmark, H.7
  • 49
    • 80052821897 scopus 로고    scopus 로고
    • Cortactin controls cell motility and lamellipodial dynamics by regulating ECM secretion
    • CrossRef PubMed
    • Sung, B.H., Zhu, X., Kaverina, I. and Weaver, A.M. (2011) Cortactin controls cell motility and lamellipodial dynamics by regulating ECM secretion. Curr. Biol. 21, 1460-1469 CrossRef PubMed
    • (2011) Curr. Biol. , vol.21 , pp. 1460-1469
    • Sung, B.H.1    Zhu, X.2    Kaverina, I.3    Weaver, A.M.4
  • 50
    • 84864277708 scopus 로고    scopus 로고
    • Syndecans play dual roles as cell adhesion receptors and docking receptors
    • CrossRef PubMed
    • Kwon, M.-J., Jang, B., Yi, J.Y., Han, I.-O. and Oh, E.S. (2012) Syndecans play dual roles as cell adhesion receptors and docking receptors. FEBS Lett. 586, 2207-2211 CrossRef PubMed
    • (2012) FEBS Lett. , vol.586 , pp. 2207-2211
    • Kwon, M.-J.1    Jang, B.2    Yi, J.Y.3    Han, I.-O.4    Oh, E.S.5
  • 52
    • 0034003019 scopus 로고    scopus 로고
    • Control of extracellular matrix assembly by syndecan-2 proteoglycan
    • PubMed
    • Klass, C.M., Couchman, J.R. and Woods, A. (2000) Control of extracellular matrix assembly by syndecan-2 proteoglycan. J. Cell Sci. 113, 493-506 PubMed
    • (2000) J. Cell Sci. , vol.113 , pp. 493-506
    • Klass, C.M.1    Couchman, J.R.2    Woods, A.3
  • 53
    • 84891414527 scopus 로고    scopus 로고
    • Epithelial-mesenchymal status influences how cells deposit fibrillin microfibrils
    • CrossRef PubMed
    • Baldwin, A.K., Cain, S.A., Lennon, R., Godwin, A., Merry, C.L.R. and Kielty, C.M. (2014) Epithelial-mesenchymal status influences how cells deposit fibrillin microfibrils. J. Cell Sci. 127, 158-171 CrossRef PubMed
    • (2014) J. Cell Sci. , vol.127 , pp. 158-171
    • Baldwin, A.K.1    Cain, S.A.2    Lennon, R.3    Godwin, A.4    Merry, C.L.R.5    Kielty, C.M.6
  • 54
    • 70350029643 scopus 로고    scopus 로고
    • Extra-embryonic syndecan 2 regulates organ primordia migration and fibrillogenesis throughout the zebrafish embryo
    • CrossRef PubMed
    • Arrington, C.B. and Yost, H.J. (2009) Extra-embryonic syndecan 2 regulates organ primordia migration and fibrillogenesis throughout the zebrafish embryo. Development 136, 3143-3152 CrossRef PubMed
    • (2009) Development , vol.136 , pp. 3143-3152
    • Arrington, C.B.1    Yost, H.J.2
  • 55
    • 45349086241 scopus 로고    scopus 로고
    • P190RhoGAP is the convergence point of adhesion signals from α5β1 integrin and syndecan-4
    • CrossRef PubMed
    • Bass, M.D., Morgan, M.R., Roach, K.A., Settleman, J., Goryachev, A.B. and Humphries, M.J. (2008) p190RhoGAP is the convergence point of adhesion signals from α5β1 integrin and syndecan-4. J. Cell Biol. 181, 1013-1026 CrossRef PubMed
    • (2008) J. Cell Biol. , vol.181 , pp. 1013-1026
    • Bass, M.D.1    Morgan, M.R.2    Roach, K.A.3    Settleman, J.4    Goryachev, A.B.5    Humphries, M.J.6
  • 56
    • 33746918654 scopus 로고    scopus 로고
    • PKCβ-dependent activation of RhoA by syndecan-4 during focal adhesion formation
    • CrossRef PubMed
    • Dovas, A., Yoneda, A. and Couchman, J.R. (2006) PKCβ-dependent activation of RhoA by syndecan-4 during focal adhesion formation. J. Cell Sci. 119, 2837-2846 CrossRef PubMed
    • (2006) J. Cell Sci. , vol.119 , pp. 2837-2846
    • Dovas, A.1    Yoneda, A.2    Couchman, J.R.3
  • 57
    • 65649087873 scopus 로고    scopus 로고
    • A fresh prospect of extracellular matrix hydrolytic enzymes and their substrates
    • CrossRef PubMed
    • Roycik, M.D., Fang, X. and Sang, Q.X. (2009) A fresh prospect of extracellular matrix hydrolytic enzymes and their substrates. Curr. Pharm. Des. 15, 1295-1308 CrossRef PubMed
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 1295-1308
    • Roycik, M.D.1    Fang, X.2    Sang, Q.X.3
  • 58
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • CrossRef PubMed
    • Nagase, H., Visse, R. and Murphy, G. (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 69, 562-573 CrossRef PubMed
    • (2006) Cardiovasc. Res. , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 59
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • CrossRef PubMed
    • Andreasen, P.A., Egelund, R. and Petersen, H.H. (2000) The plasminogen activation system in tumor growth, invasion, and metastasis. Cell. Mol. Life Sci. 57, 25-40 CrossRef PubMed
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 60
    • 33748683743 scopus 로고    scopus 로고
    • Regulation, function and clinical significance of heparanase in cancer metastasis and angiogenesis
    • CrossRef PubMed
    • Ilan, N., Elkin, M. and Vlodavsky, I. (2006) Regulation, function and clinical significance of heparanase in cancer metastasis and angiogenesis. Int. J. Biochem. Cell Biol. 38, 2018-2039 CrossRef PubMed
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 2018-2039
    • Ilan, N.1    Elkin, M.2    Vlodavsky, I.3
  • 61
    • 80255126187 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase regulates fibronectin assembly to promote cell motility
    • CrossRef PubMed
    • Takino, T., Nagao, R., Manabe, R.-i., Domoto, T., Sekiguchi, K. and Sato, H. (2011) Membrane-type 1 matrix metalloproteinase regulates fibronectin assembly to promote cell motility. FEBS Lett. 585, 3378-3384 CrossRef PubMed
    • (2011) FEBS Lett. , vol.585 , pp. 3378-3384
    • Takino, T.1    Nagao, R.2    Manabe, R.-I.3    Domoto, T.4    Sekiguchi, K.5    Sato, H.6
  • 62
    • 84856840530 scopus 로고    scopus 로고
    • MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin
    • CrossRef PubMed
    • Shi, F. and Sottile, J. (2011) MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin. J. Cell Sci. 124, 4039-4050 CrossRef PubMed
    • (2011) J. Cell Sci. , vol.124 , pp. 4039-4050
    • Shi, F.1    Sottile, J.2
  • 63
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • CrossRef PubMed
    • Sottile, J. and Hocking, D.C. (2002) Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol. Biol. Cell 13, 3546-3559 CrossRef PubMed
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3546-3559
    • Sottile, J.1    Hocking, D.C.2
  • 65
    • 0037064589 scopus 로고    scopus 로고
    • ECM regulates MT1-MMP localization with beta1 or alphavbeta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells
    • Galvez, B. G., Matias-Roman, S., Yanez-Mo, M., Sanchez-Madrid, F. and Arroyo, A. G. (2002) ECM regulates MT1-MMP localization with beta1 or alphavbeta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells. J. Cell Biol. 159, 509-521
    • (2002) J. Cell Biol. , vol.159 , pp. 509-521
    • Galvez, B.G.1    Matias-Roman, S.2    Yanez-Mo, M.3    Sanchez-Madrid, F.4    Arroyo, A.G.5
  • 66
    • 0035861560 scopus 로고    scopus 로고
    • Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway
    • Morrison, C. J., Butler, G. S., Bigg, H. F., Roberts, C. R., Soloway, P. D. and Overall, C. M. (2001) Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway. J. Biol. Chem. 276, 47402-47410
    • (2001) J. Biol. Chem. , vol.276 , pp. 47402-47410
    • Morrison, C.J.1    Butler, G.S.2    Bigg, H.F.3    Roberts, C.R.4    Soloway, P.D.5    Overall, C.M.6
  • 67
    • 0035864376 scopus 로고    scopus 로고
    • MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells
    • Deryugina, E. I., Ratnikov, B., Monosov, E., Postnova, T. I., DiScipio, R., Smith, J. W. and Strongin, A. Y. (2001) MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells. Exp. Cell Res. 263, 209-223
    • (2001) Exp. Cell Res. , vol.263 , pp. 209-223
    • Deryugina, E.I.1    Ratnikov, B.2    Monosov, E.3    Postnova, T.I.4    Discipio, R.5    Smith, J.W.6    Strongin, A.Y.7
  • 68
    • 27144557959 scopus 로고    scopus 로고
    • Dissecting the role of matrix metalloproteinases (MMP) and integrin alpha(v)beta3 in angiogenesis in vitro: Absence of hemopexin C domain bioactivity, but membrane-Type 1-MMP and alpha(v)beta3 are critical
    • Nisato, R. E., Hosseini, G., Sirrenberg, C., Butler, G. S., Crabbe, T., Docherty, A. J., Wiesner, M., Murphy, G., Overall, C. M., Goodman, S. L. and Pepper, M. S. (2005) Dissecting the role of matrix metalloproteinases (MMP) and integrin alpha(v)beta3 in angiogenesis in vitro: absence of hemopexin C domain bioactivity, but membrane-Type 1-MMP and alpha(v)beta3 are critical. Cancer Res. 65, 9377-9387
    • (2005) Cancer Res. , vol.65 , pp. 9377-9387
    • Nisato, R.E.1    Hosseini, G.2    Sirrenberg, C.3    Butler, G.S.4    Crabbe, T.5    Docherty, A.J.6    Wiesner, M.7    Murphy, G.8    Overall, C.M.9    Goodman, S.L.10    Pepper, M.S.11
  • 69
    • 72949116366 scopus 로고    scopus 로고
    • Regulation of cell signalling by uPAR
    • CrossRef PubMed
    • Smith, H.W. and Marshall, C.J. (2010) Regulation of cell signalling by uPAR. Nat. Rev. Mol. Cell Biol. 11, 23-36 CrossRef PubMed
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 23-36
    • Smith, H.W.1    Marshall, C.J.2
  • 71
    • 33646920445 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor regulates a novel pathway of fibronectin matrix assembly requiring Src-dependent transactivation of epidermalgrowth factor receptor
    • CrossRef PubMed
    • Monaghan-Benson, E. and McKeown-Longo, P.J. (2006) Urokinase-type plasminogen activator receptor regulates a novel pathway of fibronectin matrix assembly requiring Src-dependent transactivation of epidermalgrowth factor receptor. J. Biol. Chem. 281, 9450-9459 CrossRef PubMed
    • (2006) J. Biol. Chem. , vol.281 , pp. 9450-9459
    • Monaghan-Benson, E.1    McKeown-Longo, P.J.2
  • 72
    • 0347723887 scopus 로고    scopus 로고
    • The receptor for urokinase-type plasminogen activator regulates fibronectin matrix assembly in human skin fibroblasts
    • CrossRef PubMed
    • Monaghan, E., Gueorguiev, V., Wilkins-Port, C. and McKeown-Longo, P.J. (2004) The receptor for urokinase-type plasminogen activator regulates fibronectin matrix assembly in human skin fibroblasts. J. Biol. Chem. 279, 1400-1407 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 1400-1407
    • Monaghan, E.1    Gueorguiev, V.2    Wilkins-Port, C.3    McKeown-Longo, P.J.4
  • 73
    • 33646163227 scopus 로고    scopus 로고
    • Coordinate regulation of fibronectin matrix assembly by the plasminogen activator system and vitronectin in human osteosarcoma cells
    • CrossRef PubMed
    • Vial, D., Monaghan-Benson, E. and McKeown-Longo, P.J. (2006) Coordinate regulation of fibronectin matrix assembly by the plasminogen activator system and vitronectin in human osteosarcoma cells. Cancer Cell Int. 6, 8 CrossRef PubMed
    • (2006) Cancer Cell Int. , vol.6 , pp. 8
    • Vial, D.1    Monaghan-Benson, E.2    McKeown-Longo, P.J.3
  • 74
    • 78649737455 scopus 로고    scopus 로고
    • The extracellular matrix at a glance
    • CrossRef PubMed
    • Frantz, C., Stewart, K.M. and Weaver, V.M. (2010) The extracellular matrix at a glance. J. Cell Sci. 123, 4195-4200 CrossRef PubMed
    • (2010) J. Cell Sci. , vol.123 , pp. 4195-4200
    • Frantz, C.1    Stewart, K.M.2    Weaver, V.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.