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Volumn 307, Issue 2, 2005, Pages 342-353

Subconfluent endothelial cells form podosomes downstream of cytokine and RhoGTPase signaling

Author keywords

Cell migration; Cytokines; Endothelial cells; Matrix degradation; Matrix metalloproteases; Podosomes; RhoGTPases

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; MATRIX METALLOPROTEINASE; PROTEIN TYROSINE KINASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; TUMOR NECROSIS FACTOR ALPHA; VASCULOTROPIN;

EID: 20444391054     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.03.035     Document Type: Article
Times cited : (113)

References (33)
  • 1
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: Adhesion hot-spots of invasive cells
    • S. Linder, and M. Aepfelbacher Podosomes: adhesion hot-spots of invasive cells Trends Cell Biol. 13 2003 376 385
    • (2003) Trends Cell Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 2
    • 3543114271 scopus 로고    scopus 로고
    • Foot and mouth: Podosomes, invadopodia and circular dorsal ruffles
    • R. Buccione, J.D. Orth, and M.A. McNiven Foot and mouth: podosomes, invadopodia and circular dorsal ruffles Nat. Rev., Mol. Cell Biol. 5 2004 647 657
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.5 , pp. 647-657
    • Buccione, R.1    Orth, J.D.2    McNiven, M.A.3
  • 3
    • 0025844889 scopus 로고
    • Myofibrillar and cytoskeletal assembly in neonatal rat cardiac myocytes cultured on laminin and collagen
    • L.L. Hilenski, L. Terracio, and T.K. Borg Myofibrillar and cytoskeletal assembly in neonatal rat cardiac myocytes cultured on laminin and collagen Cell Tissue Res. 264 1991 577 587
    • (1991) Cell Tissue Res. , vol.264 , pp. 577-587
    • Hilenski, L.L.1    Terracio, L.2    Borg, T.K.3
  • 5
    • 0141669167 scopus 로고    scopus 로고
    • Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA
    • V. Moreau, F. Tatin, C. Varon, and E. Genot Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA Mol. Cell. Biol. 23 2003 6809 6822
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6809-6822
    • Moreau, V.1    Tatin, F.2    Varon, C.3    Genot, E.4
  • 6
    • 0034447622 scopus 로고    scopus 로고
    • Integrating the VEGF signals leading to actin-based motility in vascular endothelial cells
    • S. Rousseau, F. Houle, and J. Huot Integrating the VEGF signals leading to actin-based motility in vascular endothelial cells Trends Cardiovasc. Med. 10 2000 321 327
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 321-327
    • Rousseau, S.1    Houle, F.2    Huot, J.3
  • 10
    • 1242296871 scopus 로고    scopus 로고
    • Rho activity critically and selectively regulates endothelial cell organization during angiogenesis
    • M.V. Hoang, M.C. Whelan, and D.R. Senger Rho activity critically and selectively regulates endothelial cell organization during angiogenesis Proc. Natl. Acad. Sci. U. S. A. 101 2004 1874 1879
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1874-1879
    • Hoang, M.V.1    Whelan, M.C.2    Senger, D.R.3
  • 11
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • A.J. Ridley Rho GTPases and cell migration J. Cell. Sci. 114 2001 2713 2722
    • (2001) J. Cell. Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 12
    • 0042344706 scopus 로고    scopus 로고
    • Rho GTPases and the regulation of endothelial permeability
    • B. Wojciak-Stothard, and A.J. Ridley Rho GTPases and the regulation of endothelial permeability Vasc. Pharmacol. 39 2002 187 199
    • (2002) Vasc. Pharmacol. , vol.39 , pp. 187-199
    • Wojciak-Stothard, B.1    Ridley, A.J.2
  • 13
    • 2642615752 scopus 로고    scopus 로고
    • Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endothelial cells
    • B. Wojciak-Stothard, A. Entwistle, R. Garg, and A.J. Ridley Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endothelial cells J. Cell. Physiol. 176 1998 150 165
    • (1998) J. Cell. Physiol. , vol.176 , pp. 150-165
    • Wojciak-Stothard, B.1    Entwistle, A.2    Garg, R.3    Ridley, A.J.4
  • 15
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • M. Raftopoulou, and A. Hall Cell migration: Rho GTPases lead the way Dev. Biol. 265 2004 23 32
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 16
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • H.N. Higgs, and T.D. Pollard Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins Annu. Rev. Biochem. 70 2001 649 676
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 17
    • 0042324235 scopus 로고    scopus 로고
    • Cytotoxic necrotizing factor 1 of Escherichia coli stimulates Rho/Rho-kinase-dependent myosin light-chain phosphorylation without inactivating myosin light-chain phosphatase in endothelial cells
    • M. Essler, S. Linder, B. Schell, K. Hufner, A. Wiedemann, K. Randhahn, J.M. Staddon, and M. Aepfelbacher Cytotoxic necrotizing factor 1 of Escherichia coli stimulates Rho/Rho-kinase-dependent myosin light-chain phosphorylation without inactivating myosin light-chain phosphatase in endothelial cells Infect. Immun. 71 2003 5188 5193
    • (2003) Infect. Immun. , vol.71 , pp. 5188-5193
    • Essler, M.1    Linder, S.2    Schell, B.3    Hufner, K.4    Wiedemann, A.5    Randhahn, K.6    Staddon, J.M.7    Aepfelbacher, M.8
  • 18
    • 0009720961 scopus 로고
    • An in vitro cell invasion assay: Determination of cell surface proteolytic activity that degrades extracellular matrix
    • W.T. Chen, Y. Yeh, and H. Nakahara An in vitro cell invasion assay: Determination of cell surface proteolytic activity that degrades extracellular matrix J. Tissue Cult. Methods 16 1994 177 181
    • (1994) J. Tissue Cult. Methods , vol.16 , pp. 177-181
    • Chen, W.T.1    Yeh, Y.2    Nakahara, H.3
  • 19
    • 0037070640 scopus 로고    scopus 로고
    • The acidic regions of WASp and N-WASP can synergize with Cdc42Hs and Rac1 to induce filopodia and lamellipodia
    • K. Hüfner, B. Schell, M. Aepfelbacher, and S. Linder The acidic regions of WASp and N-WASP can synergize with Cdc42Hs and Rac1 to induce filopodia and lamellipodia FEBS Lett. 514 2002 168 174
    • (2002) FEBS Lett. , vol.514 , pp. 168-174
    • Hüfner, K.1    Schell, B.2    Aepfelbacher, M.3    Linder, S.4
  • 20
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages
    • S. Linder, D. Nelson, M. Weiss, and M. Aepfelbacher Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages Proc. Natl. Acad. Sci. U. S. A. 96 1999 9648 9653
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9648-9653
    • Linder, S.1    Nelson, D.2    Weiss, M.3    Aepfelbacher, M.4
  • 21
    • 0033199252 scopus 로고    scopus 로고
    • Dichotomous regulation of myosin phosphorylation and shape change by Rho-kinase and calcium in intact human platelets
    • M. Bauer, M. Retzer, J.I. Wilde, P. Maschberger, M. Essler, M. Aepfelbacher, S.P. Watson, and W. Siess Dichotomous regulation of myosin phosphorylation and shape change by Rho-kinase and calcium in intact human platelets Blood 94 1999 1665 1672
    • (1999) Blood , vol.94 , pp. 1665-1672
    • Bauer, M.1    Retzer, M.2    Wilde, J.I.3    Maschberger, P.4    Essler, M.5    Aepfelbacher, M.6    Watson, S.P.7    Siess, W.8
  • 22
    • 0031694935 scopus 로고    scopus 로고
    • Integrin signaling: Tyrosine phosphorylation events in focal adhesions
    • K. Vuori Integrin signaling: tyrosine phosphorylation events in focal adhesions J. Membr. Biol. 165 1998 191 199
    • (1998) J. Membr. Biol. , vol.165 , pp. 191-199
    • Vuori, K.1
  • 23
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • G. Tarone, D. Cirillo, F.G. Giancotti, P.M. Comoglio, and P.C. Marchisio Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes Exp. Cell Res. 159 1985 141 157
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 25
    • 0037109144 scopus 로고    scopus 로고
    • Engagement of glycoprotein IIb/IIIa (alpha(IIb)beta3) on platelets upregulates CD40L and triggers CD40L-dependent matrix degradation by endothelial cells
    • A.E. May, T. Kalsch, S. Massberg, Y. Herouy, R. Schmidt, and M. Gawaz Engagement of glycoprotein IIb/IIIa (alpha(IIb)beta3) on platelets upregulates CD40L and triggers CD40L-dependent matrix degradation by endothelial cells Circulation 106 2002 2111 2117
    • (2002) Circulation , vol.106 , pp. 2111-2117
    • May, A.E.1    Kalsch, T.2    Massberg, S.3    Herouy, Y.4    Schmidt, R.5    Gawaz, M.6
  • 26
    • 0030791315 scopus 로고    scopus 로고
    • Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion
    • H. Nakahara, L. Howard, E.W. Thompson, H. Sato, M. Seiki, Y. Yeh, and W.T. Chen Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion Proc. Natl. Acad. Sci. U. S. A. 94 1997 7959 7964
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7959-7964
    • Nakahara, H.1    Howard, L.2    Thompson, E.W.3    Sato, H.4    Seiki, M.5    Yeh, Y.6    Chen, W.T.7
  • 27
    • 0033393771 scopus 로고    scopus 로고
    • Selective requirement for Src kinases during VEGF-induced angiogenesis and vascular permeability
    • B.P. Eliceiri, R. Paul, P.L. Schwartzberg, J.D. Hood, J. Leng, and D.A. Cheresh Selective requirement for Src kinases during VEGF-induced angiogenesis and vascular permeability Mol. Cell 4 1999 915 924
    • (1999) Mol. Cell , vol.4 , pp. 915-924
    • Eliceiri, B.P.1    Paul, R.2    Schwartzberg, P.L.3    Hood, J.D.4    Leng, J.5    Cheresh, D.A.6
  • 28
    • 0035242371 scopus 로고    scopus 로고
    • VEGF-induced activation of phosphoinositide 3-kinase is dependent on focal adhesion kinase
    • J.H. Qi, and L. Claesson-Welsh VEGF-induced activation of phosphoinositide 3-kinase is dependent on focal adhesion kinase Exp. Cell Res. 263 2001 173 182
    • (2001) Exp. Cell Res. , vol.263 , pp. 173-182
    • Qi, J.H.1    Claesson-Welsh, L.2
  • 31
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • D.C. Edwards, L.C. Sanders, G.M. Bokoch, and G.N. Gill Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics Nat. Cell Biol. 1 1999 253 259
    • (1999) Nat. Cell Biol. , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 32
    • 0033611107 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2
    • T. Sumi, K. Matsumoto, Y. Takai, and T. Nakamura Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2 J. Cell Biol. 147 1999 1519 1532
    • (1999) J. Cell Biol. , vol.147 , pp. 1519-1532
    • Sumi, T.1    Matsumoto, K.2    Takai, Y.3    Nakamura, T.4


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