메뉴 건너뛰기




Volumn 112, Issue 19, 1999, Pages 3205-3213

Regulation of the RhoA pathway in human endothelial cell spreading on type IV collagen: Role of calcium influx

Author keywords

Actin stress fiber; Angiogenesis; Calcium; RhoA

Indexed keywords

ACTIN; CALCIUM ION; COLLAGEN TYPE 1; COLLAGEN TYPE 4; IONOMYCIN; MEMBRANE PROTEIN; RHO FACTOR; THAPSIGARGIN;

EID: 0032746309     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (66)

References (34)
  • 2
    • 0030932943 scopus 로고    scopus 로고
    • Elementary and global aspects of calcium signalling
    • Berridge, M. J. (1997). Elementary and global aspects of calcium signalling. J. Physiol. 499, 290-306.
    • (1997) J. Physiol. , vol.499 , pp. 290-306
    • Berridge, M.J.1
  • 3
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga, V. M. M., Machesky, L. M., Hall, A. and Hotchin, N. A. (1997). The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137, 1421-1431.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 4
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., Fath, K., Kelly, G., Nuckolls, G. and Turner, C. E. (1988). Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4, 487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, G.3    Nuckolls, G.4    Turner, C.E.5
  • 5
    • 0029153801 scopus 로고
    • c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation
    • Chang, J. H., Gill, S., Settleman, J. and Parsons, S. J. (1995). c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following Epidermal Growth Factor stimulation. J. Cell Biol. 130, 355-368.
    • (1995) J. Cell Biol. , vol.130 , pp. 355-368
    • Chang, J.H.1    Gill, S.2    Settleman, J.3    Parsons, S.J.4
  • 6
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Charzanowska-Wodnicka, M. and Burridge, K. (1996). Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Charzanowska-Wodnicka, M.1    Burridge, K.2
  • 7
    • 0025772585 scopus 로고
    • The antiproliferative and antimetastatic compound L651582, inhibits muscarinic acetylcholine receptor-stimulated calcium influx and arachidonic acid release
    • Felder, C. C., Ma, A. L., Liotta, L. A. and Kohn, E. C. (1991). The antiproliferative and antimetastatic compound L651582, inhibits muscarinic acetylcholine receptor-stimulated calcium influx and arachidonic acid release. J. Pharmacol. Exp. Therap. 257, 967-971.
    • (1991) J. Pharmacol. Exp. Therap. , vol.257 , pp. 967-971
    • Felder, C.C.1    Ma, A.L.2    Liotta, L.A.3    Kohn, E.C.4
  • 8
    • 12644264656 scopus 로고    scopus 로고
    • Differential translocation of Rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor
    • Fleming, I. N., Elliott, C. M. and Exton, J. H. (1996). Differential translocation of Rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor. J. Biol. Chem. 271, 33067-33073.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33067-33073
    • Fleming, I.N.1    Elliott, C.M.2    Exton, J.H.3
  • 9
    • 0030929149 scopus 로고    scopus 로고
    • Identification of a novel, putative Rho-specific GDP-GTP exchange factor and a Rho A binding protein: Control of neuronal morphology
    • Gebbink, M. F. B. G., Kranenburg, O., Poland, M., Van Horck, F. P. G., Houssa, B. and Moolenaar, W. H. (1997). Identification of a novel, putative Rho-specific GDP-GTP exchange factor and a Rho A binding protein: control of neuronal morphology. J. Cell Biol. 137, 1603-1613.
    • (1997) J. Cell Biol. , vol.137 , pp. 1603-1613
    • Gebbink, M.F.B.G.1    Kranenburg, O.2    Poland, M.3    Van Horck, F.P.G.4    Houssa, B.5    Moolenaar, W.H.6
  • 10
    • 0000668505 scopus 로고    scopus 로고
    • Translocation of RhoA associated with Ca++ sensitization of smooth muscle
    • Gong, M. C., Fujihara, H., Somlyo, A. and Solmyo, A. P. (1997). Translocation of RhoA associated with Ca++ sensitization of smooth muscle. J. Biol. Chem.. 272, 10704-10709.
    • (1997) J. Biol. Chem.. , vol.272 , pp. 10704-10709
    • Gong, M.C.1    Fujihara, H.2    Somlyo, A.3    Solmyo, A.P.4
  • 11
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. (1994). Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10, 31-54.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 12
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • Hildebrand, J. D., Taylor, J. M. and Parsons, T. (1996). An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with Focal Adhesion Kinase. Mol. Cell Biol. 16, 3169-3178.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, T.3
  • 13
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1 and Cdc42Hs regulate transcriptional activation by SRF
    • Hill, C. S., Wynne, J. and Treisman, R. (1995). The Rho family GTPases RhoA, Rac1 and Cdc42Hs regulate transcriptional activation by SRF. Cell 81, 1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 14
    • 0028205812 scopus 로고
    • Structure-function analysis of signal and growth inhibition by carboxyamido-triazole, CAI
    • Kohn, E. C., Felder, C. C., Jacobs, W., Holmes, K. A., Day, A., Freer, R. and Liotta, L. A. (1994). Structure-function analysis of signal and growth inhibition by carboxyamido-triazole, CAI. Cancer Res. 54, 935-942.
    • (1994) Cancer Res. , vol.54 , pp. 935-942
    • Kohn, E.C.1    Felder, C.C.2    Jacobs, W.3    Holmes, K.A.4    Day, A.5    Freer, R.6    Liotta, L.A.7
  • 16
    • 0030056720 scopus 로고    scopus 로고
    • Identification and molecular characterization of a m5 muscarinic receptor in A2058 human melanoma cells
    • Kohn, E. C., Alessandro, R., Probst, J., Jacobs, W., Brilley, E. and Felder, C. C. (1996). Identification and molecular characterization of a m5 muscarinic receptor in A2058 human melanoma cells. J. Biol. Chem. 271, 17476-17484.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17476-17484
    • Kohn, E.C.1    Alessandro, R.2    Probst, J.3    Jacobs, W.4    Brilley, E.5    Felder, C.C.6
  • 17
    • 0000315614 scopus 로고    scopus 로고
    • Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA
    • Kranenburg, O., Poland, M., Gebbink, M., Oomen, L. and Moolenaar, W. H. (1997). Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J. Cell Sci. 110, 2417-2427.
    • (1997) J. Cell Sci. , vol.110 , pp. 2417-2427
    • Kranenburg, O.1    Poland, M.2    Gebbink, M.3    Oomen, L.4    Moolenaar, W.H.5
  • 18
    • 0030977123 scopus 로고    scopus 로고
    • Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation
    • Kureishi, Y., Kobayashi, S., Amano, M., Kimura, K., Kanaide, H., Nakano, T., Kaibuchi, K. and Ito, M. (1997). Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272, 12257-12260.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12257-12260
    • Kureishi, Y.1    Kobayashi, S.2    Amano, M.3    Kimura, K.4    Kanaide, H.5    Nakano, T.6    Kaibuchi, K.7    Ito, M.8
  • 19
    • 0030953445 scopus 로고    scopus 로고
    • Integrin-mediated focal adhesion kinase is independent of focal adhesion formation or integrin activation
    • Lyman, S., Gilmore, A., Burridge, K., Gidwitz, S. and White II, G. C. (1997). Integrin-mediated focal adhesion kinase is independent of focal adhesion formation or integrin activation. J. Biol. Chem. 272, 22538-22547.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22538-22547
    • Lyman, S.1    Gilmore, A.2    Burridge, K.3    Gidwitz, S.4    White G.C. II5
  • 20
    • 0026050850 scopus 로고
    • Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps
    • Lytton, J., Westlin, M. and Hanley, M. R. (1991). Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps. J. Biol. Chem. 266, 17067-17071.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17067-17071
    • Lytton, J.1    Westlin, M.2    Hanley, M.R.3
  • 21
    • 0030222377 scopus 로고    scopus 로고
    • Rho: A connection between membrane receptor signalling and the cytoskeleton
    • Machesky, L. M. and Hall, A. (1996). Rho: a connection between membrane receptor signalling and the cytoskeleton. Trends Cell Biol. 6, 304-310.
    • (1996) Trends Cell Biol. , vol.6 , pp. 304-310
    • Machesky, L.M.1    Hall, A.2
  • 22
    • 16844366239 scopus 로고    scopus 로고
    • Evidence for Rhomediated agonist of phospholipase D in Rat 1 fibroblasts
    • Malcolm, K. C., Elliott, C. M. and Exton, J. H. (1996). Evidence for Rhomediated agonist of phospholipase D in Rat 1 fibroblasts. J. Biol. Chem. 271, 13135-13139.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 23
    • 0028961293 scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. and Hall, A. (1995). Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.1    Hall, A.2
  • 25
    • 0025609411 scopus 로고
    • Capacitative calcium entry revisited
    • Putney, J. W. (1990). Capacitative calcium entry revisited. Cell Calcium 11, 611-624.
    • (1990) Cell Calcium , vol.11 , pp. 611-624
    • Putney, J.W.1
  • 26
    • 0027426068 scopus 로고
    • Excitement about calcium signaling in inexcitable cells
    • Putney, J. W. (1993). Excitement about calcium signaling in inexcitable cells. Science 262, 676-678.
    • (1993) Science , vol.262 , pp. 676-678
    • Putney, J.W.1
  • 27
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. and Hall, A. (1992). The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.1    Hall, A.2
  • 28
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. and Hall, A. (1992). The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 30
    • 0031044227 scopus 로고    scopus 로고
    • Thapsigargin-induced gene expression in nonexcitable cells is dependent on calcium influx
    • Rodland, K. D., Wersto, R. P., Hobson, S. and Kohn, E. C. (1997). Thapsigargin-induced gene expression in nonexcitable cells is dependent on calcium influx. Mol. Endo. 11, 281-291.
    • (1997) Mol. Endo. , vol.11 , pp. 281-291
    • Rodland, K.D.1    Wersto, R.P.2    Hobson, S.3    Kohn, E.C.4
  • 31
    • 0024457508 scopus 로고
    • From signal to pseudopod: How cells control cytoplasmic actin polymerization
    • Stossel, T. P. (1989). From signal to pseudopod: how cells control cytoplasmic actin polymerization. J. Biol. Chem. 264, 18261-18264.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18261-18264
    • Stossel, T.P.1
  • 33
    • 0028846966 scopus 로고
    • Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends
    • Tardif, M., Huang, S., Redmond, T., Safer, D., Pring, M. and Zigmond, S. H. (1995). Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends. J. Biol. Chem. 270, 28075-28083.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28075-28083
    • Tardif, M.1    Huang, S.2    Redmond, T.3    Safer, D.4    Pring, M.5    Zigmond, S.H.6
  • 34
    • 0030849454 scopus 로고    scopus 로고
    • Regulation of actin polymerization in cell-free system by GTPγS and Cdc42
    • Zigmond, S. H., Joyce, M., Borleis, J., Bokoch, G. M. and Devreotes, P. N. (1997). Regulation of actin polymerization in cell-free system by GTPγS and Cdc42. J. Cell Biol. 138, 363-374.
    • (1997) J. Cell Biol. , vol.138 , pp. 363-374
    • Zigmond, S.H.1    Joyce, M.2    Borleis, J.3    Bokoch, G.M.4    Devreotes, P.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.