메뉴 건너뛰기




Volumn 251, Issue 1, 1999, Pages 57-66

Cytokines modulate integrin α(v)β3-mediated human endothelial cell adhesion and calcium signaling

Author keywords

Angiogenesis; Basic fibroblast growth factor; Cytokines; Disintegrin; Tumor necrosis factor; (v) 3 integrin

Indexed keywords

CYTOKINE; DISINTEGRIN; FIBROBLAST GROWTH FACTOR; INTEGRIN; PHOSPHATIDYLINOSITOL 3 KINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 0033603888     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4560     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 84975525035 scopus 로고
    • Clinical applications of research on angiogenesis
    • Folkman J. Clinical applications of research on angiogenesis. N. Engl. J. Med. 333:1995;1757-1763.
    • (1995) N. Engl. J. Med. , vol.333 , pp. 1757-1763
    • Folkman, J.1
  • 3
    • 0024439457 scopus 로고
    • How does extracellular matrix control capillary morphogenesis?
    • Ingber D. E., Folkman J. How does extracellular matrix control capillary morphogenesis? Cell. 58:1989;803-805.
    • (1989) Cell , vol.58 , pp. 803-805
    • Ingber, D.E.1    Folkman, J.2
  • 4
    • 0027008419 scopus 로고
    • Basic FGF and TGF-β differentially modulate integrin expression of human microvascular endothelial cells
    • Enenstein J., Waleh N. S., Kramer R. H. Basic FGF and TGF-β differentially modulate integrin expression of human microvascular endothelial cells. Exp. Cell Res. 203:1992;499-503.
    • (1992) Exp. Cell Res. , vol.203 , pp. 499-503
    • Enenstein, J.1    Waleh, N.S.2    Kramer, R.H.3
  • 5
    • 0027442793 scopus 로고
    • Basic fibroblast growth factor modulates integrin expression in microvascular endothelial cells
    • Klein S., Giancotti F. G., Presta M., Albelda S. M., Buck C. A., Rifkin D. B. Basic fibroblast growth factor modulates integrin expression in microvascular endothelial cells. Mol. Biol. Cell. 4:1993;973-982.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 973-982
    • Klein, S.1    Giancotti, F.G.2    Presta, M.3    Albelda, S.M.4    Buck, C.A.5    Rifkin, D.B.6
  • 6
    • 0026770377 scopus 로고
    • Integrins: Versatiltiy, modulation, and signaling in cell adhesion
    • Hynes R. O. Integrins: Versatiltiy, modulation, and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 7
    • 0030821648 scopus 로고    scopus 로고
    • Cell adhesion and angiogenesis
    • Bischoff J. Cell adhesion and angiogenesis. J. Clin. Invest. 99:1997;373-376.
    • (1997) J. Clin. Invest. , vol.99 , pp. 373-376
    • Bischoff, J.1
  • 8
    • 0029087897 scopus 로고
    • Function and regulation of β3 integrin in hemostasis and vascular biology
    • Shattil S. J. Function and regulation of β3 integrin in hemostasis and vascular biology. Thromb. Haemostasis. 74:1995;149-155.
    • (1995) Thromb. Haemostasis , vol.74 , pp. 149-155
    • Shattil, S.J.1
  • 9
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • Brooks P. C., Clark R. A. F., Cheresh D. A. Requirement of vascular integrin αvβ3 for angiogenesis. Science. 264:1994;569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.F.2    Cheresh, D.A.3
  • 13
    • 0027513593 scopus 로고
    • Integrin β1- And β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms
    • Leavesley P. I., Schwartz M. A., Rosenfeld M., Cheresh D. A. Integrin β1- and β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms. J. Cell Biol. 121:1993;163-170.
    • (1993) J. Cell Biol. , vol.121 , pp. 163-170
    • Leavesley, P.I.1    Schwartz, M.A.2    Rosenfeld, M.3    Cheresh, D.A.4
  • 18
    • 0029903239 scopus 로고    scopus 로고
    • Disintegrin interaction with αvβ3 integrin on human umbilical vein endothelial cells: Expression of ligand-induced binding site on β3 subunit
    • Juliano D., Wang Y., Marcinkiewicz C., Rosenthal L. A., Stewart G. J., Niewiarowski S. Disintegrin interaction with αvβ3 integrin on human umbilical vein endothelial cells: Expression of ligand-induced binding site on β3 subunit. Exp. Cell Res. 255:1996;132-142.
    • (1996) Exp. Cell Res. , vol.255 , pp. 132-142
    • Juliano, D.1    Wang, Y.2    Marcinkiewicz, C.3    Rosenthal, L.A.4    Stewart, G.J.5    Niewiarowski, S.6
  • 19
    • 0001562465 scopus 로고    scopus 로고
    • Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by acting as integrin αvβ3 antagonist and inducing apoptosis
    • Yeh C. H., Peng H. C., Huang T. F. Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by acting as integrin αvβ3 antagonist and inducing apoptosis. Blood. 92:1998;3268-3276.
    • (1998) Blood , vol.92 , pp. 3268-3276
    • Yeh, C.H.1    Peng, H.C.2    Huang, T.F.3
  • 20
    • 0030781352 scopus 로고    scopus 로고
    • Application of recombinant rhodostomin in studying cell adhesion
    • Chang H. H., Chang C. P., Chang J. C., Dung S. Z., Lo S. J. Application of recombinant rhodostomin in studying cell adhesion. J. Biomed. Sci. 4:1997;235-243.
    • (1997) J. Biomed. Sci. , vol.4 , pp. 235-243
    • Chang, H.H.1    Chang, C.P.2    Chang, J.C.3    Dung, S.Z.4    Lo, S.J.5
  • 21
    • 0025753506 scopus 로고
    • Purification and characterization of a antiplatelet peptide, arietin, from Bitis arietans venom
    • Huang T. F., Wang W. J., Teng C. M., Lieu C. S., Ouyang C. Purification and characterization of a antiplatelet peptide, arietin, from Bitis arietans venom. Biochim. Biophys. Acta. 1074:1991;136-143.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 136-143
    • Huang, T.F.1    Wang, W.J.2    Teng, C.M.3    Lieu, C.S.4    Ouyang, C.5
  • 22
    • 0003267658 scopus 로고
    • Rhodostomin, A snake venom peptide and its fragment inhibit platelet aggregation by acting as fibrinogen receptor antagonist
    • Ljubljana, Yogoslavia. [abstract 141]
    • Huang, T. F, Ouyang, C, and, Teng, C. M. 1990, Rhodostomin, a snake venom peptide and its fragment inhibit platelet aggregation by acting as fibrinogen receptor antagonist, 11th International Congress on Thrombosis, Ljubljana, Yogoslavia. [abstract 141].
    • (1990) 11th International Congress on Thrombosis
    • Huang, T.F.1    Ouyang, C.2    Teng, C.M.3
  • 23
    • 0021965983 scopus 로고
    • A new murin monoclonal antibody reports on activation-dependent change in the conformation and/or microenvironment of the platelet glycoprotein IIb/IIIa complex
    • Coller B. S. A new murin monoclonal antibody reports on activation-dependent change in the conformation and/or microenvironment of the platelet glycoprotein IIb/IIIa complex. J. Clin. Invest. 76:1985;101-108.
    • (1985) J. Clin. Invest. , vol.76 , pp. 101-108
    • Coller, B.S.1
  • 24
    • 0025241904 scopus 로고
    • Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers
    • Frelinger III A. L., Cohen I., Plow E. F., Smith M. A., Robert J., Lam S. C. T., Ginsberg M. H. Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers. J. Biol. Chem. 265:1990;6346-6352.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6346-6352
    • Frelinger A.L. III1    Cohen, I.2    Plow, E.F.3    Smith, M.A.4    Robert, J.5    Lam, S.C.T.6    Ginsberg, M.H.7
  • 25
    • 0005306564 scopus 로고
    • Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor
    • Cheresh D. A. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc. Natl. Sci. USA. 84:1987;6471-6475.
    • (1987) Proc. Natl. Sci. USA , vol.84 , pp. 6471-6475
    • Cheresh, D.A.1
  • 26
    • 0027513593 scopus 로고
    • Integrin β1- And β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms
    • Leavesley D. I., Schwartz M. A., Rosenfeld M., Cheresh D. A. Integrin β1- and β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms. J. Cell Biol. 121:1993;163-170.
    • (1993) J. Cell Biol. , vol.121 , pp. 163-170
    • Leavesley, D.I.1    Schwartz, M.A.2    Rosenfeld, M.3    Cheresh, D.A.4
  • 27
    • 0028610549 scopus 로고
    • Analysis of human platelet glycoprotein IIb-IIIa by fluorescein isothiocyanate-conjugated disintegrins with flow cytometry
    • Liu C. Z., Wang Y. W., Shen M. C., Huang T. F. Analysis of human platelet glycoprotein IIb-IIIa by fluorescein isothiocyanate-conjugated disintegrins with flow cytometry. Thromb. Haemostasis. 72:1994;919-925.
    • (1994) Thromb. Haemostasis , vol.72 , pp. 919-925
    • Liu, C.Z.1    Wang, Y.W.2    Shen, M.C.3    Huang, T.F.4
  • 28
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins
    • Jaffe E. A., Nachamn R. L., Becker C. G., Minnick C. R. Culture of human endothelial cells derived from umbilical veins. J. Clin. Invest. 52:1973;2745-2756.
    • (1973) J. Clin. Invest. , vol.52 , pp. 2745-2756
    • Jaffe, E.A.1    Nachamn, R.L.2    Becker, C.G.3    Minnick, C.R.4
  • 29
    • 0031788405 scopus 로고    scopus 로고
    • A new short chain RGD-containing disintegrin, accutin, inhibits the common pathway of human platelet aggregation
    • Yeh C. H., Peng H. C., Yih J. B., Huang T. F. A new short chain RGD-containing disintegrin, accutin, inhibits the common pathway of human platelet aggregation. Biochim. Biophys. Acta. 1425:1998;493-504.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 493-504
    • Yeh, C.H.1    Peng, H.C.2    Yih, J.B.3    Huang, T.F.4
  • 30
    • 0028675975 scopus 로고
    • Do adhesion molecules signal via FGF receptors?
    • Mason J. Do adhesion molecules signal via FGF receptors? Curr. Biol. 4:1994;1158-1161.
    • (1994) Curr. Biol. , vol.4 , pp. 1158-1161
    • Mason, J.1
  • 32
    • 0027979834 scopus 로고
    • A mechanism for divalent cation regulation of β3-integrin
    • Smith J. W., Piotrowicz R. S., Mathis D. A mechanism for divalent cation regulation of β3-integrin. J. Biol. Chem. 269:1994;960-967.
    • (1994) J. Biol. Chem. , vol.269 , pp. 960-967
    • Smith, J.W.1    Piotrowicz, R.S.2    Mathis, D.3
  • 33
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering B. M., Coffer P. J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature. 376:1995;599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 34
    • 0023639428 scopus 로고
    • Trigramin, a low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex
    • Huang T. F., Holt J. C., Lukasiewicz H., Niewiarowski S. Trigramin, a low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex. J. Biol. Chem. 262:1987;16157-16163.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16157-16163
    • Huang, T.F.1    Holt, J.C.2    Lukasiewicz, H.3    Niewiarowski, S.4
  • 35
    • 0030709254 scopus 로고    scopus 로고
    • The biological activities of disintegrins and their possible applications
    • Huang T. F., Liu C. Z. The biological activities of disintegrins and their possible applications. J. Toxicol.-Toxin Rev. 16:1997;135-161.
    • (1997) J. Toxicol.-Toxin Rev. , vol.16 , pp. 135-161
    • Huang, T.F.1    Liu, C.Z.2
  • 36
    • 0031814234 scopus 로고    scopus 로고
    • What have snakes taught us about integrins?
    • Huang T. F. What have snakes taught us about integrins? Cell. Mol. Life Sci. 54:1998;527-540.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 527-540
    • Huang, T.F.1
  • 37
    • 0031865984 scopus 로고    scopus 로고
    • Full-spreading platelets induced by the recombinant rhodostomin are via binding to integrins and correlated with FAK phosphorylation
    • Chang H. H., Lo S. J. Full-spreading platelets induced by the recombinant rhodostomin are via binding to integrins and correlated with FAK phosphorylation. Toxicon. 36:1998;1087-1099.
    • (1998) Toxicon , vol.36 , pp. 1087-1099
    • Chang, H.H.1    Lo, S.J.2
  • 38
    • 0023157363 scopus 로고
    • Angiogenic factors
    • Folkman J., Klagsbrum M. Angiogenic factors. Science. 235:1987;442-447.
    • (1987) Science , vol.235 , pp. 442-447
    • Folkman, J.1    Klagsbrum, M.2
  • 39
    • 0026093190 scopus 로고
    • Tumor necrosis factor induces apoptosis (programmed cell death) in normal endothelial cells in vitro
    • Robaye B., Mosselmans R., Fiers W., Dumont J. E., Galand P. Tumor necrosis factor induces apoptosis (programmed cell death) in normal endothelial cells in vitro. Am. J. Pathol. 138:1991;447-453.
    • (1991) Am. J. Pathol. , vol.138 , pp. 447-453
    • Robaye, B.1    Mosselmans, R.2    Fiers, W.3    Dumont, J.E.4    Galand, P.5
  • 40
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper G. E., McNamee H. P., Dike L. E., Bojanowski K., Ingber D. E. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell. 6:1995;1349-1365.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 41
    • 0032168738 scopus 로고    scopus 로고
    • Integrin affinity modulation
    • Hughes P. E., Pfaff M. Integrin affinity modulation. Trends Cell Biol. 8:1998;359-364.
    • (1998) Trends Cell Biol. , vol.8 , pp. 359-364
    • Hughes, P.E.1    Pfaff, M.2
  • 42
    • 0027235439 scopus 로고
    • Regulation of vascular integrins
    • Smith S. S., Joneckis C. C., Parise L. V. Regulation of vascular integrins. Blood. 81:1993;2827-2843.
    • (1993) Blood , vol.81 , pp. 2827-2843
    • Smith, S.S.1    Joneckis, C.C.2    Parise, L.V.3
  • 43
    • 0032576475 scopus 로고    scopus 로고
    • Activation of αvβ3 on vascular cells controls recognition of prothrombin
    • Byzova T. V., Plow E. F. Activation of αvβ3 on vascular cells controls recognition of prothrombin. J. Cell Biol. 143:1998;2081-2092.
    • (1998) J. Cell Biol. , vol.143 , pp. 2081-2092
    • Byzova, T.V.1    Plow, E.F.2
  • 44
    • 0040887215 scopus 로고    scopus 로고
    • Evidence for the involvement of endothelial cell integrin αvβ3 in the disruption of tumor vasculature induced by TNF and INF-γ
    • Ruegg C., Yimaz A., Bieler G., Bamat J., Chaubert P., Lejeune F. J. Evidence for the involvement of endothelial cell integrin αvβ3 in the disruption of tumor vasculature induced by TNF and INF-γ Nature Med. 4:1998;408-414.
    • (1998) Nature Med. , vol.4 , pp. 408-414
    • Ruegg, C.1    Yimaz, A.2    Bieler, G.3    Bamat, J.4    Chaubert, P.5    Lejeune, F.J.6
  • 45
    • 0029670835 scopus 로고    scopus 로고
    • Activation of the integrin αvβ3 involves a discrete cation-binding site that regulates conformation
    • Pelletier A. J., Kunicki T., Quaranta V. Activation of the integrin αvβ3 involves a discrete cation-binding site that regulates conformation. J. Biol. Chem. 271:1996;1364-1370.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1364-1370
    • Pelletier, A.J.1    Kunicki, T.2    Quaranta, V.3
  • 46
    • 0025807704 scopus 로고
    • Tumor necrosis factor α and interferon γ modulate the expression of the vitronectin receptor (integrin β3) in human endothelial cells
    • Defilippi P., Truffa G., Stefanuto G., Altruda F., Silengo L., Tarone G. Tumor necrosis factor α and interferon γ modulate the expression of the vitronectin receptor (integrin β3) in human endothelial cells. J. Biol. Chem. 266:1991;7638-7645.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7638-7645
    • Defilippi, P.1    Truffa, G.2    Stefanuto, G.3    Altruda, F.4    Silengo, L.5    Tarone, G.6
  • 47
    • 0030948723 scopus 로고    scopus 로고
    • Cytokines treatment of endothelial cells increases glycoprotein Ibα-dependent adhesion to von Willebrand factor
    • Beacham D. A., Tran L. P., Shapiro S. S. Cytokines treatment of endothelial cells increases glycoprotein Ibα-dependent adhesion to von Willebrand factor. Blood. 89:1997;4071-4077.
    • (1997) Blood , vol.89 , pp. 4071-4077
    • Beacham, D.A.1    Tran, L.P.2    Shapiro, S.S.3
  • 48
    • 0030458412 scopus 로고    scopus 로고
    • Regulating integrin-mediated adhesion: One more function for PI-3 kinase?
    • Shimizu Y., Hunt S. W. Regulating integrin-mediated adhesion: one more function for PI-3 kinase? Immunol. Today. 17:1996;565-573.
    • (1996) Immunol. Today , vol.17 , pp. 565-573
    • Shimizu, Y.1    Hunt, S.W.2
  • 49
    • 0029964243 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase gamma and p85/phosphoinositide 3-kinase in platelets. Relative activation by thrombin receptor or beta-phorbol myristate acetate and roles in promoting the ligand-binding function of αiIbβ3 integrin
    • Zhang J., Shattil S. J., Cunningham M. C., Rittenhouse S. E. Phosphoinositide 3-kinase gamma and p85/phosphoinositide 3-kinase in platelets. Relative activation by thrombin receptor or beta-phorbol myristate acetate and roles in promoting the ligand-binding function of αIIbβ3 integrin. J. Biol. Chem. 271:1996;6265-6272.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6265-6272
    • Zhang, J.1    Shattil, S.J.2    Cunningham, M.C.3    Rittenhouse, S.E.4
  • 50
    • 0032498640 scopus 로고    scopus 로고
    • Integrin αvβ3 requirement for sustained mitogen-activated protein kinase activity during angiogenesis
    • Eliceiri B. P., Klemke R., Stromblad S., Cheresh D. A. Integrin αvβ3 requirement for sustained mitogen-activated protein kinase activity during angiogenesis. J. Cell Biol. 140:1998;1255-1263.
    • (1998) J. Cell Biol. , vol.140 , pp. 1255-1263
    • Eliceiri, B.P.1    Klemke, R.2    Stromblad, S.3    Cheresh, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.