메뉴 건너뛰기




Volumn 12, Issue 4, 1998, Pages 205-210

Molecular interactions between the urokinase receptor and integrins in the vasculature

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; UROKINASE RECEPTOR;

EID: 0031735388     PISSN: 13690191     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-9499(98)80014-3     Document Type: Review
Times cited : (9)

References (65)
  • 1
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis
    • Andreasen P A, Kjoller L, Christensen L, Duffy M J. The urokinase-type plasminogen activator system in cancer metastasis. Int J Cancer 1997; 72: 1-22.
    • (1997) Int J Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjoller, L.2    Christensen, L.3    Duffy, M.J.4
  • 3
    • 0028175457 scopus 로고
    • Release of GPI-anchored membrane proteins by a cell-associated GPI-specific phospholipase D
    • Metz C N, Brunner G, Choi-Muira N H, et al. Release of GPI-anchored membrane proteins by a cell-associated GPI-specific phospholipase D. EMBO J 1994; 13: 1741-1751.
    • (1994) EMBO J , vol.13 , pp. 1741-1751
    • Metz, C.N.1    Brunner, G.2    Choi-Muira, N.H.3
  • 4
    • 0025336879 scopus 로고
    • The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes
    • Estreicher A, Mühlhauser J, Carpentier J-L, Orci L, Vassalli J-D. The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes. J Cell Biol 1990; 111: 783-792.
    • (1990) J Cell Biol , vol.111 , pp. 783-792
    • Estreicher, A.1    Mühlhauser, J.2    Carpentier, J.-L.3    Orci, L.4    Vassalli, J.-D.5
  • 5
    • 0028058734 scopus 로고
    • Pericellular enyzmatic hydrolysis: Implications for the regulation of cell proliferation in the vessel wall and the bone marrow
    • Brunner G, Preissner K T. Pericellular enyzmatic hydrolysis: implications for the regulation of cell proliferation in the vessel wall and the bone marrow. Blood Coagul Fibrinolysis 1994; 5: 625-639.
    • (1994) Blood Coagul Fibrinolysis , vol.5 , pp. 625-639
    • Preissner, B.G.1
  • 6
    • 0026341460 scopus 로고
    • In vivo paracrine interaction between urokinase and its receptor: Effect on tumor cell invasion
    • Ossowski L, Clunie G, Masucci M, Blasi F. In vivo paracrine interaction between urokinase and its receptor: effect on tumor cell invasion. J Cell Biol 1993; 115: 1107-1112.
    • (1993) J Cell Biol , vol.115 , pp. 1107-1112
    • Ossowski, L.1    Clunie, G.2    Masucci, M.3    Blasi, F.4
  • 7
    • 0029013774 scopus 로고
    • Urokinase-type plasminogen activator (uPA) and its receptor (CD87): A new target in tumor invasion and metastasis
    • Schmitt M, Wilhelm O, Janicke F, et al. Urokinase-type plasminogen activator (uPA) and its receptor (CD87): a new target in tumor invasion and metastasis. J Obstet Gynaecol 1995; 21: 151-165.
    • (1995) J Obstet Gynaecol , vol.21 , pp. 151-165
    • Schmitt, M.1    Wilhelm, O.2    Janicke, F.3
  • 8
    • 0027385945 scopus 로고
    • Urokinase-type plasminogen activator and malignancy
    • Duffy M J. Urokinase-type plasminogen activator and malignancy. Fibrinolysis 1993; 7: 295-302.
    • (1993) Fibrinolysis , vol.7 , pp. 295-302
    • Duffy, M.J.1
  • 9
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992; 69: 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 10
    • 0030814976 scopus 로고    scopus 로고
    • 3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF
    • 3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF. EMBO J 1997; 16: 5600-5607.
    • (1997) EMBO J , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 11
    • 0030877824 scopus 로고    scopus 로고
    • Molecular crosstalk between adhesion receptors and proteolytic cascades in vascular remodeling
    • Preissner K T, May A E, Wohn K D, Germer M, Kanse S M. Molecular crosstalk between adhesion receptors and proteolytic cascades in vascular remodeling. Thromb Haemost 1997; 78: 88-95.
    • (1997) Thromb Haemost , vol.78 , pp. 88-95
    • Preissner, K.T.1    May, A.E.2    Wohn, K.D.3    Germer, M.4    Kanse, S.M.5
  • 12
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • Chapman H A. Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration. Curr Opin Cell Biol 1997; 9: 714-724.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 714-724
    • Chapman, H.A.1
  • 13
    • 0029932651 scopus 로고    scopus 로고
    • Integrins as promiscuous signal transduction devices
    • Petty H R, Todd R F. Integrins as promiscuous signal transduction devices. Immunol Today 1996; 17: 209-212.
    • (1996) Immunol Today , vol.17 , pp. 209-212
    • Petty, H.R.1    Todd, R.F.2
  • 14
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer T A. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 1994; 76: 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 15
    • 0012008473 scopus 로고
    • Adhesive receptor Mac-1 coordinates the activation of factor X on stimulated cells of monocytic and myeloid differentiation: An alternative initiation of the coagulation protease cascade
    • Altieri D C, Morrissey J H, Edgington T S. Adhesive receptor Mac-1 coordinates the activation of factor X on stimulated cells of monocytic and myeloid differentiation: an alternative initiation of the coagulation protease cascade. Proc Natl Acad Sci USA 1988; 85: 7462-7466.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7462-7466
    • Altieri, D.C.1    Morrissey, J.H.2    Edgington, T.S.3
  • 16
    • 0023819126 scopus 로고
    • Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contacts
    • Pöllänen J, Hedman K, Nielsen L S, Dano K, Vaheri A. Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contacts. J Cell Biol 1988; 106: 87-95.
    • (1988) J Cell Biol , vol.106 , pp. 87-95
    • Pöllänen, J.1    Hedman, K.2    Nielsen, L.S.3    Dano, K.4    Vaheri, A.5
  • 17
    • 0028173624 scopus 로고
    • Physical association of complement receptor type 3 and urokinase-type plasminogen activator receptor in neutrophil membranes
    • Xue W, Kindzelskii A L, Todd R F, Petty H R. Physical association of complement receptor type 3 and urokinase-type plasminogen activator receptor in neutrophil membranes. J Immunol 1994; 152: 4630.
    • (1994) J Immunol , vol.152 , pp. 4630
    • Xue, W.1    Kindzelskii, A.L.2    Todd, R.F.3    Petty, H.R.4
  • 18
    • 0028925552 scopus 로고
    • 2-integrins, and scr-kinases within a single receptor complex of human monocytes
    • 2-integrins, and scr-kinases within a single receptor complex of human monocytes. J Exp Med 1995; 181: 1381-1390.
    • (1995) J Exp Med , vol.181 , pp. 1381-1390
    • Bohuslav, J.1    Horejsi, V.2    Hansmann, C.3
  • 19
    • 0030000470 scopus 로고    scopus 로고
    • The urokinase receptor (CD87) facilitates CD11B/CD18-mediated adhesion of human monocytes
    • Sitrin R G, Todd R F, Petty H R, et al. The urokinase receptor (CD87) facilitates CD11B/CD18-mediated adhesion of human monocytes. J Clin Invest 1996; 97: 1942-1951.
    • (1996) J Clin Invest , vol.97 , pp. 1942-1951
    • Sitrin, R.G.1    Todd, R.F.2    Petty, H.R.3
  • 20
    • 0029958368 scopus 로고    scopus 로고
    • Mac-1 (CD11b/CD18) and the urokinase receptor (CD87) form a functional unit on monocytic cells
    • Simon D I, Rao N K, Xu H, et al. Mac-1 (CD11b/CD18) and the urokinase receptor (CD87) form a functional unit on monocytic cells. Blood 1996; 88: 3185-3194.
    • (1996) Blood , vol.88 , pp. 3185-3194
    • Simon, D.I.1    Rao, N.K.2    Xu, H.3
  • 21
    • 0028870478 scopus 로고
    • Human urokinase-type plasminogen activator primes neutrophils for superoxide anion release - Possible roles of complement receptor type 3 and calcium
    • Cao D R, Mizukami I F, Garniwagner B A, et al. Human urokinase-type plasminogen activator primes neutrophils for superoxide anion release - possible roles of complement receptor type 3 and calcium. J Immunol 1995; 154: 1817-1829.
    • (1995) J Immunol , vol.154 , pp. 1817-1829
    • Cao, D.R.1    Mizukami, I.F.2    Garniwagner, B.A.3
  • 22
    • 0027506444 scopus 로고
    • Interaction of urokinase-type plasminogenactivator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDA protein
    • Dumler I, Petri T, Schleuning W-D. Interaction of urokinase-type plasminogenactivator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDA protein. FEBS Lett 1993; 322: 37-40.
    • (1993) FEBS Lett , vol.322 , pp. 37-40
    • Dumler, I.1    Petri, T.2    Schleuning, W.-D.3
  • 23
    • 0028305433 scopus 로고
    • Induction of cell migration by pro-urokinase binding to its receptor: Possible mechanism for signal transduction in human epithelial cells
    • Busso N, Masur S K, Lazega D, Waxman S, Ossowski L. Induction of cell migration by pro-urokinase binding to its receptor: possible mechanism for signal transduction in human epithelial cells. J Cell Biol 1994; 126: 259-270.
    • (1994) J Cell Biol , vol.126 , pp. 259-270
    • Busso, N.1    Masur, S.K.2    Lazega, D.3    Waxman, S.4    Ossowski, L.5
  • 24
    • 0029923744 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F. Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. EMBO J 1996; 15: 1572-1582.
    • (1996) EMBO J , vol.15 , pp. 1572-1582
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3    Sidenius, N.4    Blasi, F.5    Fazioli, F.6
  • 25
    • 0030716909 scopus 로고    scopus 로고
    • Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumor cell line TCL-598
    • Koshelnick Y, Ehart M, Hufnagl P, Heinrich P C, Binder B R. Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumor cell line TCL-598. J Biol Chem 1997; 272: 28563-28567.
    • (1997) J Biol Chem , vol.272 , pp. 28563-28567
    • Koshelnick, Y.1    Ehart, M.2    Hufnagl, P.3    Heinrich, P.C.4    Binder, B.R.5
  • 26
    • 0031983177 scopus 로고    scopus 로고
    • The JAK/STAT pathway and urokinase receptor signaling in human aortic vascular smooth muscle cells
    • Dumler I, Weis A, Mayboroda O A, et al. The JAK/STAT pathway and urokinase receptor signaling in human aortic vascular smooth muscle cells. J Biol Chem 1998; 273: 315-321.
    • (1998) J Biol Chem , vol.273 , pp. 315-321
    • Dumler, I.1    Weis, A.2    Mayboroda, O.A.3
  • 28
    • 0029113231 scopus 로고
    • Urokinase receptor is a multifunctional protein: Influence of receptor occupancy on macrophage gene expression
    • Rao N K, Shi G-P, Chapman H A. Urokinase receptor is a multifunctional protein: influence of receptor occupancy on macrophage gene expression. J Clin Invest 1995; 96: 465-474.
    • (1995) J Clin Invest , vol.96 , pp. 465-474
    • Rao, N.K.1    Shi, G.-P.2    Chapman, H.A.3
  • 29
    • 0029757446 scopus 로고    scopus 로고
    • Integrin-dependent induction of functional urokinase receptors in primary T lymphocytes
    • Bianchi E, Ferrero E, Fazioli F, et al. Integrin-dependent induction of functional urokinase receptors in primary T lymphocytes. J Clin Invest 1996; 98: 1133-1141.
    • (1996) J Clin Invest , vol.98 , pp. 1133-1141
    • Bianchi, E.1    Ferrero, E.2    Fazioli, F.3
  • 30
    • 15844379199 scopus 로고    scopus 로고
    • LFA-1-deficient mice show normal CTL responses to virus, but fail to reject immunogenic tumor
    • Schmits R, Kundig T M, Baker D M, et al. LFA-1-deficient mice show normal CTL responses to virus, but fail to reject immunogenic tumor. J Exp Med 1996; 183: 1415-1426.
    • (1996) J Exp Med , vol.183 , pp. 1415-1426
    • Schmits, R.1    Kundig, T.M.2    Baker, D.M.3
  • 31
    • 0027326544 scopus 로고
    • Inflammatory and immune responses are impaired in mice deficient in intercellular adhesion molecule 1
    • Sligh J E, Ballantyne C M, Rich S S, et al. Inflammatory and immune responses are impaired in mice deficient in intercellular adhesion molecule 1. Proc Natl Acad Sci USA 1993; 90: 8529-8533.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8529-8533
    • Sligh, J.E.1    Ballantyne, C.M.2    Rich, S.S.3
  • 32
    • 0030916129 scopus 로고    scopus 로고
    • 3-integrins of fibrosarcoma cells - Dependence on extracellular matrix components
    • 3-integrins of fibrosarcoma cells - dependence on extracellular matrix components. Cancer Res 1997; 57: 1682-1689.
    • (1997) Cancer Res , vol.57 , pp. 1682-1689
    • Xue, W.1    Mizukami, I.2    Todd, R.F.3    Petty, H.R.4
  • 33
    • 0029764639 scopus 로고    scopus 로고
    • Regulation of integrin function by the urokinase receptor
    • Wei Y, Lukashev M, Simon D I, et al. Regulation of integrin function by the urokinase receptor. Science 1996; 273: 1551-1555.
    • (1996) Science , vol.273 , pp. 1551-1555
    • Wei, Y.1    Lukashev, M.2    Simon, D.I.3
  • 34
    • 0030602819 scopus 로고    scopus 로고
    • 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytpolasmic regulatory molecule
    • 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytpolasmic regulatory molecule. Cell 1996; 86: 233-242.
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3
  • 35
    • 0030718565 scopus 로고    scopus 로고
    • Signal transduction via urokinase receptor - Is a transmembrane adapter molecule really necessary
    • Dumler I, Hucho F, Gulba D. Signal transduction via urokinase receptor - is a transmembrane adapter molecule really necessary. Fibrinolysis & Proteolysis 1997; 11 (Suppl 2): 165-169.
    • (1997) Fibrinolysis & Proteolysis , vol.11 , Issue.SUPPL. 2 , pp. 165-169
    • Dumler, I.1    Hucho, F.2    Gulba, D.3
  • 37
    • 0028887861 scopus 로고
    • Vessel wall-dependent metabolic pathways of the adhesive proteins, von-Willebrand-factor and vitronectin
    • Preissner K T, Pötzsch B. Vessel wall-dependent metabolic pathways of the adhesive proteins, von-Willebrand-factor and vitronectin. Histol Histopathol 1995; 10: 239-251.
    • (1995) Histol Histopathol , vol.10 , pp. 239-251
    • Preissner, K.T.1    Pötzsch, B.2
  • 38
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronection
    • Wei Y, Waltz D A, Rao N, Drummond R J, Rosenberg S, Chapman H A. Identification of the urokinase receptor as an adhesion receptor for vitronection. J Biol Chem 1994; 269: 32380-32388.
    • (1994) J Biol Chem , vol.269 , pp. 32380-32388
    • Wei, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6
  • 39
    • 0029873910 scopus 로고    scopus 로고
    • The urokinase receptor is a major vitronectin binding protein on endothelial cells
    • Kanse S M, Kost C, Wilhelm O G, Andreasen P A, Preissner K T. The urokinase receptor is a major vitronectin binding protein on endothelial cells. Exp Cell Res 1996; 224: 344-353.
    • (1996) Exp Cell Res , vol.224 , pp. 344-353
    • Kanse, S.M.1    Kost, C.2    Wilhelm, O.G.3    Andreasen, P.A.4    Preissner, K.T.5
  • 40
    • 0029617773 scopus 로고
    • Internalization of vitronectin-thrombin-antithrombin complex by endothelial cells leads to deposition of the complex into the subendothelial matrix
    • de Boer H C, Preissner K T, Bouma B N, de Groot P G. Internalization of vitronectin-thrombin-antithrombin complex by endothelial cells leads to deposition of the complex into the subendothelial matrix. J Biol Chem 1995; 270: 30733-30740.
    • (1995) J Biol Chem , vol.270 , pp. 30733-30740
    • Boer, H.C.1    Preissner, K.T.2    Bouma, B.N.3    De Groot, P.G.4
  • 41
    • 0027232315 scopus 로고
    • 5 integrin receptor regulates receptor-mediated endocytosis of vitronectin
    • 5 integrin receptor regulates receptor-mediated endocytosis of vitronectin. J Biol Chem 1993; 268: 11492-11495.
    • (1993) J Biol Chem , vol.268 , pp. 11492-11495
    • Panetti, T.S.1    McKeown-Longo, P.J.2
  • 42
    • 0024365697 scopus 로고
    • Immunohistochemical demonstration of age-related deposition of vitronectin (S-protein of complement) and terminal complement complex on dermal elastic fibers
    • Dahlbäck K, Löfberg H, Alumets J, Dahlbäck B. Immunohistochemical demonstration of age-related deposition of vitronectin (S-protein of complement) and terminal complement complex on dermal elastic fibers. J Invest Dermatol 1989; 92: 727-733.
    • (1989) J Invest Dermatol , vol.92 , pp. 727-733
    • Dahlbäck, K.1    Löfberg, H.2    Alumets, J.3    Dahlbäck, B.4
  • 43
    • 0030191756 scopus 로고    scopus 로고
    • Molecular framework for angiogenesis. a complex web of interactions between extravasated plasma proteins and endothelial cell proteins induced by angiogenic cytokines
    • Senger D R. Molecular framework for angiogenesis. A complex web of interactions between extravasated plasma proteins and endothelial cell proteins induced by angiogenic cytokines. Am J Pathol 1996; 149: 1-7
    • (1996) Am J Pathol , vol.149 , pp. 1-7
    • Senger, D.R.1
  • 44
    • 0029816265 scopus 로고    scopus 로고
    • Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?
    • Deng G, Curriden S A, Wang S, Rosenberg S, Loskutoff D J. Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?; Cell Biol 1996; 134: 1563-1571.
    • (1996) Cell Biol , vol.134 , pp. 1563-1571
    • Deng, G.1    Curriden, S.A.2    Wang, S.3    Rosenberg, S.4    Loskutoff, D.J.5
  • 45
    • 0028334672 scopus 로고
    • Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy
    • Waltz D A, Chapman H A. Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy. J Biol Chem 1994; 269: 14746-14750.
    • (1994) J Biol Chem , vol.269 , pp. 14746-14750
    • Waltz, D.A.1    Chapman, H.A.2
  • 46
    • 1842270862 scopus 로고    scopus 로고
    • Vitronectin as link between protease cascades and cell adhesion in haemostasis
    • van Hinsbergh V W M (ed). Amsterdam: Harwood Academic Publications
    • Preissner K T. Vitronectin as link between protease cascades and cell adhesion in haemostasis. In: van Hinsbergh V W M (ed). Vascular Control of Hemostasis. Amsterdam: Harwood Academic Publications, 1996: 169-186.
    • (1996) Vascular Control of Hemostasis , pp. 169-186
    • Preissner, K.T.1
  • 47
    • 0030823246 scopus 로고    scopus 로고
    • Binding of high molecular weight kininogen to human endothelial cells is medited via a site within domains 2 and 3 of the urokinase receptor
    • Colman R W, Pixley R A, Najamunnisa S, et al. Binding of high molecular weight kininogen to human endothelial cells is medited via a site within domains 2 and 3 of the urokinase receptor. J Clin Invest 1997; 100: 1481-1487.
    • (1997) J Clin Invest , vol.100 , pp. 1481-1487
    • Colman, R.W.1    Pixley, R.A.2    Najamunnisa, S.3
  • 49
    • 0030219756 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator-induced monocyte adhesion is modulated by kininogen, kallikrein, factor XII, and plasminogen
    • Li C Z, Gurewich V, Liu J N. Urokinase-type plasminogen activator-induced monocyte adhesion is modulated by kininogen, kallikrein, factor XII, and plasminogen. Exp Cell Res 1996; 226: 239-242.
    • (1996) Exp Cell Res , vol.226 , pp. 239-242
    • Li, C.Z.1    Gurewich, V.2    Liu, J.N.3
  • 50
    • 0026680818 scopus 로고
    • Vitronectin regulates the synthesis and localization of urokinase-type plasminogen activator in HT-1080 cells
    • Ciambrone G J, McKeown-Longo PJ. Vitronectin regulates the synthesis and localization of urokinase-type plasminogen activator in HT-1080 cells. J Biol Chem 1992; 267: 13617-13622.
    • (1992) J Biol Chem , vol.267 , pp. 13617-13622
    • Ciambrone, G.J.1    McKeown-Longo, P.J.2
  • 51
    • 0028086379 scopus 로고
    • The effect of antisense inhibition of urokinase receptor in human squamous cell carcinoma on malignancy
    • Kook Y H, Adamski J, Zelent A, Ossowski L. The effect of antisense inhibition of urokinase receptor in human squamous cell carcinoma on malignancy. EMBO J 1994; 13: 3983-3991.
    • (1994) EMBO J , vol.13 , pp. 3983-3991
    • Kook, Y.H.1    Adamski, J.2    Zelent, A.3    Ossowski, L.4
  • 52
    • 0029053053 scopus 로고
    • Specific binding of urinary-type plasminogen activator (u-PA) to vitronectin and its role in mediating u-PA dependent adhesion of U937 cells
    • Moser T L, Enghild J J, Pizzo S V, Stack M S. Specific binding of urinary-type plasminogen activator (u-PA) to vitronectin and its role in mediating u-PA dependent adhesion of U937 cells. Biochem J 1995; 307: 867-873.
    • (1995) Biochem J , vol.307 , pp. 867-873
    • Moser, T.L.1    Enghild, J.J.2    Pizzo, S.V.3    Stack, M.S.4
  • 53
    • 8944221645 scopus 로고    scopus 로고
    • Interaction of single-chain urokinase with its receptor induces the appearance and disappearance of binding epitopes within the resultant complex for other cell surface proteins
    • Higazi A A-R, Upson R H, Cohen R L, et al. Interaction of single-chain urokinase with its receptor induces the appearance and disappearance of binding epitopes within the resultant complex for other cell surface proteins. Blood 1996; 88: 542-551.
    • (1996) Blood , vol.88 , pp. 542-551
    • Higazi, A.A.-R.1    Upson, R.H.2    Cohen, R.L.3
  • 54
    • 0032055937 scopus 로고    scopus 로고
    • Vitronectin concentrates proteolytic activity on the cell surface and extracellular matrix by trapping soluble urokinase receptor-urokinase complexes
    • Chavakis T, Kanse S M, Yutzy B, Lijnen H R, Preissner K T. Vitronectin concentrates proteolytic activity on the cell surface and extracellular matrix by trapping soluble urokinase receptor-urokinase complexes. Blood 1998; 91: 2305-2312.
    • (1998) Blood , vol.91 , pp. 2305-2312
    • Chavakis, T.1    Kanse, S.M.2    Yutzy, B.3    Lijnen, H.R.4    Preissner, K.T.5
  • 55
    • 0030811592 scopus 로고    scopus 로고
    • Vitronectin binding to urokinase receptor in human breast cancer
    • Carriero M V, Del Vecchio S, Franco P, et al. Vitronectin binding to urokinase receptor in human breast cancer. Clin Cancer Res 1997; 3: 1299-1308.
    • (1997) Clin Cancer Res , vol.3 , pp. 1299-1308
    • Carriero, M.V.1    Del Vecchio, S.2    Franco, P.3
  • 58
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin- And vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • Kjoller L, Kanse SM, Kirkegaard T, et al. Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation. Exp Cell Res 1997; 232: 420-429.
    • (1997) Exp Cell Res , vol.232 , pp. 420-429
    • Kjoller, L.1    Kanse, S.M.2    Kirkegaard, T.3
  • 59
    • 0025127815 scopus 로고
    • Urokinase-type plasminogen activator (u-PA) antigen is a predictor of early relapse in breast cancer
    • Jänicke F, Schmitt M, Hafter R, et al. Urokinase-type plasminogen activator (u-PA) antigen is a predictor of early relapse in breast cancer. Fibrinolysis 1990; 4: 69-78.
    • (1990) Fibrinolysis , vol.4 , pp. 69-78
    • Jänicke, F.1    Schmitt, M.2    Hafter, R.3
  • 61
    • 0030924624 scopus 로고    scopus 로고
    • Molecular genetics of the fibrinolytic and coagulation systems in haemostasis, thrombogenesis, restenosis and atherosclerosis
    • Carmeliet P, Collen D. Molecular genetics of the fibrinolytic and coagulation systems in haemostasis, thrombogenesis, restenosis and atherosclerosis. Curr Opin Lipidol 1997; 8: 118-125.
    • (1997) Curr Opin Lipidol , vol.8 , pp. 118-125
    • Carmeliet, P.1    Collen, D.2
  • 62
    • 0030765720 scopus 로고    scopus 로고
    • Recent advances in cell adhesion molecules and extracellular matrix proteins: Potential clinical implications
    • Mousa S A, Cheresh D A. Recent advances in cell adhesion molecules and extracellular matrix proteins: potential clinical implications. Drug Dev Ther 1997; 2: 187-199.
    • (1997) Drug Dev Ther , vol.2 , pp. 187-199
    • Mousa, S.A.1    Cheresh, D.A.2
  • 63
    • 0029925079 scopus 로고    scopus 로고
    • Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization
    • Hammes H P, Brownlee M, Joncyk A, Sutter A, Preissner K T. Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization. Nat Med 1996; 2: 529-533.
    • (1996) Nat Med , vol.2 , pp. 529-533
    • Hammes, H.P.1    Brownlee, M.2    Joncyk, A.3    Sutter, A.4    Preissner, K.T.5
  • 65
    • 0001453577 scopus 로고    scopus 로고
    • Urokinase receptor antagonist inhibit angiogenesis and primary tumor growth in syngeneic mice
    • Min H Y, Doyle L V, Vitt C R, et al. Urokinase receptor antagonist inhibit angiogenesis and primary tumor growth in syngeneic mice. Cancer Res 1996; 56: 2428-2433.
    • (1996) Cancer Res , vol.56 , pp. 2428-2433
    • Min, H.Y.1    Doyle, L.V.2    Vitt, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.