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Volumn 39, Issue 4, 2013, Pages 347-355

Urokinase plasminogen activator receptor: A functional integrator of extracellular proteolysis, cell adhesion, and signal transduction

Author keywords

adhesion; proteolysis; signaling; uPAR; vitronectin

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; INTEGRIN; MITOGEN ACTIVATED PROTEIN KINASE P38; TYROSINE KINASE RECEPTOR; UROKINASE RECEPTOR; VITRONECTIN;

EID: 84878280950     PISSN: 00946176     EISSN: 10989064     Source Type: Journal    
DOI: 10.1055/s-0033-1334485     Document Type: Article
Times cited : (28)

References (79)
  • 1
    • 77949897126 scopus 로고    scopus 로고
    • Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation
    • Andronicos N. M., Chen E. I., Baik N., et al. Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation. Blood: 2010; 115 7 1319 1330
    • (2010) Blood , vol.115 , Issue.7 , pp. 1319-1330
    • Andronicos, N.M.1    Chen, E.I.2    Baik, N.3
  • 2
    • 0025883277 scopus 로고
    • Plasminogen activation by receptor-bound urokinase: A kinetic study with both cell-associated and isolated receptor
    • Ellis V., Behrendt N., Dano K. Plasminogen activation by receptor-bound urokinase. A kinetic study with both cell-associated and isolated receptor. J Biol Chem: 1991; 266 19 12752 12758 (Pubitemid 21907159)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.19 , pp. 12752-12758
    • Ellis, V.1    Behrendt, N.2    Dano, K.3
  • 3
    • 0030584083 scopus 로고    scopus 로고
    • Loss of fibrinogen rescues mice from the pleiotropic effects of plasminogen deficiency
    • DOI 10.1016/S0092-8674(00)81390-2
    • Bugge T. H., Kombrinck K. W., Flick M. J., Daugherty C. C., Danton M. J., Degen J. L. Loss of fibrinogen rescues mice from the pleiotropic effects of plasminogen deficiency. Cell: 1996; 87 4 709 719 (Pubitemid 26386944)
    • (1996) Cell , vol.87 , Issue.4 , pp. 709-719
    • Bugge, T.H.1    Kombrinck, K.W.2    Flick, M.J.3    Daugherty, C.C.4    Danton, M.J.S.5    Degen, J.L.6
  • 5
    • 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 2 783 792
    • (1990) J Cell Biol , vol.111 , Issue.2 , pp. 783-792
    • Estreicher, A.1    Mühlhauser, J.2    Carpentier, J.L.3    Orci, L.4    Vassalli, J.D.5
  • 6
    • 77956561594 scopus 로고    scopus 로고
    • Selective abrogation of the uPA-uPAR interaction in vivo reveals a novel role in suppression of fibrin-associated inflammation
    • Connolly B. M., Choi E. Y., Gårdsvoll H., et al. Selective abrogation of the uPA-uPAR interaction in vivo reveals a novel role in suppression of fibrin-associated inflammation. Blood: 2010; 116 9 1593 1603
    • (2010) Blood , vol.116 , Issue.9 , pp. 1593-1603
    • Connolly, B.M.1    Choi, E.Y.2    Gårdsvoll, H.3
  • 7
    • 0025273735 scopus 로고
    • Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1
    • Cubellis M. V., Wun T. C., Blasi F. Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1. EMBO J: 1990; 9 4 1079 1085
    • (1990) EMBO J , vol.9 , Issue.4 , pp. 1079-1085
    • Cubellis, M.V.1    Wun, T.C.2    Blasi, F.3
  • 10
    • 0025774971 scopus 로고
    • Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin
    • Seiffert D., Loskutoff D. J. Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin. J Biol Chem: 1991; 266 5 2824 2830 (Pubitemid 21909141)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.5 , pp. 2824-2830
    • Seiffert, D.1    Loskutoff, D.J.2
  • 11
    • 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? J Cell Biol: 1996; 134 6 1563 1571 (Pubitemid 26318027)
    • (1996) Journal of Cell Biology , vol.134 , Issue.6 , pp. 1563-1571
    • Deng, G.1    Curriden, S.A.2    Wang, S.3    Rosenberg, S.4    Loskutoff, D.J.5
  • 12
    • 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 Pt 3 867 873
    • (1995) Biochem J , vol.307 , Issue.PART 3 , pp. 867-873
    • Moser, T.L.1    Enghild, J.J.2    Pizzo, S.V.3    Stack, M.S.4
  • 13
    • 0025327959 scopus 로고
    • Specific binding of plasminogen to vitronectin. Evidence for a modulatory role of vitronectin on fibrin(ogen)-induced plasmin formation by tissue plasminogen activator
    • DOI 10.1016/0006-291X(90)91123-A
    • Preissner K. T. Specific binding of plasminogen to vitronectin. Evidence for a modulatory role of vitronectin on fibrin(ogen)-induced plasmin formation by tissue plasminogen activator. Biochem Biophys Res Commun: 1990; 168 3 966 971 (Pubitemid 20175974)
    • (1990) Biochemical and Biophysical Research Communications , vol.168 , Issue.3 , pp. 966-971
    • Preissner, K.T.1
  • 16
    • 0027174189 scopus 로고
    • Cytokines induce urokinase-dependent adhesion of human myeloid cells. A regulatory role for plasminogen activator inhibitors
    • Waltz D. A., Sailor L. Z., Chapman H. A. Cytokines induce urokinase-dependent adhesion of human myeloid cells. A regulatory role for plasminogen activator inhibitors. J Clin Invest: 1993; 91 4 1541 1552 (Pubitemid 23127356)
    • (1993) Journal of Clinical Investigation , vol.91 , Issue.4 , pp. 1541-1552
    • Waltz, D.A.1    Sailor, L.Z.2    Chapman, H.A.3
  • 17
    • 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 20 14746 14750 (Pubitemid 24194041)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.20 , pp. 14746-14750
    • Waltz, D.A.1    Chapman, H.A.2
  • 18
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • 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 vitronectin. J Biol Chem: 1994; 269 51 32380 32388
    • (1994) J Biol Chem , vol.269 , Issue.51 , pp. 32380-32388
    • Wei, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6
  • 19
    • 0037008781 scopus 로고    scopus 로고
    • Urokinase regulates vitronectin binding by controlling urokinase receptor oligomerization
    • DOI 10.1074/jbc.M111736200
    • Sidenius N., Andolfo A., Fesce R., Blasi F. Urokinase regulates vitronectin binding by controlling urokinase receptor oligomerization. J Biol Chem: 2002; 277 31 27982 27990 (Pubitemid 34966747)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 27982-27990
    • Sidenius, N.1    Andolfo, A.2    Fesce, R.3    Blasi, F.4
  • 20
    • 34250318934 scopus 로고    scopus 로고
    • Mapping of the vitronectin-binding site on the urokinase receptor involvement of a coherent receptor: Interface consisting of residues from both domain I and the flanking interdomain linker region
    • DOI 10.1074/jbc.M610184200
    • Gårdsvoll H., Ploug M. Mapping of the vitronectin-binding site on the urokinase receptor: involvement of a coherent receptor interface consisting of residues from both domain I and the flanking interdomain linker region. J Biol Chem: 2007; 282 18 13561 13572 (Pubitemid 47100512)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13561-13572
    • Gardsvoll, H.1    Ploug, M.2
  • 21
    • 84863125697 scopus 로고    scopus 로고
    • Crystal structure of the urokinase receptor in a ligand-free form
    • Xu X., Gårdsvoll H., Yuan C., Lin L., Ploug M., Huang M. Crystal structure of the urokinase receptor in a ligand-free form. J Mol Biol: 2012; 416 5 629 641
    • (2012) J Mol Biol , vol.416 , Issue.5 , pp. 629-641
    • Xu, X.1    Gårdsvoll, H.2    Yuan, C.3    Lin, L.4    Ploug, M.5    Huang, M.6
  • 22
    • 84867242361 scopus 로고    scopus 로고
    • A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR)
    • Mertens H. D., Kjaergaard M., Mysling S., et al. A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). J Biol Chem: 2012; 287 41 34304 34315
    • (2012) J Biol Chem , vol.287 , Issue.41 , pp. 34304-34315
    • Mertens, H.D.1    Kjaergaard, M.2    Mysling, S.3
  • 23
    • 0344442849 scopus 로고    scopus 로고
    • Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions
    • DOI 10.1093/emboj/cdg588
    • Cunningham O., Andolfo A., Santovito M. L., Iuzzolino L., Blasi F., Sidenius N. Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions. EMBO J: 2003; 22 22 5994 6003 (Pubitemid 37463243)
    • (2003) EMBO Journal , vol.22 , Issue.22 , pp. 5994-6003
    • Cunningham, O.1    Andolfo, A.2    Santovito, M.L.3    Iuzzolino, L.4    Blasi, F.5    Sidenius, N.6
  • 25
    • 0029931231 scopus 로고    scopus 로고
    • Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin
    • Deng G., Royle G., Wang S., Crain K., Loskutoff D. J. Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin. J Biol Chem: 1996; 271 22 12716 12723
    • (1996) J Biol Chem , vol.271 , Issue.22 , pp. 12716-12723
    • Deng, G.1    Royle, G.2    Wang, S.3    Crain, K.4    Loskutoff, D.J.5
  • 26
    • 20044363847 scopus 로고    scopus 로고
    • Urokinase-induced signaling in human vascular smooth muscle cells is mediated by PDGFR-β
    • DOI 10.1038/sj.emboj.7600669
    • Kiyan J., Kiyan R., Haller H., Dumler I. Urokinase-induced signaling in human vascular smooth muscle cells is mediated by PDGFR-beta. EMBO J: 2005; 24 10 1787 1797 (Pubitemid 40769498)
    • (2005) EMBO Journal , vol.24 , Issue.10 , pp. 1787-1797
    • Kiyan, J.1    Kiyan, R.2    Haller, H.3    Dumler, I.4
  • 27
    • 0036596352 scopus 로고    scopus 로고
    • EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma
    • DOI 10.1016/S1535-6108(02)00072-7
    • Liu D., Aguirre Ghiso J., Estrada Y., Ossowski L. EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma. Cancer Cell: 2002; 1 5 445 457 (Pubitemid 41039125)
    • (2002) Cancer Cell , vol.1 , Issue.5 , pp. 445-457
    • Liu, D.1    Aguirre Ghiso, J.A.2    Estrada, Y.3    Ossowski, L.4
  • 28
    • 84862650960 scopus 로고    scopus 로고
    • A transformation in the mechanism by which the urokinase receptor signals provides a selection advantage for estrogen receptor-expressing breast cancer cells in the absence of estrogen
    • Eastman B. M., Jo M., Webb D. L., Takimoto S., Gonias S. L. A transformation in the mechanism by which the urokinase receptor signals provides a selection advantage for estrogen receptor-expressing breast cancer cells in the absence of estrogen. Cell Signal: 2012; 24 9 1847 1855
    • (2012) Cell Signal , vol.24 , Issue.9 , pp. 1847-1855
    • Eastman, B.M.1    Jo, M.2    Webb, D.L.3    Takimoto, S.4    Gonias, S.L.5
  • 29
    • 0037449805 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent and -independent cell-signaling pathways originating from the urokinase receptor
    • DOI 10.1074/jbc.M210877200
    • Jo M., Thomas K. S., O'Donnell D. M., Gonias S. L. Epidermal growth factor receptor-dependent and -independent cell-signaling pathways originating from the urokinase receptor. J Biol Chem: 2003; 278 3 1642 1646 (Pubitemid 36801395)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 1642-1646
    • Jo, M.1    Thomas, K.S.2    O'Donnell, D.M.3    Gonias, S.L.4
  • 30
    • 0346725841 scopus 로고    scopus 로고
    • EGF receptor transactivation by urokinase receptor stimulus through a mechanism involving Src and matrix metalloproteinases
    • DOI 10.1016/j.yexcr.2003.08.011
    • Guerrero J., Santibañez J. F., González A., Martínez J. EGF receptor transactivation by urokinase receptor stimulus through a mechanism involving Src and matrix metalloproteinases. Exp Cell Res: 2004; 292 1 201 208 (Pubitemid 38058276)
    • (2004) Experimental Cell Research , vol.292 , Issue.1 , pp. 201-208
    • Guerrero, J.1    Santibanez, J.F.2    Gonzalez, A.3    Martinez, J.4
  • 31
    • 59349083983 scopus 로고    scopus 로고
    • UPAR-deficient mouse keratinocytes fail to produce EGFR-dependent laminin-5, affecting migration in vivo and in vitro
    • D'Alessio S., Gerasi L., Blasi F. uPAR-deficient mouse keratinocytes fail to produce EGFR-dependent laminin-5, affecting migration in vivo and in vitro. J Cell Sci: 2008; 121 Pt 23 3922 3932
    • (2008) J Cell Sci , vol.121 , Issue.PT 23 , pp. 3922-3932
    • D'Alessio, S.1    Gerasi, L.2    Blasi, F.3
  • 32
    • 34247340196 scopus 로고    scopus 로고
    • Urokinase receptor primes cells to proliferate in response to epidermal growth factor
    • DOI 10.1038/sj.onc.1210066, PII 1210066
    • Jo M., Thomas K. S., Takimoto S., et al. Urokinase receptor primes cells to proliferate in response to epidermal growth factor. Oncogene: 2007; 26 18 2585 2594 (Pubitemid 46632010)
    • (2007) Oncogene , vol.26 , Issue.18 , pp. 2585-2594
    • Jo, M.1    Thomas, K.S.2    Takimoto, S.3    Gaultier, A.4    Hsieh, E.H.5    Lester, R.D.6    Gonias, S.L.7
  • 33
    • 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 7 1572 1582 (Pubitemid 26112379)
    • (1996) EMBO Journal , vol.15 , Issue.7 , pp. 1572-1582
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3    Sidenius, N.4    Blasi, F.5    Fazioli, F.6
  • 34
    • 0031463337 scopus 로고    scopus 로고
    • A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity
    • DOI 10.1093/emboj/16.24.7279
    • Fazioli F., Resnati M., Sidenius N., Higashimoto Y., Appella E., Blasi F. A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity. EMBO J: 1997; 16 24 7279 7286 (Pubitemid 28010488)
    • (1997) EMBO Journal , vol.16 , Issue.24 , pp. 7279-7286
    • Fazioli, F.1    Resnati, M.2    Sidenius, N.3    Higashimoto, Y.4    Appella, E.5    Blasi, F.6
  • 35
    • 33744463114 scopus 로고    scopus 로고
    • The urokinase receptor: A ligand or a receptor? Story of a sociable molecule
    • DOI 10.1007/s00018-005-5428-1
    • Ragno P. The urokinase receptor: a ligand or a receptor? Story of a sociable molecule. Cell Mol Life Sci: 2006; 63 9 1028 1037 (Pubitemid 43800773)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.9 , pp. 1028-1037
    • Ragno, P.1
  • 37
    • 0035884209 scopus 로고    scopus 로고
    • Urokinase-catalysed cleavage of the urokinase receptor requires an intact glycolipid anchor
    • DOI 10.1042/0264-6021:3580673
    • Hoyer-Hansen G., Pessara U., Holm A., et al. Urokinase-catalysed cleavage of the urokinase receptor requires an intact glycolipid anchor. Biochem J: 2001; 358 Pt 3 673 679 (Pubitemid 32896955)
    • (2001) Biochemical Journal , vol.358 , Issue.3 , pp. 673-679
    • Hoyer-Hansen, G.1    Pessara, U.2    Holm, A.3    Pass, J.4    Weidle, U.5    Dano, K.6    Behrendt, N.7
  • 38
    • 0346736507 scopus 로고    scopus 로고
    • The cleavage of the urokinase receptor regulates its multiple functions
    • DOI 10.1074/jbc.M207494200
    • Montuori N., Carriero M. V., Salzano S., Rossi G., Ragno P. The cleavage of the urokinase receptor regulates its multiple functions. J Biol Chem: 2002; 277 49 46932 46939 (Pubitemid 36159197)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 46932-46939
    • Montuori, N.1    Carriero, M.V.2    Salzano, S.3    Rossi, G.4    Ragno, P.5
  • 39
    • 79960946347 scopus 로고    scopus 로고
    • The cross-talk between the urokinase receptor and fMLP receptors regulates the activity of the CXCR4 chemokine receptor
    • Montuori N., Bifulco K., Carriero M. V., et al. The cross-talk between the urokinase receptor and fMLP receptors regulates the activity of the CXCR4 chemokine receptor. Cell Mol Life Sci: 2011; 68 14 2453 2467
    • (2011) Cell Mol Life Sci , vol.68 , Issue.14 , pp. 2453-2467
    • Montuori, N.1    Bifulco, K.2    Carriero, M.V.3
  • 41
    • 66149167316 scopus 로고    scopus 로고
    • Regulation of urokinase receptor function and pericellular proteolysis by the integrin alpha(5)beta(1)
    • Bass R., Ellis V. Regulation of urokinase receptor function and pericellular proteolysis by the integrin alpha(5)beta(1). Thromb Haemost: 2009; 101 5 954 962
    • (2009) Thromb Haemost , vol.101 , Issue.5 , pp. 954-962
    • Bass, R.1    Ellis, V.2
  • 43
    • 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. III, Petty H. R. Physical association of complement receptor type 3 and urokinase-type plasminogen activator receptor in neutrophil membranes. J Immunol: 1994; 152 9 4630 4640
    • (1994) J Immunol , vol.152 , Issue.9 , pp. 4630-4640
    • Xue, W.1    Kindzelskii, A.L.2    Todd III, R.F.3    Petty, H.R.4
  • 44
    • 0028925552 scopus 로고
    • Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes
    • Bohuslav J., Horejsí V., Hansmann C., et al. Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes. J Exp Med: 1995; 181 4 1381 1390
    • (1995) J Exp Med , vol.181 , Issue.4 , pp. 1381-1390
    • Bohuslav, J.1    Horejsí, V.2    Hansmann, C.3
  • 45
    • 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 8 3185 3194 (Pubitemid 26357403)
    • (1996) Blood , vol.88 , Issue.8 , pp. 3185-3194
    • Simon, D.I.1    Rao, N.K.2    Xu, H.3    Wei, Y.4    Majdic, O.5    Ronne, E.6    Kobzik, L.7    Chapman, H.A.8
  • 49
    • 33744948988 scopus 로고    scopus 로고
    • A region in urokinase plasminogen receptor domain III controlling a functional association with α5β1 integrin and tumor growth
    • DOI 10.1074/jbc.M512311200
    • Chaurasia P., Aguirre-Ghiso J. A., Liang O. D., Gardsvoll H., Ploug M., Ossowski L. A region in urokinase plasminogen receptor domain III controlling a functional association with alpha5beta1 integrin and tumor growth. J Biol Chem: 2006; 281 21 14852 14863 (Pubitemid 43855190)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14852-14863
    • Chaurasia, P.1    Aguirre-Ghiso, J.A.2    Liang, O.D.3    Gardsvoll, H.4    Ploug, M.5    Ossowski, L.6
  • 51
    • 0035158527 scopus 로고    scopus 로고
    • Urokinase receptors promote β1 integrin function through interactions with integrin α3β1
    • Wei Y., Eble J. A., Wang Z., Kreidberg J. A., Chapman H. A. Urokinase receptors promote beta1 integrin function through interactions with integrin alpha3beta1. Mol Biol Cell: 2001; 12 10 2975 2986 (Pubitemid 33062955)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.10 , pp. 2975-2986
    • Wei, Y.1    Eble, J.A.2    Wang, Z.3    Kreidberg, J.A.4    Chapman, H.A.5
  • 53
    • 38049032013 scopus 로고    scopus 로고
    • Modification of kidney barrier function by the urokinase receptor
    • Wei C., Möller C. C., Altintas M. M., et al. Modification of kidney barrier function by the urokinase receptor. Nat Med: 2008; 14 1 55 63
    • (2008) Nat Med , vol.14 , Issue.1 , pp. 55-63
    • Wei, C.1    Möller, C.C.2    Altintas, M.M.3
  • 54
    • 50249145697 scopus 로고    scopus 로고
    • UPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180
    • Smith H. W., Marra P., Marshall C. J. uPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180. J Cell Biol: 2008; 182 4 777 790
    • (2008) J Cell Biol , vol.182 , Issue.4 , pp. 777-790
    • Smith, H.W.1    Marra, P.2    Marshall, C.J.3
  • 55
    • 0033549558 scopus 로고    scopus 로고
    • Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner
    • DOI 10.1083/jcb.146.1.149
    • Nguyen D. H., Catling A. D., Webb D. J., et al. Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner. J Cell Biol: 1999; 146 1 149 164 (Pubitemid 29349971)
    • (1999) Journal of Cell Biology , vol.146 , Issue.1 , pp. 149-164
    • Nguyen, D.H.D.1    Catling, A.D.2    Webb, D.J.3    Sankovic, M.4    Walker, L.A.5    Somlyo, A.V.6    Weber, M.J.7    Gonias, S.L.8
  • 56
    • 0035911966 scopus 로고    scopus 로고
    • Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin
    • DOI 10.1083/jcb.152.6.1145
    • Kjoller L., Hall A. Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin. J Cell Biol: 2001; 152 6 1145 1157 (Pubitemid 34280173)
    • (2001) Journal of Cell Biology , vol.152 , Issue.6 , pp. 1145-1157
    • Kjoller, L.1    Hall, A.2
  • 58
    • 33845241732 scopus 로고    scopus 로고
    • Vitronectin in human hepatic tumours contributes to the recruitment of lymphocytes in an αvΒ3-independent manner
    • DOI 10.1038/sj.bjc.6603467, PII 6603467
    • Edwards S., Lalor P. F., Tuncer C., Adams D. H. Vitronectin in human hepatic tumours contributes to the recruitment of lymphocytes in an alpha v beta3-independent manner. Br J Cancer: 2006; 95 11 1545 1554 (Pubitemid 44863358)
    • (2006) British Journal of Cancer , vol.95 , Issue.11 , pp. 1545-1554
    • Edwards1    Lalor, P.F.2    Tuncer, C.3    Adams, D.H.4
  • 59
    • 47249106994 scopus 로고    scopus 로고
    • A composite role of vitronectin and urokinase in the modulation of cell morphology upon expression of the urokinase receptor
    • Hillig T., Engelholm L. H., Ingvarsen S., et al. A composite role of vitronectin and urokinase in the modulation of cell morphology upon expression of the urokinase receptor. J Biol Chem: 2008; 283 22 15217 15223
    • (2008) J Biol Chem , vol.283 , Issue.22 , pp. 15217-15223
    • Hillig, T.1    Engelholm, L.H.2    Ingvarsen, S.3
  • 60
    • 83355169691 scopus 로고    scopus 로고
    • Mimicry of the regulatory role of urokinase in lamellipodia formation by introduction of a non-native interdomain disulfide bond in its receptor
    • Gårdsvoll H., Kjaergaard M., Jacobsen B., Kriegbaum M. C., Huang M., Ploug M. Mimicry of the regulatory role of urokinase in lamellipodia formation by introduction of a non-native interdomain disulfide bond in its receptor. J Biol Chem: 2011; 286 50 43515 43526
    • (2011) J Biol Chem , vol.286 , Issue.50 , pp. 43515-43526
    • Gårdsvoll, H.1    Kjaergaard, M.2    Jacobsen, B.3    Kriegbaum, M.C.4    Huang, M.5    Ploug, M.6
  • 61
    • 84866708012 scopus 로고    scopus 로고
    • Single amino acid substitutions in the chemotactic sequence of urokinase receptor modulate cell migration and invasion
    • Bifulco K., Longanesi-Cattani I., Franco P., et al. Single amino acid substitutions in the chemotactic sequence of urokinase receptor modulate cell migration and invasion. PLoS ONE: 2012; 7 9 e44806
    • (2012) PLoS ONE , vol.7 , Issue.9
    • Bifulco, K.1    Longanesi-Cattani, I.2    Franco, P.3
  • 62
    • 33748309166 scopus 로고    scopus 로고
    • Adhesion-mediated mechanosensitivity: A time to experiment, and a time to theorize
    • DOI 10.1016/j.ceb.2006.08.012, PII S0955067406001232
    • Bershadsky A., Kozlov M., Geiger B. Adhesion-mediated mechanosensitivity: a time to experiment, and a time to theorize. Curr Opin Cell Biol: 2006; 18 5 472 481 (Pubitemid 44332917)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.5 , pp. 472-481
    • Bershadsky, A.1    Kozlov, M.2    Geiger, B.3
  • 63
    • 0026680818 scopus 로고
    • Vitronectin regulates the synthesis and localization of urokinase-type plasminogen activator in HT-1080 cells
    • Ciambrone G. J., McKeown-Longo P. J. Vitronectin regulates the synthesis and localization of urokinase-type plasminogen activator in HT-1080 cells. J Biol Chem: 1992; 267 19 13617 13622
    • (1992) J Biol Chem , vol.267 , Issue.19 , pp. 13617-13622
    • Ciambrone, G.J.1    McKeown-Longo, P.J.2
  • 64
    • 0030320516 scopus 로고    scopus 로고
    • Localization of urokinase to focal adhesions by human fibrosarcoma cells synthesizing recombinant vitronectin
    • Wilcox S. A., Reho T., Higgins P. J., Tominna-Sebald E., McKeown-Longo P. J. Localization of urokinase to focal adhesions by human fibrosarcoma cells synthesizing recombinant vitronectin. Biochem Cell Biol: 1996; 74 6 899 910 (Pubitemid 126733750)
    • (1996) Biochemistry and Cell Biology , vol.74 , Issue.6 , pp. 899-910
    • McKeown-Longo, P.J.1
  • 65
    • 34249035764 scopus 로고    scopus 로고
    • The uPA receptor and the somatomedin B region of vitronectin direct the localization of uPA to focal adhesions in microvessel endothelial cells
    • DOI 10.1016/j.matbio.2007.01.009, PII S0945053X07000194
    • Salasznyk R. M., Zappala M., Zheng M., Yu L., Wilkins-Port C., McKeown-Longo P. J. The uPA receptor and the somatomedin B region of vitronectin direct the localization of uPA to focal adhesions in microvessel endothelial cells. Matrix Biol: 2007; 26 5 359 370 (Pubitemid 46803257)
    • (2007) Matrix Biology , vol.26 , Issue.5 , pp. 359-370
    • Salasznyk, R.M.1    Zappala, M.2    Zheng, M.3    Yu, L.4    Wilkins-Port, C.5    McKeown-Longo, P.J.6
  • 66
    • 0026644421 scopus 로고
    • Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain
    • Hoyer-Hansen G., Ronne E., Solberg H., et al. Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain. J Biol Chem: 1992; 267 25 18224 18229
    • (1992) J Biol Chem , vol.267 , Issue.25 , pp. 18224-18229
    • Hoyer-Hansen, G.1    Ronne, E.2    Solberg, H.3
  • 67
    • 0035874516 scopus 로고    scopus 로고
    • Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: Implication for angiogenesis in fibrin matrices
    • Koolwijk P., Sidenius N., Peters E., et al. Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: implication for angiogenesis in fibrin matrices. Blood: 2001; 97 10 3123 3131
    • (2001) Blood , vol.97 , Issue.10 , pp. 3123-3131
    • Koolwijk, P.1    Sidenius, N.2    Peters, E.3
  • 68
    • 0036332150 scopus 로고    scopus 로고
    • Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor
    • Andolfo A., English W. R., Resnati M., Murphy G., Blasi F., Sidenius N. Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor. Thromb Haemost: 2002; 88 2 298 306 (Pubitemid 34873713)
    • (2002) Thrombosis and Haemostasis , vol.88 , Issue.2 , pp. 298-306
    • Andolfo, A.1    English, W.R.2    Resnati, M.3    Murphy, G.4    Blasi, F.5    Sidenius, N.6
  • 70
    • 0026644421 scopus 로고
    • Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain
    • Hoyer-Hansen G., Ronne E., Solberg H., et al. Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain. J Biol Chem: 1992; 267 25 18224 18229
    • (1992) J Biol Chem , vol.267 , Issue.25 , pp. 18224-18229
    • Hoyer-Hansen, G.1    Ronne, E.2    Solberg, H.3
  • 71
    • 33845666597 scopus 로고    scopus 로고
    • Domain 1 of the urokinase-type plasminogen activator receptor is required for its morphologic and functional, β2 integrin-mediated connection with actin cytoskeleton in human microvascular endothelial cells: Failure of association in systemic sclerosis endothelial cells
    • DOI 10.1002/art.22263
    • Margheri F., Manetti M., Serratì S., et al. Domain 1 of the urokinase-type plasminogen activator receptor is required for its morphologic and functional, beta2 integrin-mediated connection with actin cytoskeleton in human microvascular endothelial cells: failure of association in systemic sclerosis endothelial cells. Arthritis Rheum: 2006; 54 12 3926 3938 (Pubitemid 44955896)
    • (2006) Arthritis and Rheumatism , vol.54 , Issue.12 , pp. 3926-3938
    • Margheri, F.1    Manetti, M.2    Serrati, S.3    Nosi, D.4    Pucci, M.5    Matucci-Cerinic, M.6    Kahaleh, B.7    Bazzichi, L.8    Fibbi, G.9    Ibba-Manneschi, L.10    Del Rosso, M.11
  • 72
    • 84873278736 scopus 로고    scopus 로고
    • UPAR regulates pericellular proteolysis through a mechanism involving integrins and fMLF-receptors
    • Montuori N., Cosimato V., Rinaldi L., Rea V. E., Alfano D., Ragno P. uPAR regulates pericellular proteolysis through a mechanism involving integrins and fMLF-receptors. Thromb Haemost: 2012; 109 2 109
    • (2012) Thromb Haemost , vol.109 , Issue.2 , pp. 109
    • Montuori, N.1    Cosimato, V.2    Rinaldi, L.3    Rea, V.E.4    Alfano, D.5    Ragno, P.6
  • 73
    • 21644432642 scopus 로고    scopus 로고
    • Domain 2 of the urokinase receptor contains an integrin-interacting epitope with intrinsic signaling activity: Generation of a new integrin inhibitor
    • DOI 10.1074/jbc.M413954200
    • Degryse B., Resnati M., Czekay R. P., Loskutoff D. J., Blasi F. Domain 2 of the urokinase receptor contains an integrin-interacting epitope with intrinsic signaling activity: generation of a new integrin inhibitor. J Biol Chem: 2005; 280 26 24792 24803 (Pubitemid 40934570)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24792-24803
    • Degryse, B.1    Resnati, M.2    Czekay, R.-P.3    Loskutoff, D.J.4    Blasi, F.5
  • 77
    • 0031583964 scopus 로고    scopus 로고
    • The intact urokinase receptor is required for efficient vitronectin binding: Receptor cleavage prevents ligand interaction
    • DOI 10.1016/S0014-5793(97)01491-9, PII S0014579397014919
    • Hoyer-Hansen G., Behrendt N., Ploug M., Dano K., Preissner K. T. The intact urokinase receptor is required for efficient vitronectin binding: receptor cleavage prevents ligand interaction. FEBS Lett: 1997; 420 1 79 85 (Pubitemid 28037204)
    • (1997) FEBS Letters , vol.420 , Issue.1 , pp. 79-85
    • Hoyer-Hansen, G.1    Behrendt, N.2    Ploug, M.3    Dano, K.4    Preissner, K.T.5
  • 78
    • 0034678053 scopus 로고    scopus 로고
    • Domain 1 of the urokinase receptor (uPAR) is required for uPAR-mediated cell binding to vitronectin
    • DOI 10.1016/S0014-5793(00)01282-5, PII S0014579300012825
    • Sidenius N., Blasi F. Domain 1 of the urokinase receptor (uPAR) is required for uPAR-mediated cell binding to vitronectin. FEBS Lett: 2000; 470 1 40 46 (Pubitemid 30155620)
    • (2000) FEBS Letters , vol.470 , Issue.1 , pp. 40-46
    • Sidenius, N.1    Blasi, F.2
  • 79
    • 0025911764 scopus 로고
    • Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1
    • Chain D., Kreizman T., Shapira H., Shaltiel S. Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1. FEBS Lett: 1991; 285 2 251 256
    • (1991) FEBS Lett , vol.285 , Issue.2 , pp. 251-256
    • Chain, D.1    Kreizman, T.2    Shapira, H.3    Shaltiel, S.4


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