메뉴 건너뛰기




Volumn 287, Issue 27, 2012, Pages 22450-22462

Dissecting mannose 6-phosphate-insulin-like growth factor 2 receptor complexes that control activation and uptake of plasminogen in cells

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MOLECULES; CELL MIGRATION; CELL SURFACES; ENDOCYTIC PATHWAYS; GROWTH FACTOR; HUMAN CELL LINES; IN-VITRO; KNOCK OUTS; LIPID RAFT; LYSATES; MOUSE EMBRYONIC FIBROBLASTS; PATHOLOGICAL PROCESS; RECEPTOR COMPLEX; REGULATORY FACTORS; REGULATORY FUNCTIONS; SPECIFIC SITES; UROKINASE-TYPE PLASMINOGEN ACTIVATOR;

EID: 84863313484     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.339663     Document Type: Article
Times cited : (17)

References (65)
  • 2
    • 16844384895 scopus 로고    scopus 로고
    • Structure and function of the plasminogen/plasmin system
    • DOI 10.1160/TH04-12-0842
    • Castellino, F. J., and Ploplis, V. A. (2005) Structure and function of the plasminogen/plasmin system. Thromb. Haemost. 93, 647-654 (Pubitemid 40485399)
    • (2005) Thrombosis and Haemostasis , vol.93 , Issue.4 , pp. 647-654
    • Castellino, F.J.1    Ploplis, V.A.2
  • 5
    • 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., Bai, H., Parmer, C. M., Kiosses, W. B., Kamps, M. P., Yates, J. R., 3rd, Parmer, R. J., and Miles, L. A. (2010) Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation. Blood 115, 1319-1330
    • (2010) Blood , vol.115 , pp. 1319-1330
    • Andronicos, N.M.1    Chen, E.I.2    Baik, N.3    Bai, H.4    Parmer, C.M.5    Kiosses, W.B.6    Kamps, M.P.7    Yates III, J.R.8    Parmer, R.J.9    Miles, L.A.10
  • 6
    • 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., and Sidenius, N. (2003) Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions. EMBO J. 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
  • 7
    • 33744463114 scopus 로고    scopus 로고
    • The urokinase receptor. A ligand or a receptor? Story of a sociable molecule
    • Ragno, P. (2006) The urokinase receptor. A ligand or a receptor? Story of a sociable molecule. Cell. Mol. Life Sci. 63, 1028-1037
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1028-1037
    • Ragno, P.1
  • 8
    • 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., and Ragno, P. (2002) The cleavage of the urokinase receptor regulates its multiple functions. J. Biol. Chem. 277, 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
  • 9
    • 0035860127 scopus 로고    scopus 로고
    • The topology of plasminogen binding and activation on the surface of human breast cancer cells
    • DOI 10.1054/bjoc.2001.2022
    • Andronicos, N. M., and Ranson, M. (2001) The topology of plasminogen binding and activation on the surface of human breast cancer cells. Br. J. Cancer 85, 909-916 (Pubitemid 33010561)
    • (2001) British Journal of Cancer , vol.85 , Issue.6 , pp. 909-916
    • Andronicos, N.M.1    Ranson, M.2
  • 10
    • 0642308407 scopus 로고    scopus 로고
    • Plasminogen activation at the cell surface
    • Ellis, V. (2003) Plasminogen activation at the cell surface. Curr. Top. Dev. Biol. 54, 263-312
    • (2003) Curr. Top. Dev. Biol. , vol.54 , pp. 263-312
    • Ellis, V.1
  • 14
    • 61349170301 scopus 로고    scopus 로고
    • Interactions of IGF-II with the IGF2R/cation-independent mannose 6-phosphate receptor mechanism and biological outcomes
    • Brown, J., Jones, E. Y., and Forbes, B. E. (2009) Interactions of IGF-II with the IGF2R/cation-independent mannose 6-phosphate receptor mechanism and biological outcomes. Vitam. Horm. 80, 699-719
    • (2009) Vitam. Horm. , vol.80 , pp. 699-719
    • Brown, J.1    Jones, E.Y.2    Forbes, B.E.3
  • 15
    • 61349146609 scopus 로고    scopus 로고
    • Insulin-like growth factor-2/mannose-6 phosphate receptors
    • El-Shewy, H. M., and Luttrell, L. M. (2009) Insulin-like growth factor-2/mannose-6 phosphate receptors. Vitam. Horm. 80, 667-697
    • (2009) Vitam. Horm. , vol.80 , pp. 667-697
    • El-Shewy, H.M.1    Luttrell, L.M.2
  • 16
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • DOI 10.1038/nrm1050
    • Ghosh, P., Dahms, N. M., and Kornfeld, S. (2003) Mannose 6-phosphate receptors. New twists in the tale. Nat. Rev. Mol. Cell Biol. 4, 202-212 (Pubitemid 36288042)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 17
    • 0344026339 scopus 로고    scopus 로고
    • M6P/IGFII-receptor complexes urokinase receptor and plasminogen for activation of transforming growth factor-β1
    • Godár, S., Horejsi, V., Weidle, U. H., Binder, B. R., Hansmann, C., and Stockinger, H. (1999) M6P/IGFII receptor complexes urokinase receptor and plasminogen for activation of transforming growth factor-β1. Eur. J. Immunol. 29, 1004-1013 (Pubitemid 29119081)
    • (1999) European Journal of Immunology , vol.29 , Issue.3 , pp. 1004-1013
    • Godar, S.1    Horejsi, V.2    Weidle, U.H.3    Binder, B.R.4    Hansmann, C.5    Stockinger, H.6
  • 18
    • 0037174862 scopus 로고    scopus 로고
    • The N terminus of mannose 6-phosphate/insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration
    • DOI 10.1074/jbc.M207979200
    • Leksa, V., Godár, S., Cebecauer, M., Hilgert, I., Breuss, J., Weidle, U. H., Horejsí, V., Binder, B. R., and Stockinger, H. (2002) The N terminus of mannose 6-phosphate/insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration. J. Biol. Chem. 277, 40575-40582 (Pubitemid 35215637)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40575-40582
    • Leksa, V.1    Godar, S.2    Cebecauer, M.3    Hilgert, I.4    Breuss, J.5    Weidle, U.H.6    Horejsi, V.7    Binder, B.R.8    Stockinger, H.9
  • 20
    • 2942558373 scopus 로고    scopus 로고
    • Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor
    • DOI 10.1038/sj.emboj.7600215
    • Olson, L. J., Yammani, R. D., Dahms, N. M., and Kim, J. J. (2004) Structure of uPAR, plasminogen, and sugar-binding sites of the 300-kDa mannose 6-phosphate receptor. EMBO J. 23, 2019-2028 (Pubitemid 38737729)
    • (2004) EMBO Journal , vol.23 , Issue.10 , pp. 2019-2028
    • Olson, L.J.1    Yammani, R.D.2    Dahms, N.M.3    Kim, J.-J.P.4
  • 21
    • 64049103845 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor 2 receptor limits cell invasion by controlling αVβ3 integrin expression and proteolytic processing of urokinase-type plasminogen activator receptor
    • Schiller, H. B., Szekeres, A., Binder, B. R., Stockinger, H., and Leksa, V. (2009) Mannose 6-phosphate/insulin-like growth factor 2 receptor limits cell invasion by controlling αVβ3 integrin expression and proteolytic processing of urokinase-type plasminogen activator receptor. Mol. Biol. Cell 20, 745-756
    • (2009) Mol. Biol. Cell , vol.20 , pp. 745-756
    • Schiller, H.B.1    Szekeres, A.2    Binder, B.R.3    Stockinger, H.4    Leksa, V.5
  • 23
    • 33645553587 scopus 로고    scopus 로고
    • Direct interaction of the kringle domain of urokinase-type plasminogen activator (uPA) and integrin αvβ3 induces signal transduction and enhances plasminogen activation
    • Tarui, T., Akakura, N., Majumdar, M., Andronicos, N., Takagi, J., Mazar, A. P., Bdeir, K., Kuo, A., Yarovoi, S. V., Cines, D. B., and Takada, Y. (2006) Direct interaction of the kringle domain of urokinase-type plasminogen activator (uPA) and integrin αvβ3 induces signal transduction and enhances plasminogen activation. Thromb. Haemost. 95, 524-534
    • (2006) Thromb. Haemost. , vol.95 , pp. 524-534
    • Tarui, T.1    Akakura, N.2    Majumdar, M.3    Andronicos, N.4    Takagi, J.5    Mazar, A.P.6    Bdeir, K.7    Kuo, A.8    Yarovoi, S.V.9    Cines, D.B.10    Takada, Y.11
  • 24
    • 0037072784 scopus 로고    scopus 로고
    • Plasmin-induced migration of endothelial cells. A potential target for the anti-angiogenic action of angiostatin
    • Tarui, T., Majumdar, M., Miles, L. A., Ruf, W., and Takada, Y. (2002) Plasmin-induced migration of endothelial cells. A potential target for the anti-angiogenic action of angiostatin. J. Biol. Chem. 277, 33564-33570
    • (2002) J. Biol. Chem. , vol.277 , pp. 33564-33570
    • Tarui, T.1    Majumdar, M.2    Miles, L.A.3    Ruf, W.4    Takada, Y.5
  • 25
    • 26144478319 scopus 로고    scopus 로고
    • Mason, D., Andre, P., Bensussan, A., Buckley, C., Civin, C., Clark, E., de Haas, M., Goyert, S., Hadam, M., Hart, D., Horejsi, V., Jones, Y., Meuer, S., Morrissey, J., Schwarz-Albiez, R., Shaw, S., Simmons, D., Turni, L., Uguccioni, M., van der Schoot, E., Vivier, E., and Zola, H., eds. Oxford University Press, Oxford, New York, Tokyo
    • Godár, S., Leksa, V., Cebecauer, M., Hilgert, I., Horejsi, V., and Stockinger, H. (2002) in Leukocyte Typing VII (Mason, D., Andre, P., Bensussan, A., Buckley, C., Civin, C., Clark, E., de Haas, M., Goyert, S., Hadam, M., Hart, D., Horejsi, V., Jones, Y., Meuer, S., Morrissey, J., Schwarz-Albiez, R., Shaw, S., Simmons, D., Turni, L., Uguccioni, M., van der Schoot, E., Vivier, E., and Zola, H., eds.) pp. 482-485, Oxford University Press, Oxford, New York, Tokyo
    • (2002) Leukocyte Typing VII , pp. 482-485
    • Godár, S.1    Leksa, V.2    Cebecauer, M.3    Hilgert, I.4    Horejsi, V.5    Stockinger, H.6
  • 26
    • 0027962976 scopus 로고
    • An efficient expression, purification and immunodetection system for recombinant gene products
    • Baier, G., Baier-Bitterlich, G., Couture, C., Telford, D., Giampa, L., and Altman, A. (1994) An efficient expression, purification, and immunodetection system for recombinant gene products Biotechniques 17, 94-99 (Pubitemid 2114948)
    • (1994) BioTechniques , vol.17 , Issue.1 , pp. 94-99
    • Baier, G.1    Baier-Bitterlich, G.2    Couture, C.3    Telford, D.4    Giampa, L.5    Altman, A.6
  • 27
    • 0003059314 scopus 로고    scopus 로고
    • Coligan, J. E., Kruisbeek, A. M., Margulies, D. H., Shevach, E. M., and Strober, W., eds Green Publishing Associates and Wiley-Interscience, New York
    • Swift, S., Lorens, J., Achacoso, P., and Nolan, G. P. (1999) in Current Protocols in Immunology (Coligan, J. E., Kruisbeek, A. M., Margulies, D. H., Shevach, E. M., and Strober, W., eds) pp. 10.17.14-10.17.29, Green Publishing Associates and Wiley-Interscience, New York
    • (1999) Current Protocols in Immunology
    • Swift, S.1    Lorens, J.2    Achacoso, P.3    Nolan, G.P.4
  • 28
    • 0029018537 scopus 로고
    • Expression of the human urokinase-type plasminogen activator receptor in E. coli and Chinese hamster ovary cells. Purification of the recombinant proteins and generation of polyclonal antibodies in chicken
    • Magdolen, V., Rettenberger, P., Lopens, A., Oi, H., Lottspeich, F., Kellermann, J., Creutzburg, S., Goretzki, L., Weidle, U. H., and Wilhelm, O. (1995) Expression of the human urokinase-type plasminogen activator receptor in E. coli and Chinese hamster ovary cells. Purification of the recombinant proteins and generation of polyclonal antibodies in chicken. Electrophoresis 16, 813-816
    • (1995) Electrophoresis , vol.16 , pp. 813-816
    • Magdolen, V.1    Rettenberger, P.2    Lopens, A.3    Oi, H.4    Lottspeich, F.5    Kellermann, J.6    Creutzburg, S.7    Goretzki, L.8    Weidle, U.H.9    Wilhelm, O.10
  • 29
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L., Blömer, U., Gallay, P., Ory, D., Mulligan, R., Gage, F. H., Verma, I. M., and Trono, D. (1996) In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272, 263-267 (Pubitemid 26119138)
    • (1996) Science , vol.272 , Issue.5259 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 30
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • DOI 10.1006/abio.1994.1112
    • Schägger, H., Cramer, W. A., and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230 (Pubitemid 24080754)
    • (1994) Analytical Biochemistry , vol.217 , Issue.2 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 31
    • 2642529334 scopus 로고    scopus 로고
    • Two-dimensional Blue Native/SDS gel electrophoresiss of multi-protein complexes from whole cellular lysates: A proteomics approach
    • DOI 10.1074/mcp.T300010-MCP200
    • Camacho-Carvajal, M. M., Wollscheid, B., Aebersold, R., Steimle, V., and Schamel, W. W. (2004) Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates.Aproteomics approach. Mol. Cell Proteomics 3, 176-182 (Pubitemid 38714275)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.2 , pp. 176-182
    • Camacho-Carvcajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.A.5
  • 32
    • 0026558556 scopus 로고
    • Urokinase activity in the developing avian heart. A spatial and temporal analysis
    • McGuire, P. G., and Orkin, R. W. (1992) Urokinase activity in the developing avian heart. A spatial and temporal analysis. Dev. Dyn. 193, 24-33
    • (1992) Dev. Dyn. , vol.193 , pp. 24-33
    • McGuire, P.G.1    Orkin, R.W.2
  • 33
    • 0037732938 scopus 로고    scopus 로고
    • Inhibition of plasminogen activation protects against ganglion cell loss in a mouse model of retinal damage
    • Zhang, X., Chaudhry, A., and Chintala, S. K. (2003) Inhibition of plasminogen activation protects against ganglion cell loss in a mouse model of retinal damage. Mol. Vis. 9, 238-248 (Pubitemid 38097593)
    • (2003) Molecular Vision , vol.9 , pp. 238-248
    • Zhang, X.1    Chaudhry, A.2    Chintala, S.K.3
  • 34
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts. New tools and insights
    • Simons, K., and Gerl, M. J. (2010) Revitalizing membrane rafts. New tools and insights. Nat. Rev. Mol. Cell Biol. 11, 688-699
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 35
    • 77951643625 scopus 로고    scopus 로고
    • A new type of membrane raft-like microdomains and their possible involvement in TCR signaling
    • Otáhal, P., Angelisová, P., Hrdinka, M., Brdicka, T., Novák, P., Drbal, K., and Horejsí, V. (2010) A new type of membrane raft-like microdomains and their possible involvement in TCR signaling. J. Immunol. 184, 3689-3696
    • (2010) J. Immunol. , vol.184 , pp. 3689-3696
    • Otáhal, P.1    Angelisová, P.2    Hrdinka, M.3    Brdicka, T.4    Novák, P.5    Drbal, K.6    Horejsí, V.7
  • 37
    • 0036369295 scopus 로고    scopus 로고
    • Urokinase as a multidomain protein and polyfunctional cell regulator
    • Stepanova, V. V., and Tkachuk, V. A. (2002) Urokinase as a multidomain protein and polyfunctional cell regulator. Biochemistry 67, 109-118
    • (2002) Biochemistry , vol.67 , pp. 109-118
    • Stepanova, V.V.1    Tkachuk, V.A.2
  • 38
    • 0026321613 scopus 로고
    • Effects of brefeldin A on the endocytic route: Redistribution of mannose 6-phosphate/insulin-like growth factor II receptors to the cell surface
    • Damke, H., Klumperman, J., von Figura, K., and Braulke, T. (1991) Effects of brefeldin A on the endocytic route. Redistribution of mannose 6-phosphate/insulin-like growth factor II receptors to the cell surface. J. Biol. Chem. 266, 24829-24833 (Pubitemid 21909015)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.36 , pp. 24829-24833
    • Damke, H.1    Klumperman, J.2    Von Figura, K.3    Braulke, T.4
  • 39
    • 0742288050 scopus 로고    scopus 로고
    • Endocytosed Cation-Independent Mannose 6-Phosphate Receptor Traffics via the Endocytic Recycling Compartment en Route to the trans-Golgi Network and a Subpopulation of Late Endosomes
    • DOI 10.1091/mbc.E03-07-0497
    • Lin, S. X., Mallet, W. G., Huang, A. Y., and Maxfield, F. R. (2004) Endocytosed cation-independent mannose 6-phosphate receptor traffics via the endocytic recycling compartment en route to the trans-Golgi network and a subpopulation of late endosomes. Mol. Biol. Cell 15, 721-733 (Pubitemid 38146488)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 721-733
    • Lin, S.X.1    Mallet, W.G.2    Huang, A.Y.3    Maxfield, F.R.4
  • 40
    • 0028085865 scopus 로고
    • Quantification of low density lipoprotein and transferrin endocytic sorting in HEp2 cells using confocal microscopy
    • Ghosh, R. N., Gelman, D. L., and Maxfield, F. R. (1994) Quantification of low density lipoprotein and transferrin endocytic sorting HEp2 cells using confocal microscopy. J. Cell Sci. 107, 2177-2189 (Pubitemid 24273484)
    • (1994) Journal of Cell Science , vol.107 , Issue.8 , pp. 2177-2189
    • Ghosh, R.N.1    Gelman, D.L.2    Maxfield, F.R.3
  • 44
    • 0034635387 scopus 로고    scopus 로고
    • Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes
    • DOI 10.1074/jbc.275.6.3745
    • Rubino, M., Miaczynska, M., Lippé, R., and Zerial, M. (2000) Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes. J. Biol. Chem. 275, 3745-3748 (Pubitemid 30094593)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3745-3748
    • Rubino, M.1    Miaczynska, M.2    Lippe, R.3    Zerial, M.4
  • 45
    • 0032540248 scopus 로고    scopus 로고
    • Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages: Enrichment of cathepsin H in early endosomes
    • DOI 10.1074/jbc.273.16.9842
    • Claus, V., Jahraus, A., Tjelle, T., Berg, T., Kirschke, H., Faulstich, H., and Griffiths, G. (1998) Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes. J. Biol. Chem. 273, 9842-9851 (Pubitemid 28183080)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9842-9851
    • Claus, V.1    Jahraus, A.2    Tjelle, T.3    Berg, T.4    Kirschke, H.5    Faulstich, H.6    Griffiths, G.7
  • 46
    • 0036566039 scopus 로고    scopus 로고
    • Endolysosomal proteolysis and its regulation
    • DOI 10.1042/0264-6021:3630417
    • Pillay, C. S., Elliott, E., and Dennison, C. (2002) Endolysosomal proteolysis and its regulation. Biochem. J. 363, 417-429 (Pubitemid 34526362)
    • (2002) Biochemical Journal , vol.363 , Issue.3 , pp. 417-429
    • Pillay, C.S.1    Elliott, E.2    Dennison, C.3
  • 47
    • 0030463150 scopus 로고    scopus 로고
    • Isolation and characterization of early endosomes, late endosomes and terminal lysosomes: Their role in protein degradation
    • Tjelle, T. E., Brech, A., Juvet, L. K., Griffiths, G., and Berg, T. (1996) Isolation and characterization of early endosomes, late endosomes, and terminal lysosomes. Their role in protein degradation. J. Cell Sci. 109, 2905-2914 (Pubitemid 27029261)
    • (1996) Journal of Cell Science , vol.109 , Issue.12 , pp. 2905-2914
    • Tjelle, T.E.1    Brech, A.2    Juvet, L.K.3    Griffiths, G.4    Berg, T.5
  • 48
    • 56649115742 scopus 로고    scopus 로고
    • Clathrin and LRP-1-independent constitutive endocytosis and recycling of uPAR
    • Cortese, K., Sahores, M., Madsen, C. D., Tacchetti, C., and Blasi, F. (2008) Clathrin and LRP-1-independent constitutive endocytosis and recycling of uPAR. PLoS One 3, e3730
    • (2008) PLoS One , vol.3
    • Cortese, K.1    Sahores, M.2    Madsen, C.D.3    Tacchetti, C.4    Blasi, F.5
  • 49
    • 0034756167 scopus 로고    scopus 로고
    • Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity
    • Czekay, R. P., Kuemmel, T. A., Orlando, R. A., and Farquhar, M. G. (2001) Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity. Mol. Biol. Cell 12, 1467-1479 (Pubitemid 33044425)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.5 , pp. 1467-1479
    • Czekay, R.-P.1    Kuemmel, T.A.2    Orlando, R.A.3    Farquhar, M.G.4
  • 50
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • DOI 10.1172/JCI200113992
    • Herz, J., and Strickland, D. K. (2001) LRP. A multifunctional scavenger and signaling receptor. J. Clin. Invest. 108, 779-784 (Pubitemid 32880284)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.6 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 51
    • 80051682259 scopus 로고    scopus 로고
    • Regulation of the urokinase receptor (uPAR) by LDL receptor-related protein-1 (LRP1)
    • Gonias, S. L., Gaultier, A., and Jo, M. (2011) Regulation of the urokinase receptor (uPAR) by LDL receptor-related protein-1 (LRP1). Curr. Pharm. Des. 17, 1962-1969
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 1962-1969
    • Gonias, S.L.1    Gaultier, A.2    Jo, M.3
  • 52
    • 0034977870 scopus 로고    scopus 로고
    • The urokinase receptor associated protein (uPARAP/Endo180): A novel internalization receptor connected to the plasminogen activation system
    • DOI 10.1016/S1050-1738(01)00076-7, PII S1050173801000767
    • Engelholm, L. H., Nielsen, B. S., Danø, K., and Behrendt, N. (2001) The urokinase receptor associated protein (uPARAP/endo180). A novel internalization receptor connected to the plasminogen activation system. Trends Cardiovasc. Med. 11, 7-13 (Pubitemid 32547233)
    • (2001) Trends in Cardiovascular Medicine , vol.11 , Issue.1 , pp. 7-13
    • Engelholm, L.H.1    Nielsen, B.S.2    Dano, K.3    Behrendt, N.4
  • 54
    • 3042784666 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-2-induced initial endothelial cell migration depends on the presence of the urokinase receptor
    • DOI 10.1161/01.RES.0000131498.36194.6b
    • Prager, G. W., Breuss, J. M., Steurer, S., Olcaydu, D., Mihaly, J., Brunner, P. M., Stockinger, H., and Binder, B. R. (2004) Vascular endothelial growth factor receptor-2-induced initial endothelial cell migration depends on the presence of the urokinase receptor. Circ. Res. 94, 1562-1570 (Pubitemid 38856963)
    • (2004) Circulation Research , vol.94 , Issue.12 , pp. 1562-1570
    • Prager, G.W.1    Breuss, J.M.2    Steurer, S.3    Olcaydu, D.4    Mihaly, J.5    Brunner, P.M.6    Stockinger, H.7    Binder, B.R.8
  • 55
    • 0035511837 scopus 로고    scopus 로고
    • Cytokeratin 8 functions as a major plasminogen receptor in select epithelial and carcinoma cells
    • Gonias, S. L., Hembrough, T. A., and Sankovic, M. (2001) Cytokeratin 8 functions as a major plasminogen receptor in select epithelial and carcinoma cells. Front. Biosci. 6, D1403-D1411
    • (2001) Front. Biosci. , vol.6
    • Gonias, S.L.1    Hembrough, T.A.2    Sankovic, M.3
  • 56
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II
    • Hajjar, K. A., Jacovina, A. T., and Chacko, J. (1994) An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. J. Biol. Chem. 269, 21191-21197
    • (1994) J. Biol. Chem. , vol.269 , pp. 21191-21197
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 57
    • 38449115465 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPP IV/CD26) is a cell-surface plasminogen receptor
    • DOI 10.2741/2785
    • Gonzalez-Gronow, M., Kaczowka, S., Gawdi, G., and Pizzo, S. V. (2008) Dipeptidyl peptidase IV (DPP IV/CD26) is a cell-surface plasminogen receptor. Front. Biosci. 13, 1610-1618 (Pubitemid 351599720)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.5 , pp. 1610-1618
    • Gonzalez-Gronow, M.1    Kaczowka, S.2    Gawdi, G.3    Pizzo, S.V.4
  • 58
    • 80155192757 scopus 로고    scopus 로고
    • Plasminogen receptor S100A10 is essential for the migration of tumor-promoting macrophages into tumor sites
    • Phipps, K. D., Surette, A. P., O'Connell, P. A., and Waisman, D. M. (2011) Plasminogen receptor S100A10 is essential for the migration of tumor-promoting macrophages into tumor sites. Cancer Res. 71, 6676-6683
    • (2011) Cancer Res. , vol.71 , pp. 6676-6683
    • Phipps, K.D.1    Surette, A.P.2    O'Connell, P.A.3    Waisman, D.M.4
  • 59
    • 0034707048 scopus 로고    scopus 로고
    • Binding of disease-associated prion protein to plasminogen
    • Fischer, M. B., Roeckl, C., Parizek, P., Schwarz, H. P., and Aguzzi, A. (2000) Binding of disease-associated prion protein to plasminogen. Nature 408, 479-483
    • (2000) Nature , vol.408 , pp. 479-483
    • Fischer, M.B.1    Roeckl, C.2    Parizek, P.3    Schwarz, H.P.4    Aguzzi, A.5
  • 60
    • 57749189817 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • Rijken, D. C., and Lijnen, H. R. (2009) New insights into the molecular mechanisms of the fibrinolytic system. J. Thromb. Haemost. 7, 4-13
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 4-13
    • Rijken, D.C.1    Lijnen, H.R.2
  • 61
    • 0033547790 scopus 로고    scopus 로고
    • Assembly of urokinase receptor-mediated plasminogen activation complexes involves direct, non-active-site interactions between urokinase and plasminogen
    • Ellis, V., Whawell, S. A., Werner, F., and Deadman, J. J. (1999) Assembly of urokinase receptor-mediated plasminogen activation complexes involves direct, non-active-site interactions between urokinase and plasminogen. Biochemistry 38, 651-659
    • (1999) Biochemistry , vol.38 , pp. 651-659
    • Ellis, V.1    Whawell, S.A.2    Werner, F.3    Deadman, J.J.4
  • 62
    • 34248195625 scopus 로고    scopus 로고
    • Plasminogen binding and activation at the breast cancer cell surface. The integral role of urokinase activity
    • Stillfried, G. E., Saunders, D. N., and Ranson, M. (2007) Plasminogen binding and activation at the breast cancer cell surface. The integral role of urokinase activity. Breast Cancer Res. 9, R14
    • (2007) Breast Cancer Res. , vol.9
    • Stillfried, G.E.1    Saunders, D.N.2    Ranson, M.3
  • 63
    • 0030666519 scopus 로고    scopus 로고
    • The atherogenic lipoprotein Lp(a) is internalized and degraded in a process mediated by the VLDL receptor
    • Argraves, K. M., Kozarsky, K. F., Fallon, J. T., Harpel, P. C., and Strickland, D. K. (1997) The atherogenic lipoprotein Lp(a) is internalized and degraded in a process mediated by the VLDL receptor. J. Clin. Invest. 100, 2170-2181 (Pubitemid 27500138)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.9 , pp. 2170-2181
    • Argraves, K.M.1    Kozarsky, K.F.2    Fallon, J.T.3    Harpel, P.C.4    Strickland, D.K.5
  • 64
    • 0027404489 scopus 로고
    • Streptokinase and human fibronectin share a common epitope: Implications for regulation of fibrinolysis and rheumatoid arthritis
    • DOI 10.1016/0925-4439(93)90051-2
    • Gonzalez-Gronow, M., Enghild, J. J., and Pizzo, S. V. (1993) Streptokinase and human fibronectin share a common epitope. Implications for regulation of fibrinolysis and rheumatoid arthritis. Biochim. Biophys. Acta 1180, 283-288 (Pubitemid 23033021)
    • (1993) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1180 , Issue.3 , pp. 283-288
    • Gonzalez-Gronow, M.1    Enghild, J.J.2    Pizzo, S.V.3
  • 65
    • 74949084342 scopus 로고    scopus 로고
    • Residues essential for plasminogen binding by the cation-independent mannose 6-phosphate receptor
    • Bohnsack, R. N., Patel, M., Olson, L. J., Twining, S. S., and Dahms, N. M. (2010) Residues essential for plasminogen binding by the cation-independent mannose 6-phosphate receptor. Biochemistry 49, 635-644
    • (2010) Biochemistry , vol.49 , pp. 635-644
    • Bohnsack, R.N.1    Patel, M.2    Olson, L.J.3    Twining, S.S.4    Dahms, N.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.