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Volumn 192, Issue 9, 2014, Pages 4398-4408

High molecular weight kininogen binds phosphatidylserine and opsonizes urokinase plasminogen activator receptor-mediated efferocytosis

Author keywords

[No Author keywords available]

Indexed keywords

BRADYKININ; CELL PROTEIN; COMPLEMENTARY DNA; CRK ASSOCIATED SUBSTRATE PROTEIN; DOCK 180 PROTEIN; HIGH MOLECULAR WEIGHT KININOGEN; LIPOCORTIN 5; LIPOSOME; PHOSPHATIDYLSERINE; PROTEIN CRKII; RAC1 PROTEIN; UNCLASSIFIED DRUG; UROKINASE RECEPTOR;

EID: 84899527153     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1302590     Document Type: Article
Times cited : (19)

References (53)
  • 1
    • 33645845142 scopus 로고    scopus 로고
    • Phosphatidylserine recognition by phagocytes: A view to a kill
    • Wu, Y., N. Tibrewal, and R. B. Birge. 2006. Phosphatidylserine recognition by phagocytes: A view to a kill. Trends Cell Biol. 16: 189-197
    • (2006) Trends Cell Biol , vol.16 , pp. 189-197
    • Wu, Y.1    Tibrewal, N.2    Birge, R.B.3
  • 2
    • 80755180853 scopus 로고    scopus 로고
    • Beginnings of a good apoptotic meal: The find-me and eat-me signaling pathways
    • Ravichandran, K. S. 2011. Beginnings of a good apoptotic meal: The find-me and eat-me signaling pathways. Immunity 35: 445-455
    • (2011) Immunity , vol.35 , pp. 445-455
    • Ravichandran, K.S.1
  • 7
    • 14644411712 scopus 로고    scopus 로고
    • A role for Mer tyrosine kinase in alphavbeta5 integrin-mediated phagocytosis of apoptotic cells
    • Wu, Y., S. Singh, M. M. Georgescu, and R. B. Birge. 2005. A role for Mer tyrosine kinase in alphavbeta5 integrin-mediated phagocytosis of apoptotic cells. J. Cell Sci. 118: 539-553
    • (2005) J. Cell Sci , vol.118 , pp. 539-553
    • Wu, Y.1    Singh, S.2    Georgescu, M.M.3    Birge, R.B.4
  • 8
    • 3242699717 scopus 로고    scopus 로고
    • UPA and uPAR in fibrinolysis, immunity and pathology
    • Mondino, A., and F. Blasi. 2004. uPA and uPAR in fibrinolysis, immunity and pathology. Trends Immunol. 25: 450-455
    • (2004) Trends Immunol , vol.25 , pp. 450-455
    • Mondino, A.1    Blasi, F.2
  • 12
    • 84859812544 scopus 로고    scopus 로고
    • The urokinase system in the pathogenesis of atherosclerosis
    • Fuhrman, B. 2012. The urokinase system in the pathogenesis of atherosclerosis. Atherosclerosis 222: 8-14
    • (2012) Atherosclerosis , vol.222 , pp. 8-14
    • Fuhrman, B.1
  • 13
    • 84866865815 scopus 로고    scopus 로고
    • Aggregated low-density lipoprotein induce impairment of the cytoskeleton dynamics through urokinasetype plasminogen activator/urokinase-type plasminogen activator receptor in human vascular smooth muscle cell
    • Lugano, R., E. Peña, L. Badimon, and T. Padró. 2012. Aggregated low-density lipoprotein induce impairment of the cytoskeleton dynamics through urokinasetype plasminogen activator/urokinase-type plasminogen activator receptor in human vascular smooth muscle cell. J. Thromb. Haemost. 10: 2158-2167
    • (2012) J. Thromb. Haemost , vol.10 , pp. 2158-2167
    • Lugano, R.1    Peña, E.2    Badimon, L.3    Padró, T.4
  • 17
    • 68249134202 scopus 로고    scopus 로고
    • Participation of the urokinase receptor in neutrophil efferocytosis
    • Park, Y. J., G. Liu, Y. Tsuruta, E. Lorne, and E. Abraham. 2009. Participation of the urokinase receptor in neutrophil efferocytosis. Blood 114: 860-870
    • (2009) Blood , vol.114 , pp. 860-870
    • Park, Y.J.1    Liu, G.2    Tsuruta, Y.3    Lorne, E.4    Abraham, E.5
  • 18
    • 67650559449 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor promotes efferocytosis of apoptotic cells
    • D?mello, V., S. Singh, Y. Wu, and R. B. Birge. 2009. The urokinase plasminogen activator receptor promotes efferocytosis of apoptotic cells. J. Biol. Chem. 284: 17030-17038
    • (2009) J. Biol. Chem , vol.284 , pp. 17030-17038
    • Dmello, V.1    Singh, S.2    Wu, Y.3    Birge, R.B.4
  • 19
    • 70449475311 scopus 로고    scopus 로고
    • Efferocytosis: Another function of uPAR
    • Blasi, F., and N. Sidenius. 2009. Efferocytosis: Another function of uPAR. Blood 114: 752-753
    • (2009) Blood , vol.114 , pp. 752-753
    • Blasi, F.1    Sidenius, N.2
  • 21
    • 0027452929 scopus 로고
    • Deletion mutagenesis of high molecular weight kininogen light chain identification of two anionic surface binding subdomains
    • Kunapuli, S. P., R. A. DeLa Cadena, and R. W. Colman. 1993. Deletion mutagenesis of high molecular weight kininogen light chain. Identification of two anionic surface binding subdomains. J. Biol. Chem. 268: 2486-2492
    • (1993) J. Biol. Chem , vol.268 , pp. 2486-2492
    • Kunapuli, S.P.1    Dela Cadena, R.A.2    Colman, R.W.3
  • 22
    • 0029096807 scopus 로고
    • Mapping the cell binding site on high molecular weight kininogen domain 5
    • Hasan, A. A., D. B. Cines, H. Herwald, A. H. Schmaier, and W. Muller-Esterl. 1995. Mapping the cell binding site on high molecular weight kininogen domain 5. J. Biol. Chem. 270: 19256-19261
    • (1995) J. Biol. Chem , vol.270 , pp. 19256-19261
    • Hasan, A.A.1    Cines, D.B.2    Herwald, H.3    Schmaier, A.H.4    Muller-Esterl, W.5
  • 25
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung, T., G. E. Gilbert, J. Shi, J. Silvius, A. Kapus, and S. Grinstein. 2008. Membrane phosphatidylserine regulates surface charge and protein localization. Science 319: 210-213
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 28
    • 0037438495 scopus 로고    scopus 로고
    • Internalization of circulating apoptotic cells by splenic marginal zone dendritic cells: Dependence on complement receptors and effect on cytokine production
    • Morelli, A. E., A. T. Larregina, W. J. Shufesky, A. F. Zahorchak, A. J. Logar, G. D. Papworth, Z. Wang, S. C. Watkins, L. D. Falo, Jr., and A. W. Thomson. 2003. Internalization of circulating apoptotic cells by splenic marginal zone dendritic cells: Dependence on complement receptors and effect on cytokine production. Blood 101: 611-620
    • (2003) Blood , vol.101 , pp. 611-620
    • Morelli, A.E.1    Larregina, A.T.2    Shufesky, W.J.3    Zahorchak, A.F.4    Logar, A.J.5    Papworth, G.D.6    Wang, Z.7    Watkins, S.C.8    Falo Jr., L.D.9    Thomson, A.W.10
  • 29
    • 77953768762 scopus 로고    scopus 로고
    • AMPKalpha1 deletion shortens erythrocyte life span in mice: Role of oxidative stress
    • Wang, S., G. L. Dale, P. Song, B. Viollet, and M. H. Zou. 2010. AMPKalpha1 deletion shortens erythrocyte life span in mice: Role of oxidative stress. J. Biol. Chem. 285: 19976-19985
    • (2010) J. Biol. Chem , vol.285 , pp. 19976-19985
    • Wang, S.1    Dale, G.L.2    Song, P.3    Viollet, B.4    Zou, M.H.5
  • 30
    • 34548173742 scopus 로고    scopus 로고
    • Kininostatin associates with membrane rafts and inhibits a(v)beta3 integrin activation in human umbilical vein endothelial cells
    • Wu, Y., V. Rizzo, Y. Liu, I. M. Sainz, N. G. Schmuckler, and R. W. Colman. 2007. Kininostatin associates with membrane rafts and inhibits a(v)beta3 integrin activation in human umbilical vein endothelial cells. Arterioscler. Thromb. Vasc. Biol. 27: 1968-1975
    • (2007) Arterioscler. Thromb. Vasc. Biol , vol.27 , pp. 1968-1975
    • Wu, Y.1    Rizzo, V.2    Liu, Y.3    Sainz, I.M.4    Schmuckler, N.G.5    Colman, R.W.6
  • 31
    • 0030823246 scopus 로고    scopus 로고
    • Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor
    • Colman, R. W., R. A. Pixley, S. Najamunnisa, W. Yan, J. Wang, A. Mazar, and K. R. McCrae. 1997. Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor. J. Clin. Invest. 100: 1481-1487
    • (1997) J. Clin. Invest , vol.100 , pp. 1481-1487
    • Colman, R.W.1    Pixley, R.A.2    Najamunnisa, S.3    Yan, W.4    Wang, J.5    Mazar, A.6    McCrae, K.R.7
  • 32
    • 77951883821 scopus 로고    scopus 로고
    • The urokinase receptor: Focused cell surface proteolysis, cell adhesion and signaling
    • Blasi, F., and N. Sidenius. 2010. The urokinase receptor: Focused cell surface proteolysis, cell adhesion and signaling. FEBS Lett. 584: 1923-1930
    • (2010) FEBS Lett , vol.584 , pp. 1923-1930
    • Blasi, F.1    Sidenius, N.2
  • 33
    • 2142717277 scopus 로고    scopus 로고
    • Fine mapping of the sequences in domain 5 of high molecular weight kininogen (HK) interacting with heparin and zinc
    • Pixley, R. A., Y. Lin, I. Isordia-Salas, and R. W. Colman. 2003. Fine mapping of the sequences in domain 5 of high molecular weight kininogen (HK) interacting with heparin and zinc. J. Thromb. Haemost. 1: 1791-1798
    • (2003) J. Thromb. Haemost , vol.1 , pp. 1791-1798
    • Pixley, R.A.1    Lin, Y.2    Isordia-Salas, I.3    Colman, R.W.4
  • 34
    • 0035911966 scopus 로고    scopus 로고
    • Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin
    • Kjøller, L., and A. Hall. 2001. Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin. J. Cell Biol. 152: 1145-1157
    • (2001) J. Cell Biol , vol.152 , pp. 1145-1157
    • Kjøller, L.1    Hall, A.2
  • 35
    • 50249145697 scopus 로고    scopus 로고
    • Upar promotes formation of the p130cas-crk complex to activate rac through dock180
    • Smith, H. W., P. Marra, and C. J. Marshall. 2008. uPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180. J. Cell Biol. 182: 777-790
    • (2008) J. Cell Biol , vol.182 , pp. 777-790
    • Smith, H.W.1    Marra, P.2    Marshall, C.J.3
  • 37
    • 20244362188 scopus 로고    scopus 로고
    • Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells
    • Anderson, H. A., C. A. Maylock, J. A. Williams, C. P. Paweletz, H. Shu, and E. Shacter. 2003. Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells. Nat. Immunol. 4: 87-91
    • (2003) Nat. Immunol , vol.4 , pp. 87-91
    • Anderson, H.A.1    Maylock, C.A.2    Williams, J.A.3    Paweletz, C.P.4    Shu, H.5    Shacter, E.6
  • 38
    • 0028846868 scopus 로고
    • Autoantibodies to phosphatidylethanolamine( PE) recognize a kininogen-PE complex
    • Sugi, T., and J. A. McIntyre. 1995. Autoantibodies to phosphatidylethanolamine( PE) recognize a kininogen-PE complex. Blood 86: 3083-3089
    • (1995) Blood , vol.86 , pp. 3083-3089
    • Sugi, T.1    McIntyre, J.A.2
  • 42
    • 79958133035 scopus 로고    scopus 로고
    • Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (biacore
    • Pixley, R. A., R. G. Espinola, B. Ghebrehiwet, K. Joseph, A. Kao, K. Bdeir, D. B. Cines, and R. W. Colman. 2011. Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore). Thromb. Haemost. 105: 1053-1059
    • (2011) Thromb. Haemost , vol.105 , pp. 1053-1059
    • Pixley, R.A.1    Espinola, R.G.2    Ghebrehiwet, B.3    Joseph, K.4    Kao, A.5    Bdeir, K.6    Cines, D.B.7    Colman, R.W.8
  • 43
    • 84863628119 scopus 로고    scopus 로고
    • Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKa) on adhesion and survival signaling in endothelial cells
    • Tesfay, L., A. J. Huhn, H. Hatcher, F. M. Torti, and S. V. Torti. 2012. Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKa) on adhesion and survival signaling in endothelial cells. PLoS ONE 7: E40030
    • (2012) PLoS ONE , vol.7
    • Tesfay, L.1    Huhn, A.J.2    Hatcher, H.3    Torti, F.M.4    Torti, S.V.5
  • 47
    • 65249150136 scopus 로고    scopus 로고
    • Membrane-anchored uPAR regulates the proliferation, marrow pool size, engraftment, and mobilization of mouse hematopoietic stem/progenitor cells
    • Tjwa, M., N. Sidenius, R. Moura, S. Jansen, K. Theunissen, A. Andolfo, M. De Mol, M. Dewerchin, L. Moons, F. Blasi, et al. 2009. Membrane-anchored uPAR regulates the proliferation, marrow pool size, engraftment, and mobilization of mouse hematopoietic stem/progenitor cells. J. Clin. Invest. 119: 1008-1018
    • (2009) J. Clin. Invest , vol.119 , pp. 1008-1018
    • Tjwa, M.1    Sidenius, N.2    Moura, R.3    Jansen, S.4    Theunissen, K.5    Andolfo, A.6    De Mol, M.7    Dewerchin, M.8    Moons, L.9    Blasi, F.10
  • 48
    • 0032555894 scopus 로고    scopus 로고
    • Urokinase receptor (CD87) regulates leukocyte recruitment via b 2 integrins in vivo
    • May, A. E., S. M. Kanse, L. R. Lund, R. H. Gisler, B. A. Imhof, and K. T. Preissner. 1998. Urokinase receptor (CD87) regulates leukocyte recruitment via b 2 integrins in vivo. J. Exp. Med. 188: 1029-1037
    • (1998) J. Exp. Med , vol.188 , pp. 1029-1037
    • May, A.E.1    Kanse, S.M.2    Lund, L.R.3    Gisler, R.H.4    Imhof, B.A.5    Preissner, K.T.6
  • 49
    • 73049085206 scopus 로고    scopus 로고
    • Soluble urokinase-type plasminogen activator receptor forms in plasma as markers of atherosclerotic plaque vulnerability
    • Olson, F. J., T. Thurison, M. Ryndel, G. Høyer-Hansen, and B. Fagerberg. 2010. Soluble urokinase-type plasminogen activator receptor forms in plasma as markers of atherosclerotic plaque vulnerability. Clin. Biochem. 43: 124-130
    • (2010) Clin. Biochem , vol.43 , pp. 124-130
    • Olson, F.J.1    Thurison, T.2    Ryndel, M.3    Høyer-Hansen, G.4    Fagerberg, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.