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Volumn 11, Issue 1, 2013, Pages 26-34

Plasminogen receptors and their role in the pathogenesis of inflammatory, autoimmune and malignant disease

Author keywords

Fibrinolysis; Inflammation; Plasminogen; Receptors; Thrombosis; Tumorogenesis

Indexed keywords

BETA2 GLYCOPROTEIN 1; ENOLASE; ENOLASE 1; GELATINASE B; HIGH MOBILITY GROUP B1 PROTEIN; HISTONE H2B; INTERLEUKIN 1; INTERLEUKIN 6; JANUS KINASE 1; LIPOCORTIN 2; MONOCYTE CHEMOTACTIC PROTEIN 1; PLASMIN; PLASMINOGEN; PROTEIN S 100; S100A10 PROTEIN; SCLEROPROTEIN; STAT3 PROTEIN; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84873047947     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/jth.12064     Document Type: Review
Times cited : (90)

References (58)
  • 2
    • 84861503406 scopus 로고    scopus 로고
    • Effect of tranexamic acid on surgical bleeding: systematic review and cumulative meta-analysis
    • Ker K, Edwards P, Perel P, Shakur H, Roberts I. Effect of tranexamic acid on surgical bleeding: systematic review and cumulative meta-analysis. BMJ 2012; 344: e3054.
    • (2012) BMJ , vol.344
    • Ker, K.1    Edwards, P.2    Perel, P.3    Shakur, H.4    Roberts, I.5
  • 3
    • 67649592636 scopus 로고    scopus 로고
    • Acute myocardial infarction associated with ST segment elevation and the new European Society of Cardiology guidelines
    • Verheugt FW. Acute myocardial infarction associated with ST segment elevation and the new European Society of Cardiology guidelines. Heart 2009; 95: 1112-7.
    • (2009) Heart , vol.95 , pp. 1112-1117
    • Verheugt, F.W.1
  • 5
    • 18444386848 scopus 로고    scopus 로고
    • Molecular mechanisms of fibrinolysis
    • Cesarman-Maus G, Hajjar KA. Molecular mechanisms of fibrinolysis. Br J Haematol 2005; 129: 307-21.
    • (2005) Br J Haematol , vol.129 , pp. 307-321
    • Cesarman-Maus, G.1    Hajjar, K.A.2
  • 6
    • 0037340432 scopus 로고    scopus 로고
    • Molecular mechanisms of initiation of fibrinolysis by fibrin
    • Medved L, Nieuwenhuizen W. Molecular mechanisms of initiation of fibrinolysis by fibrin. Thromb Haemost 2003; 89: 409-19.
    • (2003) Thromb Haemost , vol.89 , pp. 409-419
    • Medved, L.1    Nieuwenhuizen, W.2
  • 7
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen PA, Egelund R, Petersen HH. The plasminogen activation system in tumor growth, invasion, and metastasis. Cell Mol Life Sci 2000; 57: 25-40.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 8
    • 0025261396 scopus 로고
    • Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system
    • Petersen TE, Martzen MR, Ichinose A, Davie EW. Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system. J Biol Chem 1990; 265: 6104-11.
    • (1990) J Biol Chem , vol.265 , pp. 6104-6111
    • Petersen, T.E.1    Martzen, M.R.2    Ichinose, A.3    Davie, E.W.4
  • 9
    • 77955700229 scopus 로고    scopus 로고
    • Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape
    • Christen MT, Frank P, Schaller J, Llinas M. Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape. Biochemistry 2010; 49: 7131-50.
    • (2010) Biochemistry , vol.49 , pp. 7131-7150
    • Christen, M.T.1    Frank, P.2    Schaller, J.3    Llinas, M.4
  • 10
    • 0030852456 scopus 로고    scopus 로고
    • Ligand preferences of kringle 2 and homologous domains of human plasminogen: canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR
    • Marti DN, Hu CK, An SS, von Haller P, Schaller J, Llinas M. Ligand preferences of kringle 2 and homologous domains of human plasminogen: canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR. Biochemistry 1997; 36: 11591-604.
    • (1997) Biochemistry , vol.36 , pp. 11591-11604
    • Marti, D.N.1    Hu, C.K.2    An, S.S.3    von Haller, P.4    Schaller, J.5    Llinas, M.6
  • 11
    • 84863429651 scopus 로고    scopus 로고
    • Crystal structure of the native plasminogen reveals an activation-resistant compact conformation
    • Xue Y, Bodin C, Olsson K. Crystal structure of the native plasminogen reveals an activation-resistant compact conformation. J Thromb Haemost 2012; 10: 1385-96.
    • (2012) J Thromb Haemost , vol.10 , pp. 1385-1396
    • Xue, Y.1    Bodin, C.2    Olsson, K.3
  • 13
    • 0035374672 scopus 로고    scopus 로고
    • Conversion of Glu-plasminogen to Lys-plasminogen is necessary for optimal stimulation of plasminogen activation on the endothelial cell surface
    • Gong Y, Kim SO, Felez J, Grella DK, Castellino FJ, Miles LA. Conversion of Glu-plasminogen to Lys-plasminogen is necessary for optimal stimulation of plasminogen activation on the endothelial cell surface. J Biol Chem 2001; 276: 19078-83.
    • (2001) J Biol Chem , vol.276 , pp. 19078-19083
    • Gong, Y.1    Kim, S.O.2    Felez, J.3    Grella, D.K.4    Castellino, F.J.5    Miles, L.A.6
  • 15
    • 0035808318 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a
    • Hawley SB, Tamura T, Miles LA. Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a. J Biol Chem 2001; 276: 179-86.
    • (2001) J Biol Chem , vol.276 , pp. 179-186
    • Hawley, S.B.1    Tamura, T.2    Miles, L.A.3
  • 16
    • 0026080007 scopus 로고
    • Interactions of plasminogen and tissue plasminogen activator (t-PA) with amphoterin. Enhancement of t-PA-catalyzed plasminogen activation by amphoterin
    • Parkkinen J, Rauvala H. Interactions of plasminogen and tissue plasminogen activator (t-PA) with amphoterin. Enhancement of t-PA-catalyzed plasminogen activation by amphoterin. J Biol Chem 1991; 266: 16730-5.
    • (1991) J Biol Chem , vol.266 , pp. 16730-16735
    • Parkkinen, J.1    Rauvala, H.2
  • 17
    • 0035511837 scopus 로고    scopus 로고
    • Cytokeratin 8 functions as a major plasminogen receptor in select epithelial and carcinoma cells
    • Gonias SL, Hembrough TA, Sankovic M. Cytokeratin 8 functions as a major plasminogen receptor in select epithelial and carcinoma cells. Front Biosci 2001; 6: D1403-11.
    • (2001) Front Biosci , vol.6
    • Gonias, S.L.1    Hembrough, T.A.2    Sankovic, M.3
  • 18
    • 0022469565 scopus 로고
    • Plasminogen interacts with human platelets through two distinct mechanisms
    • Miles LA, Ginsberg MH, White JG, Plow EF. Plasminogen interacts with human platelets through two distinct mechanisms. J Clin Invest 1986; 77: 2001-9.
    • (1986) J Clin Invest , vol.77 , pp. 2001-2009
    • Miles, L.A.1    Ginsberg, M.H.2    White, J.G.3    Plow, E.F.4
  • 19
    • 0029817448 scopus 로고    scopus 로고
    • Endothelial cell surface actin serves as a binding site for plasminogen, tissue plasminogen activator and lipoprotein(a)
    • Dudani AK, Ganz PR. Endothelial cell surface actin serves as a binding site for plasminogen, tissue plasminogen activator and lipoprotein(a). Br J Haematol 1996; 95: 168-78.
    • (1996) Br J Haematol , vol.95 , pp. 168-178
    • Dudani, A.K.1    Ganz, P.R.2
  • 20
    • 0027515051 scopus 로고
    • Competition between plasminogen and tissue plasminogen activator for cellular binding sites
    • Felez J, Chanquia CJ, Fabregas P, Plow EF, Miles LA. Competition between plasminogen and tissue plasminogen activator for cellular binding sites. Blood 1993; 82: 2433-41.
    • (1993) Blood , vol.82 , pp. 2433-2441
    • Felez, J.1    Chanquia, C.J.2    Fabregas, P.3    Plow, E.F.4    Miles, L.A.5
  • 21
    • 0022415067 scopus 로고
    • Glu-plasminogen I and II: their activation by urokinase and streptokinase in the presence of fibrin and fibrinogen
    • Takada Y, Makino Y, Takada A. Glu-plasminogen I and II: their activation by urokinase and streptokinase in the presence of fibrin and fibrinogen. Thromb Res 1985; 39: 289-96.
    • (1985) Thromb Res , vol.39 , pp. 289-296
    • Takada, Y.1    Makino, Y.2    Takada, A.3
  • 22
    • 0037097715 scopus 로고    scopus 로고
    • Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells
    • Gonzalez-Gronow M, Gawdi G, Pizzo SV. Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells. Blood 2002; 99: 4562-7.
    • (2002) Blood , vol.99 , pp. 4562-4567
    • Gonzalez-Gronow, M.1    Gawdi, G.2    Pizzo, S.V.3
  • 24
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • Deora AB, Kreitzer G, Jacovina AT, Hajjar KA. An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface. J Biol Chem 2004; 279: 43411-8.
    • (2004) J Biol Chem , vol.279 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 25
    • 68049102910 scopus 로고    scopus 로고
    • L-type calcium channel blockers exert an antiinflammatory effect by suppressing expression of plasminogen receptors on macrophages
    • Das R, Burke T, van Wagoner DR, Plow EF. L-type calcium channel blockers exert an antiinflammatory effect by suppressing expression of plasminogen receptors on macrophages. Circ Res 2009; 105: 167-75.
    • (2009) Circ Res , vol.105 , pp. 167-175
    • Das, R.1    Burke, T.2    van Wagoner, D.R.3    Plow, E.F.4
  • 26
    • 0038491346 scopus 로고    scopus 로고
    • Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin
    • MacLeod TJ, Kwon M, Filipenko NR, Waisman DM. Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin. J Biol Chem 2003; 278: 25577-84.
    • (2003) J Biol Chem , vol.278 , pp. 25577-25584
    • MacLeod, T.J.1    Kwon, M.2    Filipenko, N.R.3    Waisman, D.M.4
  • 27
    • 36248933738 scopus 로고    scopus 로고
    • Annexin A2 is a soluble mediator of macrophage activation
    • Swisher JF, Khatri U, Feldman GM. Annexin A2 is a soluble mediator of macrophage activation. J Leukoc Biol 2007; 82: 1174-84.
    • (2007) J Leukoc Biol , vol.82 , pp. 1174-1184
    • Swisher, J.F.1    Khatri, U.2    Feldman, G.M.3
  • 28
    • 77955425795 scopus 로고    scopus 로고
    • A role for the annexin A2 amino-terminal peptide in the plasmin-induced activation of human peripheral monocytes
    • Li Q, Ke F, Zhang W, Laumonnier Y, Syrovets T, Simmet T, Wang H. A role for the annexin A2 amino-terminal peptide in the plasmin-induced activation of human peripheral monocytes. Mol Immunol 2010; 47: 2405-10.
    • (2010) Mol Immunol , vol.47 , pp. 2405-2410
    • Li, Q.1    Ke, F.2    Zhang, W.3    Laumonnier, Y.4    Syrovets, T.5    Simmet, T.6    Wang, H.7
  • 29
    • 77449113227 scopus 로고    scopus 로고
    • Annexin A2 tetramer activates human and murine macrophages through TLR4
    • Swisher JF, Burton N, Bacot SM, Vogel SN, Feldman GM. Annexin A2 tetramer activates human and murine macrophages through TLR4. Blood 2010; 115: 549-58.
    • (2010) Blood , vol.115 , pp. 549-558
    • Swisher, J.F.1    Burton, N.2    Bacot, S.M.3    Vogel, S.N.4    Feldman, G.M.5
  • 34
    • 84862909113 scopus 로고    scopus 로고
    • A novel pathway for human endothelial cell activation by antiphospholipid/anti-beta2 glycoprotein I antibodies
    • Allen KL, Fonseca FV, Betapudi V, Willard B, Zhang J, McCrae KR. A novel pathway for human endothelial cell activation by antiphospholipid/anti-beta2 glycoprotein I antibodies. Blood 2012; 119: 884-93.
    • (2012) Blood , vol.119 , pp. 884-893
    • Allen, K.L.1    Fonseca, F.V.2    Betapudi, V.3    Willard, B.4    Zhang, J.5    McCrae, K.R.6
  • 36
    • 77950628360 scopus 로고    scopus 로고
    • Breast cancer cell surface annexin II induces cell migration and neoangiogenesis via tPA dependent plasmin generation
    • Sharma M, Ownbey RT, Sharma MC. Breast cancer cell surface annexin II induces cell migration and neoangiogenesis via tPA dependent plasmin generation. Exp Mol Pathol 2010; 88: 278-86.
    • (2010) Exp Mol Pathol , vol.88 , pp. 278-286
    • Sharma, M.1    Ownbey, R.T.2    Sharma, M.C.3
  • 37
    • 0037311084 scopus 로고    scopus 로고
    • p11 regulates extracellular plasmin production and invasiveness of HT1080 fibrosarcoma cells
    • Choi KS, Fogg DK, Yoon CS, Waisman DM. p11 regulates extracellular plasmin production and invasiveness of HT1080 fibrosarcoma cells. FASEB J 2003; 17: 235-46.
    • (2003) FASEB J , vol.17 , pp. 235-246
    • Choi, K.S.1    Fogg, D.K.2    Yoon, C.S.3    Waisman, D.M.4
  • 39
    • 84155176820 scopus 로고    scopus 로고
    • Antibody-directed neutralization of annexin II (ANX II) inhibits neoangiogenesis and human breast tumor growth in a xenograft model
    • Sharma M, Blackman MR, Sharma MC. Antibody-directed neutralization of annexin II (ANX II) inhibits neoangiogenesis and human breast tumor growth in a xenograft model. Exp Mol Pathol 2011; 92: 175-84.
    • (2011) Exp Mol Pathol , vol.92 , pp. 175-184
    • Sharma, M.1    Blackman, M.R.2    Sharma, M.C.3
  • 41
    • 79958720444 scopus 로고    scopus 로고
    • The expression of annexin II and its role in the fibrinolytic activity in acute promyelocytic leukemia
    • Liu Y, Wang Z, Jiang M, Dai L, Zhang W, Wu D, Ruan C. The expression of annexin II and its role in the fibrinolytic activity in acute promyelocytic leukemia. Leuk Res 2011; 35: 879-84.
    • (2011) Leuk Res , vol.35 , pp. 879-884
    • Liu, Y.1    Wang, Z.2    Jiang, M.3    Dai, L.4    Zhang, W.5    Wu, D.6    Ruan, C.7
  • 42
    • 4644219614 scopus 로고    scopus 로고
    • Expression of receptors for plasminogen activators on endothelial cell surface depends on their origin
    • Kwaan HC, Wang J, Weiss I. Expression of receptors for plasminogen activators on endothelial cell surface depends on their origin. J Thromb Haemost 2004; 2: 306-12.
    • (2004) J Thromb Haemost , vol.2 , pp. 306-312
    • Kwaan, H.C.1    Wang, J.2    Weiss, I.3
  • 43
    • 83555165967 scopus 로고    scopus 로고
    • The pathogenesis and management of the coagulopathy of acute promyelocytic leukaemia
    • Breen KA, Grimwade D, Hunt BJ. The pathogenesis and management of the coagulopathy of acute promyelocytic leukaemia. Br J Haematol 2012; 156: 24-36.
    • (2012) Br J Haematol , vol.156 , pp. 24-36
    • Breen, K.A.1    Grimwade, D.2    Hunt, B.J.3
  • 45
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: its role in diseases
    • Pancholi V. Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 2001; 58: 902-20.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 48
    • 79952830765 scopus 로고    scopus 로고
    • Alpha-Enolase: a promising therapeutic and diagnostic tumor target
    • Capello M, Ferri-Borgogno S, Cappello P, Novelli F. Alpha-Enolase: a promising therapeutic and diagnostic tumor target. FEBS J 2011; 278: 1064-74.
    • (2011) FEBS J , vol.278 , pp. 1064-1074
    • Capello, M.1    Ferri-Borgogno, S.2    Cappello, P.3    Novelli, F.4
  • 50
    • 33747093008 scopus 로고    scopus 로고
    • Identification of histone H2B as a regulated plasminogen receptor
    • Herren T, Burke TA, Das R, Plow EF. Identification of histone H2B as a regulated plasminogen receptor. Biochemistry 2006; 45: 9463-74.
    • (2006) Biochemistry , vol.45 , pp. 9463-9474
    • Herren, T.1    Burke, T.A.2    Das, R.3    Plow, E.F.4
  • 51
    • 36348985036 scopus 로고    scopus 로고
    • Histone H2B as a functionally important plasminogen receptor on macrophages
    • Das R, Burke T, Plow EF. Histone H2B as a functionally important plasminogen receptor on macrophages. Blood 2007; 110: 3763-72.
    • (2007) Blood , vol.110 , pp. 3763-3772
    • Das, R.1    Burke, T.2    Plow, E.F.3
  • 52
    • 79251541489 scopus 로고    scopus 로고
    • Phosphatidylserine as an anchor for plasminogen and its plasminogen receptor, histone H2B, to the macrophage surface
    • Das R, Plow EF. Phosphatidylserine as an anchor for plasminogen and its plasminogen receptor, histone H2B, to the macrophage surface. J Thromb Haemost 2011; 9: 339-49.
    • (2011) J Thromb Haemost , vol.9 , pp. 339-349
    • Das, R.1    Plow, E.F.2
  • 53
    • 0034607631 scopus 로고    scopus 로고
    • Molecular and structural properties of three autoimmune IgG monoclonal antibodies to histone H2B
    • Monestier M, Decker P, Briand JP, Gabriel JL, Muller S. Molecular and structural properties of three autoimmune IgG monoclonal antibodies to histone H2B. J Biol Chem 2000; 275: 13558-63.
    • (2000) J Biol Chem , vol.275 , pp. 13558-13563
    • Monestier, M.1    Decker, P.2    Briand, J.P.3    Gabriel, J.L.4    Muller, S.5
  • 54
    • 0031754491 scopus 로고    scopus 로고
    • Antigen specificity of antihistone antibodies in systemic sclerosis
    • Hasegawa M, Sato S, Kikuchi K, Takehara K. Antigen specificity of antihistone antibodies in systemic sclerosis. Ann Rheum Dis 1998; 57: 470-5.
    • (1998) Ann Rheum Dis , vol.57 , pp. 470-475
    • Hasegawa, M.1    Sato, S.2    Kikuchi, K.3    Takehara, K.4
  • 55
    • 11144337155 scopus 로고    scopus 로고
    • Antinucleosome antibody is a major autoantibody in localized scleroderma
    • Sato S, Kodera M, Hasegawa M, Fujimoto M, Takehara K. Antinucleosome antibody is a major autoantibody in localized scleroderma. Br J Dermatol 2004; 151: 1182-8.
    • (2004) Br J Dermatol , vol.151 , pp. 1182-1188
    • Sato, S.1    Kodera, M.2    Hasegawa, M.3    Fujimoto, M.4    Takehara, K.5
  • 57
    • 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 NM, Chen EI, Baik N, Bai H, Parmer CM, Kiosses WB, Kamps MP, Yates JR III, Parmer RJ, Miles LA. 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: 1319-30.
    • (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


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