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Volumn 43, Issue 2, 2017, Pages 135-142

Plasmin(ogen) at the Nexus of Fibrinolysis, Inflammation, and Complement

Author keywords

complement; fibrinolysis; inflammation; plasminogen receptors; wound healing

Indexed keywords

ALTERNATIVE COMPLEMENT PATHWAY C3 C5 CONVERTASE; BINDING PROTEIN; COMPLEMENT; COMPLEMENT INHIBITOR; CPB2 PROTEIN; FIBRIN; FIBRINOLYTIC FACTOR; LIPOCORTIN 2; PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR; PLASMINOGEN RECEPTOR; PLASMINOGEN[LYSINE]; TRANEXAMIC ACID; UNCLASSIFIED DRUG;

EID: 85008316411     PISSN: 00946176     EISSN: 10989064     Source Type: Journal    
DOI: 10.1055/s-0036-1592302     Document Type: Article
Times cited : (57)

References (86)
  • 1
    • 0021736924 scopus 로고
    • Thrombin stimulates tissue plasminogen activator release from cultured human endothelial cells
    • Levin E G Marzec U Anderson J Harker L A Thrombin stimulates tissue plasminogen activator release from cultured human endothelial cells J Clin Invest 1984 74 6 1988 1995
    • (1984) J Clin Invest , vol.74 , Issue.6 , pp. 1988-1995
    • Levin, E.G.1    Marzec, U.2    Anderson, J.3    Harker, L.A.4
  • 2
    • 0029036323 scopus 로고
    • Alpha-thrombin stimulates urokinase production and DNA synthesis in cultured human cerebral microvascular endothelial cells
    • Shatos M A Orfeo T Doherty J M Penar P L Collen D Mann K G Alpha-thrombin stimulates urokinase production and DNA synthesis in cultured human cerebral microvascular endothelial cells Arterioscler Thromb Vasc Biol 1995 15 7 903 911
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , Issue.7 , pp. 903-911
    • Shatos, M.A.1    Orfeo, T.2    Doherty, J.M.3    Penar, P.L.4    Collen, D.5    Mann, K.G.6
  • 3
    • 84856884891 scopus 로고    scopus 로고
    • A high affinity interaction of plasminogen with fibrin is not essential for efficient activation by tissue-type plasminogen activator
    • Kim P Y Tieu L D Stafford A R Fredenburgh J C Weitz J I A high affinity interaction of plasminogen with fibrin is not essential for efficient activation by tissue-type plasminogen activator J Biol Chem 2012 287 7 4652 4661
    • (2012) J Biol Chem , vol.287 , Issue.7 , pp. 4652-4661
    • Kim, P.Y.1    Tieu, L.D.2    Stafford, A.R.3    Fredenburgh, J.C.4    Weitz, J.I.5
  • 4
    • 0031035376 scopus 로고    scopus 로고
    • A steady-state template model that describes the kinetics of fibrin-stimulated [Glu1]- and [Lys78]plasminogen activation by native tissue-type plasminogen activator and variants that lack either the finger or kringle-2 domain
    • Horrevoets A J Pannekoek H Nesheim M E A steady-state template model that describes the kinetics of fibrin-stimulated [Glu1]-and [Lys78]plasminogen activation by native tissue-type plasminogen activator and variants that lack either the finger or kringle-2 domain J Biol Chem 1997 272 4 2183 2191
    • (1997) J Biol Chem , vol.272 , Issue.4 , pp. 2183-2191
    • Horrevoets, A.J.1    Pannekoek, H.2    Nesheim, M.E.3
  • 5
    • 0035793601 scopus 로고    scopus 로고
    • A kinetic analysis of the tissue plasminogen activator and DSPAalpha1 cofactor activities of untreated and TAFIa-treated soluble fibrin degradation products of varying size
    • Walker J B Nesheim M E A kinetic analysis of the tissue plasminogen activator and DSPAalpha1 cofactor activities of untreated and TAFIa-treated soluble fibrin degradation products of varying size J Biol Chem 2001 276 5 3138 3148
    • (2001) J Biol Chem , vol.276 , Issue.5 , pp. 3138-3148
    • Walker, J.B.1    Nesheim, M.E.2
  • 7
    • 0020673587 scopus 로고
    • A comparison of the abilities of plasma kallikrein, beta-Factor XIIa, Factor XIa and urokinase to activate plasminogen
    • Miles L A Greengard J S Griffin J H A comparison of the abilities of plasma kallikrein, beta-Factor XIIa, Factor XIa and urokinase to activate plasminogen Thromb Res 1983 29 4 407 417
    • (1983) Thromb Res , vol.29 , Issue.4 , pp. 407-417
    • Miles, L.A.1    Greengard, J.S.2    Griffin, J.H.3
  • 8
    • 84964608755 scopus 로고    scopus 로고
    • Plasmin is a natural trigger for bradykinin production in patients with hereditary angioedema with factor XII mutations
    • de Maat S Björkqvist J Suffritti C, et al. Plasmin is a natural trigger for bradykinin production in patients with hereditary angioedema with factor XII mutations J Allergy Clin Immunol 2016 138 5 1414 1423.e9
    • (2016) J Allergy Clin Immunol , vol.138 , Issue.5 , pp. 1414.e9-1423.e9
    • De Maat, S.1    Björkqvist, J.2    Suffritti, C.3
  • 9
    • 79957611298 scopus 로고    scopus 로고
    • Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites
    • Foley J H Cook P F Nesheim M E Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites J Biol Chem 2011 286 22 19280 19286
    • (2011) J Biol Chem , vol.286 , Issue.22 , pp. 19280-19286
    • Foley, J.H.1    Cook, P.F.2    Nesheim, M.E.3
  • 10
    • 84873047947 scopus 로고    scopus 로고
    • Plasminogen receptors and their role in the pathogenesis of inflammatory, autoimmune and malignant disease
    • Godier A Hunt B J Plasminogen receptors and their role in the pathogenesis of inflammatory, autoimmune and malignant disease J Thromb Haemost 2013 11 1 26 34
    • (2013) J Thromb Haemost , vol.11 , Issue.1 , pp. 26-34
    • Godier, A.1    Hunt, B.J.2
  • 12
    • 0037077252 scopus 로고    scopus 로고
    • Cancer-associated cleavage of cytokeratin 8/18 heterotypic complexes exposes a neoepitope in human adenocarcinomas
    • Ditzel H J Strik M C Larsen M K, et al. Cancer-associated cleavage of cytokeratin 8/18 heterotypic complexes exposes a neoepitope in human adenocarcinomas J Biol Chem 2002 277 24 21712 21722
    • (2002) J Biol Chem , vol.277 , Issue.24 , pp. 21712-21722
    • Ditzel, H.J.1    Strik, M.C.2    Larsen, M.K.3
  • 13
    • 0034733665 scopus 로고    scopus 로고
    • 2A proteinase of human rhinovirus cleaves cytokeratin 8 in infected HeLa cells
    • Seipelt J Liebig H D Sommergruber W Gerner C Kuechler E 2A proteinase of human rhinovirus cleaves cytokeratin 8 in infected HeLa cells J Biol Chem 2000 275 26 20084 20089
    • (2000) J Biol Chem , vol.275 , Issue.26 , pp. 20084-20089
    • Seipelt, J.1    Liebig, H.D.2    Sommergruber, W.3    Gerner, C.4    Kuechler, E.5
  • 14
    • 67449093858 scopus 로고    scopus 로고
    • MMP-9 sheds the beta2 integrin subunit (CD18) from macrophages
    • Vaisar T Kassim S Y Gomez I G, et al. MMP-9 sheds the beta2 integrin subunit (CD18) from macrophages Mol Cell Proteomics 2009 8 5 1044 1060
    • (2009) Mol Cell Proteomics , vol.8 , Issue.5 , pp. 1044-1060
    • Vaisar, T.1    Kassim, S.Y.2    Gomez, I.G.3
  • 15
    • 79959840888 scopus 로고    scopus 로고
    • Cathepsin X cleavage of the beta2 integrin regulates talin-binding and LFA-1 affinity in T cells
    • Jevnikar Z Obermajer N Doljak B, et al. Cathepsin X cleavage of the beta2 integrin regulates talin-binding and LFA-1 affinity in T cells J Leukoc Biol 2011 90 1 99 109
    • (2011) J Leukoc Biol , vol.90 , Issue.1 , pp. 99-109
    • Jevnikar, Z.1    Obermajer, N.2    Doljak, B.3
  • 16
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • Deora A B Kreitzer G Jacovina A T Hajjar K A An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface J Biol Chem 2004 279 42 43411 43418
    • (2004) J Biol Chem , vol.279 , Issue.42 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 17
    • 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 T J Kwon M Filipenko N R Waisman D M 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 28 25577 25584
    • (2003) J Biol Chem , vol.278 , Issue.28 , pp. 25577-25584
    • MacLeod, T.J.1    Kwon, M.2    Filipenko, N.R.3    Waisman, D.M.4
  • 18
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation
    • Kassam G Le B H Choi K S, et al. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation Biochemistry 1998 37 48 16958 16966
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 16958-16966
    • Kassam, G.1    Le, B.H.2    Choi, K.S.3
  • 19
    • 36248933738 scopus 로고    scopus 로고
    • Annexin A2 is a soluble mediator of macrophage activation
    • Swisher J F Khatri U Feldman G M Annexin A2 is a soluble mediator of macrophage activation J Leukoc Biol 2007 82 5 1174 1184
    • (2007) J Leukoc Biol , vol.82 , Issue.5 , pp. 1174-1184
    • Swisher, J.F.1    Khatri, U.2    Feldman, G.M.3
  • 20
    • 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 7 902 920
    • (2001) Cell Mol Life Sci , vol.58 , Issue.7 , pp. 902-920
    • Pancholi, V.1
  • 21
    • 36348985036 scopus 로고    scopus 로고
    • Histone H2B as a functionally important plasminogen receptor on macrophages
    • Das R Burke T Plow E F Histone H2B as a functionally important plasminogen receptor on macrophages Blood 2007 110 10 3763 3772
    • (2007) Blood , vol.110 , Issue.10 , pp. 3763-3772
    • Das, R.1    Burke, T.2    Plow, E.F.3
  • 22
    • 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 D R Plow E F L-type calcium channel blockers exert an antiinflammatory effect by suppressing expression of plasminogen receptors on macrophages Circ Res 2009 105 2 167 175
    • (2009) Circ Res , vol.105 , Issue.2 , pp. 167-175
    • Das, R.1    Burke, T.2    Van Wagoner, D.R.3    Plow, E.F.4
  • 23
    • 79251541489 scopus 로고    scopus 로고
    • Phosphatidylserine as an anchor for plasminogen and its plasminogen receptor, histone H2B, to the macrophage surface
    • Das R Plow E F Phosphatidylserine as an anchor for plasminogen and its plasminogen receptor, histone H2B, to the macrophage surface J Thromb Haemost 2011 9 2 339 349
    • (2011) J Thromb Haemost , vol.9 , Issue.2 , pp. 339-349
    • Das, R.1    Plow, E.F.2
  • 24
    • 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
  • 25
    • 84958213231 scopus 로고    scopus 로고
    • Natural heterogeneity of α2-antiplasmin: functional and clinical consequences
    • Abdul S Leebeek F W Rijken D C Uitte de Willige S Natural heterogeneity of α2-antiplasmin: functional and clinical consequences Blood 2016 127 5 538 545
    • (2016) Blood , vol.127 , Issue.5 , pp. 538-545
    • Abdul, S.1    Leebeek, F.W.2    Rijken, D.C.3    Uitte de Willige, S.4
  • 26
    • 0025786961 scopus 로고
    • Inhibition of cell surface receptor-bound plasmin by alpha 2-antiplasmin and alpha 2-macroglobulin
    • Hall S W Humphries J E Gonias S L Inhibition of cell surface receptor-bound plasmin by alpha 2-antiplasmin and alpha 2-macroglobulin J Biol Chem 1991 266 19 12329 12336
    • (1991) J Biol Chem , vol.266 , Issue.19 , pp. 12329-12336
    • Hall, S.W.1    Humphries, J.E.2    Gonias, S.L.3
  • 27
    • 1842678168 scopus 로고    scopus 로고
    • A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis
    • Schneider M Nesheim M A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis J Biol Chem 2004 279 14 13333 13339
    • (2004) J Biol Chem , vol.279 , Issue.14 , pp. 13333-13339
    • Schneider, M.1    Nesheim, M.2
  • 28
    • 84958279850 scopus 로고    scopus 로고
    • Activation of protein C and thrombin activable fibrinolysis inhibitor on cultured human endothelial cells
    • Wu C Kim P Y Swystun L L Liaw P C Weitz J I Activation of protein C and thrombin activable fibrinolysis inhibitor on cultured human endothelial cells J Thromb Haemost 2016 14 2 366 374
    • (2016) J Thromb Haemost , vol.14 , Issue.2 , pp. 366-374
    • Wu, C.1    Kim, P.Y.2    Swystun, L.L.3    Liaw, P.C.4    Weitz, J.I.5
  • 29
    • 0028815556 scopus 로고
    • Plasma carboxypeptidases as regulators of the plasminogen system
    • Redlitz A Tan A K Eaton D L Plow E F Plasma carboxypeptidases as regulators of the plasminogen system J Clin Invest 1995 96 5 2534 2538
    • (1995) J Clin Invest , vol.96 , Issue.5 , pp. 2534-2538
    • Redlitz, A.1    Tan, A.K.2    Eaton, D.L.3    Plow, E.F.4
  • 30
    • 67049088421 scopus 로고    scopus 로고
    • Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung
    • Wygrecka M Marsh L M Morty R E, et al. Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung Blood 2009 113 22 5588 5598
    • (2009) Blood , vol.113 , Issue.22 , pp. 5588-5598
    • Wygrecka, M.1    Marsh, L.M.2    Morty, R.E.3
  • 31
    • 0024431112 scopus 로고
    • Examination of the role of the urokinase receptor in human colon cancer mediated laminin degradation
    • Schlechte W Murano G Boyd D Examination of the role of the urokinase receptor in human colon cancer mediated laminin degradation Cancer Res 1989 49 21 6064 6069
    • (1989) Cancer Res , vol.49 , Issue.21 , pp. 6064-6069
    • Schlechte, W.1    Murano, G.2    Boyd, D.3
  • 32
    • 38549180575 scopus 로고    scopus 로고
    • Tranexamic acid attenuates inflammatory response in cardiopulmonary bypass surgery through blockade of fibrinolysis: a case control study followed by a randomized double-blind controlled trial
    • Jimenez J J Iribarren J L Lorente L, et al. Tranexamic acid attenuates inflammatory response in cardiopulmonary bypass surgery through blockade of fibrinolysis: a case control study followed by a randomized double-blind controlled trial Crit Care 2007 11 6 R117
    • (2007) Crit Care , vol.11 , Issue.6 , pp. R117
    • Jimenez, J.J.1    Iribarren, J.L.2    Lorente, L.3
  • 33
    • 80053999848 scopus 로고    scopus 로고
    • Safety and effectiveness of two treatment regimes with tranexamic acid to minimize inflammatory response in elective cardiopulmonary bypass patients: a randomized double-blind, dose-dependent, phase IV clinical trial
    • Jiménez J J Iribarren J L Brouard M, et al. Safety and effectiveness of two treatment regimes with tranexamic acid to minimize inflammatory response in elective cardiopulmonary bypass patients: a randomized double-blind, dose-dependent, phase IV clinical trial J Cardiothorac Surg 2011 6 138
    • (2011) J Cardiothorac Surg , vol.6 , pp. 138
    • Jiménez, J.J.1    Iribarren, J.L.2    Brouard, M.3
  • 34
    • 84877810645 scopus 로고    scopus 로고
    • Antifibrinolytics attenuate inflammatory gene expression after cardiac surgery
    • 1616.e1-1616.e4
    • Later A F Sitniakowsky L S van Hilten J A, et al. Antifibrinolytics attenuate inflammatory gene expression after cardiac surgery J Thorac Cardiovasc Surg 2013 145 6 1611 1616, 1616.e1-1616.e4
    • (2013) J Thorac Cardiovasc Surg , vol.145 , Issue.6 , pp. 1611-1616
    • Later, A.F.1    Sitniakowsky, L.S.2    Van Hilten, J.A.3
  • 35
    • 0345356441 scopus 로고    scopus 로고
    • Antifibrinolytic therapy during cardiopulmonary bypass reduces proinflammatory cytokine levels: a randomized, double-blind, placebo-controlled study of epsilon-aminocaproic acid and aprotinin
    • Greilich P E Brouse C F Whitten C W Chi L Dimaio J M Jessen M E Antifibrinolytic therapy during cardiopulmonary bypass reduces proinflammatory cytokine levels: a randomized, double-blind, placebo-controlled study of epsilon-aminocaproic acid and aprotinin J Thorac Cardiovasc Surg 2003 126 5 1498 1503
    • (2003) J Thorac Cardiovasc Surg , vol.126 , Issue.5 , pp. 1498-1503
    • Greilich, P.E.1    Brouse, C.F.2    Whitten, C.W.3    Chi, L.4    Dimaio, J.M.5    Jessen, M.E.6
  • 36
    • 84859751812 scopus 로고    scopus 로고
    • Differential effects of aprotinin and tranexamic acid on outcomes and cytokine profiles in neonates undergoing cardiac surgery
    • Graham E M Atz A M Gillis J, et al. Differential effects of aprotinin and tranexamic acid on outcomes and cytokine profiles in neonates undergoing cardiac surgery J Thorac Cardiovasc Surg 2012 143 5 1069 1076
    • (2012) J Thorac Cardiovasc Surg , vol.143 , Issue.5 , pp. 1069-1076
    • Graham, E.M.1    Atz, A.M.2    Gillis, J.3
  • 37
    • 1542283776 scopus 로고    scopus 로고
    • Inhibition of plasmin activity by tranexamic acid does not influence inflammatory pathways during human endotoxemia
    • Renckens R Weijer S de Vos A F, et al. Inhibition of plasmin activity by tranexamic acid does not influence inflammatory pathways during human endotoxemia Arterioscler Thromb Vasc Biol 2004 24 3 483 488
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , Issue.3 , pp. 483-488
    • Renckens, R.1    Weijer, S.2    De Vos, A.F.3
  • 39
    • 0030007064 scopus 로고    scopus 로고
    • Impaired wound healing in mice with a disrupted plasminogen gene
    • Romer J Bugge T H Pyke C, et al. Impaired wound healing in mice with a disrupted plasminogen gene Nat Med 1996 2 3 287 292
    • (1996) Nat Med , vol.2 , Issue.3 , pp. 287-292
    • Romer, J.1    Bugge, T.H.2    Pyke, C.3
  • 40
    • 84939250653 scopus 로고    scopus 로고
    • Fibrinolysis is essential for fracture repair and prevention of heterotopic ossification
    • Yuasa M Mignemi N A Nyman J S, et al. Fibrinolysis is essential for fracture repair and prevention of heterotopic ossification J Clin Invest 2015 125 8 3117 3131
    • (2015) J Clin Invest , vol.125 , Issue.8 , pp. 3117-3131
    • Yuasa, M.1    Mignemi, N.A.2    Nyman, J.S.3
  • 41
    • 14644424644 scopus 로고    scopus 로고
    • The plasminogen activator/plasmin system is essential for development of the joint inflammatory phase of collagen type II-induced arthritis
    • Li J Ny A Leonardsson G Nandakumar K S Holmdahl R Ny T The plasminogen activator/plasmin system is essential for development of the joint inflammatory phase of collagen type II-induced arthritis Am J Pathol 2005 166 3 783 792
    • (2005) Am J Pathol , vol.166 , Issue.3 , pp. 783-792
    • Li, J.1    Ny, A.2    Leonardsson, G.3    Nandakumar, K.S.4    Holmdahl, R.5    Ny, T.6
  • 42
    • 55949112237 scopus 로고    scopus 로고
    • Plasminogen mediates the atherogenic effects of macrophage-expressed urokinase and accelerates atherosclerosis in apoE-knockout mice
    • Kremen M Krishnan R Emery I, et al. Plasminogen mediates the atherogenic effects of macrophage-expressed urokinase and accelerates atherosclerosis in apoE-knockout mice Proc Natl Acad Sci U S A 2008 105 44 17109 17114
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.44 , pp. 17109-17114
    • Kremen, M.1    Krishnan, R.2    Emery, I.3
  • 43
    • 70349784400 scopus 로고    scopus 로고
    • The role of plasminogen-plasmin system in cancer
    • Kwaan H C McMahon B The role of plasminogen-plasmin system in cancer Cancer Treat Res 2009 148 43 66
    • (2009) Cancer Treat Res , vol.148 , pp. 43-66
    • Kwaan, H.C.1    McMahon, B.2
  • 44
    • 0035877968 scopus 로고    scopus 로고
    • Plasmin-induced expression of cytokines and tissue factor in human monocytes involves AP-1 and IKKbeta-mediated NF-kappaB activation
    • Syrovets T Jendrach M Rohwedder A Schüle A Simmet T Plasmin-induced expression of cytokines and tissue factor in human monocytes involves AP-1 and IKKbeta-mediated NF-kappaB activation Blood 2001 97 12 3941 3950
    • (2001) Blood , vol.97 , Issue.12 , pp. 3941-3950
    • Syrovets, T.1    Jendrach, M.2    Rohwedder, A.3    Schüle, A.4    Simmet, T.5
  • 45
    • 0037031851 scopus 로고    scopus 로고
    • The serine protease plasmin triggers expression of MCP-1 and CD40 in human primary monocytes via activation of p38 MAPK and janus kinase (JAK)/STAT signaling pathways
    • Burysek L Syrovets T Simmet T The serine protease plasmin triggers expression of MCP-1 and CD40 in human primary monocytes via activation of p38 MAPK and janus kinase (JAK)/STAT signaling pathways J Biol Chem 2002 277 36 33509 33517
    • (2002) J Biol Chem , vol.277 , Issue.36 , pp. 33509-33517
    • Burysek, L.1    Syrovets, T.2    Simmet, T.3
  • 46
    • 0029846337 scopus 로고    scopus 로고
    • Plasmin is a specific stimulus of the 5-lipoxygenase pathway of human peripheral monocytes
    • Weide I Tippler B Syrovets T Simmet T Plasmin is a specific stimulus of the 5-lipoxygenase pathway of human peripheral monocytes Thromb Haemost 1996 76 4 561 568
    • (1996) Thromb Haemost , vol.76 , Issue.4 , pp. 561-568
    • Weide, I.1    Tippler, B.2    Syrovets, T.3    Simmet, T.4
  • 47
    • 0030996390 scopus 로고    scopus 로고
    • Plasmin is a potent and specific chemoattractant for human peripheral monocytes acting via a cyclic guanosine monophosphate-dependent pathway
    • Syrovets T Tippler B Rieks M Simmet T Plasmin is a potent and specific chemoattractant for human peripheral monocytes acting via a cyclic guanosine monophosphate-dependent pathway Blood 1997 89 12 4574 4583
    • (1997) Blood , vol.89 , Issue.12 , pp. 4574-4583
    • Syrovets, T.1    Tippler, B.2    Rieks, M.3    Simmet, T.4
  • 48
    • 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 Takada Y Plasmin-induced migration of endothelial cells. A potential target for the anti-angiogenic action of angiostatin J Biol Chem 2002 277 37 33564 33570
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 33564-33570
    • Tarui, T.1    Majumdar, M.2    Miles, L.A.3    Ruf, W.4    Takada, Y.5
  • 49
    • 33645733466 scopus 로고    scopus 로고
    • Identification of the annexin A2 heterotetramer as a receptor for the plasmin-induced signaling in human peripheral monocytes
    • Laumonnier Y Syrovets T Burysek L Simmet T Identification of the annexin A2 heterotetramer as a receptor for the plasmin-induced signaling in human peripheral monocytes Blood 2006 107 8 3342 3349
    • (2006) Blood , vol.107 , Issue.8 , pp. 3342-3349
    • Laumonnier, Y.1    Syrovets, T.2    Burysek, L.3    Simmet, T.4
  • 50
    • 77649150754 scopus 로고    scopus 로고
    • Plasmin triggers chemotaxis of monocyte-derived dendritic cells through an Akt2-dependent pathway and promotes a T-helper type-1 response
    • Li X Syrovets T Genze F, et al. Plasmin triggers chemotaxis of monocyte-derived dendritic cells through an Akt2-dependent pathway and promotes a T-helper type-1 response Arterioscler Thromb Vasc Biol 2010 30 3 582 590
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , Issue.3 , pp. 582-590
    • Li, X.1    Syrovets, T.2    Genze, F.3
  • 51
    • 84940497021 scopus 로고    scopus 로고
    • Dendritic cell-mediated phagocytosis but not immune activation is enhanced by plasmin
    • Borg R J Samson A L Au A E, et al. Dendritic cell-mediated phagocytosis but not immune activation is enhanced by plasmin PLoS ONE 2015 10 7 e0131216
    • (2015) PLoS ONE , vol.10 , Issue.7 , pp. e0131216
    • Borg, R.J.1    Samson, A.L.2    Au, A.E.3
  • 52
    • 84870940276 scopus 로고    scopus 로고
    • Mice deficient in urokinase-type plasminogen activator have delayed healing of tympanic membrane perforations
    • Shen Y Guo Y Du C Wilczynska M Hellström S Ny T Mice deficient in urokinase-type plasminogen activator have delayed healing of tympanic membrane perforations PLoS ONE 2012 7 12 e51303
    • (2012) PLoS ONE , vol.7 , Issue.12 , pp. e51303
    • Shen, Y.1    Guo, Y.2    Du, C.3    Wilczynska, M.4    Hellström, S.5    Ny, T.6
  • 53
    • 33745541642 scopus 로고    scopus 로고
    • Plasminogen activation independent of uPA and tPA maintains wound healing in gene-deficient mice
    • Lund L R Green K A Stoop A A, et al. Plasminogen activation independent of uPA and tPA maintains wound healing in gene-deficient mice EMBO J 2006 25 12 2686 2697
    • (2006) EMBO J , vol.25 , Issue.12 , pp. 2686-2697
    • Lund, L.R.1    Green, K.A.2    Stoop, A.A.3
  • 54
    • 84862491710 scopus 로고    scopus 로고
    • Plasminogen is a key proinflammatory regulator that accelerates the healing of acute and diabetic wounds
    • Shen Y Guo Y Mikus P, et al. Plasminogen is a key proinflammatory regulator that accelerates the healing of acute and diabetic wounds Blood 2012 119 24 5879 5887
    • (2012) Blood , vol.119 , Issue.24 , pp. 5879-5887
    • Shen, Y.1    Guo, Y.2    Mikus, P.3
  • 55
    • 16944363984 scopus 로고    scopus 로고
    • Urokinase-generated plasmin activates matrix metalloproteinases during aneurysm formation
    • Carmeliet P Moons L Lijnen R, et al. Urokinase-generated plasmin activates matrix metalloproteinases during aneurysm formation Nat Genet 1997 17 4 439 444
    • (1997) Nat Genet , vol.17 , Issue.4 , pp. 439-444
    • Carmeliet, P.1    Moons, L.2    Lijnen, R.3
  • 56
    • 84883718124 scopus 로고    scopus 로고
    • Diabetes is associated with posttranslational modifications in plasminogen resulting in reduced plasmin generation and enzyme-specific activity
    • Ajjan R A Gamlen T Standeven K F, et al. Diabetes is associated with posttranslational modifications in plasminogen resulting in reduced plasmin generation and enzyme-specific activity Blood 2013 122 1 134 142
    • (2013) Blood , vol.122 , Issue.1 , pp. 134-142
    • Ajjan, R.A.1    Gamlen, T.2    Standeven, K.F.3
  • 57
    • 0033552883 scopus 로고    scopus 로고
    • Atherosclerosis - an inflammatory disease
    • Ross R Atherosclerosis - an inflammatory disease N Engl J Med 1999 340 2 115 126
    • (1999) N Engl J Med , vol.340 , Issue.2 , pp. 115-126
    • Ross, R.1
  • 58
    • 84937526685 scopus 로고    scopus 로고
    • Atherosclerosis - a matter of unresolved inflammation
    • Viola J Soehnlein O Atherosclerosis - a matter of unresolved inflammation Semin Immunol 2015 27 3 184 193
    • (2015) Semin Immunol , vol.27 , Issue.3 , pp. 184-193
    • Viola, J.1    Soehnlein, O.2
  • 59
    • 0029824928 scopus 로고    scopus 로고
    • Regulation and role of urokinase plasminogen activator in vascular remodelling
    • Tkachuk V Stepanova V Little P J Bobik A Regulation and role of urokinase plasminogen activator in vascular remodelling Clin Exp Pharmacol Physiol 1996 23 9 759 765
    • (1996) Clin Exp Pharmacol Physiol , vol.23 , Issue.9 , pp. 759-765
    • Tkachuk, V.1    Stepanova, V.2    Little, P.J.3    Bobik, A.4
  • 60
    • 77950920338 scopus 로고    scopus 로고
    • Overexpression of urokinase by plaque macrophages causes histological features of plaque rupture and increases vascular matrix metalloproteinase activity in aged apolipoprotein e-null mice
    • Hu J H Du L Chu T, et al. Overexpression of urokinase by plaque macrophages causes histological features of plaque rupture and increases vascular matrix metalloproteinase activity in aged apolipoprotein e-null mice Circulation 2010 121 14 1637 1644
    • (2010) Circulation , vol.121 , Issue.14 , pp. 1637-1644
    • Hu, J.H.1    Du, L.2    Chu, T.3
  • 61
    • 84964698090 scopus 로고    scopus 로고
    • Reduction of mouse atherosclerosis by urokinase inhibition or with a limited-spectrum matrix metalloproteinase inhibitor
    • Hu J H Touch P Zhang J, et al. Reduction of mouse atherosclerosis by urokinase inhibition or with a limited-spectrum matrix metalloproteinase inhibitor Cardiovasc Res 2015 105 3 372 382
    • (2015) Cardiovasc Res , vol.105 , Issue.3 , pp. 372-382
    • Hu, J.H.1    Touch, P.2    Zhang, J.3
  • 62
    • 84957613158 scopus 로고    scopus 로고
    • Complement activation in arterial and venous thrombosis is mediated by plasmin
    • Foley J H Walton B L Aleman M M, et al. Complement activation in arterial and venous thrombosis is mediated by plasmin EBioMedicine 2016 5 175 182
    • (2016) EBioMedicine , vol.5 , pp. 175-182
    • Foley, J.H.1    Walton, B.L.2    Aleman, M.M.3
  • 63
    • 78149477844 scopus 로고    scopus 로고
    • Molecular intercommunication between the complement and coagulation systems
    • Amara U Flierl M A Rittirsch D, et al. Molecular intercommunication between the complement and coagulation systems J Immunol 2010 185 9 5628 5636
    • (2010) J Immunol , vol.185 , Issue.9 , pp. 5628-5636
    • Amara, U.1    Flierl, M.A.2    Rittirsch, D.3
  • 64
    • 84861566815 scopus 로고    scopus 로고
    • Plasminogen is a complement inhibitor
    • Barthel D Schindler S Zipfel P F Plasminogen is a complement inhibitor J Biol Chem 2012 287 22 18831 18842
    • (2012) J Biol Chem , vol.287 , Issue.22 , pp. 18831-18842
    • Barthel, D.1    Schindler, S.2    Zipfel, P.F.3
  • 65
    • 84949497174 scopus 로고    scopus 로고
    • Complement activation, regulation, and molecular basis for complement-related diseases
    • Bajic G Degn S E Thiel S Andersen G R Complement activation, regulation, and molecular basis for complement-related diseases EMBO J 2015 34 22 2735 2757
    • (2015) EMBO J , vol.34 , Issue.22 , pp. 2735-2757
    • Bajic, G.1    Degn, S.E.2    Thiel, S.3    Andersen, G.R.4
  • 66
    • 33744987414 scopus 로고    scopus 로고
    • Generation of C5a in the absence of C3: a new complement activation pathway
    • Huber-Lang M Sarma J V Zetoune F S, et al. Generation of C5a in the absence of C3: a new complement activation pathway Nat Med 2006 12 6 682 687
    • (2006) Nat Med , vol.12 , Issue.6 , pp. 682-687
    • Huber-Lang, M.1    Sarma, J.V.2    Zetoune, F.S.3
  • 67
    • 84960503773 scopus 로고    scopus 로고
    • Plasmin cleaves fibrinogen and the human complement proteins C3b and C5 in the presence of Leptospira interrogans proteins: A new role of LigA and LigB in invasion and complement immune evasion
    • Castiblanco-Valencia M M Fraga T R Pagotto A H, et al. Plasmin cleaves fibrinogen and the human complement proteins C3b and C5 in the presence of Leptospira interrogans proteins: A new role of LigA and LigB in invasion and complement immune evasion Immunobiology 2016 221 5 679 689
    • (2016) Immunobiology , vol.221 , Issue.5 , pp. 679-689
    • Castiblanco-Valencia, M.M.1    Fraga, T.R.2    Pagotto, A.H.3
  • 68
    • 84965020752 scopus 로고    scopus 로고
    • Streptococcus pyogenes Employs Strain-dependent Mechanisms of C3b Inactivation to Inhibit Phagocytosis and Killing of Bacteria
    • Agrahari G Liang Z Glinton K Lee S W Ploplis V A Castellino F J Streptococcus pyogenes Employs Strain-dependent Mechanisms of C3b Inactivation to Inhibit Phagocytosis and Killing of Bacteria J Biol Chem 2016 291 17 9181 9189
    • (2016) J Biol Chem , vol.291 , Issue.17 , pp. 9181-9189
    • Agrahari, G.1    Liang, Z.2    Glinton, K.3    Lee, S.W.4    Ploplis, V.A.5    Castellino, F.J.6
  • 70
    • 84867415024 scopus 로고    scopus 로고
    • Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b
    • Koch T K Reuter M Barthel D, et al. Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b PLoS ONE 2012 7 10 e47638
    • (2012) PLoS ONE , vol.7 , Issue.10 , pp. e47638
    • Koch, T.K.1    Reuter, M.2    Barthel, D.3
  • 71
    • 84855366615 scopus 로고    scopus 로고
    • Haemophilus influenzae uses the surface protein E to acquire human plasminogen and to evade innate immunity
    • Barthel D Singh B Riesbeck K Zipfel P F Haemophilus influenzae uses the surface protein E to acquire human plasminogen and to evade innate immunity J Immunol 2012 188 1 379 385
    • (2012) J Immunol , vol.188 , Issue.1 , pp. 379-385
    • Barthel, D.1    Singh, B.2    Riesbeck, K.3    Zipfel, P.F.4
  • 72
    • 34250736946 scopus 로고    scopus 로고
    • Fibrin and fibrinolysis in infection and host defense
    • Degen J L Bugge T H Goguen J D Fibrin and fibrinolysis in infection and host defense J Thromb Haemost 2007 5 01 24 31
    • (2007) J Thromb Haemost , vol.5 , pp. 24-31
    • Degen, J.L.1    Bugge, T.H.2    Goguen, J.D.3
  • 74
    • 84930178029 scopus 로고    scopus 로고
    • Carboxypeptidase B2 deficiency reveals opposite effects of complement C3a and C5a in a murine polymicrobial sepsis model
    • Shao Z Nishimura T Leung L L Morser J Carboxypeptidase B2 deficiency reveals opposite effects of complement C3a and C5a in a murine polymicrobial sepsis model J Thromb Haemost 2015 13 6 1090 1102
    • (2015) J Thromb Haemost , vol.13 , Issue.6 , pp. 1090-1102
    • Shao, Z.1    Nishimura, T.2    Leung, L.L.3    Morser, J.4
  • 75
    • 80052377390 scopus 로고    scopus 로고
    • Plasma carboxypeptidase B downregulates inflammatory responses in autoimmune arthritis
    • Consortium for the Longitudinal Evaluation of African Americans with Early Rheumatoid Arthritis (CLEAR) Registry
    • Song J J Hwang I Cho K H, et al; Consortium for the Longitudinal Evaluation of African Americans with Early Rheumatoid Arthritis (CLEAR) Registry. Plasma carboxypeptidase B downregulates inflammatory responses in autoimmune arthritis J Clin Invest 2011 121 9 3517 3527
    • (2011) J Clin Invest , vol.121 , Issue.9 , pp. 3517-3527
    • Song, J.J.1    Hwang, I.2    Cho, K.H.3
  • 76
    • 0345803939 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation
    • Myles T Nishimura T Yun T H, et al. Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation J Biol Chem 2003 278 51 51059 51067
    • (2003) J Biol Chem , vol.278 , Issue.51 , pp. 51059-51067
    • Myles, T.1    Nishimura, T.2    Yun, T.H.3
  • 77
    • 33847357422 scopus 로고    scopus 로고
    • Thrombin-activatable procarboxypeptidase B regulates activated complement C5a in vivo
    • Nishimura T Myles T Piliponsky A M Kao P N Berry G J Leung L L Thrombin-activatable procarboxypeptidase B regulates activated complement C5a in vivo Blood 2007 109 5 1992 1997
    • (2007) Blood , vol.109 , Issue.5 , pp. 1992-1997
    • Nishimura, T.1    Myles, T.2    Piliponsky, A.M.3    Kao, P.N.4    Berry, G.J.5    Leung, L.L.6
  • 78
    • 0014118360 scopus 로고
    • A plasmin-split fragment of C'3 as a new chemotactic factor
    • Ward P A A plasmin-split fragment of C'3 as a new chemotactic factor J Exp Med 1967 126 2 189 206
    • (1967) J Exp Med , vol.126 , Issue.2 , pp. 189-206
    • Ward, P.A.1
  • 79
    • 84926086856 scopus 로고    scopus 로고
    • Interplay between fibrinolysis and complement: plasmin cleavage of iC3b modulates immune responses
    • Foley J H Peterson E A Lei V Wan L W Krisinger M J Conway E M Interplay between fibrinolysis and complement: plasmin cleavage of iC3b modulates immune responses J Thromb Haemost 2015 13 4 610 618
    • (2015) J Thromb Haemost , vol.13 , Issue.4 , pp. 610-618
    • Foley, J.H.1    Peterson, E.A.2    Lei, V.3    Wan, L.W.4    Krisinger, M.J.5    Conway, E.M.6
  • 80
    • 0037100538 scopus 로고    scopus 로고
    • C5a stimulates production of plasminogen activator inhibitor-1 in human mast cells and basophils
    • Wojta J Kaun C Zorn G, et al. C5a stimulates production of plasminogen activator inhibitor-1 in human mast cells and basophils Blood 2002 100 2 517 523
    • (2002) Blood , vol.100 , Issue.2 , pp. 517-523
    • Wojta, J.1    Kaun, C.2    Zorn, G.3
  • 81
    • 33746585656 scopus 로고    scopus 로고
    • The complement component C5a induces the expression of plasminogen activator inhibitor-1 in human macrophages via NF-kappaB activation
    • Kastl S P Speidl W S Kaun C, et al. The complement component C5a induces the expression of plasminogen activator inhibitor-1 in human macrophages via NF-kappaB activation J Thromb Haemost 2006 4 8 1790 1797
    • (2006) J Thromb Haemost , vol.4 , Issue.8 , pp. 1790-1797
    • Kastl, S.P.1    Speidl, W.S.2    Kaun, C.3
  • 82
    • 84859995396 scopus 로고    scopus 로고
    • Complement C3 is a novel plasma clot component with anti-fibrinolytic properties
    • Howes J M Richardson V R Smith K A, et al. Complement C3 is a novel plasma clot component with anti-fibrinolytic properties Diab Vasc Dis Res 2012 9 3 216 225
    • (2012) Diab Vasc Dis Res , vol.9 , Issue.3 , pp. 216-225
    • Howes, J.M.1    Richardson, V.R.2    Smith, K.A.3
  • 83
    • 84859995395 scopus 로고    scopus 로고
    • A novel mechanism for hypofibrinolysis in diabetes: the role of complement C3
    • Hess K Alzahrani S H Mathai M, et al. A novel mechanism for hypofibrinolysis in diabetes: the role of complement C3 Diabetologia 2012 55 4 1103 1113
    • (2012) Diabetologia , vol.55 , Issue.4 , pp. 1103-1113
    • Hess, K.1    Alzahrani, S.H.2    Mathai, M.3
  • 84
    • 84904732736 scopus 로고    scopus 로고
    • Hypofibrinolysis in type 2 diabetes: the role of the inflammatory pathway and complement C3
    • Hess K Alzahrani S H Price J F, et al. Hypofibrinolysis in type 2 diabetes: the role of the inflammatory pathway and complement C3 Diabetologia 2014 57 8 1737 1741
    • (2014) Diabetologia , vol.57 , Issue.8 , pp. 1737-1741
    • Hess, K.1    Alzahrani, S.H.2    Price, J.F.3
  • 85
    • 84862161993 scopus 로고    scopus 로고
    • Human complement C3 is a substrate for transglutaminases. A functional link between non-protease-based members of the coagulation and complement cascades
    • Nikolajsen C L Scavenius C Enghild J J Human complement C3 is a substrate for transglutaminases. A functional link between non-protease-based members of the coagulation and complement cascades Biochemistry 2012 51 23 4735 4742
    • (2012) Biochemistry , vol.51 , Issue.23 , pp. 4735-4742
    • Nikolajsen, C.L.1    Scavenius, C.2    Enghild, J.J.3
  • 86
    • 84870826374 scopus 로고    scopus 로고
    • Complement C3 is a substrate for activated factor XIII that is cross-linked to fibrin during clot formation
    • Richardson V R Schroeder V Grant P J Standeven K F Carter A M Complement C3 is a substrate for activated factor XIII that is cross-linked to fibrin during clot formation Br J Haematol 2013 160 1 116 119
    • (2013) Br J Haematol , vol.160 , Issue.1 , pp. 116-119
    • Richardson, V.R.1    Schroeder, V.2    Grant, P.J.3    Standeven, K.F.4    Carter, A.M.5


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