메뉴 건너뛰기




Volumn 2014, Issue 1, 2014, Pages 60-65

Recent insights into the role of the contact pathway in thrombo-inflammatory disorders

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR;

EID: 84937571439     PISSN: 15204391     EISSN: 15204383     Source Type: Journal    
DOI: 10.1182/asheducation-2014.1.60     Document Type: Article
Times cited : (47)

References (46)
  • 1
    • 78149485329 scopus 로고    scopus 로고
    • Studies on Fletcher trait and Fitzgerald trait. A rare chance to disclose body's defense reactions against injury
    • Saito H. Studies on Fletcher trait and Fitzgerald trait. A rare chance to disclose body's defense reactions against injury. Thromb Haemost. 2010:104(5):867-874.
    • (2010) Thromb Haemost , vol.104 , Issue.5 , pp. 867-874
    • Saito, H.1
  • 2
    • 84859707412 scopus 로고    scopus 로고
    • The procoagulant and proinflammatory plasma contact system
    • Renne T. The procoagulant and proinflammatory plasma contact system. Semin Immunopathol. 2012;34(1):31-41.
    • (2012) Semin Immunopathol , vol.34 , Issue.1 , pp. 31-41
    • Renne, T.1
  • 3
    • 84937583231 scopus 로고    scopus 로고
    • The coagulation system and its function in early immune defense
    • In Press
    • van der Poll T, Herwald H. The coagulation system and its function in early immune defense. Thromb Haemost. In Press.
    • Thromb Haemost
    • Van Der Poll, T.1    Herwald, H.2
  • 4
    • 84867004428 scopus 로고    scopus 로고
    • Crosstalk of the plasma contact system with bacteria
    • Nickel KF, Renne T. Crosstalk of the plasma contact system with bacteria. Thromb Res. 2012;130(Suppl 1):S78-S83.
    • (2012) Thromb Res , vol.130 , pp. S78-S83
    • Nickel, K.F.1    Renne, T.2
  • 5
    • 84871505285 scopus 로고    scopus 로고
    • Thrombosis as an intravascular effector of innate immunity
    • Engelmann B, Massberg S. Thrombosis as an intravascular effector of innate immunity. Nat Rev Immunol. 2013;13(1):34-45.
    • (2013) Nat Rev Immunol , vol.13 , Issue.1 , pp. 34-45
    • Engelmann, B.1    Massberg, S.2
  • 6
    • 34447322451 scopus 로고    scopus 로고
    • Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation
    • Kannemeier C, Shibamiya A, Nakazawa F, et al. Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation. Proc Natl Acad Sci U S A. 2007;104(15):6388-6393.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.15 , pp. 6388-6393
    • Kannemeier, C.1    Shibamiya, A.2    Nakazawa, F.3
  • 7
    • 84862729665 scopus 로고    scopus 로고
    • Polyphosphate: An ancient molecule that links platelets, coagulation, and inflammation
    • Morrissey JH, Choi SH, Smith SA. Polyphosphate: an ancient molecule that links platelets, coagulation, and inflammation. Blood. 2012;119(25): 5972-5979.
    • (2012) Blood , vol.119 , Issue.25 , pp. 5972-5979
    • Morrissey, J.H.1    Choi, S.H.2    Smith, S.A.3
  • 8
    • 84861750668 scopus 로고    scopus 로고
    • Monocytes, neutrophils, and platelets cooperate to initiate and propagate venous thrombosis in mice in vivo
    • von Bruhl ML, Stark K, Steinhart A, et al. Monocytes, neutrophils, and platelets cooperate to initiate and propagate venous thrombosis in mice in vivo. J Exp Med. 2012;209(4):819-835.
    • (2012) J Exp Med , vol.209 , Issue.4 , pp. 819-835
    • Von Bruhl, M.L.1    Stark, K.2    Steinhart, A.3
  • 9
    • 51349160073 scopus 로고    scopus 로고
    • Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation
    • Maas C, Govers-Riemslag JW, Bouma B, et al. Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation. J Clin Invest. 2008;118(9):3208-3218.
    • (2008) J Clin Invest , vol.118 , Issue.9 , pp. 3208-3218
    • Maas, C.1    Govers-Riemslag, J.W.2    Bouma, B.3
  • 10
    • 70349578489 scopus 로고    scopus 로고
    • Activation of the human contact system on neutrophil extracellular traps
    • Oehmcke S, Morgelin M, Herwald H. Activation of the human contact system on neutrophil extracellular traps. J Innate Immun. 2009;1(3):225-230.
    • (2009) J Innate Immun , vol.1 , Issue.3 , pp. 225-230
    • Oehmcke, S.1    Morgelin, M.2    Herwald, H.3
  • 11
    • 0037124049 scopus 로고    scopus 로고
    • Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator
    • Shariat-Madar Z, Mahdi F, Schmaier AH. Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. J Biol Chem. 2002;277(20):17962-17969.
    • (2002) J Biol Chem , vol.277 , Issue.20 , pp. 17962-17969
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 12
    • 84898978532 scopus 로고    scopus 로고
    • Physiologic activities of the contact activation system
    • Schmaier AH. Physiologic activities of the contact activation system. Thromb Res. 2014;133(Suppl 1):S41-S44.
    • (2014) Thromb Res , vol.133 , pp. S41-S44
    • Schmaier, A.H.1
  • 13
    • 13444267658 scopus 로고    scopus 로고
    • Formation of bradykinin: A major contributor to the innate inflammatory response
    • Joseph K, Kaplan AP. Formation of bradykinin: a major contributor to the innate inflammatory response. Adv Immunol. 2005;86:159-208.
    • (2005) Adv Immunol , vol.86 , pp. 159-208
    • Joseph, K.1    Kaplan, A.P.2
  • 14
    • 84883216057 scopus 로고    scopus 로고
    • Plasma kallikrein: The bradykininproducing enzyme
    • Bjorkqvist J, Jamsa A, Renne T. Plasma kallikrein: the bradykininproducing enzyme. Thromb Haemost. 2013;110(3):399-407.
    • (2013) Thromb Haemost , vol.110 , Issue.3 , pp. 399-407
    • Bjorkqvist, J.1    Jamsa, A.2    Renne, T.3
  • 15
    • 33751579326 scopus 로고    scopus 로고
    • The contact system-a novel branch of innate immunity generating antibacterial peptides
    • Frick IM, Akesson P, Herwald H, et al. The contact system-a novel branch of innate immunity generating antibacterial peptides. EMBO J. 2006;25(23):5569-5578.
    • (2006) EMBO J , vol.25 , Issue.23 , pp. 5569-5578
    • Frick, I.M.1    Akesson, P.2    Herwald, H.3
  • 16
    • 67849097372 scopus 로고    scopus 로고
    • Factor XI deficiency in humans
    • Seligsohn U. Factor XI deficiency in humans. J Thromb Haemost. 2009;7(Suppl 1):84-87.
    • (2009) J Thromb Haemost , vol.7 , pp. 84-87
    • Seligsohn, U.1
  • 17
    • 81455127094 scopus 로고    scopus 로고
    • Therapeutic approaches in hereditary angioedema
    • Antoniu SA. Therapeutic approaches in hereditary angioedema. Clin Rev Allergy Immunol. 2011;41(1):114-122.
    • (2011) Clin Rev Allergy Immunol , vol.41 , Issue.1 , pp. 114-122
    • Antoniu, S.A.1
  • 18
    • 33845219794 scopus 로고    scopus 로고
    • Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III
    • Cichon S, Martin L, Hennies HC, et al. Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am J Hum Genet. 2006;79(6):1098-1104.
    • (2006) Am J Hum Genet , vol.79 , Issue.6 , pp. 1098-1104
    • Cichon, S.1    Martin, L.2    Hennies, H.C.3
  • 19
    • 80053130267 scopus 로고    scopus 로고
    • A novel mutation in the coagulation factor 12 gene in subjects with hereditary angioedema and normal C1-inhibitor
    • Bork K, Wulff K, Meinke P, Wagner N, Hardt J, Witzke G. A novel mutation in the coagulation factor 12 gene in subjects with hereditary angioedema and normal C1-inhibitor. Clin Immunol. 2011;141(1):31-35.
    • (2011) Clin Immunol , vol.141 , Issue.1 , pp. 31-35
    • Bork, K.1    Wulff, K.2    Meinke, P.3    Wagner, N.4    Hardt, J.5    Witzke, G.6
  • 20
    • 33646026697 scopus 로고    scopus 로고
    • Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor
    • Dewald G, Bork K. Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor. Biochem Biophys Res Commun. 2006;343(4):1286-1289.
    • (2006) Biochem Biophys Res Commun , vol.343 , Issue.4 , pp. 1286-1289
    • Dewald, G.1    Bork, K.2
  • 22
    • 23044453832 scopus 로고    scopus 로고
    • Effects of factor IX or factor XI deficiency on ferric chloride-induced carotid artery occlusion in mice
    • Wang X, Cheng Q, Xu L, et al. Effects of factor IX or factor XI deficiency on ferric chloride-induced carotid artery occlusion in mice. J Thromb Haemost. 2005;3(4):695-702.
    • (2005) J Thromb Haemost , vol.3 , Issue.4 , pp. 695-702
    • Wang, X.1    Cheng, Q.2    Xu, L.3
  • 23
    • 33747200433 scopus 로고    scopus 로고
    • Effects of factor XI deficiency on ferric chloride-induced vena cava thrombosis in mice
    • Wang X, Smith PL, Hsu MY, et al. Effects of factor XI deficiency on ferric chloride-induced vena cava thrombosis in mice. J Thromb Haemost. 2006:4(9):1982-1988.
    • (2006) J Thromb Haemost , vol.4 , Issue.9 , pp. 1982-1988
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3
  • 24
    • 0036212988 scopus 로고    scopus 로고
    • FXI is essential for thrombus formation following FeCl3-induced injury of the carotid artery in the mouse
    • Rosen ED, Gailani D, Castellino FJ. FXI is essential for thrombus formation following FeCl3-induced injury of the carotid artery in the mouse. Thromb Haemost. 2002;87(4):774-776.
    • (2002) Thromb Haemost , vol.87 , Issue.4 , pp. 774-776
    • Rosen, E.D.1    Gailani, D.2    Castellino, F.J.3
  • 25
    • 84863229481 scopus 로고    scopus 로고
    • Antisense inhibition of coagulation factor XI prolongs APTT without increased bleeding risk in cynomolgus monkeys
    • Younis HS, Crosby J, Huh JI, et al. Antisense inhibition of coagulation factor XI prolongs APTT without increased bleeding risk in cynomolgus monkeys. Blood. 2012;119(10):2401-2408.
    • (2012) Blood , vol.119 , Issue.10 , pp. 2401-2408
    • Younis, H.S.1    Crosby, J.2    Huh, J.I.3
  • 26
    • 78649471947 scopus 로고    scopus 로고
    • Inhibition of the intrinsic coagulation pathway factor XI by antisense oligonucleotides: A novel antithrombotic strategy with lowered bleeding risk
    • Zhang H, Lowenberg EC, Crosby JR, et al. Inhibition of the intrinsic coagulation pathway factor XI by antisense oligonucleotides: a novel antithrombotic strategy with lowered bleeding risk. Blood. 2010;116(22): 4684-4692.
    • (2010) Blood , vol.116 , Issue.22 , pp. 4684-4692
    • Zhang, H.1    Lowenberg, E.C.2    Crosby, J.R.3
  • 27
    • 78149428887 scopus 로고    scopus 로고
    • A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo
    • Cheng Q, Tucker EI, Pine MS, et al. A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo. Blood. 2010;116(19): 3981-3989.
    • (2010) Blood , vol.116 , Issue.19 , pp. 3981-3989
    • Cheng, Q.1    Tucker, E.I.2    Pine, M.S.3
  • 28
    • 84886999571 scopus 로고    scopus 로고
    • Two novel inhibitory anti-human factor XI antibodies prevent cessation of blood flow in a murine venous thrombosis model
    • van Montfoort ML, Knaup VL, Marquart JA, et al. Two novel inhibitory anti-human factor XI antibodies prevent cessation of blood flow in a murine venous thrombosis model. Thromb Haemost. 2013;110(5):1065-1073.
    • (2013) Thromb Haemost , vol.110 , Issue.5 , pp. 1065-1073
    • Van Montfoort, M.L.1    Knaup, V.L.2    Marquart, J.A.3
  • 29
    • 84879076198 scopus 로고    scopus 로고
    • Antithrombotic effect of antisense factor XI oligonucleotide treatment in primates
    • Crosby JR, Marzec U, Revenko AS, et al. Antithrombotic effect of antisense factor XI oligonucleotide treatment in primates. Arterioscler Thromb Vasc Biol. 2013;33(7):1670-1678.
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , Issue.7 , pp. 1670-1678
    • Crosby, J.R.1    Marzec, U.2    Revenko, A.S.3
  • 30
    • 59649103257 scopus 로고    scopus 로고
    • Prevention of vascular graft occlusion and thrombus-associated thrombin generation by inhibition of factor XI
    • Tucker EI, Marzec UM, White TC, et al. Prevention of vascular graft occlusion and thrombus-associated thrombin generation by inhibition of factor XI. Blood. 2009;113(4):936-944.
    • (2009) Blood , vol.113 , Issue.4 , pp. 936-944
    • Tucker, E.I.1    Marzec, U.M.2    White, T.C.3
  • 31
    • 84904573568 scopus 로고    scopus 로고
    • Factor XI regulates pathological thrombus formation on acutely ruptured atherosclerotic plaques
    • van Montfoort ML, Kuijpers MJ, Knaup VL, et al. Factor XI Regulates Pathological Thrombus Formation on Acutely Ruptured Atherosclerotic Plaques. Arterioscler Thromb Vasc Biol. 2014;34(8):1668-1673.
    • (2014) Arterioscler Thromb Vasc Biol , vol.34 , Issue.8 , pp. 1668-1673
    • Van Montfoort, M.L.1    Kuijpers, M.J.2    Knaup, V.L.3
  • 32
    • 78651487170 scopus 로고    scopus 로고
    • Comparative incidence of thrombosis in reported cases of deficiencies of factors of the contact phase of blood coagulation
    • Girolami A, Candeo N, De Marinis GB, Bonamigo E, Girolami B. Comparative incidence of thrombosis in reported cases of deficiencies of factors of the contact phase of blood coagulation. J Thromb Thrombolysis. 2011;31(1):57-63.
    • (2011) J Thromb Thrombolysis , vol.31 , Issue.1 , pp. 57-63
    • Girolami, A.1    Candeo, N.2    De Marinis, G.B.3    Bonamigo, E.4    Girolami, B.5
  • 33
    • 22944462705 scopus 로고    scopus 로고
    • Defective thrombus formation in mice lacking coagulation factor XII
    • Renne T, Pozgajova M, Gruner S, et al. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med. 2005;202(2):271-281.
    • (2005) J Exp Med , vol.202 , Issue.2 , pp. 271-281
    • Renne, T.1    Pozgajova, M.2    Gruner, S.3
  • 34
    • 77950899732 scopus 로고    scopus 로고
    • Factor XIIa inhibitor recombinant human albumin Infestin-4 abolishes occlusive arterial thrombus formation without affecting bleeding
    • Hagedorn I, Schmidbauer S, Pleines I, et al. Factor XIIa inhibitor recombinant human albumin Infestin-4 abolishes occlusive arterial thrombus formation without affecting bleeding. Circulation. 2010; 121(13):1510-1517.
    • (2010) Circulation , vol.121 , Issue.13 , pp. 1510-1517
    • Hagedorn, I.1    Schmidbauer, S.2    Pleines, I.3
  • 35
    • 71149116751 scopus 로고    scopus 로고
    • Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo
    • Muller F, Mutch NJ, Schenk WA, et al. Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo. Cell. 2009;139(6): 1143-1156.
    • (2009) Cell , vol.139 , Issue.6 , pp. 1143-1156
    • Muller, F.1    Mutch, N.J.2    Schenk, W.A.3
  • 36
    • 84904675375 scopus 로고    scopus 로고
    • Factor XII regulates the pathological process of thrombus formation on ruptured plaques
    • Kuijpers MJ, van der Meijden PE, Feijge MA, et al. Factor XII regulates the pathological process of thrombus formation on ruptured plaques. Arterioscler Thromb Vasc Biol. 2014;34(8):1674-1680.
    • (2014) Arterioscler Thromb Vasc Biol , vol.34 , Issue.8 , pp. 1674-1680
    • Kuijpers, M.J.1    Van Der Meijden, P.E.2    Feijge, M.A.3
  • 37
    • 84897538637 scopus 로고    scopus 로고
    • Factor XII inhibition reduces thrombus formation in a primate thrombosis model
    • Matafonov A, Leung PY, Gailani AE, et al. Factor XII inhibition reduces thrombus formation in a primate thrombosis model. Blood. 2014;123(11):1739-1746.
    • (2014) Blood , vol.123 , Issue.11 , pp. 1739-1746
    • Matafonov, A.1    Leung, P.Y.2    Gailani, A.E.3
  • 38
    • 84893834884 scopus 로고    scopus 로고
    • A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk
    • Larsson M, Rayzman V, Nolte MW, et al. A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk. Sci Transl Med. 2014;6(222):222ra17.
    • (2014) Sci Transl Med , vol.6 , Issue.222 , pp. 222ra17
    • Larsson, M.1    Rayzman, V.2    Nolte, M.W.3
  • 39
    • 80053641885 scopus 로고    scopus 로고
    • Factor XIIa regulates the structure of the fibrin clot independently of thrombin generation through direct interaction with fibrin
    • Konings J, Govers-Riemslag JW, Philippou H, et al. Factor XIIa regulates the structure of the fibrin clot independently of thrombin generation through direct interaction with fibrin. Blood. 2011;118(14): 3942-3951.
    • (2011) Blood , vol.118 , Issue.14 , pp. 3942-3951
    • Konings, J.1    Govers-Riemslag, J.W.2    Philippou, H.3
  • 40
    • 81155133305 scopus 로고    scopus 로고
    • Selective depletion of plasma prekallikrein or coagulation factor XII inhibits thrombosis in mice without increased risk of bleeding
    • Revenko AS, Gao D, Crosby JR, et al. Selective depletion of plasma prekallikrein or coagulation factor XII inhibits thrombosis in mice without increased risk of bleeding. Blood. 2011;118(19):5302-5311.
    • (2011) Blood , vol.118 , Issue.19 , pp. 5302-5311
    • Revenko, A.S.1    Gao, D.2    Crosby, J.R.3
  • 41
    • 84861727362 scopus 로고    scopus 로고
    • Effects of plasma kallikrein deficiency on haemostasis and thrombosis in mice: Murine ortholog of the Fletcher trait
    • Bird JE, Smith PL, Wang X, et al. Effects of plasma kallikrein deficiency on haemostasis and thrombosis in mice: murine ortholog of the Fletcher trait. Thromb Haemost. 2012;107(6):1141-1150.
    • (2012) Thromb Haemost , vol.107 , Issue.6 , pp. 1141-1150
    • Bird, J.E.1    Smith, P.L.2    Wang, X.3
  • 42
    • 79953816704 scopus 로고    scopus 로고
    • Murine prolylcarboxypeptidase depletion induces vascular dysfunction with hypertension and faster arterial thrombosis
    • Adams GN, LaRusch GA, Stavrou E, et al. Murine prolylcarboxypeptidase depletion induces vascular dysfunction with hypertension and faster arterial thrombosis. Blood. 2011;117(14):3929-3937.
    • (2011) Blood , vol.117 , Issue.14 , pp. 3929-3937
    • Adams, G.N.1    LaRusch, G.A.2    Stavrou, E.3
  • 43
    • 38949099750 scopus 로고    scopus 로고
    • Deletion of murine kininogen gene 1 (mKng1) causes loss of plasma kininogen and delays thrombosis
    • Merkulov S, Zhang WM, Komar AA, et al. Deletion of murine kininogen gene 1 (mKng1) causes loss of plasma kininogen and delays thrombosis. Blood. 2008;111(3):1274-1281.
    • (2008) Blood , vol.111 , Issue.3 , pp. 1274-1281
    • Merkulov, S.1    Zhang, W.M.2    Komar, A.A.3
  • 44
    • 84868603189 scopus 로고    scopus 로고
    • Kininogen deficiency protects from ischemic neurodegeneration in mice by reducing thrombosis, bloodbrain barrier damage, and inflammation
    • Langhauser F, Gob E, Kraft P, et al. Kininogen deficiency protects from ischemic neurodegeneration in mice by reducing thrombosis, bloodbrain barrier damage, and inflammation. Blood. 2012;120(19):4082-4092.
    • (2012) Blood , vol.120 , Issue.19 , pp. 4082-4092
    • Langhauser, F.1    Gob, E.2    Kraft, P.3
  • 45
    • 33745591921 scopus 로고    scopus 로고
    • Bradykinin B2 receptor knockout mice are protected from thrombosis by increased nitric oxide and prostacyclin
    • Shariat-Madar Z, Mahdi F, Warnock M, et al. Bradykinin B2 receptor knockout mice are protected from thrombosis by increased nitric oxide and prostacyclin. Blood. 2006;108(1):192-199.
    • (2006) Blood , vol.108 , Issue.1 , pp. 192-199
    • Shariat-Madar, Z.1    Mahdi, F.2    Warnock, M.3
  • 46
    • 84879451953 scopus 로고    scopus 로고
    • Angiotensin 1-7 and Mas decrease thrombosis in Bdkrb2-/- mice by increasing NO and prostacyclin to reduce platelet spreading and glycoprotein VI activation
    • Fang C, Stavrou E, Schmaier AA, et al. Angiotensin 1-7 and Mas decrease thrombosis in Bdkrb2-/- mice by increasing NO and prostacyclin to reduce platelet spreading and glycoprotein VI activation. Blood. 2013;121(15):3023-3032.
    • (2013) Blood , vol.121 , Issue.15 , pp. 3023-3032
    • Fang, C.1    Stavrou, E.2    Schmaier, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.