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Volumn 8, Issue 4, 2010, Pages 790-798

Dabigatran enhances clot susceptibility to fibrinolysis by mechanisms dependent on and independent of thrombin-activatable fibrinolysis inhibitor

Author keywords

Clot structure; Fibrinolysis; Procarboxypeptidase; Thrombin inhibitors

Indexed keywords

DABIGATRAN; PROTHROMBIN; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; TISSUE PLASMINOGEN ACTIVATOR;

EID: 77952738550     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2010.03739.x     Document Type: Article
Times cited : (87)

References (38)
  • 1
    • 27144505651 scopus 로고    scopus 로고
    • Molecular recognition mechanisms of thrombin
    • Huntington JA. Molecular recognition mechanisms of thrombin. J Thromb Haemost 2005, 3:1861-72.
    • (2005) J Thromb Haemost , vol.3 , pp. 1861-1872
    • Huntington, J.A.1
  • 2
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosesson MW. Fibrinogen and fibrin structure and functions. J Thromb Haemost 2005, 3:1894-904.
    • (2005) J Thromb Haemost , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 3
    • 0034972479 scopus 로고    scopus 로고
    • Factor XIII: structure, activation, and interactions with fibrinogen and fibrin
    • Lorand L. Factor XIII: structure, activation, and interactions with fibrinogen and fibrin. Ann NY Acad Sci 2001, 936:291-311.
    • (2001) Ann NY Acad Sci , vol.936 , pp. 291-311
    • Lorand, L.1
  • 4
    • 34047229067 scopus 로고    scopus 로고
    • Thrombin generation and fibrin clot structure
    • Wolberg AS. Thrombin generation and fibrin clot structure. Blood Rev 2007, 21:131-42.
    • (2007) Blood Rev , vol.21 , pp. 131-142
    • Wolberg, A.S.1
  • 5
    • 0033675696 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and an antifibrinolytic pathway
    • Bajzar L. Thrombin activatable fibrinolysis inhibitor and an antifibrinolytic pathway. Arterioscler Thromb Vasc Biol 2000, 20:2511-18.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 2511-2518
    • Bajzar, L.1
  • 6
    • 33750222459 scopus 로고    scopus 로고
    • Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis
    • Mosnier LO, Bouma BN. Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis. Arterioscler Thromb Vasc Biol 2006, 26:2445-53.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 2445-2453
    • Mosnier, L.O.1    Bouma, B.N.2
  • 7
    • 0032877624 scopus 로고    scopus 로고
    • A novel approach to arterial thrombolysis
    • Klement P, Liao P, Bajzar L. A novel approach to arterial thrombolysis. Blood 1999, 94:2735-43.
    • (1999) Blood , vol.94 , pp. 2735-2743
    • Klement, P.1    Liao, P.2    Bajzar, L.3
  • 8
    • 0032005738 scopus 로고    scopus 로고
    • Activated human protein C prevents thrombin-induced thromboembolism in mice. Evidence that activated protein C reduces intravascular fibrin accumulation through the inhibition of additional thrombin generation
    • Gresele P, Momi S, Berrettini M, Nenci GG, Schwarz HP, Semeraro N, Colucci M. Activated human protein C prevents thrombin-induced thromboembolism in mice. Evidence that activated protein C reduces intravascular fibrin accumulation through the inhibition of additional thrombin generation. J Clin Invest 1998, 101:667-76.
    • (1998) J Clin Invest , vol.101 , pp. 667-676
    • Gresele, P.1    Momi, S.2    Berrettini, M.3    Nenci, G.G.4    Schwarz, H.P.5    Semeraro, N.6    Colucci, M.7
  • 9
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar L, Nesheim ME, Tracy PB. The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 1996, 88:2093-100.
    • (1996) Blood , vol.88 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 10
    • 0141818947 scopus 로고    scopus 로고
    • Rebuttal to: effect of heparin on TAFI-dependent inhibition of fibrinolysis
    • Lisman T, de Groot PG. Rebuttal to: effect of heparin on TAFI-dependent inhibition of fibrinolysis. J Thromb Haemost 2003, 1:200-1.
    • (2003) J Thromb Haemost , vol.1 , pp. 200-201
    • Lisman, T.1    de Groot, P.G.2
  • 11
    • 36949028958 scopus 로고    scopus 로고
    • Profibrinolytic activity of the direct thrombin inhibitor melagatran and unfractionated heparin in platelet-poor and platelet-rich clots
    • Semeraro F, Piro D, Rossiello MR, Ammollo T, Colucci M. Profibrinolytic activity of the direct thrombin inhibitor melagatran and unfractionated heparin in platelet-poor and platelet-rich clots. Thromb Haemost 2007, 98:1208-14.
    • (2007) Thromb Haemost , vol.98 , pp. 1208-1214
    • Semeraro, F.1    Piro, D.2    Rossiello, M.R.3    Ammollo, T.4    Colucci, M.5
  • 14
    • 0042332086 scopus 로고    scopus 로고
    • Enhancement of fibrinolytic potential in vitro by anticoagulant drugs targeting activated factor X, but not by those inhibiting thrombin or tissue factor
    • Lisman T, Adelmeijer J, Nieuwenhuis HK, de Groot PG. Enhancement of fibrinolytic potential in vitro by anticoagulant drugs targeting activated factor X, but not by those inhibiting thrombin or tissue factor. Blood Coagul Fibrinolysis 2003, 14:557-62.
    • (2003) Blood Coagul Fibrinolysis , vol.14 , pp. 557-562
    • Lisman, T.1    Adelmeijer, J.2    Nieuwenhuis, H.K.3    de Groot, P.G.4
  • 15
    • 0037184905 scopus 로고    scopus 로고
    • Studies on the different modes of action of the anticoagulant protease inhibitors DX-9065a and Argatroban. II. Effects on fibrinolysis
    • Nagashima H. Studies on the different modes of action of the anticoagulant protease inhibitors DX-9065a and Argatroban. II. Effects on fibrinolysis. J Biol Chem 2002, 277:50445-9.
    • (2002) J Biol Chem , vol.277 , pp. 50445-50449
    • Nagashima, H.1
  • 16
    • 49149130353 scopus 로고    scopus 로고
    • Dabigatran etexilate
    • Sanford M, Plosker GL. Dabigatran etexilate. Drugs 2008, 68:1699-709.
    • (2008) Drugs , vol.68 , pp. 1699-1709
    • Sanford, M.1    Plosker, G.L.2
  • 17
    • 34447522035 scopus 로고    scopus 로고
    • In-vitro profile and ex-vivo anticoagulant activity of the direct thrombin inhibitor dabigatran and its orally active prodrug, dabigatran etexilate
    • Wienen W, Stassen JM, Priepke H, Ries UJ, Hauel N. In-vitro profile and ex-vivo anticoagulant activity of the direct thrombin inhibitor dabigatran and its orally active prodrug, dabigatran etexilate. Thromb Haemost 2007, 98:155-62.
    • (2007) Thromb Haemost , vol.98 , pp. 155-162
    • Wienen, W.1    Stassen, J.M.2    Priepke, H.3    Ries, U.J.4    Hauel, N.5
  • 18
    • 34250030035 scopus 로고    scopus 로고
    • Antithrombotic and anticoagulant effects of the direct thrombin inhibitor dabigatran, and its oral prodrug, dabigatran etexilate, in a rabbit model of venous thrombosis
    • Wienen W, Stassen JM, Priepke H, Ries UJ, Hauel N. Antithrombotic and anticoagulant effects of the direct thrombin inhibitor dabigatran, and its oral prodrug, dabigatran etexilate, in a rabbit model of venous thrombosis. J Thromb Haemost 2007, 5:1237-42.
    • (2007) J Thromb Haemost , vol.5 , pp. 1237-1242
    • Wienen, W.1    Stassen, J.M.2    Priepke, H.3    Ries, U.J.4    Hauel, N.5
  • 19
    • 64849114023 scopus 로고    scopus 로고
    • Dabigatran etexilate: an oral direct thrombin inhibitor
    • Dahl OE. Dabigatran etexilate: an oral direct thrombin inhibitor. Therapy 2008, 5:685-95.
    • (2008) Therapy , vol.5 , pp. 685-695
    • Dahl, O.E.1
  • 22
    • 33846436118 scopus 로고    scopus 로고
    • Activity and regulation of factor VIIa analogs with increased potency at the endothelial cell surface
    • Ghosh S, Ezban M, Persson E, Pendurthi U, Hedner U, Rao LV. Activity and regulation of factor VIIa analogs with increased potency at the endothelial cell surface. J Thromb Haemost 2007, 5:336-46.
    • (2007) J Thromb Haemost , vol.5 , pp. 336-346
    • Ghosh, S.1    Ezban, M.2    Persson, E.3    Pendurthi, U.4    Hedner, U.5    Rao, L.V.6
  • 23
    • 1542283733 scopus 로고    scopus 로고
    • Hyperprothrombinemia associated with prothrombin G20210A mutation inhibits plasma fibrinolysis through a TAFI-mediated mechanism
    • Colucci M, Binetti BM, Tripodi A, Chantarangkul V, Semeraro N. Hyperprothrombinemia associated with prothrombin G20210A mutation inhibits plasma fibrinolysis through a TAFI-mediated mechanism. Blood 2004, 103:2157-61.
    • (2004) Blood , vol.103 , pp. 2157-2161
    • Colucci, M.1    Binetti, B.M.2    Tripodi, A.3    Chantarangkul, V.4    Semeraro, N.5
  • 24
    • 0020645310 scopus 로고
    • Factors influencing fibrin gel structure studied by flow measurement
    • Okada M, Blombäck B. Factors influencing fibrin gel structure studied by flow measurement. Ann NY Acad Sci 1983, 408:233-53.
    • (1983) Ann NY Acad Sci , vol.408 , pp. 233-253
    • Okada, M.1    Blombäck, B.2
  • 25
    • 0027517306 scopus 로고
    • Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure
    • Collet JP, Soria J, Mirshahi M, Hirsch M, Dagonnet FB, Caen J, Soria C. Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. Blood 1993, 82:2462-9.
    • (1993) Blood , vol.82 , pp. 2462-2469
    • Collet, J.P.1    Soria, J.2    Mirshahi, M.3    Hirsch, M.4    Dagonnet, F.B.5    Caen, J.6    Soria, C.7
  • 26
    • 0001204684 scopus 로고
    • Dextran-induced changes in fibrin fiber size and density based on wavelength dependence of gel turbidity
    • Carr ME, Gabriel DA. Dextran-induced changes in fibrin fiber size and density based on wavelength dependence of gel turbidity. Macromolecules 1980, 13:1473-7.
    • (1980) Macromolecules , vol.13 , pp. 1473-1477
    • Carr, M.E.1    Gabriel, D.A.2
  • 27
    • 50349100313 scopus 로고    scopus 로고
    • Polyphosphate enhances fibrin clot structure
    • Smith SA, Morrissey JH. Polyphosphate enhances fibrin clot structure. Blood 2008, 112:2810-16.
    • (2008) Blood , vol.112 , pp. 2810-2816
    • Smith, S.A.1    Morrissey, J.H.2
  • 28
    • 0036331918 scopus 로고    scopus 로고
    • Effect of heparin on TAFI-dependent inhibition of fibrinolysis: relative importance of TAFIa generated by clot-bound and fluid phase thrombin
    • Colucci M, Pentimone A, Binetti BM, Cramarossa M, Piro D, Semeraro N. Effect of heparin on TAFI-dependent inhibition of fibrinolysis: relative importance of TAFIa generated by clot-bound and fluid phase thrombin. Thromb Haemost 2002, 88:282-7.
    • (2002) Thromb Haemost , vol.88 , pp. 282-287
    • Colucci, M.1    Pentimone, A.2    Binetti, B.M.3    Cramarossa, M.4    Piro, D.5    Semeraro, N.6
  • 29
    • 3142584783 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism
    • Leurs J, Nerme V, Sim Y, Hendriks D. Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism. J Thromb Haemost 2004, 2:416-23.
    • (2004) J Thromb Haemost , vol.2 , pp. 416-423
    • Leurs, J.1    Nerme, V.2    Sim, Y.3    Hendriks, D.4
  • 30
    • 49849089254 scopus 로고    scopus 로고
    • Mild hyperhomocysteinemia is associated with increased TAFI levels and reduced plasma fibrinolytic potential
    • Colucci M, Cattaneo M, Martinelli I, Semeraro F, Binetti BM, Semeraro N. Mild hyperhomocysteinemia is associated with increased TAFI levels and reduced plasma fibrinolytic potential. J Thromb Haemost 2008, 6:1571-7.
    • (2008) J Thromb Haemost , vol.6 , pp. 1571-1577
    • Colucci, M.1    Cattaneo, M.2    Martinelli, I.3    Semeraro, F.4    Binetti, B.M.5    Semeraro, N.6
  • 31
    • 37149005153 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of the direct oral thrombin inhibitor dabigatran in healthy elderly subjects
    • Stangier J, Stähle H, Rathgen K, Fuhr R. Pharmacokinetics and pharmacodynamics of the direct oral thrombin inhibitor dabigatran in healthy elderly subjects. Clin Pharmacokinet 2008, 47:47-59.
    • (2008) Clin Pharmacokinet , vol.47 , pp. 47-59
    • Stangier, J.1    Stähle, H.2    Rathgen, K.3    Fuhr, R.4
  • 32
    • 0022538827 scopus 로고
    • Influence of the fast-acting inhibitor of plasminogen activator on in vivo thrombolysis induced by tissue-type plasminogen activator in rabbits. Interference of tissue-derived components
    • Colucci M, Paramo JA, Stassen JM, Collen D. Influence of the fast-acting inhibitor of plasminogen activator on in vivo thrombolysis induced by tissue-type plasminogen activator in rabbits. Interference of tissue-derived components. J Clin Invest 1986, 78:138-44.
    • (1986) J Clin Invest , vol.78 , pp. 138-144
    • Colucci, M.1    Paramo, J.A.2    Stassen, J.M.3    Collen, D.4
  • 33
    • 0141819138 scopus 로고    scopus 로고
    • The protein C pathway
    • Esmon CT. The protein C pathway. Chest 2003, 124:26S-32S.
    • (2003) Chest , vol.124
    • Esmon, C.T.1
  • 34
    • 0023244130 scopus 로고
    • The inhibition of thrombin-dependent positive-feedback reactions is critical to the expression of the anticoagulant effect of heparin
    • Ofosu FA, Sie P, Modi GJ, Fernandez F, Buchanan MR, Blajchman MA, Boneu B, Hirsh J. The inhibition of thrombin-dependent positive-feedback reactions is critical to the expression of the anticoagulant effect of heparin. Biochem J 1987, 243:579-88.
    • (1987) Biochem J , vol.243 , pp. 579-588
    • Ofosu, F.A.1    Sie, P.2    Modi, G.J.3    Fernandez, F.4    Buchanan, M.R.5    Blajchman, M.A.6    Boneu, B.7    Hirsh, J.8
  • 35
    • 64849116283 scopus 로고    scopus 로고
    • The contribution of anti-Xa and anti-IIa activities to the profibrinolytic activity of low-molecular-weight heparins
    • Ammollo CT, Semeraro F, Semeraro N, Colucci M. The contribution of anti-Xa and anti-IIa activities to the profibrinolytic activity of low-molecular-weight heparins. Thromb Haemost 2009, 101:782-5.
    • (2009) Thromb Haemost , vol.101 , pp. 782-785
    • Ammollo, C.T.1    Semeraro, F.2    Semeraro, N.3    Colucci, M.4
  • 37
    • 57149108951 scopus 로고    scopus 로고
    • Argatroban enhances fibrinolysis by differential inhibition of thrombin-mediated activation of thrombin activatable fibrinolysis inhibitor and factor XIII
    • Nielsen VG, Kirklin JK. Argatroban enhances fibrinolysis by differential inhibition of thrombin-mediated activation of thrombin activatable fibrinolysis inhibitor and factor XIII. Blood Coagul Fibrinolysis 2008, 19:793-800.
    • (2008) Blood Coagul Fibrinolysis , vol.19 , pp. 793-800
    • Nielsen, V.G.1    Kirklin, J.K.2
  • 38
    • 36348956128 scopus 로고    scopus 로고
    • Three different patterns of calibrated automated thrombogram obtained with six different anticoagulants
    • Samama MM, Le Flem L, Guinet C, Gerotziafas G, Depasse F. Three different patterns of calibrated automated thrombogram obtained with six different anticoagulants. J Thromb Haemost 2007, 5:2554-6.
    • (2007) J Thromb Haemost , vol.5 , pp. 2554-2556
    • Samama, M.M.1    Le Flem, L.2    Guinet, C.3    Gerotziafas, G.4    Depasse, F.5


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