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Volumn 92, Issue 5, 2004, Pages 1025-1031

Thrombin activatable fibrinolysis inhibitor and its fibrinolytic effect in normal pregnancy

Author keywords

Clot lysis; Fibrinolysis; Pregnancy; Protein C; Thrombin activatable fibrinolysis inhibitor

Indexed keywords

ACTIVATED PROTEIN C; PROTEIN C; PROTEIN S; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; THROMBOMODULIN;

EID: 9144235693     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH04-06-0387     Document Type: Article
Times cited : (28)

References (31)
  • 1
    • 0026658954 scopus 로고
    • Enhanced thrombin generation and fibrinolytic activity in normal pregnancy and the puerperium
    • Bremme K, Ostlund E, Almqvist I, et al. Enhanced thrombin generation and fibrinolytic activity in normal pregnancy and the puerperium. Obstet Gynecol 1992; 80: 132-7.
    • (1992) Obstet. Gynecol. , vol.80 , pp. 132-137
    • Bremme, K.1    Ostlund, E.2    Almqvist, I.3
  • 2
    • 0030298277 scopus 로고    scopus 로고
    • Blood clotting activation during normal pregnancy
    • Comeglio P, Fedi S, Liotta AA, et al. Blood clotting activation during normal pregnancy. Thromb Res 1996; 84: 199-202.
    • (1996) Thromb. Res. , vol.84 , pp. 199-202
    • Comeglio, P.1    Fedi, S.2    Liotta, A.A.3
  • 3
    • 0032753063 scopus 로고    scopus 로고
    • A laboratory method for determination of overall haemostatic potential in plasma. I. Method design and preliminary results
    • He S, Bremme K, Blomback M. A laboratory method for determination of overall haemostatic potential in plasma. I. Method design and preliminary results. Thromb Res 1999; 96: 145-56.
    • (1999) Thromb. Res. , vol.96 , pp. 145-156
    • He, S.1    Bremme, K.2    Blomback, M.3
  • 4
    • 0027233840 scopus 로고
    • Fibrinolytic components in individual consecutive plasma samples during normal pregnancy
    • Lindoff C, Lecander I, Astedt B. Fibrinolytic components in individual consecutive plasma samples during normal pregnancy. Fibrinolysis 1993; 7: 190-4.
    • (1993) Fibrinolysis , vol.7 , pp. 190-194
    • Lindoff, C.1    Lecander, I.2    Astedt, B.3
  • 5
    • 0022648519 scopus 로고
    • Isolation of a new specific plasminogen activator inhibitor from pregnancy plasma
    • Lecander I, Astedt B. Isolation of a new specific plasminogen activator inhibitor from pregnancy plasma. Br J Haematol 1986; 62: 221-8.
    • (1986) Br. J. Haematol. , vol.62 , pp. 221-228
    • Lecander, I.1    Astedt, B.2
  • 6
    • 0023945096 scopus 로고
    • Fibrinolysis during normal human pregnancy: Complex inter-relationships between plasma levels of tissue plasminogen activator and inhibitors and the euglobulin clot lysis time
    • Wright JG, Cooper P, Astedt B, et al. Fibrinolysis during normal human pregnancy: complex inter-relationships between plasma levels of tissue plasminogen activator and inhibitors and the euglobulin clot lysis time. Br J Haematol 1988; 69: 253-8.
    • (1988) Br. J. Haematol. , vol.69 , pp. 253-258
    • Wright, J.G.1    Cooper, P.2    Astedt, B.3
  • 7
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • Bajzar L, Morser J, Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem 1996; 271: 16603-8.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 8
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • Nesheim M, Wang W, Boffa M, et al. Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb Haemost 1997; 78: 386-91.
    • (1997) Thromb. Haemost. , vol.78 , pp. 386-391
    • Nesheim, M.1    Wang, W.2    Boffa, M.3
  • 9
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor
    • Wang W, Boffa MB, Bajzar L, et al. A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 1998; 273: 27176-81.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27176-27181
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3
  • 10
    • 0035071928 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor (TAFI) does not inhibit in vitro thrombolysis by pharmacological concentrations of t-PA
    • Colucci M, D'Aprile AM, Italia A, et al. Thrombin activatable fibrinolysis inhibitor (TAFI) does not inhibit in vitro thrombolysis by pharmacological concentrations of t-PA. Thromb Haemost 2001; 85: 661-6.
    • (2001) Thromb. Haemost. , vol.85 , pp. 661-666
    • Colucci, M.1    D'Aprile, A.M.2    Italia, A.3
  • 11
    • 0029124884 scopus 로고
    • Fibrinolytic agents: Mechanisms of activity and pharmacology
    • Lijnen HR, Collen D. Fibrinolytic agents: mechanisms of activity and pharmacology. Thromb Haemost 1995; 74: 387-90.
    • (1995) Thromb. Haemost. , vol.74 , pp. 387-390
    • Lijnen, H.R.1    Collen, D.2
  • 12
    • 0032579276 scopus 로고    scopus 로고
    • Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor
    • Bajzar L, Nesheim M, Morser J, et al. Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor. J Biol Chem 1998; 273: 2792-8.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2792-2798
    • Bajzar, L.1    Nesheim, M.2    Morser, J.3
  • 13
    • 0030858413 scopus 로고    scopus 로고
    • Coagulation factor V: An old star shines again
    • Rosing J, Tans G. Coagulation factor V: an old star shines again. Thromb Haemost 1997; 78: 427-33.
    • (1997) Thromb. Haemost. , vol.78 , pp. 427-433
    • Rosing, J.1    Tans, G.2
  • 14
    • 0023096623 scopus 로고
    • The regulation of natural anticoagulant pathways
    • Esmon CT. The regulation of natural anticoagulant pathways. Science 1987; 235: 1348-52.
    • (1987) Science , vol.235 , pp. 1348-1352
    • Esmon, C.T.1
  • 15
    • 0027419521 scopus 로고
    • The effect of activated protein C on fibrinolysis in cell-free plasma can be attributed specifically to attenuation of prothrombin activation
    • Bajzar L, Nesheim M. The effect of activated protein C on fibrinolysis in cell-free plasma can be attributed specifically to attenuation of prothrombin activation. J Biol Chem 1993; 268: 8608-16.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8608-8616
    • Bajzar, L.1    Nesheim, M.2
  • 16
    • 0035173479 scopus 로고    scopus 로고
    • Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin
    • Mosnier LO, Meijers JC, Bouma BN. Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin. Thromb Haemost 2001; 85: 5-11.
    • (2001) Thromb. Haemost. , vol.85 , pp. 5-11
    • Mosnier, L.O.1    Meijers, J.C.2    Bouma, B.N.3
  • 17
    • 0842320987 scopus 로고    scopus 로고
    • New insights into factors affecting clot stability: A role for thrombin activatable fibrinolysis inhibitor (TAFI; plasma procarboxypeptidase B, plasma procarboxypeptidase U, procarboxypeptidase R)
    • Bouma BN, Meijers JC. New insights into factors affecting clot stability: A role for thrombin activatable fibrinolysis inhibitor (TAFI; plasma procarboxypeptidase B, plasma procarboxypeptidase U, procarboxypeptidase R). Semin Hematol 2004; 41(1 Suppl 1): 13-9.
    • (2004) Semin. Hematol. , vol.41 , Issue.1 SUPPL. 1 , pp. 13-19
    • Bouma, B.N.1    Meijers, J.C.2
  • 18
    • 0031833418 scopus 로고    scopus 로고
    • Predictive value of plasma thrombomodulin in preeclampsia and gestational hypertension
    • Boffa MC, Valsecchi L, Fausto A, et al. Predictive value of plasma thrombomodulin in preeclampsia and gestational hypertension. Thromb Haemost 1998; 79: 1092-5.
    • (1998) Thromb. Haemost. , vol.79 , pp. 1092-1095
    • Boffa, M.C.1    Valsecchi, L.2    Fausto, A.3
  • 19
    • 0031910006 scopus 로고    scopus 로고
    • Thrombomodulin levels during normal pregnancy, at delivery and in the postpartum: Comparison with tissue-type plasminogen activator and plasminogen activator inhibitor-1
    • de Moerloose P, Mermillod N, Amiral J, et al. Thrombomodulin levels during normal pregnancy, at delivery and in the postpartum: comparison with tissue-type plasminogen activator and plasminogen activator inhibitor-1. Thromb Haemost 1998; 79: 554-6.
    • (1998) Thromb. Haemost. , vol.79 , pp. 554-556
    • de Moerloose, P.1    Mermillod, N.2    Amiral, J.3
  • 20
    • 0034131501 scopus 로고    scopus 로고
    • Plasma TAFI antigen variations in healthy subjects
    • Chetaille P, Alessi MC, Kouassi D, et al. Plasma TAFI antigen variations in healthy subjects. Thromb Haemost 2000; 83: 902-5.
    • (2000) Thromb. Haemost. , vol.83 , pp. 902-905
    • Chetaille, P.1    Alessi, M.C.2    Kouassi, D.3
  • 21
    • 0034772159 scopus 로고    scopus 로고
    • TAFI antigen and D-dimer levels during normal pregnancy and at delivery
    • Chabloz P, Reber G, Boeblen F, et al. TAFI antigen and D-dimer levels during normal pregnancy and at delivery. Br J Haematol 2001; 115: 150-2.
    • (2001) Br. J. Haematol. , vol.115 , pp. 150-152
    • Chabloz, P.1    Reber, G.2    Boeblen, F.3
  • 22
    • 0037059828 scopus 로고    scopus 로고
    • Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
    • Schneider M, Boffa M, Stewart R, et al. Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. J Biol Chem 2002; 277: 1021-30.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3
  • 23
    • 0026482144 scopus 로고
    • Fibrinogen blocks the autoactivation and thrombin-mediated activation of factor XI on dextran sulfate
    • Scott CF, Colman RW. Fibrinogen blocks the autoactivation and thrombin-mediated activation of factor XI on dextran sulfate. Proc Natl Acad Sci U S A 1992; 89: 11189-93.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11189-11193
    • Scott, C.F.1    Colman, R.W.2
  • 24
    • 0037393051 scopus 로고    scopus 로고
    • Hemostatsis during normal pregnancy and puerperium
    • Hellgren M. hemostatsis during normal pregnancy and puerperium. Semin Thromb Hemostat 2003; 29: 125-30.
    • (2003) Semin. Thromb. Hemostat. , vol.29 , pp. 125-130
    • Hellgren, M.1
  • 25
    • 0030787451 scopus 로고    scopus 로고
    • Changes in activated protein C resistance during normal pregnancy
    • Walker MC, Garner PR, Keely EJ, et al. Changes in activated protein C resistance during normal pregnancy. Am J Obstet Gynecol 1997; 177: 162-9.
    • (1997) Am. J. Obstet. Gynecol. , vol.177 , pp. 162-169
    • Walker, M.C.1    Garner, P.R.2    Keely, E.J.3
  • 27
    • 0029810712 scopus 로고    scopus 로고
    • An antifibrinolytic mechanism describing the prothrombotic effect associated with factor V Leiden
    • Bajzar L, Kalafatis M, Simioni P, et al. An antifibrinolytic mechanism describing the prothrombotic effect associated with factor V Leiden. J Biol Chem 1996; 271: 22929-52.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22929-22952
    • Bajzar, L.1    Kalafatis, M.2    Simioni, P.3
  • 28
    • 2342571555 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor and the risk for recurrent venous thromboembolism
    • Eichinger S, Schonauer V, Weltermann A, et al. Thrombin-activatable fibrinolysis inhibitor and the risk for recurrent venous thromboembolism. Blood 2004; 103: 3773-6.
    • (2004) Blood , vol.103 , pp. 3773-3776
    • Eichinger, S.1    Schonauer, V.2    Weltermann, A.3
  • 29
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • van Tilburg NH, Rosendaal FR, Bertina RM. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood 2000; 95: 2855-9.
    • (2000) Blood , vol.95 , pp. 2855-2859
    • van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 30
    • 0141540528 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor in young patients with myocardial infarction and its relationship with the fibrinolytic function and the protein C system
    • Zorio E, Castello R, Falco C, et al. Thrombin-activatable fibrinolysis inhibitor in young patients with myocardial infarction and its relationship with the fibrinolytic function and the protein C system. Br J Haematol 2003; 122: 958-65.
    • (2003) Br. J. Haematol. , vol.122 , pp. 958-965
    • Zorio, E.1    Castello, R.2    Falco, C.3
  • 31
    • 0036796216 scopus 로고    scopus 로고
    • Does thrombin activatable fibrinolysis inhibitor (TAFI) contribute to impairment of fibrinolysis in patients with preeclampsia and/or intrauterine fetal growth retardation?
    • Antovic JP, Rafik Hamad R, Antovic A, et al. Does thrombin activatable fibrinolysis inhibitor (TAFI) contribute to impairment of fibrinolysis in patients with preeclampsia and/or intrauterine fetal growth retardation? Thromb Haemost 2002; 88: 644-7.
    • (2002) Thromb. Haemost. , vol.88 , pp. 644-647
    • Antovic, J.P.1    Rafik Hamad, R.2    Antovic, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.