메뉴 건너뛰기




Volumn 378, Issue 1-2, 2007, Pages 1-6

Thrombin activatable fibrinolysis inhibitor (TAFI): A role in pre-eclampsia?

Author keywords

Pre eclampsia; Pro TAFI; TAFIa

Indexed keywords

PROTEIN C; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR;

EID: 33846926328     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2006.10.014     Document Type: Review
Times cited : (5)

References (82)
  • 1
    • 0033891361 scopus 로고    scopus 로고
    • Report of the national high blood pressure education program working group on high blood pressure in pregnancy
    • Report of the national high blood pressure education program working group on high blood pressure in pregnancy. Am J Obstet Gynecol 183 (2000) S1-S22
    • (2000) Am J Obstet Gynecol , vol.183
  • 2
    • 0025513937 scopus 로고
    • National high blood pressure education program working group report on high pressure in pregnancy
    • National high blood pressure education program working group report on high pressure in pregnancy. Am J Obstet Gynecol 163 (1990) 1691-1712
    • (1990) Am J Obstet Gynecol , vol.163 , pp. 1691-1712
  • 4
    • 18044384109 scopus 로고    scopus 로고
    • Haemostasis in normal pregnancy: a balancing act?
    • Holmes V.A., and Wallace J.M. Haemostasis in normal pregnancy: a balancing act?. Biochem Soc Trans 33 2 (2005) 428-432
    • (2005) Biochem Soc Trans , vol.33 , Issue.2 , pp. 428-432
    • Holmes, V.A.1    Wallace, J.M.2
  • 5
    • 7044249206 scopus 로고    scopus 로고
    • Hemostatic changes in pregnancy
    • Brenner B. Hemostatic changes in pregnancy. Thromb Res 114 (2004) 408-414
    • (2004) Thromb Res , vol.114 , pp. 408-414
    • Brenner, B.1
  • 7
    • 0017192034 scopus 로고
    • Hepatic fibrinogen deposits in pre-eclampsia. Immunofluorescent evidence
    • Arias F., and Mancilla-Jimenez R. Hepatic fibrinogen deposits in pre-eclampsia. Immunofluorescent evidence. N Engl J Med 295 11 (1976) 578-582
    • (1976) N Engl J Med , vol.295 , Issue.11 , pp. 578-582
    • Arias, F.1    Mancilla-Jimenez, R.2
  • 8
    • 0015357706 scopus 로고
    • Hematologic evidence of disseminated intravascular coagulation in eclampsia
    • McKay D.G. Hematologic evidence of disseminated intravascular coagulation in eclampsia. Obstet Gynecol Surv 27 6 (1972) 399-417
    • (1972) Obstet Gynecol Surv , vol.27 , Issue.6 , pp. 399-417
    • McKay, D.G.1
  • 9
    • 0028800430 scopus 로고
    • The physiology of preeclampsia
    • Brown M.A. The physiology of preeclampsia. Clin Exp Pharmacol Physiol 22 (1995) 781-791
    • (1995) Clin Exp Pharmacol Physiol , vol.22 , pp. 781-791
    • Brown, M.A.1
  • 10
    • 0015146023 scopus 로고
    • Coagulation, fibrinolysis and platelet function in pre-eclampsia, essential hypertension and placental insufficiency
    • Howie P.W., Prentice C.R., and McNicol G.P. Coagulation, fibrinolysis and platelet function in pre-eclampsia, essential hypertension and placental insufficiency. J Obstet Gynaecol Br Commonw 78 11 (1971) 992-1003
    • (1971) J Obstet Gynaecol Br Commonw , vol.78 , Issue.11 , pp. 992-1003
    • Howie, P.W.1    Prentice, C.R.2    McNicol, G.P.3
  • 12
    • 0036714380 scopus 로고    scopus 로고
    • Enhanced coagulation activation in preeclampsia: the role of APC resistance, microparticles and other plasma constituents
    • VanWijk M.J., Boer K., Berckmans R.J., Meijers J.C., van der Post J.A., and Sturk A. Enhanced coagulation activation in preeclampsia: the role of APC resistance, microparticles and other plasma constituents. Thromb Haemost 88 3 (2002) 415-420
    • (2002) Thromb Haemost , vol.88 , Issue.3 , pp. 415-420
    • VanWijk, M.J.1    Boer, K.2    Berckmans, R.J.3    Meijers, J.C.4    van der Post, J.A.5    Sturk, A.6
  • 14
    • 0031660242 scopus 로고    scopus 로고
    • Hemostasis in the uteroplacental and peripheral circulations in normotensive and pre-eclamptic pregnancies
    • Higgins J.R., Walshe J.J., Darling M.R.N., Norris L., and Bonnar J. Hemostasis in the uteroplacental and peripheral circulations in normotensive and pre-eclamptic pregnancies. Am J Obstet Gynecol 179 (1998) 520-526
    • (1998) Am J Obstet Gynecol , vol.179 , pp. 520-526
    • Higgins, J.R.1    Walshe, J.J.2    Darling, M.R.N.3    Norris, L.4    Bonnar, J.5
  • 15
    • 33846895346 scopus 로고
    • Plasma antithrombin III activity: an aid in the diagnosis of preeclampsia-eclampsia
    • Weiner C.P., and Brandt J. Plasma antithrombin III activity: an aid in the diagnosis of preeclampsia-eclampsia. Lancet 2 8051 (1977) 1249-1252
    • (1977) Lancet , vol.2 , Issue.8051 , pp. 1249-1252
    • Weiner, C.P.1    Brandt, J.2
  • 16
    • 0018647298 scopus 로고
    • Platelet life-span in normal pregnancy and pre-eclampsia as determined by a non-radioisotope technique
    • Rakoczi I., Tallian F., Bagdany S., and Gati I. Platelet life-span in normal pregnancy and pre-eclampsia as determined by a non-radioisotope technique. Thromb Res 15 3-4 (1979) 553-556
    • (1979) Thromb Res , vol.15 , Issue.3-4 , pp. 553-556
    • Rakoczi, I.1    Tallian, F.2    Bagdany, S.3    Gati, I.4
  • 17
    • 0017813860 scopus 로고
    • Early platelet consumption in pre-eclampsia
    • Redman C.W., Bonnar J., and Beilen L. Early platelet consumption in pre-eclampsia. Br Med J 1 6111 (1978) 467-469
    • (1978) Br Med J , vol.1 , Issue.6111 , pp. 467-469
    • Redman, C.W.1    Bonnar, J.2    Beilen, L.3
  • 18
    • 0031952154 scopus 로고    scopus 로고
    • Abnormal expression of type 1 plasminogen activator inhibitor and tissue factor in severe pre-eclampsia
    • Estelles A., Gilabert J., Grancha S., et al. Abnormal expression of type 1 plasminogen activator inhibitor and tissue factor in severe pre-eclampsia. Thromb Haemost 79 (1998) 500-508
    • (1998) Thromb Haemost , vol.79 , pp. 500-508
    • Estelles, A.1    Gilabert, J.2    Grancha, S.3
  • 19
    • 84945736607 scopus 로고
    • Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N
    • Hendriks D., Scharpe S., van Sande M., and Lommaert M.P. Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. J Clin Chem Clin Biochem 27 5 (1989) 277-285
    • (1989) J Clin Chem Clin Biochem , vol.27 , Issue.5 , pp. 277-285
    • Hendriks, D.1    Scharpe, S.2    van Sande, M.3    Lommaert, M.P.4
  • 20
    • 24944454291 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and possible risk factor for thrombotic disease
    • Leurs J., and Hendriks D. Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and possible risk factor for thrombotic disease. Thromb Haemost 94 (2005) 471-487
    • (2005) Thromb Haemost , vol.94 , pp. 471-487
    • Leurs, J.1    Hendriks, D.2
  • 21
    • 0026787288 scopus 로고
    • Human serum carboxypeptidase U: a new kinase?
    • Hendriks D., Wang W., van Sande, and Scharpe S. Human serum carboxypeptidase U: a new kinase?. Agents Actions Suppl 38 Pt 1 (1992) 407-413
    • (1992) Agents Actions Suppl , vol.38 , Issue.PART 1 , pp. 407-413
    • Hendriks, D.1    Wang, W.2    van Sande3    Scharpe, S.4
  • 22
    • 0028815556 scopus 로고
    • Plasma carboxypeptidase as regulators of the plasminogen system
    • Redlitz A., Tan A.K., Eaton D.L., and Plow E.F. Plasma carboxypeptidase as regulators of the plasminogen system. J Clin Invest 96 5 (1995) 2104-2105
    • (1995) J Clin Invest , vol.96 , Issue.5 , pp. 2104-2105
    • Redlitz, A.1    Tan, A.K.2    Eaton, D.L.3    Plow, E.F.4
  • 23
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • Eaton D.L., Malloy B.E., Tsai S.P., Henzel W., and Drayna D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J Biol Chem 266 32 (1991) 21833-21838
    • (1991) J Biol Chem , vol.266 , Issue.32 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 24
    • 0024412863 scopus 로고
    • An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits
    • Campbell W., and Okada H. An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits. Biochem Biophys Res Commun 162 (1989) 933-939
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 933-939
    • Campbell, W.1    Okada, H.2
  • 25
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activatable fibrinolysis inhibitor
    • Bajzar L., Manuel R., and Nesheim M.E. Purification and characterization of TAFI, a thrombin-activatable fibrinolysis inhibitor. J Biol Chem 270 (1995) 14477-14484
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 26
    • 0038454527 scopus 로고    scopus 로고
    • Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets
    • Mosnier L.O., Buijtenhuijs P., Marx P.F., et al. Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets. Blood 101 (2003) 4844-4846
    • (2003) Blood , vol.101 , pp. 4844-4846
    • Mosnier, L.O.1    Buijtenhuijs, P.2    Marx, P.F.3
  • 27
  • 28
    • 0032769932 scopus 로고    scopus 로고
    • Arginine carboxypeptidase (CPR) in human plasma determined with sandwich ELISA
    • Guo X., Morioka A., Kaneko Y., Okada N., Obata K., and Nomura T. Arginine carboxypeptidase (CPR) in human plasma determined with sandwich ELISA. Microbiol Immunol 43 (1999) 691-698
    • (1999) Microbiol Immunol , vol.43 , pp. 691-698
    • Guo, X.1    Morioka, A.2    Kaneko, Y.3    Okada, N.4    Obata, K.5    Nomura, T.6
  • 29
    • 0035173479 scopus 로고    scopus 로고
    • Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin
    • Mosnier L.O., Meijers J.C.M., and Bouma B.N. Regulation of fibrinolysis in plasma by TAFI and protein C is dependent on the concentration of thrombomodulin. Thromb Haemost 85 (2001) 5-11
    • (2001) Thromb Haemost , vol.85 , pp. 5-11
    • Mosnier, L.O.1    Meijers, J.C.M.2    Bouma, B.N.3
  • 30
    • 0034725622 scopus 로고    scopus 로고
    • Elements of the primary structure of thrombomodulin required for efficient thrombin-activatable fibrinolysis inhibitor activation
    • Wang W., Nagashima M., Schneider M., et al. Elements of the primary structure of thrombomodulin required for efficient thrombin-activatable fibrinolysis inhibitor activation. J Biol Chem 275 (2000) 22942-22947
    • (2000) J Biol Chem , vol.275 , pp. 22942-22947
    • Wang, W.1    Nagashima, M.2    Schneider, M.3
  • 31
    • 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., and Hendriks D. Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism. J Thromb Haemost 2 (2004) 416-423
    • (2004) J Thromb Haemost , vol.2 , pp. 416-423
    • Leurs, J.1    Nerme, V.2    Sim, Y.3    Hendriks, D.4
  • 32
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • Bajzar L., Moser J., and Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem 271 (1996) 16603-16608
    • (1996) J Biol Chem , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Moser, J.2    Nesheim, M.3
  • 33
    • 29744453508 scopus 로고    scopus 로고
    • Measurements of pro carboxypeptidase U (TAFI) in human plasma: a laboratory challenge
    • Willemse J.L., and Hendriks D.F. Measurements of pro carboxypeptidase U (TAFI) in human plasma: a laboratory challenge. Clin Chem 52 (2006) 30-36
    • (2006) Clin Chem , vol.52 , pp. 30-36
    • Willemse, J.L.1    Hendriks, D.F.2
  • 34
    • 14044259258 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis
    • Bouma B.N., and Laurent O.M. Thrombin-activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis. Pathophysiol Haemost Thromb 33 (2003/2004) 375-381
    • (2003) Pathophysiol Haemost Thromb , vol.33 , pp. 375-381
    • Bouma, B.N.1    Laurent, O.M.2
  • 35
    • 0141707850 scopus 로고    scopus 로고
    • Thrombin and fibrinolysis
    • Neiheim M. Thrombin and fibrinolysis. Chest 124 (2003) 33S-39S
    • (2003) Chest , vol.124
    • Neiheim, M.1
  • 36
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activatable fibrinolysis inhibitor
    • Wang W., Boffa M.B., Bajzar L., Walker J.B., and Nesheim M.E. A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activatable fibrinolysis inhibitor. J Biol Chem 273 42 (1998) 27176-27181
    • (1998) J Biol Chem , vol.273 , Issue.42 , pp. 27176-27181
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 37
    • 0038660605 scopus 로고    scopus 로고
    • Acute phase mediators modulate thrombin-activatable fibrinolysis inhibitor (TAFI) gene expression in Hep G2 cells
    • Boffa M.D., Hamill J.D., Maret D., Brown D., Scott M.L., and Nesheim M.E. Acute phase mediators modulate thrombin-activatable fibrinolysis inhibitor (TAFI) gene expression in Hep G2 cells. J Biol Chem 278 11 (2003) 9250-9257
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 9250-9257
    • Boffa, M.D.1    Hamill, J.D.2    Maret, D.3    Brown, D.4    Scott, M.L.5    Nesheim, M.E.6
  • 38
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell W.D., Lazoura E., Okada N., and Okada H. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol Immunol 46 (2002) 131-134
    • (2002) Microbiol Immunol , vol.46 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3    Okada, H.4
  • 39
    • 0034996440 scopus 로고    scopus 로고
    • Carboxypeptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis
    • Campbell W.D., Okada N., and Okada H. Carboxypeptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis. Immunol Rev 180 (2001) 162-166
    • (2001) Immunol Rev , vol.180 , pp. 162-166
    • Campbell, W.D.1    Okada, N.2    Okada, H.3
  • 40
    • 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 278 (2003) 51059-51067
    • (2003) J Biol Chem , vol.278 , pp. 51059-51067
    • Myles, T.1    Nishimura, T.2    Yun, T.H.3
  • 41
    • 0033520366 scopus 로고    scopus 로고
    • Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains
    • Hall S.W., Nagashima M., Zhao, Morser J., and Leune L.L. Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains. J Biol Chem 274 36 (1999) 25510-25516
    • (1999) J Biol Chem , vol.274 , Issue.36 , pp. 25510-25516
    • Hall, S.W.1    Nagashima, M.2    Zhao3    Morser, J.4    Leune, L.L.5
  • 42
    • 0034703059 scopus 로고    scopus 로고
    • Fluorescence properties and functional roles of tryptophan residues 60d, 96,148, 207, and 215 of thrombin
    • Bell R., Stevens W.K., Jia Z., et al. Fluorescence properties and functional roles of tryptophan residues 60d, 96,148, 207, and 215 of thrombin. J Biol Chem 2759380 (2000) 29513-29520
    • (2000) J Biol Chem , vol.2759380 , pp. 29513-29520
    • Bell, R.1    Stevens, W.K.2    Jia, Z.3
  • 43
    • 0031915389 scopus 로고    scopus 로고
    • Plasma and recombinant thrombin-activatable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties
    • Boffa M.B., Wang W., Bajzar L., and Nesheim M.E. Plasma and recombinant thrombin-activatable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties. J Biol Chem 273 4 (1998) 2127-2135
    • (1998) J Biol Chem , vol.273 , Issue.4 , pp. 2127-2135
    • Boffa, M.B.1    Wang, W.2    Bajzar, L.3    Nesheim, M.E.4
  • 44
    • 0032524918 scopus 로고    scopus 로고
    • Activation of thrombin-activatable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C
    • Kokame K., Zheng X., and Sadler J.E. Activation of thrombin-activatable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C. J Biol Chem 273 (1998) 12135-12139
    • (1998) J Biol Chem , vol.273 , pp. 12135-12139
    • Kokame, K.1    Zheng, X.2    Sadler, J.E.3
  • 45
    • 0026464017 scopus 로고
    • The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13
    • Tsai S.P., and Drayana D. The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13. Genomics 14 (1992) 549-550
    • (1992) Genomics , vol.14 , pp. 549-550
    • Tsai, S.P.1    Drayana, D.2
  • 46
    • 0031766583 scopus 로고    scopus 로고
    • Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms
    • Zhao L., Morser J., Bajzar L., Neisheim M., and Nagashima M. Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms. Thromb Haemost 80 (1998) 949-955
    • (1998) Thromb Haemost , vol.80 , pp. 949-955
    • Zhao, L.1    Morser, J.2    Bajzar, L.3    Neisheim, M.4    Nagashima, M.5
  • 47
    • 0035885942 scopus 로고    scopus 로고
    • A novel, possibly functional, single nucleotide polymorphism in the coding region of the thrombin-activatable fibrinolysis inhibitor (TAFI) gene is also associated with TAFI levels
    • Brouwers G.J., Vos H.L., Leebeek F.W., Bulk S., Scheineder M., and Boffa M. A novel, possibly functional, single nucleotide polymorphism in the coding region of the thrombin-activatable fibrinolysis inhibitor (TAFI) gene is also associated with TAFI levels. Blood 98 (2001) 1992-1993
    • (2001) Blood , vol.98 , pp. 1992-1993
    • Brouwers, G.J.1    Vos, H.L.2    Leebeek, F.W.3    Bulk, S.4    Scheineder, M.5    Boffa, M.6
  • 48
    • 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., Rahman M., Koschinsky M., and Nesheim M. 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 277 (2002) 1021-1030
    • (2002) J Biol Chem , vol.277 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3    Rahman, M.4    Koschinsky, M.5    Nesheim, M.6
  • 49
    • 0034725120 scopus 로고    scopus 로고
    • Roles of thermal instability and proteolytic cleavage in regulation of thrombin-activatable fibrinolysis inhibitor
    • Boffa M.B., Bell R., Stevens W.K., and Nesheim M.E. Roles of thermal instability and proteolytic cleavage in regulation of thrombin-activatable fibrinolysis inhibitor. J Biol Chem 275 17 (2000) 12868-12878
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12868-12878
    • Boffa, M.B.1    Bell, R.2    Stevens, W.K.3    Nesheim, M.E.4
  • 50
    • 0034725047 scopus 로고    scopus 로고
    • Inactivation of active thrombin-activatable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than a proteolytic cleavage
    • Marx P.F., Hackeng T.M., Dawson P.E., Griffin J.H., Meijers J.C., and Bouma B.N. Inactivation of active thrombin-activatable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than a proteolytic cleavage. J Biol Chem 275 (2000) 12410-12415
    • (2000) J Biol Chem , vol.275 , pp. 12410-12415
    • Marx, P.F.1    Hackeng, T.M.2    Dawson, P.E.3    Griffin, J.H.4    Meijers, J.C.5    Bouma, B.N.6
  • 51
    • 0035351215 scopus 로고    scopus 로고
    • Identification of polymorphisms in the 5'-untranslated region of the TAFI gene: relationship with plasma TAFI levels and risk of venous thrombosis
    • Franco R.F., Fagundes M.G., Meijers J.C., et al. Identification of polymorphisms in the 5'-untranslated region of the TAFI gene: relationship with plasma TAFI levels and risk of venous thrombosis. Haematologica 86950 (2001) 510-517
    • (2001) Haematologica , vol.86950 , pp. 510-517
    • Franco, R.F.1    Fagundes, M.G.2    Meijers, J.C.3
  • 52
    • 0036172375 scopus 로고    scopus 로고
    • Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in type 2 diabetic patients
    • Hori Y., Gabazza E.C., Yano Y., et al. Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in type 2 diabetic patients. J Clin Endocrinol Metab 87 2 (2002) 660-665
    • (2002) J Clin Endocrinol Metab , vol.87 , Issue.2 , pp. 660-665
    • Hori, Y.1    Gabazza, E.C.2    Yano, Y.3
  • 53
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor and risk for deep vein thrombosis
    • Van Tilburg N.H., Rosendaal F.R., and Bertina R.M. Thrombin-activatable fibrinolysis inhibitor and risk for deep vein thrombosis. Blood 95 (2000) 2855-2859
    • (2000) Blood , vol.95 , pp. 2855-2859
    • Van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 54
    • 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 103 (2004) 3773-3776
    • (2004) Blood , vol.103 , pp. 3773-3776
    • Eichinger, S.1    Schonauer, V.2    Weltermann, A.3
  • 55
    • 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 122 6 (2003) 958-965
    • (2003) Br J Haematol , vol.122 , Issue.6 , pp. 958-965
    • Zorio, E.1    Castello, R.2    Falco, C.3
  • 56
    • 0033832483 scopus 로고    scopus 로고
    • Plasma carboxypeptidase U in men with symptomatic coronary artery disease
    • Silveira A., Schatteman K., Grossens F., et al. Plasma carboxypeptidase U in men with symptomatic coronary artery disease. Thromb Haemost 84 (2000) 364-368
    • (2000) Thromb Haemost , vol.84 , pp. 364-368
    • Silveira, A.1    Schatteman, K.2    Grossens, F.3
  • 57
    • 0035073313 scopus 로고    scopus 로고
    • Low levels of thrombin-activatable fibrinolysis inhibitor (TAFI) in patients with chronic liver disease
    • Van Thiel D.H., George M., and Fareed J. Low levels of thrombin-activatable fibrinolysis inhibitor (TAFI) in patients with chronic liver disease. Thromb Haemost 85 (2001) 667-670
    • (2001) Thromb Haemost , vol.85 , pp. 667-670
    • Van Thiel, D.H.1    George, M.2    Fareed, J.3
  • 58
    • 0034117225 scopus 로고    scopus 로고
    • Reduced activity of TAFI (thrombin-activatable fibrinolysis inhibitor) in acute promyelocytic leukaemia
    • Meijers J.C.M., Oudijk E.J.D., Mosnier L.O., et al. Reduced activity of TAFI (thrombin-activatable fibrinolysis inhibitor) in acute promyelocytic leukaemia. Br J Haematol 108 (2000) 518-523
    • (2000) Br J Haematol , vol.108 , pp. 518-523
    • Meijers, J.C.M.1    Oudijk, E.J.D.2    Mosnier, L.O.3
  • 59
    • 0035479232 scopus 로고    scopus 로고
    • Activity and antigen levels of thrombin-activatable fibrinolysis inhibitor in plasma of patients with disseminated intravascular coagulation
    • Watanabe R., Wada H., Watanabe Y., et al. Activity and antigen levels of thrombin-activatable fibrinolysis inhibitor in plasma of patients with disseminated intravascular coagulation. Thromb Res 104 (2001) 1-6
    • (2001) Thromb Res , vol.104 , pp. 1-6
    • Watanabe, R.1    Wada, H.2    Watanabe, Y.3
  • 60
    • 10744228937 scopus 로고    scopus 로고
    • Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as a novel antithrombotics
    • Barrow J.C., Nantermet P.G., Stauffer S.R., et al. Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as a novel antithrombotics. J Med Chem 46 25 (2003) 5294-5297
    • (2003) J Med Chem , vol.46 , Issue.25 , pp. 5294-5297
    • Barrow, J.C.1    Nantermet, P.G.2    Stauffer, S.R.3
  • 61
    • 10744221306 scopus 로고    scopus 로고
    • Design and synthesis of the first potent, orally active, inhibitors of carboxypeptidase U (TAFIa)
    • Polla M., Tottie L., Norden C., et al. Design and synthesis of the first potent, orally active, inhibitors of carboxypeptidase U (TAFIa). Bioorg Med Chem 12 5 (2004) 1151-1175
    • (2004) Bioorg Med Chem , vol.12 , Issue.5 , pp. 1151-1175
    • Polla, M.1    Tottie, L.2    Norden, C.3
  • 62
    • 11144356646 scopus 로고    scopus 로고
    • Enhancement of fibrinolysis by EF6265, a specific inhibitor of plasma carboxypeptidase B
    • Suzuki K., Muto Y., Fushihara K., et al. Enhancement of fibrinolysis by EF6265, a specific inhibitor of plasma carboxypeptidase B. J Pharmacol Exp Ther 309 2 (2004) 607-615
    • (2004) J Pharmacol Exp Ther , vol.309 , Issue.2 , pp. 607-615
    • Suzuki, K.1    Muto, Y.2    Fushihara, K.3
  • 64
    • 0034772159 scopus 로고    scopus 로고
    • TAFI antigen and D-Dimer levels during normal pregnancy and at delivery
    • Chabloz P., Reber G., Boehlen F., Hohfeld P., and de Moerloose P. TAFI antigen and D-Dimer levels during normal pregnancy and at delivery. Br J Haematol 115 1 (2001) 150-152
    • (2001) Br J Haematol , vol.115 , Issue.1 , pp. 150-152
    • Chabloz, P.1    Reber, G.2    Boehlen, F.3    Hohfeld, P.4    de Moerloose, P.5
  • 65
    • 9144235693 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor and its fibrinolytic effect in normal pregnancy
    • Mousa H.A., Downey C., Alfirevic Z., and Toh C.H. Thrombin-activatable fibrinolysis inhibitor and its fibrinolytic effect in normal pregnancy. Thromb Haemost 92 5 (2004) 1025-1031
    • (2004) Thromb Haemost , vol.92 , Issue.5 , pp. 1025-1031
    • Mousa, H.A.1    Downey, C.2    Alfirevic, Z.3    Toh, C.H.4
  • 67
    • 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 J.P., Rafik Hamad R., Antovic A., Blomback M., and Bremme K. Does thrombin-activatable fibrinolysis inhibitor (TAFI) contribute to impairment of fibrinolysis in patients with preeclampsia and/or intrauterine fetal growth retardation?. Thromb Haemost 88 4 (2002) 644-647
    • (2002) Thromb Haemost , vol.88 , Issue.4 , pp. 644-647
    • Antovic, J.P.1    Rafik Hamad, R.2    Antovic, A.3    Blomback, M.4    Bremme, K.5
  • 68
    • 4444231438 scopus 로고    scopus 로고
    • Plasma levels of thrombin-activatable fibrinolysis inhibitor in normal and preeclamptic pregnant women
    • Alacacioglu I., Ozcan M.A., Alacacioglu A., et al. Plasma levels of thrombin-activatable fibrinolysis inhibitor in normal and preeclamptic pregnant women. Thromb Res 114 3 (2004) 155-159
    • (2004) Thromb Res , vol.114 , Issue.3 , pp. 155-159
    • Alacacioglu, I.1    Ozcan, M.A.2    Alacacioglu, A.3
  • 69
    • 19944431329 scopus 로고    scopus 로고
    • Preeclampsia and its interaction with common variants in thrombophilia genes
    • De Maat M.P., Jansen N.W., Hille E.T., et al. Preeclampsia and its interaction with common variants in thrombophilia genes. J Thromb Haemost 2 9 (2004) 1588-1593
    • (2004) J Thromb Haemost , vol.2 , Issue.9 , pp. 1588-1593
    • De Maat, M.P.1    Jansen, N.W.2    Hille, E.T.3
  • 70
    • 3242663458 scopus 로고    scopus 로고
    • Pre-eclampsia and cardiovascular disease: metabolic syndrome of pregnancy?
    • Rodie V.A., Freeman D.J., Sattar N., and Greer I.A. Pre-eclampsia and cardiovascular disease: metabolic syndrome of pregnancy?. Atherosclerosis 175 (2004) 189-202
    • (2004) Atherosclerosis , vol.175 , pp. 189-202
    • Rodie, V.A.1    Freeman, D.J.2    Sattar, N.3    Greer, I.A.4
  • 72
    • 0034912277 scopus 로고    scopus 로고
    • Low molecular weight heparin for the prevention of obstetric complications in women with thrombophilia
    • Kupferminc M.J., Fait G., Many A., et al. Low molecular weight heparin for the prevention of obstetric complications in women with thrombophilia. Hypertens Pregnancy 20 1 (2001) 35-44
    • (2001) Hypertens Pregnancy , vol.20 , Issue.1 , pp. 35-44
    • Kupferminc, M.J.1    Fait, G.2    Many, A.3
  • 75
    • 0030803395 scopus 로고    scopus 로고
    • Trial of calcium to prevent preeclampsia
    • Levine R.J., Hauth J.C., Curet L.B., et al. Trial of calcium to prevent preeclampsia. N Engl J Med 337 2 (1997) 69-76
    • (1997) N Engl J Med , vol.337 , Issue.2 , pp. 69-76
    • Levine, R.J.1    Hauth, J.C.2    Curet, L.B.3
  • 76
    • 0023894588 scopus 로고
    • The relationship between calcium intake and pregnancy-induced hypertension: Up-to-date evidence
    • Belizan J.M., Villar J., and Repke J. The relationship between calcium intake and pregnancy-induced hypertension: Up-to-date evidence. Am J Obstet Gynecol 158 (1988) 898-902
    • (1988) Am J Obstet Gynecol , vol.158 , pp. 898-902
    • Belizan, J.M.1    Villar, J.2    Repke, J.3
  • 77
    • 13244258254 scopus 로고    scopus 로고
    • Effects of prolongated oral supplementation with L-arginine on blood pressure and nitric oxide synthesis in PEC
    • Rytlewski K., Olszanecki R., Korbut R., and Zdebski Z. Effects of prolongated oral supplementation with L-arginine on blood pressure and nitric oxide synthesis in PEC. Eur J Clin Invest 35 (2005) 32-37
    • (2005) Eur J Clin Invest , vol.35 , pp. 32-37
    • Rytlewski, K.1    Olszanecki, R.2    Korbut, R.3    Zdebski, Z.4
  • 78
    • 14644432960 scopus 로고    scopus 로고
    • Fish oil, and other prostaglandin precursor supllementation during pregnancy for reducing pre-eclampsia, preterm birth, low birth weight and intrauterine growth restriction
    • Makrides M., Duley L., and Oslen S.F. Fish oil, and other prostaglandin precursor supllementation during pregnancy for reducing pre-eclampsia, preterm birth, low birth weight and intrauterine growth restriction. Cochrane Database Syst Rev 4 (2001) CD003402
    • (2001) Cochrane Database Syst Rev , vol.4
    • Makrides, M.1    Duley, L.2    Oslen, S.F.3
  • 79
    • 4644311708 scopus 로고    scopus 로고
    • Oxidative stress and preeclampsia. Rationale for antioxidant clinical trials
    • Raijmakers M.T.M., Dechend R., and Poston L. Oxidative stress and preeclampsia. Rationale for antioxidant clinical trials. Hypertension 44 (2004) 374-380
    • (2004) Hypertension , vol.44 , pp. 374-380
    • Raijmakers, M.T.M.1    Dechend, R.2    Poston, L.3
  • 80
    • 0033523401 scopus 로고    scopus 로고
    • Effect of antioxidants on the occurrence of pre-eclampsia in women at increased risk: a randomised trial
    • Chappell L.C., Seed P.T., Briley A.L., et al. Effect of antioxidants on the occurrence of pre-eclampsia in women at increased risk: a randomised trial. Lancet 354 (1999) 810-816
    • (1999) Lancet , vol.354 , pp. 810-816
    • Chappell, L.C.1    Seed, P.T.2    Briley, A.L.3
  • 81
    • 0031725594 scopus 로고    scopus 로고
    • Prevention of preeclampsia: a big disappointment
    • Sibai B.M. Prevention of preeclampsia: a big disappointment. Am J Obstet Gynecol 179 (1998) 1275-1278
    • (1998) Am J Obstet Gynecol , vol.179 , pp. 1275-1278
    • Sibai, B.M.1
  • 82
    • 14844360661 scopus 로고    scopus 로고
    • Eclampsia: Morbidity, Mortality, and Management
    • Aagaard-Tillery K.M., and Belford M.A. Eclampsia: Morbidity, Mortality, and Management. Clin Obstet Gynecol 48 1 (2005) 12-23
    • (2005) Clin Obstet Gynecol , vol.48 , Issue.1 , pp. 12-23
    • Aagaard-Tillery, K.M.1    Belford, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.