Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and its Role in Regulation of Fibrinolysis;Trombínom Aktivovatel'ný Inhibítor Fibrinolýzy (TAFI) a Jeho Význam v Regulácii Fibrinolýzy

Vnitrni Lekarstvi

Volumn 50, Issue 1, 2004, Pages 36-44

  Staško, Ján ^a   Hudecek J ^a   Kubisz, P ^a  

^a Martinska Fakultna Nemocnica   (Slovakia)

Author keywords

Carboxypeptidase; Coagulation; Fibrinolysis; TAFI

Indexed keywords

ACTIVATED PROTEIN C; BLOOD CLOTTING FACTOR 11; BLOOD CLOTTING FACTOR 5 LEIDEN; FIBRIN; FIBRINOLYTIC AGENT; LYSINE; PLASMIN; PLASMINOGEN; THROMBIN; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; THROMBOMODULIN; TISSUE PLASMINOGEN ACTIVATOR;

ARTICLE; BLEEDING; BLOOD CLOTTING; BLOOD CLOTTING FACTOR 11 DEFICIENCY; FIBRINOLYSIS; HEMOPHILIA A; HEMOPHILIA B; HEMOSTASIS; HUMAN; THROMBOSIS;

BLOOD COAGULATION; BLOOD COAGULATION DISORDERS; CARBOXYPEPTIDASE U; FIBRINOLYSIS; HEMORRHAGIC DISORDERS; HUMANS;

EID: 0842263709     PISSN: 0042773X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (76)

1. Alexander, S. S. A., Greenfield, R. S.: Aspirin and aspirin metabolites inhibit thrombin activatable fibrinolysis inhibitor (TAFI): a novel mechanism to explain the profibrinolytic effects associated with anti-thrombotic therapy. Blood, 100, 2002; 11: 703a
2. Asakai, R., Chung, D. W., Davie, E. W. et al.: Factor XI deficiency in Ashkenazi Jews in Israel. N. Engl. J. Med., 325, 1991; 153-158
3. Bajzar, L., Fredenburgh, J. C., Nesheim, M. E.: The activated protein C-mediated enhancement of tissue-type plasminogen activator-induced fibrinolysis in a cell-free system. J. Biol. Chem., 265, 1990; 16948-16954
4. Bajzar, L., Nesheim, M. E.: The effect of activated protein C on fibrinolysis in a cell-free plasma can be attributed specifically to attenuation of prothrombin activation. J. Biol. Chem., 268, 1993; 8608-8616
5. Bajzar, L., Manuel, R., Nesheim, M. E.: Purification and characterization of TAFI, a thrombin-activatable fibrinolysis inhibitor. J. Biol. Chem., 270, 1995; 14477-14484
6. Bajzar, L., Kalafatis, M., Simioni, P. et al.: An antifibrinolytic mechanism describing the prothrombotic effect associated with factor V Leiden. J. Biol. Chem., 271, 1996; 22949-22952
7. Bajzar, L., Nesheim, M. E., Tracy, P. B.: The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood, 88, 1996; 2093-2100
8. Bajzar, L., Morser, J., Nesheim, M. E.: TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J. Biol. Chem., 271, 1996; 16603-16608
9. Bajzar, L.: Thrombin activatable fibrinolysis inhibitor and an antifibrinolytic pathway. Arterioscler. Thromb. Vasc. Biol., 20, 2000; 2511-2518
10. Bauer, K. A., Rosenberg, R. D.: The pathophysiology of the prethrombotic state in humans: insights gained from studies using markers of hemostatic system activation. Blood, 70, 1987; 343-350
11. Berliner, S., Horowitz, I., Martinowitz, U. et al.: Dental surgery in patients with severe factor XI deficiency without plasma replacement. Blood Coagul. Fibrinolysis, 3, 1992; 465-468
12. Boffa, M. B., Wang, W., Bajzar, L. et al.: 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, 1998; 2127-2135
13. Boffa, M. B., Bell, R., Stevens, W. K. et al.: Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activatable fibrinolysis inhibitor. J. Biol. Chem., 275, 2000; 12868-12878
14. Bouma, B. N., Mosnier, L. O., Meijers, J. C. M. et al.: Factor XI dependent and independent activation of thrombin-activatable fibrinolysis inhibitor (TAFI) in plasma associated with clot formation. Thromb. Haemost., 82, 1999; 1703-1708
15. Bouma, B. N., Marx, P. F., Mosnier, L. O. et al.: Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U). Thromb. Res., 101, 2001; 329-354
16. Burgos, F. J., Salva, M., Villegas, V. et al.: Analysis of the activation process of porcine procarboxypeptidase B and determination of the sequence of its activation segment. Biochemistry, 30, 1991; 4082-4089
17. Campbell, W., 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; 86-92
18. Campbell, W., Yonezu, K., Shinohara, T. et al.: An arginine carboxypeptidase generated during coagulation is diminished or absent in patients with rheumatoid arthritis. J. Lab. Clin. Med., 115, 1990, 610-612
19. Carmeliet, P., Collen, D.: Gene targeting and gene transfer studies of the plasminogen/plasmin system: implications in thrombosis, hemostasis, neointima formation and atherosclerosis. FASEB J., 9, 1995; 934-938
20. Collen, D.: On the regulation and control of fibrinolysis. Thromb. Haemost., 43, 1980; 77-89
21. Collen, D., Lijnen, H. R.: Basic and clinical aspects of fibrinolysis and thrombolysis. Blood, 78, 1991; 3114-3124
22. De Fouw, N. J., Haverkate, F., Bertina, R. M.: Protein C and fibrinolysis: a link between coagulation and fibrinolysis. Adv. Exp. Med. Biol., 281, 1990; 235-243
23. Delk, A. S., Durie, P. R., Fletcher, T. S. et al.: Radioimmunoassay of active pancreatic enzymes in sera from patients with acute pancreatitis: I. Active carboxypeptidase B. Clin. Chem., 31, 1985; 1294-1300
24. Eaton, D. L., Malloy, B. E., Tsai, S. P. et al.: Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem., 266, 1991; 21833-21838
25. Eichinger, S., Schönauer, V., Weltermann, A. et al.: An elevated thrombin activatable fibrinolysis inhibitor (TAFI) is a risk factor of reccurent venous thromboembolism. Blood, 100, 2002; 11: 270a
26. Erdös, E. G., Sloane, E. M.: An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem. Pharmacol., 11, 1962; 585-592
27. Fleury, V., Angles-Cano, E.: Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxy-terminal lysines. Biochemistry, 30, 1991; 7630-7638
28. Florian, M., Hoppensteadt, D., Tobu, M. et al.: Differential inhibition of thrombin activatable fibrinolytic inhibitor by low molecular weight heparins. Therapeutic implications in the management of thrombotic disorders. Blood, 100, 2002; 11: 131b
29. Folk, J. E., Gladner, J. A.: Carboxypeptidase B: I. Purification of the zymogen and specificity of the enzyme. J. Biol. Chem., 231, 1958, 379-391
30. Griffin, J. H.: Blood coagulation - the thrombin paradox. Nature, 378, 1995; 337-338
31. Gurewich, V., Pannell, R.: Inactivation of single-chain urokinase (pro-urokinase) by thrombin and thrombin-like enzymes: relevance of the findings to the interpretation of fibrin-binding experiments. Blood, 69, 1987; 769-772
32. Hackeng, T. M., Tans, G., Koppelman, S. J., et al.: Protein C activation on endothelial cells by prothrombin activation products generated in situ: meizothrombin is a better protein C activator than a thrombin. Biochem. J., 319, 1996; 399-405
33. Hanson, S. R., Griffin, J. H., Harker, L. A. et al.: Antithrombotic effects of thrombin-induced activation of endogenous protein C in primates. J. Clin. Invest., 92, 1993; 2003-2012
34. Hendriks, D., Scharpé, S., van Sande, M. et al.: A labile enzyme in fresh human serum interferes with the assay of carboxypeptidase N. Clin. Chem., 35, 1989; 177
35. Hendriks, D., Scharpé, S., van Sande, M. et al.: Characterization of a carboxypeptidase in human serum distinct from carboxypeptidase N. J. Clin. Chem. Clin. Biochem., 27, 1989, 277-285
36. Hendriks, D., Wang, W., Scharpé, S. et al.: Purification and characterization of a new arginine carboxypeptidase in human serum. Biochim. Biophys. Acta, 1034, 1990; 86-92
37. Hosaka, Y., Takahashi, Y., Ishii, H.: Thrombomodulin in human plasma contributes to inhibit fibrinolysis through acceleration of thrombin-dependent activation of plasma procarboxypeptidase B. Thromb. Haemost., 79, 1998; 371-377
38. Hoylaerts, M., Rijken, D. C., Lijnen, H. R. et al.: Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J. Biol. Chem., 257, 1982; 2912-2919
39. Hryszko, T., Malyszko, J., Malyszko, J. S. et al.: Renal replacement therapy (RRT) influences thrombin activatable fibrinolysis inhibitor (TAFI) concentration and its activity. Thromb. Haemost., Suppl., July 2001; P2006
40. Chetaille, P., Alessi, M. C., Kouassi, D. et al.: Plasma TAFI antigen variations in healthy subjects. Thromb. Haemost., 83, 2000; 902-905
41. Christensen, U.: C-terminal lysine residues of fibrinogen fragments essential for binding to plasminogen. FEBS Lett., 182, 1985; 43-46
42. Ichinose, A.: The physiology and biochemistry of factor XIII. In: Bloom, A. L., Forbes, C. D., Thomas, D. P., Tuddenham, E. G., editors. Hemostasis and thrombosis. Edinburgh: Livingstone, 1994; 531-546
43. Kato, T., Akatsu, H., Sato, T. et al.: Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N. Microbiol. Immunol., 44, 2000; 719-728
44. Kokame, K., Zheng, X. L., 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
45. Koster, T., Blann, A. D., Briët, E. et al.: Role of clotting factor VIII in effect of von Willebrand factor on occurrence of deep vein thrombosis. Lancet, 345, 1995; 152-155
46. Kurosawa, S., Stearns, D. J., Jackson, K. W. et al.: A 10-kDa cyanogen bromide fragment from the epidermal growth factor homology domain of rabbit thrombomodulin contains the primary thrombin binding site. J. Biol. Chem., 263, 1988; 5993-5996
47. Lenich, C., Pannell, R., Gurewich, V.: Assembly and activation of the intrinsic fibrinolytic pathway on the surface of humen endothelial cells in culture. Thromb. Haemost., 74, 1995; 698-703
48. Lijnen, H. R., Van Hoef, B., Collen, D.: Activation with plasmin of two-chain urokinase-type plasminogen activator derived from single-chain urokinase-type plasminogen activator by treatment with thrombin. Eur. J. Biochem., 169, 1987; 359-364
49. Mao, S. S., Cooper, C. M., Wood, T. et al.: Characterization of plasmin-mediated activation of plasma proca: carboxypeptidase B-modulation by glycosaminoglycans. J. Biol. Chem., 274, 1999; 35046-35052
50. Marlar, R. A., Endres-Brooks, J., Miller, C.: Serial studies of protein C and its plasma inhibitor in patients with disseminated intravascular coagulation. Blood, 66, 1985; 59-63
51. Marx, P. F., Hackeng, T. M., Dawson, P. E. et al.: Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. J. Biol. Chem., 275, 2000; 12410-12415
52. Meijers, J. C. M., Middeldorp, S., Tekelenburg, W. et al.: Increased fibrinolytic activity during use of oral contraceptives is counteracted by an enhanced factor XI-independent down regulation of fibrinolysis - randomized cross-over study of two low-dose oral contraceptives. Thromb. Haemost., 84, 2000; 9-14
53. Meijers, J. C. M., Tekelenburg, W., Bouma, B. N. et al.: High levels of coagulation factor XI as a risk factor for venous thrombosis. N. Engl. J. Med., 342, 2000; 696-701
54. Meijers, J. C. M., Oudijk, E. J., Mosnier, L. O. et al.: Reduced activity of TAFI (thrombin-activatable fibrinolysis inhibitor) in acute promyelocytic leukaemia. Br. J. Haematol., 108, 2000; 518-523
55. Mosnier, L. O., Von dem Borne, P. A. K., Meijers, J. C. M. et al.: Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation. Thromb. Haemost., 80, 1998; 829-835
56. Mosnier, L. O., Meijers, J. C. M., 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
57. Redlitz, A., Tan, A. K., Eaton, D. L. et al.: Plasma carboxypeptidases as regulators of the plasminogen system. J. Clin. Invest., 96, 1995; 2534-2538
58. Sakata, Y., Loskutoff, D. J., Gladson, C.L. et al.: Mechanism of protein C-dependent clot lysis: role of plasminogen activator inhibitor. Blood, 68, 1986; 1218-1223
59. Sakharov, D. V., Plow, E. F., Rijken, D. C.: On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B. J. Biol. Chem., 272, 1997; 14477-14482
60. Sato, T., Miwa, T., Akatsu, H. et al.: Procarboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not. J. Immunol., 165, 2000; 1053-1058
61. Schatteman, K. A., Goossens, F.J., Scharpé, S. S. et al.: Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. Clin. Chem., 45, 1999; 807-813
62. Silveira, A., Schatteman, K. A., Goosens, F. J. et al.: Plasma procarboxypeptidase U in men with symptomatic coronary artery disease. Thromb. Haemost., 84, 2000; 364-368
63. Skidgel, R. A.: Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol. Sci., 9, 1988; 299-304
64. Skidgel, R. A.: Human carboxypeptidase N: lysine carboxypeptidase. Methods Enzymol., 248, 1995; 653-663
65. Staško, J., Ivanková, J., Holman, B. et al.: TAFI v diagnostike porúch fibrinolýzy u nefropatií, 36. In: Pecka, M., Malý, J.: Laboratorní hematologie, Hradec Králové, HK Credit, 2002; 93.
66. Stewart, R. J., Fredenburgh, J. C., Rischke, J. A. et al.: Thrombin-activatable fibrinolysis inhibitor attenuates (DD)E-mediated stimulation of plasminogen activation by reducing the affinity of (DD)E for tissue plasminogen activator: a potential mechanism for enhancing fibrin specificity of tissue plasminogen activator. J. Biol. Chem., 275, 2000; 36612-36620
67. Takano, S., Kimura, S., Ohdama, S. et al.: Plasma thrombomodulin in health and disease. Blood, 76, 1990; 2024-2029
68. Tan, A. K., Eaton, D. L.: Activation and characterization of procarboxypeptidase B from human plasma. Biochemistry, 34, 1995; 5811-5816
69. 2-macroglobulin and pregnancy zone protein. J. Biol. Chem., 271, 1996; 12937-12943
70. Van Tilburg, N. H., Rosendaal, F. R., Bertina, R. M.: Thrombin-activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood, 95, 2000; 2855-2859
71. Vlieg, A. V., Van der Linden, I. K., Bertina, R. M. et al.: High levels of factor IX increase the risk of venous thrombosis. Blood, 95, 2000; 3678-3682
72. Von dem Borne, P. A. K., Bajzar, L., Meijers, J. C. M. et al.: Thrombin-mediated activation of factor XI results in a thrombin-activatable fibrinolysis inhibitor-dependent inhibition of fibrinolysis. J. Clin. Invest., 99, 1997; 2323-2327
73. Walenga, J. M., Florian, M., Hoppensteadt, A. et al.: Heparin, LMW heparins and HCII binding oligosaccharides, but not pentasaccharide, regulate TAFI (thrombin activatable fibrinolysis inhibitor). Thromb. Haemost., Suppl., July 2001; P2011
74. Wang, W., Hendriks, D. F., Scharpé, S. S.: Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J. Biol. Chem., 269, 1994; 15937-15944
75. Wang, W., Boffa, P. B., Bajzar, L. et al.: A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activatable fibrinolysis inhibitor. J. Biol. Chem., 273, 1998; 27176-27181
76. 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