Subscribe to RSS
DOI: 10.1055/s-0038-1650002
Interaction of Plasmin with Tranexamic Acid and α2 Plasmin Inhibitor in the Plasma and Clot
Publication History
Publication Date:
13 July 2018 (online)
Summary
Interaction of urokinase (UK) activated plasmin with tranexamic acid and α2 plasmin inhibitor (α2PI) was studied by using a chromogenic substrate (S-2251) and immunoelectrophoresis. Plasma was activated by UK (P+U) in the presence of tranexamic acid (P+U + t) or in the presence of thrombin (P+U+thr) and thrombin plus tranexamic acid (P+U+thr+t). These mixtures were incubated for 10, 20, and 30 min at 37°C, then an aliquot of each mixture was added to S-2251, and incubated for 3 or 10 min at 37°C. Hydrolysis of S-2251 after 3 min incubation was significant in the presence of tranexamic acid or clot formation, thus the presence of tranexamic acid or clot formation enhancing the UK activation of plasminogen in both plasma and clot. Hydrolysis of S-2251 after 10 min incubation was higher in the presence of tranexamic acid than in its absence or clot formation without tranexamic acid. Tranexamic acid seems to be more effective in enhancement of activation of plasminogen by UK than clot formation. Plasmin formed by UK was coexistent with α2PI in the plasma in contrast to a purified system in which α2PI formed a complex with plasmin instantaneously. In an even purified system, clot formation and the presence of tranexamic acid protected plasmin from its inactivation by α2PI to some extent.
-
References
- 1 Müllertz S. Different molecular forms of plasminogen and plasmin produced by urokinase in human plasma and their relation to protease inhibitors and lysis of fibrinogen and fibrin. Biochem J. 1974; 143: 273-283
- 2 Collen D, De Cock F, Verstraete M. Immunochemical distinstion between antiplasmin and alpha-antitrypsin. Thromb Res. 1975; 7: 245-249
- 3 Collen D. Identification and some properties of a new fast-reacting plasmin inhibitor in human plasma. Eur J Biochem. 1976; 69: 209-216
- 4 Moroi M, Aoki N. Isolation and characterization of α2-palsmin inhibitor from human plasma. J Biol Chem. 1976; 251: 5956-5965
- 5 Mullertz S, Clemmensen I. The primary inhibitor of plasmin in human plasma. Biochem J. 1976; 159: 545-553
- 6 Wiman B, Collen D. On the reaction between plasmin and antiplasmin. Abstracts (I) of XVII Congress of International Society of Haematology. 1978. p 30
- 7 Norman PS, Hill B. Studies of the plasmin system. III. Physical properties of the two plasmin inhibitors in plasma. J Exp Med. 1958; 108: 639-649
- 8 Christensen U, Clemmensen I. Kinetic properties of the primary inhibitor of plasmin from human plasma. Biochem J. 1977; 163: 389-391
- 9 Naito K, Aoki N. Assay of α2 plasmin inhibitor activity by means of a plasmin specific tripeptide substrate. Thromb Res. 1978; 12: 1147-1156
- 10 Claeys H, Vermylen J. Physico-chemical and proenzyme properties of NH2-terminal glutamic acid and NH2-terminal lysine human plasminogen. Influence of 6-aminohexanoic acid. Biochim Biophys Acta. 1974; 342: 351-359
- 11 Wallen P. Chemistry of plasminogen and plasminogen activation. In: Progress in chemical fibrinolysis and thrombolysis. Davidson JF, Martin RM, Samama MM, Desnoyers PC. Eds Raven Press, New York: 1978. vol 3 P 167-181
- 12 Takada A, Takada Y. Effect of tranexamic acid, t-AMCHA, and its cis-isomer on the complement system in vitro and in vivo: Possible relationship between coagulation and complement systems. Thromb Res. 1978; 13: 193-205
- 13 Takada A, Sumi H, Takada Y. Influence of coagulation on the activation of plasminogen and C1s. Abstracts (I) of XVII Cong, of international society of haematology. 1978 p 116
- 14 Takada A, Ohashi H, Matsuda H, Takada Y. Effects of tranexamic acid, cis-AMCHA, and 6-aminohexanoic acid on the activation rate of plasminogen by urokinase in the presence of a clot. Thromb Res. 1979; 14: 915-923
- 15 Wiman B, Wallen P. The specific interaction between plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen. Thromb Res. 1977; 10: 213-222
- 16 Aoki N, Moroi M, Matsuda M, Tachiya K. The behavior of α2 plasmin inhibitor in fibrinolytic states. J Clin Invest. 1977; 60: 361-369
- 17 Mullertz S. The primary plasmin inhibitor, α2-plasmin inhibitor or α2-antiplasmin: A review. In: The physiological inhibitors of blood coagulation and fibrinolysis. 1979. p 87-101 Collen D, Wiman M, Verstraete M. Eds Elsevier/North-Holland Biomedical Press, Amsterdam:
- 18 Wiman B, Collen D. On the kinetics of the reaction between human antiplasmin and plasmin. Eur J Biochem 1978; 573-578
- 19 Wiman B, Boman L, Collen D. On the kinetics of the reaction between human antiplasmin and a low molecular weight form of plasmin. Eur J Biochem. 1978; 87: 143-146