PMID: 9184410May 1, 1997Paper

Tridegin, a novel peptidic inhibitor of factor XIIIa from the leech, Haementeria ghilianii, enhances fibrinolysis in vitro

Thrombosis and Haemostasis
L SealeR B Wallis

Abstract

Tridegin is a potent inhibitor of factor XIIIa from the leech, Haementeria ghilianii, which inhibits protein cross-linking. It modifies plasmin-mediated fibrin degradation as shown by the absence of D-dimer and approximately halves the time for fibrinolysis. Plasma clots formed in the presence of Tridegin lyse more rapidly when either streptokinase, tissue plasminogen activator or hementin is added 2 h after clot formation. The effect of Tridegin is markedly increased if clots are formed from platelet-rich plasma. Platelet-rich plasma clots are lysed much more slowly by the fibrinolytic enzymes used and if Tridegin is present, the rate of lysis returns almost to that of platelet-free clots. These studies indicate the important role of platelets in conferring resistance to commonly used fibrinolytic enzymes and suggest that protein cross-linking is an important step in this effect. Moreover they indicate that Tridegin, a small polypeptide, may have potential as an adjunct to thrombolytic therapy.

Related Concepts

Related Feeds

Blood Clotting Disorders

Thrombophilia includes conditions with increased tendency for excessive blood clotting. Blood clotting occurs when the body has insufficient amounts of specialized proteins that make blood clot and stop bleeding. Here is the latest research on blood clotting disorders.

Related Papers

Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis
R B WallisS B Ross-Murphy
Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis
M E Carr, B M Alving
The Journal of Biological Chemistry
L A Falls, D H Farrell
Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis
S KawakamiJ S Lee
© 2021 Meta ULC. All rights reserved