Thromb Haemost 1997; 77(05): 0959-0963
DOI: 10.1055/s-0038-1656085
Fibrinolysis
Schattauer GmbH Stuttgart

Tridegin, a Novel Peptidic Inhibitor of Factor XIIIa from the Leech, Haementeria ghilianii, Enhances Fibrinolysis In Vitro

Lisa Seale
Biopharm (UK) Limited, Hendy, Dyfed, UK
,
Sarah Finney
Biopharm (UK) Limited, Hendy, Dyfed, UK
,
Roy T Sawyer
Biopharm (UK) Limited, Hendy, Dyfed, UK
,
Robert B Wallis
Biopharm (UK) Limited, Hendy, Dyfed, UK
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Publikationsverlauf

Received 25. September 1996

Accepted after resubmission 28. Januar 1997

Publikationsdatum:
11. Juli 2018 (online)

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Summary

Tridegin is a potent inhibitor of factor Xllla 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.