Tridegin, a novel peptidic inhibitor of factor XIIIa from the leech, Haementeria ghilianii, enhances fibrinolysis in vitro.
Thromb Haemost
; 77(5): 959-63, 1997 May.
Article
em En
| MEDLINE
| ID: mdl-9184410
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fator XIIa
/
Fibrinólise
/
Fibrinolíticos
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Thromb Haemost
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Reino Unido