L. Seale et al., TRIDEGIN, A NOVEL PEPTIDIC INHIBITOR OF FACTOR XIIIA FROM THE LEECH, HAEMENTERIA-GHILIANII, ENHANCES FIBRINOLYSIS IN-VITRO, Thrombosis and haemostasis, 77(5), 1997, pp. 959-963
Tridegin is a potent inhibitor of factor XIIIa from the leech, Haement
eria ghilianii, which inhibits protein cross-linking. It modifies plas
min-mediated fibrin degradation as shown by the absence of D-dimer and
approximately halves the time for fibrinolysis. Plasma clots formed i
n the presence of Tridegin lyse more rapidly when either streptokinase
, tissue plasminogen activator or hementin is added 2 h after clot for
mation. The effect of Tridegin is markedly increased if clots are form
ed from platelet-rich plasma. Platelet-rich plasma clots are lysed muc
h more slowly by the fibrinolytic enzymes used and if Tridegin is pres
ent, the rate of lysis returns almost to that of platelet-free clots.
These studies indicate the important role of platelets in conferring r
esistance to commonly used fibrinolytic enzymes and suggest that prote
in cross-linking is an important step in this effect. Moreover they in
dicate that Tridegin, a small polypeptide, may have potential as an ad
junct to thrombolytic therapy.