Effect of a synthetic carboxy-terminal peptide of alpha(2)-antiplasmin on urokinase-induced fibrinolysis

Thrombosis Research
K N LeeP A McKee

Abstract

alpha(2)-Antiplasmin (alpha(2)AP) interferes with the binding of plasminogen to fibrin because lysine residues in its carboxy-terminal region compete with those in fibrin, presumably the same way that free lysine or epsilon-aminocaproic acid (EACA) inhibits plasminogen binding to fibrin. While this overall process causes an inhibition of fibrinolysis, the converse was observed with a 26-residue synthetic peptide (AP26) corresponding to the carboxy-terminal region of alpha(2)AP. The AP26 peptide, in fact, accelerated urokinase-induced lysis of (1) fully crosslinked fibrin with complete gamma-dimer and alpha-polymer formation; (2) partially crosslinked fibrin that had undergone only gamma-dimerization; and (3) noncrosslinked fibrin. The AP26 peptide also inhibited factor XIIIa-catalyzed crosslinking of fibrin alpha-chains, and this also accelerated lysis of fibrin. EACA had no effect. In the presence of noncrosslinked fibrin, AP26 promoted plasminogen activation by urokinase and fibrinolysis. EACA only slightly increased the rate of plasminogen activation, and as expected, it inhibited fibrinolysis. Since AP26 peptide enhanced the lysis of partially crosslinked and noncrosslinked fibrin, our results indicate that inhibition of fa...Continue Reading

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Sep 24, 2005·The FEBS Journal·Paul B Coughlin
Mar 11, 2017·Cardiovascular Diabetology·Katherine KearneyRamzi Ajjan
Jun 21, 2017·BioMed Research International·Nathan E Hudson
Jan 12, 2021·Frontiers in Cardiovascular Medicine·Satish SinghGuy L Reed

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