Thrombin-activable fibrinolysis inhibitor attenuates (DD) E-mediated stimulation of plasminogen activation by reducing the affinity of (DD) E for tissue plasminogen …
RJ Stewart, JC Fredenburgh, JA Rischke… - Journal of Biological …, 2000 - ASBMB
A complex of d-dimer noncovalently associated with fragment E ((DD) E), a degradation
product of cross-linked fibrin that binds tissue plasminogen activator (t-PA) and plasminogen
(Pg) with affinities similar to those of fibrin, compromises the fibrin specificity of t-PA by
stimulating systemic Pg activation. In this study, we examined the effect of thrombin-activable
fibrinolysis inhibitor (TAFI), a latent carboxypeptidase B (CPB)-like enzyme, on the
stimulatory activity of (DD) E. Incubation of (DD) E with activated TAFI (TAFIa) or CPB (a) …
product of cross-linked fibrin that binds tissue plasminogen activator (t-PA) and plasminogen
(Pg) with affinities similar to those of fibrin, compromises the fibrin specificity of t-PA by
stimulating systemic Pg activation. In this study, we examined the effect of thrombin-activable
fibrinolysis inhibitor (TAFI), a latent carboxypeptidase B (CPB)-like enzyme, on the
stimulatory activity of (DD) E. Incubation of (DD) E with activated TAFI (TAFIa) or CPB (a) …
