COPY: Plasma Proteins and Fibrinolysis Quiz

Plasminogen is synthesized in the kidney as an active enzyme.

Plasminogen binds to fibrin throughout the developing thrombus.

Urokinase Plasminogen Activator (UPA) is an extrinsic plasminogen activator.

Plasmin has narrow substrate specificity, mainly targeting fibrin polymer degradation.

TAFI activity is not localized to the fibrin clot and remains active when not associated with fibrin surfaces.

PAI-1 binds to circulating active plasmin, inhibiting its fibrinolytic activity.

Thrombin-activatable fibrinolysis inhibitor (TAFI) is a pro-inflammatory protein.

The binding of TPA to fibrin enhances its susceptibility to PAI-1 inhibition.

Plasminogen Activator Inhibitors (PAIs) are synthesized in the liver.

The activation of the antifibrinolytic enzyme leads to increased plasminogen and TPA binding to fibrin.

Fibrin degradation products (FDP/FSP) are rapidly cleared from circulation by the kidneys.

Fragment X from fibrin degradation has an anticoagulant effect by promoting the formation of fibrin.

Plasminogen activators accelerate the hydrolysis of fibrin by bound plasmin.

Tissue plasminogen activator (tPA) is a serine protease with high specificity for converting plasminogen to plasmin.

Excessive fibrinolysis leads to thrombosis due to premature clot extension.

Plasminogen is the active enzyme involved in degrading fibrin.

Plasminogen activators are released in response to inflammation and coagulation.

The main function of tissue plasminogen activator (tPA) is to promote clot extension.