Mechanism of Action of Thrombolytics

Urokinase is a serine protease that directly converts plasminogen to plasmin (2). It has no fibrin specificity; therefore, it has no clot specificity. Although urokinase has historical merit, it is not currently used clinically. However, its precursor—recombinant prourokinase (rpro-UK)—has been used in intra-arterial (IA) clinical trials.

Streptokinase is a secreted product of beta-hemolytic streptococci, which works by forming a complex with plasminogen, and this complex proteolytically converts plasminogen to plasmin (3). Streptokinase has been used in multiple clinical trials, but it is not currently on the market for thrombolytic therapy.

rtPA is a naturally occurring enzyme that is made by the endothelial cells in response to arterial wall injury and potentiates the conversion of plasminogen to plasmin. Unlike other thrombolytics, rtPA has high specificity for fibrin and is therefore clot specific (4). Fibrin stimulates the activity of rtPA, which minimizes the probability of hemorrhage due to decreased

Vessel Damage

Extrinsic Pathway

Intrinsic Pathway

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