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Tissue-type plasminogen activator (tPA) is a vital serine protease that serves as the primary initiator of fibrinolysis, the physiological process of dissolving blood clots. Synthesized and secreted by vascular endothelial cells, tPA binds to fibrin and catalyzes the conversion of the zymogen plasminogen into the active enzyme plasmin [1][2]. This localized activation ensures that plasmin degrades the fibrin meshwork of a thrombus without causing systemic proteolysis [3]. Recombinant versions of tPA, including alteplase and tenecteplase, are essential therapeutic agents used to restore blood flow in patients suffering from acute ischemic stroke, myocardial infarction, and massive pulmonary embolism [4]. Despite its life-saving potential, tPA administration carries a significant risk of major bleeding, most notably symptomatic intracranial hemorrhage, which necessitates careful patient selection and adherence to strict treatment windows [5]. Additionally, tPA plays non-fibrinolytic roles in the brain, where it modulates synaptic plasticity and may contribute to neurotoxicity under certain pathological conditions [6].
Serine protease that catalyzes the conversion of the zymogen plasminogen into the active enzyme plasmin, which subsequently degrades fibrin in blood clots.
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