Fibrinolüütiline

Fibrinolüütiline refers to the process of breaking down fibrin, a protein that forms a meshwork to stabilize blood clots. This process is crucial for preventing excessive clot formation and for tissue repair after injury.

The primary mechanism of fibrinolysis involves a cascade of enzymatic reactions. Plasmin, a key enzyme, is responsible for degrading fibrin. Plasminogen, an inactive precursor, circulates in the blood and is converted to its active form, plasmin, by plasminogen activators. Tissue plasminogen activator (tPA) and urokinase plasminogen activator (uPA) are the main physiological activators. Once plasmin is formed, it binds to fibrin and cleaves it into smaller fragments, effectively dissolving the clot.

This process is tightly regulated to ensure that clots are only broken down when necessary. Inhibitors of plasminogen activators, such as plasminogen activator inhibitor-1 (PAI-1), and inhibitors of plasmin itself, like alpha-2-antiplasmin, prevent premature or excessive fibrinolysis.

Disruptions in fibrinolysis can have significant health implications. Excessive fibrinolysis can lead to bleeding disorders, while insufficient fibrinolysis can contribute to thrombotic events, such as heart attacks and strokes, where clots block blood flow. Therapeutic agents that promote fibrinolysis, known as thrombolytics or fibrinolytics, are used to dissolve existing blood clots in acute medical emergencies like myocardial infarction or ischemic stroke.