Plasminogen (PLG) (PLG)

Plasminogen is a 92 kDa glycoprotein zymogen synthesized primarily in the liver and circulating in the blood at high concentrations [1, 4]. It is the precursor to plasmin, a major serine protease responsible for fibrinolysis, the process of breaking down fibrin clots into soluble fragments [2, 3]. Activation of plasminogen is mediated by tissue-type plasminogen activator (tPA) or urokinase-type plasminogen activator (uPA), which cleave a specific peptide bond to generate the active two-chain enzyme [1, 2]. Beyond its role in hemodynamics, the plasminogen system participates in extracellular matrix degradation, wound healing, and cell migration [2, 4]. Clinically, this system is targeted by thrombolytic agents to treat acute myocardial infarction and stroke, and by antifibrinolytics to manage surgical or traumatic bleeding [3, 5]. Additionally, purified human plasminogen is used as a replacement therapy for patients with congenital plasminogen deficiency, a rare condition characterized by the formation of fibrin-rich pseudomembranes on mucous membranes [5, 6].

Other names

PlasminPLGActivation peptideAngiostatinSerum plasminogen

Therapeutic agents either activate plasminogen to promote fibrinolysis (thrombolytics), inhibit its activation or activity to prevent clot breakdown (antifibrinolytics), or replace the protein in cases of congenital deficiency [2, 3, 5].