  urokinase (trade name abbokinase), also called urokinase-type plasminogen activator (upa), is a serine protease (). it was discovered in 1947 by mcfarlane.nursing grand rounds pdfs.journals.lww.com/.../nursing_grand_rounds.8.pdf j vitello-cicciu - 1987 urokinase was originally isolated from human urine, but is present in several physiological locations, such as blood stream and the extracellular matrix. the primary physiological substrate is plasminogen, which is an inactive form (zymogen) of the serine protease plasmin. activation of plasmin triggers a proteolysis cascade that, depending on the physiological environment, participates in thrombolysis or extracellular matrix degradation. this links urokinase to vascular diseases and cancer. == molecular characteristics == urokinase is a 411-residue protein, consisting of three domains: the serine protease domain, the kringle domain, and the growth factor domain. urokinase is synthesized as a zymogen form (prourokinase or single-chain urokinase), and is activated by proteolytic cleavage between lys158 and ile159. the two resulting chains are kept together by a disulfide bond. == interaction partners == the most important inhibitors of urokinase are the serpins plasminogen activator inhibitor-1 (pai-1) and plasminogen activator inhibitor-2 (pai-2), which inhibit the protease activity irreversibly. in the extracellular matrix, urokinase is tethered to the cell membrane by its interaction to the urokinase receptor. center|framed|fibrinolysis (simplified). blue arrows denote stimulation, and red arrows inhibition. the molecular weight of (high molecular weight) urokinase is about 54000 daltons. only
Antithrombotic_enzymes EC_3.4.21 Genes_on_chromosome_10