プラスミノーゲンは血栓のフィブリンを溶解するほか、多くの過程でタンパク質分解因子として働く。（胎児の発達、組織のリモデリング、腫瘍の浸潤、炎症など）
排卵ではグラーフ卵胞の破裂を促す。ウロキナーゼ型のプラスミノーゲンアクチベーター、コラゲナーゼや他の多くの補体のチモーゲン（C1とC5）により活性化される。
フィブロネクチンやラミニンの切断は細胞の遊離とアポトーシスをもたらす。フィブリンやトロンボスポンジン、VWFを分解する。
Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.
Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.
Miscellaneous
Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
Catalytic activity
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.1 Publication
Enzyme regulation
Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Activated with catalytic amounts of streptokinase. Plasmin activity inhibited by SERPINE2.
Post-translational modificationi
N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity).
In the presence of the inhibitor, the activation involves only cleavage after Arg-580, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide.
