S100A10: A Key Regulator of Fibrinolysis

摘要: Regulation of fibrinolytic activity can be achieved by several mechanisms, ranging from regulating the production and localization plasminogen activators their inhibitors, degradation inactivation plasmin via autoproteolysis, synthesis cell surface receptors for plasminogen. Binding inactive zymogen to its has been shown significantly increase rate conversion active serine-protease co-localizing with activators, tissue-type activator (tPA) urokinase-type (uPA) [1–3].One such receptor is S100A10 (p11) [4]. S100A10, a member S100 protein family, was initially discovered as an annexin A2 (p36) binding partner [5–7]. also found interact other cellular proteins including Rho GTPase-activating DLC1 [8], cytosolic phospholipase [9], serotonin 1B [10] various ion channels, potassium channel TASK-1 [11], sodium Na(V)1.8 [12] calcium channels TRPV5 TRPV6 [13]. However, major partners on are tPA [14]. The focus this review will discuss role that extracellular plays in physiological consequences process (Figure 1).