Biopolymers and cell. 2010; 26 (4): 255 - 264
Structural and functional peculiarities of plasminogen activator inhibitor PAI-1
D. D. Zhernossekov, E. N. Zolotareva, A. S. Kondratuk
Palladin Institute of Biochemistry of the NAS of Ukraine 9 Leontovicha Str., Kyiv, Ukraine, 01601
PAI-1, an important component of the hemostasis system, is a specific inhibitor of both urokinase type and tissue type plasminogen activators. PAI-1 belongs to the serpin family. The interaction between somatomedin-like domain of vitronectin and PAI-1 leads to stabilization of the latter. PAI-1 latency transition is related to the conformational changes in the reactive central loop. The inhibitory mechanism of PAI-1 is in accordance with the classic scheme of serpin action. PAI-1 blocks the adhesion mediated by UPA and integrins, so this inhibitor plays an important role in adhesion process and angiogenesis. An altered PAI-1level is associated with the development of cardiovascular diseases, kidney fibrosis, diabetis, cancerogenesis.
Keywords: PAI-1, fibrinolysis, cell migration.