Biopolym. Cell. 2010; 26(4):255-264.
http://dx.doi.org/10.7124/bc.00015D
Reviews
Structural and functional peculiarities of plasminogen activator inhibitor PAI-1
1Zhernossekov D. D., 1Zolotareva E. N., 1Kondratuk A. S.
  1. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovycha Str., Kyiv, Ukraine, 01601

Abstract

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
Full text: (PDF, in English) (PDF, in Russian)

References

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