Inhibition of plasminogen activator inhibitor-1: its mechanism and effectiveness on coagulation and fibrosis.

نویسندگان

  • Yuko Izuhara
  • Satoru Takahashi
  • Masaomi Nangaku
  • Shunya Takizawa
  • Hideyuki Ishida
  • Kiyoshi Kurokawa
  • Charles van Ypersele de Strihou
  • Noriaki Hirayama
  • Toshio Miyata
چکیده

OBJECTIVE Serine protease inhibitors (serpin) play a central role in various pathological processes including coagulation, fibrinolysis, malignancy, and inflammation. Inhibition of serpins may prove therapeutic. As yet, however, only very few small molecule serpin inhibitors have been reported. For the first time, we apply a new approach of virtual screening to discover novel, orally active, small molecule serpin inhibitors and report their effectiveness. METHODS AND RESULTS We focused on a clinically important serpin, plasminogen activator inhibitor-1 (PAI-1), whose crystal structure has been described. We identify novel, orally active molecules able to enter into the strand 4 position (s4A) of the A beta-sheet of PAI-I as a mock compound. In vitro they specifically inhibit the PAI-1 activity and enhance fibrinolysis activity. In vivo the most effective molecule (TM5007) inhibits coagulation in 2 models: a rat arteriovenous (AV) shunt model and a mouse model of ferric chloride-induced testicular artery thrombosis. It also prevents the fibrotic process initiated by bleomycin in mouse lung. CONCLUSIONS The present study demonstrates beneficial in vitro and in vivo effects of novel PAI-1 inhibitors. Our methodology proves to be a useful tool to obtain effective inhibitors of serpin activity.

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عنوان ژورنال:
  • Arteriosclerosis, thrombosis, and vascular biology

دوره 28 4  شماره 

صفحات  -

تاریخ انتشار 2008