Abstract
We prepared heparin-inserted phospholipid liposomes as a functional model of heparan sulfate present on the vascular surface and examined tissue plasminogen activator (t-PA) catalyzed plasminogen activation on the liposome surface. Kinetic analyses showed a marked increase in the affinity of t-PA for Lys-plasminogen in the presence of heparin-inserted phosphatidylcholine (PC) liposomes. The catalytic efficiency (kcat/Km) of t-PA for the plasminogen activation on the surface of heparin-inserted PC liposomes was 5.4 times that on the surface of heparin-free PC liposomes. This stimulatory action of immobilized heparin was apparently affected by changing the phospholipid component of liposomes. Phosphatidylethanolamine or stearylamine, having a positively charged group, reduced the catalytic efficiency of t-PA by raising its Km value (10-fold), whereas negatively charged phospholipids, phosphatidylserine and phosphatidylinositol, did not affect the efficiency. t-PA and generated plasmin bound to the liposome surface heparin were protected from inhibition by plasminogen activator inhibitor type 1 and alpha 2-plasmin inhibitor, respectively. t-PA-induced clot lysis of euglobulin or whole plasma, which contained native (Glu-) plasmino...Continue Reading
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