Effect of recombinant forms of urokinase plasminogen activator on platelet aggregation and intracellular calcium accumulation

Abstract

Urokinase caused plasmin-dependent inhibition of platelet aggregation in platelet-rich plasma, while its proteolytically inactive form had no such effect. Both forms potentiated the increase in platelet calcium concentration induced by aggregation inductors and facilitated aggregation of washed platelets. In contrast to full-length urokinase molecule, its aminoterminal fragment inhibited platelet aggregation and the corresponding elevation of intracellular calcium. These data suggest that urokinase exerts a plasmin-independent effect on platelet activity. This effect depends on urokinase structure.