Inhibition of Human Platelet Aggregation by the Proteolytic Effect of Streptokinase Role of the Human Factor-VIII-Related Protein

Defective ADP-induced aggregation was observed in in vitro streptokinase (SK)-treated normal platelet-rich plasma. Classic haemophilia and normal platelet-poor plasmas (PPP) treated with SK inhibit the aggregation of washed platelets; plasmin-treated normal human serum also shows an inhibitory effect on platelet aggregation. However, SK-treated von Willebrand plasmas do not inhibit the aggregation of washed platelets. This confirms the fact that the anti-aggregating effect is mainly linked to the digested factor VIII but not to the digested fibrinogen. Defective ristocetin-induced platelet aggregation has also been observed in SK-treated plasmas. The presence of normal PPP does not modify the inhibition of the ADP-induced aggregation of washed platelets in SK-treated PPP. However, it does correct the ristocetin-induced aggregation. These results suggest that the inhibition of the ADP-induced aggregation is caused by the factor VIII degradation products, while the inhibition of the ristocetin-induced aggregation appears because of a defective von Willebrand activity of the factor VIII molecule.