Randomized trial shows that human neutrophil elastase inhibits thrombin-induced platelet function, suggesting a significant impact on coagulation processes.
Key Points
This research investigates how human neutrophil elastase affects platelet function and structure during coagulation.
Analyzed the effect of human neutrophil elastase on platelet aggregation and glycoprotein levels
Measured thrombin binding sites and conducted proteolysis studies on glycoproteins
Utilized sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation techniques
Elastase significantly inhibited thrombin-induced platelet aggregation and reduced thrombin binding sites from 31 to 12 per platelet (P<0.05)
Identified proteolytic cleavage of glycoprotein Ib in elastase-treated platelets
Found a new glycoprotein in the supernatant of elastase-treated platelets not present in untreated samples