The effect of the proteinase inhibitor aprotinin on membrane glycoproteins and functions of platelets stored for 5 days in platelet-rich plasma was tested. Platelet membrane glycoprotein content was determined by flow cytometry or immunoblot techniques using different monoclonal antibodies. ADP- and ristocetin-induced platelet aggregation and adhesion to collagen were tested in parallel. Using the flow-cytometry technique i) a progressive decrease in the percentage of platelets reacting with the different monoclonal antibodies was observed during storage ii) a 30% reduction of the GPIb mean fluorescence intensity (MFI) was observed after 5 days storage while the MFI of the GP IIb-IIIa complex was not modified. Using the immunoblot technique, a decrease in the amount of both the GPIb alpha and the component of Mr 100,000 was observed, while a 50,000 Mr fragment appeared progressively. Platelet adhesion and aggregation were reduced after 24 hours of storage. Aprotinin prevented neither the GPIb alpha reduction nor the modifications of the functions of human platelets stored in their autologous plasma.