Human platelets that were preincubated with porcine elastase aggregated spontaneously upon the addition of fibrinogen. Maximal aggregation to fibrinogen was observed with platelets pretreated with an elastase concentration of 111 tg/ml, and halfmaximal aggregation occurred after treatment with 11 ,ug/ml elastase. Binding of radiolabeled fibrinogen to elastase-treated platelets was specific, saturable, and showed a single class of 48,400±9,697 fibrinogen-binding sites per platelet with a dissociation constant of 6.30±1.48 X i0-M. ATP, apyrase, and the stimulators of platelet adenylate cyclase forskolin, prostaglandin El, prostacyclin, and N6, 2'-O-dibutyryl cyclic AMP did not inhibit the fibrinogen-induced aggregation of elastase-treated platelets. EDTA completely blocked the initiation of aggregation and reversed the fibrinogen-induced aggregation of elastasetreated platelets. Monoclonal and polyclonal antibodies directed against glycoproteins (GP) Ilb and II1a completely blocked the fibrinogen-induced aggregation of elastase-treated platelets. Immunoprecipitates with these antibodies obtained from detergent extracts of surface-radiolabeled, intact, and elastase-treated platelets contained the glycoproteins IUb and IIIa. We conclude that surface proteolysis by low concentrations of elastase can expose fibrinogen-binding sites associated with GPIIb and GPIIIa on the platelet surface, resulting in spontaneous aggregation upon the addition of fibrinogen. These findings may be relevant to hemostatic changes observed in patients with increased levels of circulating elastase.

The intact human fibroblast has been used in clinical and basic research studies of receptor-mediated control of cell function, however there is little information about the relationship between muscarinic receptor density and the regulation of cyclic AMP (cAMP)

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