Inhibition of human platelet function by sulfatides.

Sulfatides are glycolipid constituents of human platelet cell membranes and have been shown to interact with platelet-binding proteins involved in hemostasis. Because little is known about the physiological role of sulfatides in platelet function, the effect of sulfatide on platelet adhesion, aggregation, release, and ristocetin-induced platelet agglutination (RIPA) was studied. These processes are inhibited when exogenous sulfatide is present in vitro. Inhibition of aggregation induced by collagen, thrombin, and ristocetin by sulfatide was dose dependent. Adenosine diphosphate-mediated adhesion and aggregation were not significantly affected by sulfatide, nor was serotonin- and epinephrine-mediated aggregation. Collagen mediate release of serotonin was reduced sulfatide. RIPA demonstrated dose-dependent inhibition in response to sulfatide. These results suggest that sulfatide may play a role in modulating platelet activation.