Plasma components are required for platelet activation by the toxin of Loxosceles reclusa.

We have used a partially purified toxin from the venom of the brown recluse spider, Loxosceles reclusa, to study its effects on human platelets isolated from plasma proteins. This toxin, which produced skin necrosis in rabbits, contained sphingomyelinase D activity. The toxin induced platelet aggregation and secretion of [3H]serotonin in human plasma but not in buffer or in human neonate plasma. Ca2+ was required for the interaction of toxin, platelets, and plasma factor(s). The addition of C-reactive protein restored aggregation and serotonin release of platelets incubated in human neonate plasma. The ADP-degrading enzyme, apyrase, and the non-steroidal, anti-inflammatory drug, indomethacin, inhibited platelet aggregation, suggesting that ADP secreted from platelet storage granules and indomethacin-sensitive pathway(s) are involve in the toxin-induced human platelet activation (aggregation and serotonin release). Generation of platelet activating factor (PAF) from the platelet by brown recluse toxin is not likely since the PAF receptor antagonist, BN 52021, did not inhibit platelet aggregation induced by the brown recluse toxin.