Abstract
The role of phospholipase A 2 (PLA 2) in the formation of platelet-activating factor (PAF-acether) by rabbit platelets is supported by several pieces of evidence. First, the release of PAF-acether was accompanied by that of its deacetylated analog, lyso-PAF-acether. Second, EDTA, EGTA, db-AMPc, p′-bromophenacylbromide and 874 CB, which, in spite of their structural diversity, are all PLA 2 blockers, inhibited the release of both PAF-acether and of the lyso-compound. Third, addition of hog pancreas PLA 2 to platelets as well as platelet lysis resulted in the release of lyso-PAF-acether, thus mimicking the metabolic events initiating formation of PAF-acether. These results indicate that PLA 2 activation triggers both the second and the third pathway of platelet activation.
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