Abstract
Reticulocyte-type 15-lipoxygenase is known to dioxygenate phospholipids without preceding action of phospholipases A 2 (PLA 2). Therefore we studied the reaction of the secretory PLA 2s (sPLA 2) from pancreas and snake venom, and of the human cytosolic PLA 2 (cPLA 2) with 1-palmitoyl-2-arachidonoyl phosphatidylcholine (PAPC) and their 15-lipoxygenated species (PAPC-OOH and PAPC-OH) either alone or as equimolar mixtures. These PLA 2s cleaved PAPC-O(O)H with higher (sPLA 2) or similar rates (cPLA 2) as compared with native PAPC. In mixtures, however, PAPC proved to be the preferred, albeit not exclusive substrate for all three PLA 2s. Thus, partial 15-lipoxygenation of phospholipids may also trigger liberation of arachidonic acid.
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