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Glycerophospholipids are major components of cell membranes and have enormous variation in the composition of fatty acyl chains esterified on the sn-1 and sn-2 position as well as the polar head groups on the sn-3 position of the glycerol backbone. Phospholipase A₂ (PLA₂) enzymes constitute a superfamily of enzymes which play a critical role in metabolism and signal transduction by hydrolyzing the sn-2 acyl chains of glycerophospholipids. In human cell membranes, in addition to the conventional diester phospholipids, a significant amount is the sn-1 ether-linked phospholipids which play a critical role in numerous biological activities. However, precisely how PLA₂s distinguish the sn-1 acyl chain linkage are not understood. In the present study, we expanded the technique of lipidomics to determine the unique in vitro specificity of three major human PLA₂s, including Group IVA cytosolic cPLA₂, Group VIA …