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Phospholipase inhibitors target enzymes that hydrolyze membrane phospholipids into lipid messengers. Phospholipase A2 (PLA2) enzymes release arachidonic acid, the precursor of prostaglandins and leukotrienes. A cytosolic PLA2 that prefers arachidonic acid was cloned in 1991 and carries a calcium-dependent membrane-binding domain. Phospholipase C (PLC) instead produces inositol trisphosphate and diacylglycerol, two second messengers of receptor signaling. U 73122 was characterized in 1990 as an inhibitor of receptor-coupled, PLC-dependent responses in platelets and neutrophils. D609 is used as an inhibitor of the phosphatidylcholine-specific form of PLC. Varespladib targets secreted PLA2 enzymes, and tanshinone I, a diterpenoid from Salvia miltiorrhiza, is described as a PLA2 inhibitor.
