Deacylation of dipalmitoyllecithin by phospholipases A in alveolar macrophages.

Optimal conditions in vitro were established for the assay of phospholipases A of Bacillus Calmette Guerin-induced alveolar macrophages that deacylated dipalmitoyllecithin in the alkaline pH range. Sodium deoxycholate and Ca++ were found to stimulate both phospholipases A1 and A2, whereas sodium dodecylsulfate strongly inhibited both enzyme activities. Other detergents like Triton X-100, Triton WR-1339, and Tween-20 activated phospholipase A1, whereas they had no effect on or slightly inhibited the phospholipase A2 enzyme. These phospholipases preferentially removed palmitic acid regardless of the position of palmitic acid on the phospholipid molecule and were more active on phosphatidylcholines than phosphatidylethanolamines. This suggests a role for macrophage phospholipases A in the clearance of saturated lecithins in the pulmonary surfactant complex.