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Highly purified Ca2+-dependent phospholipases A2 that were isolated from human platelets, rabbit alveolar macrophages and peritoneal polymorphonuclear leucocytes and were active in the neutral-to-alkaline pH range were inhibited 50% by 75 microM-indomethacin in the presence of 5.0 mM added Ca2+. Sodium meclofenamate and sodium flufenamate were also inhibitory; the sensitivity to inhibition was a function of Ca2+ concentration. The dose for 50% inhibition (ID50) with meclofenamate was 0.4 mM in the presence of 2.5 mM added Ca2+, but 50nM in the presence of 0.5 mM added Ca2+. Thus, inhibition of phospholipase A2 activity by non-steroidal anti-inflammatory agents via Ca2+ antagonism may significantly contribute to the mechanism of drug action.

Inhibition of highly purified mammalian phospholipases A2 by non-steroidal anti-inflammatory agents. Modulation by calcium ions