Phospholipase A2 activity in carrageenin-induced inflammatory tissue of rats.

Phospholipase A2 activity was detected in 7-day-old carrageenin-induced inflammatory tissue of rats using a synthetic substrate. 1-acyl-2-[3H]arachidonyl-phosphatidylcholine. The inflammatory tissue was homogenized in saline containing 1 M KCl, and the 105,000 g supernatant fraction was placed on a Sephadex G-100 column. The partially purified phospholipase A2 had a pH optimum at 6-7 and was Ca2+ dependent. p-Bromophenacyl bromide was strongly inhibitory to the partially purified phospholipase A2 (IC50 = 1.44 x 10(-5) M). A moderate inhibition was observed with indomethacin. Cycloheximide and dexamethasone, which inhibit prostaglandin production in inflammatory tissue, exerted no direct inhibitory action on the phospholipase A2. There were no direct inhibitory effects of quinacrine, bradykinin, or actinomycin D. The cell-free supernatant fraction of the inflammatory exudate of 7-day-old carrageenin-induced granulation tissue was found to have no phospholipase A2 activity.