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- W2022942510 abstract "The effect of the antiinflammatory agent sulindac sulfide, a sulfated analog of indomethacin and an inhibitor of prostaglandin synthesis in vitro, on the action of partially purified rabbit polymorphonuclear leukocyte phospholipase A2 (EC 3.1.1.4) was examined. Sulindac sulfide produces a dose-dependent inhibition of this phospholipase A2 (I50 = 10 μM) that is still recognizable at 1 μM. This inhibition is of the noncompetitive type with an apparent K of 5 μM and in all aspects examined cannot be distinguished from the effects, recently reported (Kaplan, L., Weiss, J. and Elsbach, P. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 2955–2958), of indomethacin on the enzyme. In contrast, the pharmacologically inactive analogs sulindac sulfoxide and sulindac sulfone are without any inhibitory effect at 100 μM. Other antiinflammatory agents, including the steroids dexamethasone and hydrocortisone hemisuccinate, and the non-steroids acetylsalicyclic acid, sodium salicylate, sulfinpyrazone and quinacrine also do not inhibit the leukocyte phospholipase A2 at concentrations as high as 100 μM. Meclofenamic acid and flufenamic acid are weakly inhibitory (I50 = 100–500 μM). The apparent specificity of the inhibition of leukocyte phospholipase A2 by low concentrations of pharmacologically active analogs of indomethacin supports our contention that this effect may contribute to the effects of these agents on prostaglandin synthesis." @default.
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- W2022942510 title "The antiinflammatory activity of analogs of indomethacin correlates with their inhibitory effects on phospholipase A2 of rabbit polymorphonuclear leukocytes" @default.
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