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Biochim Biophys Acta. 1982 Jul 20;712(1):177-85.

Dexamethasone-induced inhibition of prostaglandin production dose not result from a direct action on phospholipase activities but is mediated through a steroid-inducible factor.


Investigations were carried out to define the mechanisms of steroid-induced inhibition of prostaglandin secretion by rat renomedullary cells in tissue culture. Although it was strongly proposed that glucocorticoids may inhibit phospholipase A2 activity, we present several pieces of evidence against a direct action of dexamethasone on phospholipase activities. First, dexamethasone, which significantly decreases the release of labeled material from cells prelabeled with [3H]arachidonate, does not significantly alter the pattern of distribution of the radioactivity among the various classes of cell lipids. In addition, direct measurement of phospholipase A3 activity in dexamethasone-treated cells failed to show any significant decrease in the deacylation capacity. On the other hand, several indications suggest that dexamethasone may induce the secretion of a non-dialysable, transferable factor able to inhibit prostaglandin production, the mechanism of which remains to be investigated.

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