Bradykinin-increased phospholipid deacylation-reacylation in rat renal medulla is inhibited by dBc AMP.

The effect of bradykinin on the mobilization of arachidonic acid was analyzed separately by acylation and degradation. Acylating activity was determined by the incorporation of [14C]arachidonic acid into the phospholipids at different times. Different concentrations of bradykinin had no effect on the phospholipid acylating activities. The degradation of the phospholipids was performed on renal medullary slices prelabeled with [14C]arachidonic acid. Treatment with bradykinin produced an initial degradation of phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol, with a concomitant increase in lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylinositol within 5 min of incubation. Phosphatidylcholine-, phosphatidylethanolamine- and phosphatidylinositol increased thereafter and reached the control values after 10 min of incubation. After 30 min, incubation of prelabeled slices with bradykinin produced a significant concentration-dependent increase in the phospholipid-labeling by reutilization of [14C]arachidonic acid. The effect of bradykinin on the phospholipid-labeling was blocked by preincubation with increasing concentrations of dBc AMP. Mepacrine also blocked the bradykinin stimulation in phosphatidylcholine and phosphatidylethanolamine, but had no effect on bradykinin-induced changes in the phosphatidylinositol arachidonic acid moiety.