Arachidonic acid induces phosphorylation of an 18 kDa protein in electrically permeabilised rat islets of Langerhans.

Arachidonic acid (AA) was shown to induce concentration-dependent, calcium-independent, in situ phosphorylation of a protein of approximate molecular weight 18 kDa in electrically permeabilised rat islets of Langerhans. This protein did not appear to be a substrate for protein kinase C (PKC) since stimulation of PKC by 4 beta phorbol myristate acetate (4 beta PMA) did not result in 32P incorporation into an 18 kDa protein, and since AA-induced phosphorylation was observed in islets in which PKC had been down-regulated by prolonged exposure of islets to 4 beta PMA. These results suggest that AA stimulates protein phosphorylation by a mechanism other than PKC activation.