Translocation of protein kinase C in rat islets of Langerhans. Effects of a phorbol ester, carbachol and glucose.

In unstimulated rat islets (2 mM glucose), most of the ion-exchange purified protein kinase C (PKC) activity was associated with the cytosolic fraction. Both carbachol and phorbol myristate acetate caused a significant translocation of PKC activity from cytosolic to membrane fractions, but under the same conditions, glucose (20 mM) did not cause such a redistribution of PKC activity. PMA-induced translocation of PKC to the membrane fraction was also observed in electrically permeabilised islets, in which recovery of the enzyme activity was enhanced by buffering the intracellular Ca2+ concentration to 50 nM and supplying the permeabilised islets with protease inhibitors.