Translocation of protein kinase C in rat islets of Langerhans. Effects of a phorbol ester, carbachol and glucose |
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Authors: | S J Persaud P M Jones D Sugden S L Howell |
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Affiliation: | Biomedical Sciences Division, King's College London, Kensington, England. |
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Abstract: | 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. |
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