Abstract

We have studied the effects of the phosphatase inhibitor, okadaic acid, on insulin secretion and protein phosphorylation in intact and electrically permeabilized pancreatic islets. Okadaic acid inhibited glucose-induced insulin secretion from intact islets, although this effect was probably non-specific since similar effects were obtained using 1-nor-okadaone, a virtually inactive analogue of okadaic acid. In permeabilized islets, okadaic acid enhanced basal and cyclic-AMP-induced insulin secretion and protein phosphorylation. These results indicate that protein phosphatases may play a role in the regulation of insulin release.

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