Possible role of phosphatidylinositol turnover in insulin release from isolated rat pancreatic islets.
We have previously reported occurrence of Ca2+-activated, phospholipid-dependent protein kinase (referred as protein kinase C) in the rat pancreatic islets. It has been suggested that unsaturated diacylglycerol which results from hydrolysis of phosphatidylinositol by phospholipase C-like enzyme activates protein kinase C. Therefore, we studied the effect of exogenous phospholipase C on insulin release from isolated islets of rat pancreas. Bacterial phospholipase C enhanced insulin release induced by glucose in a dose dependent manner. The effect, however, was decreased in the islets pretreated with colchicine. Both phospholipase C and glucose caused an increase in 32p incorporation into phosphatidylinositol. These results indicate that phospholipid metabolism is linked to the insulin release mechanism.
D000818:Animals; D005947:Glucose / Q000494:pharmacology; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism*; D000078790:Insulin Secretion; D007515:Islets of Langerhans / Q000378:metabolism*; D008297:Male; D010716:Phosphatidylinositols / Q000378:metabolism* / Q000502:physiology; D051381:Rats; D011919:Rats, Inbred Strains; D010738:Type C Phospholipases / Q000494:pharmacology
D007328:Insulin; D010716:Phosphatidylinositols; D010738:Type C Phospholipases; D005947:Glucose