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Activation of protein kinase C by a tumor-promoting phorbol ester in pancreatic islets

par Hubinont, Corinne ;Best, Leonard;Sener, Abdullah ;Malaisse, Willy
Référence FEBS letters, 170, 2, page (247-253)
Publication Publié, 1984

Article révisé par les pairs

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Résumé :

Rat pancreatic islet homogenates display protein kinase C activity. This phospholipid-dependent and calcium-sensitive enzyme is activated by diacylglycerol or the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA). In the presence of TPA, the K(a) for Ca2+ is close to 5 μM. TPA does not affect phosphoinositide turnover but stimulates [32P]- and [3H]choline-labelling of phosphatidylcholine in intact islets. Exogenous phospholipase C stimulates insulin release, in a sustained and glucose-independent fashion. The secretory response to phospholipase C persists in media deprived of CaCl2. It is proposed that protein kinase C participates in the coupling of stimulus recognition to insulin release evoked by TPA, phospholipase C and, possibly, those secretatogues causing phosphoinositide breakdown in pancreatic islets.