Key result
Gap junction channel closure by cholinergic stimulation in pancreatic acinar cells is mediated by a G-protein, acting via phosphatidylinositol biphosphate breakdown and protein kinase C activity.
Provides the first evidence suggesting that gap junction channel closure by cholinergic stimulation in pancreatic acinar cells is mediated by a G-protein acting via phosphatidylinositol biphosphate breakdown and protein kinase C activity.
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No immediate clinical implications; leaves open relevance to human pancreatic secretion or disease.
Using the double whole-cell patch-clamp technique, we determined that dialysis of cell pairs by GTP[S] potentiated electrical uncoupling induced by extracellular addition of carbamylcholine (CCh). An inhibitor of diglyceride lipase, RHC 80267, further potentiated CCh/GTP[S]-induced junctional channel closure, probably by accumulation of diacylglycerol. Moreover, the protein kinase C inhibitor polymyxin B completely blocked uncoupling elicited by CCh/GTP[S]. These results provide the first evidence suggesting that gap junction channel closure by cholinergic stimulation is mediated by a G-protein, which acts by increasing phosphatidylinositol biphosphate breakdown and protein kinase C activity.
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Somogyi et al. (1989) studied this question. Carbamylcholine (CCh) and GTP[S] was evaluated on Gap junctional channel closure / electrical uncoupling. Gap junction channel closure by cholinergic stimulation in pancreatic acinar cells is mediated by a G-protein, acting via phosphatidylinositol biphosphate breakdown and protein kinase C activity.
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