Interactions of intracellular messengers of amylase secretion in pancreatic acini

点击翻译按钮获取中文摘要

To investigate the interactions of intracellular messengers of amylase secretion in stimulus-secretion coupling in pancreatic acini, we studied the effects of A23187, TPA,dbcAMP on amylase secretion. These experiments reveal that Ca^<2+> plays a crucial role in the interactions of intracellular mediators. Then we studied the effect of W7, a calmodulin inhibitor, and KN62, a specific inhibitor of calmodulindependent protein kinase II, on amylase secretion to investigate the role of calmodulin and calmodulin-dependent kinase in Ca^<2+>-dependent amylase secretion. W7 and KN62 reduced amylase secretion stimulated by CCK. W7 and KN62 did not inhibit amylase secretion stimulated by A23187 or TPA, but reduced a synergistic secretion by both A23187 and TPA. W7 and KM62 had no effects on Ca^<2+>-dependent amylase secretion from permeabilized acini, but inhibited the enhancement of Ca^<2+>-dependent amylase secretion by GTPyS, TPA or cAMP. These data suggest that calmodulin plays an important role in Ca^<2+>-dependent amylase secretion from pancreatic acinar cells and in the interactions between Ca^<2+> and other intracellular messengers.