Interactions of intracellular messengers of amylase secretion in pancreatic acini

为探讨胰腺腺泡细胞内淀粉酶分泌信使在刺激-分泌偶联中的相互作用，我们研究了A23187、TPA、DBcAMP对胰腺腺泡细胞淀粉酶分泌的影响。这些实验表明，钙离子在细胞内介质的相互作用中起着至关重要的作用。然后，我们研究了钙调蛋白抑制剂W7和钙调素非依赖性蛋白激酶II的特异性抑制剂KN62对淀粉酶分泌的影响，以探讨钙调蛋白和钙调蛋白依赖性蛋白激酶在钙调蛋白依赖性淀粉酶分泌中的作用。W7和KN62抑制CCK刺激的淀粉酶分泌。W7和KN62不抑制A23187或TPA刺激的淀粉酶分泌，但抑制A23187和TPA的协同分泌。W7和KM62对通透性腺泡分泌依赖于Ca^-lt；2&gt；的淀粉酶没有影响，但抑制了GTPyS、TPA或cAMP对依赖于Ca^-lt；2&gt；的淀粉酶的分泌。这些数据表明，钙调蛋白在依赖钙离子的胰腺腺泡细胞淀粉酶的分泌以及钙离子与其他细胞内信使的相互作用中起着重要作用。

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.