| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1992: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1991: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Research Abstract |
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.
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