Protein kinase A modulates Ca(2+)- and protein kinase C-dependent amylase release in permeabilized rat pancreatic acini.
Protein kinase A modulates Ca(2+)- and protein kinase C-dependent amylase release in permeabilized rat pancreatic acini.
复制标题
蛋白激酶 A 调节透化大鼠胰腺腺泡中 Ca(2 ) 和蛋白激酶 C 依赖性淀粉酶的释放。
DOI：
10.1042/bj2870403
复制
发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Jamieson,JD
中科院分区：
文献类型：
--
作者：
O'Sullivan,AJ;Jamieson,JD
本文研究了蛋白激酶A（PKA）在透化胰腺腺泡释放淀粉酶中的作用。向透性化腺泡中加入环腺苷酸（cAMP）可增强Ca（2+）依赖性淀粉酶的释放，使Ca（2+）剂量/反应曲线左移。与蛋白激酶C（PKC）激活一样，这是由于主动放电时间的增加。cAMP的作用被PKA的两种抑制剂H89和PKI-（5-24）-肽阻断。在低浓度下，cAMP与佛波醇12-肉豆蔻酸酯13-乙酸酯（PMA）协同作用，而在最佳浓度下，cAMP和PMA是相加的。PKA和PKC似乎通过相似但不相同的机制起作用。
The role of protein kinase A (PKA) in the release of amylase from permeabilized pancreatic acini was investigated. Addition of cyclic AMP (cAMP) to permeabilized acini resulted in a potentiation of Ca(2+)-dependent amylase release, shifting the Ca2+ dose/response curve leftwards. As with protein kinase C (PKC) activation, this is due to an increase in the time of active discharge. The effect of cAMP was shown to be blocked by two inhibitors of PKA, H89 and the PKI-(5-24)-peptide. At low concentration, cAMP synergizes from phorbol 12-myristate 13-acetate (PMA), while at optimal concentrations cAMP and PMA are additive. PKA and PKC appear to work via similar, but not identical mechanisms.