蛋白激酶A调节通透化大鼠胰腺腺泡中钙和蛋白激酶C依赖性淀粉酶的释放。
Protein kinase A modulates Ca(2+)- and protein kinase C-dependent amylase release in permeabilized rat pancreatic acini.
作者信息
O'Sullivan A J, Jamieson J D
机构信息
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
出版信息
Biochem J. 1992 Oct 15;287 ( Pt 2)(Pt 2):403-6. doi: 10.1042/bj2870403.
Abstract
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.
摘要
研究了蛋白激酶A（PKA）在通透化胰腺腺泡淀粉酶释放中的作用。向通透化腺泡中添加环磷酸腺苷（cAMP）可增强Ca(2+)依赖性淀粉酶释放，使Ca2+剂量/反应曲线向左移动。与蛋白激酶C（PKC）激活一样，这是由于主动分泌时间增加所致。cAMP的作用被两种PKA抑制剂H89和PKI-(5-24)-肽阻断。在低浓度时，cAMP与佛波醇12-肉豆蔻酸酯13-乙酸酯（PMA）协同作用，而在最佳浓度时，cAMP和PMA具有加和性。PKA和PKC似乎通过相似但不完全相同的机制发挥作用。
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