Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini.
Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini.
复制标题
蛋白激酶 C 的激活并不是透化大鼠胰腺腺泡释放淀粉酶的绝对必要条件。
DOI：
10.1042/bj2850597
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
本文观察了蛋白激酶C（PKC）对大鼠胰腺腺泡释放淀粉酶的影响。加入佛波醇12-肉豆蔻酸酯13-乙酸酯（PMA）的透性细胞加强钙（2+）刺激的释放，但在非刺激钙浓度的放电没有影响。PMA通过增加透化细胞释放淀粉酶的时间，使淀粉酶的Ca（2+）浓度依赖性放电明显向左移动。此作用可被星形孢菌素和PKC-19-31-酰胺肽抑制剂抑制，表明PMA的作用是由于其对PKC的作用。Staurosporine也部分抑制淀粉酶释放的最佳浓度的Ca 2+，这种效果是不复制的更具体的PKC-19-31-酰胺肽抑制剂，可能是由于对另一个第二信使系统的影响。PKC似乎是胰腺腺泡释放的重要调节因子，但其激活不是Ca（2+）依赖性淀粉酶释放的绝对要求。
The effect of protein kinase C (PKC) on amylase discharge from streptolysin-O-permeabilized rat pancreatic acini was investigated. Addition of phorbol 12-myristate 13-acetate (PMA) to permeabilized cells potentiated Ca(2+)-stimulated release, but had no effect on discharge at non-stimulatory Ca2+ concentrations. PMA markedly shifted the Ca(2+)-concentration-dependence of amylase discharge to the left, by enhancing the time over which the permeabilized cells release. This effect was inhibited by both staurosporine and PKC-19-31-amide peptide inhibitor, indicating that the effect of PMA was due to its action on PKC. Staurosporine also partially inhibited amylase release at the optimal concentration of Ca2+; this effect was not replicated by the more specific PKC-19-31-amide peptide inhibitor and may be due to an effect on another second-messenger system. PKC appears to be an important modulator of release in pancreatic acini, but its activation is not an absolute requirement for Ca(2+)-dependent amylase discharge.