THE PHOSPHORYLATION OF PROTEIN KINASE-C AS A POTENTIAL MEASURE OF ACTIVATION
THE PHOSPHORYLATION OF PROTEIN KINASE-C AS A POTENTIAL MEASURE OF ACTIVATION
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DOI：
10.1042/bj2610131
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发表时间：
1989-07-01
影响因子：
4.1
通讯作者：
PARKER, PJ
中科院分区：
文献类型：
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作者：
MITCHELL, FE;MARAIS, RM;PARKER, PJ
作为确定蛋白激酶C在新的生长因子和激素的信号转导中的作用的一种手段，我们研究了表征良好的试剂对蛋白激酶C本身磷酸化状态的影响。这些研究表明，直接刺激蛋白激酶C（佛波酯）或通过磷脂酰肌醇分解（血小板衍生生长因子）间接刺激蛋白激酶C的药物可诱导激酶磷酸化状态的增加。相比之下，表皮生长因子不刺激成纤维细胞中的蛋白激酶C，不增加蛋白激酶C的磷酸化状态，但导致降低。这些数据表明，蛋白激酶C的磷酸化状态是动态控制的，可以用来提供蛋白激酶C激活的证据。
As a means of determining the role of protein kinase C in the signal transduction from novel growth factors and hormones, we investigated the effects of well-characterized agents on the phosphorylation state of protein kinase C itself. These studies show that agents that stimulate protein kinase C either directly (phorbol ester) or indirectly through phosphatidylinositol breakdown (platelet-derived growth factor) induced an increase in the phosphorylation state of the kinase. By contrast, epidermal growth factor, which does not stimulate protein kinase C in fibroblasts, does no increase the phosphorylation state of protein kinase C, but leads to a decrease. The data suggest that the phosphorylation state of protein kinase C is dynamically controlled and can be used to provide evidence of protein kinase C activation.