Nestler E J, Greengard P
Proc Natl Acad Sci U S A. 1980 Dec;77(12):7479-83. doi: 10.1073/pnas.77.12.7479.
The regulation of the state of phosphorylation of protein I, a specific neuronal protein that appears to be associated predominantly with synaptic vesicles, has been studied in intact sections of bovine superior cervical ganglion. For this purpose, a technique was developed that made possible the quantitation of the state of phosphorylation of as little as 5 fmol of protein I. Incubation of ganglion sections in the presence of dopamine, 8-bromo-cyclic AMP, or depolarizing agents (i.e., high K+ concentration or veratridine) increased the state of phosphorylation of protein I relative to that of control ganglion sections. Other results indicated that the effect of dopamine is probably mediated via the activation of a cyclic AMP-dependent protein kinase and that the effect of high K+ concentration is probably mediated via the activation of a calcium-dependent protein kinase.
蛋白I是一种特定的神经元蛋白,似乎主要与突触小泡相关,其磷酸化状态的调节已在牛颈上神经节的完整切片中进行了研究。为此,开发了一种技术,该技术能够对低至5飞摩尔的蛋白I的磷酸化状态进行定量。在多巴胺、8-溴环磷酸腺苷或去极化剂(即高钾浓度或藜芦碱)存在的情况下孵育神经节切片,相对于对照神经节切片,蛋白I的磷酸化状态增加。其他结果表明,多巴胺的作用可能是通过激活环磷酸腺苷依赖性蛋白激酶介导的,高钾浓度的作用可能是通过激活钙依赖性蛋白激酶介导的。