Cahill A L, Perlman R L
Neurochem Res. 1986 Mar;11(3):327-38. doi: 10.1007/BF00965007.
The phosphorylation of proteins in the superior cervical ganglion of the rat was investigated. Ganglia were incubated with 32Pi, and the 32P-labeled proteins in the ganglion were separated by two-dimensional electrophoresis and visualized by autoradiography. Approximately 40 distinct phosphoproteins could be visualized by these methods. The most heavily labeled ganglionic protein was an acidic protein with an Mr of approximately 83,000. Tyrosine hydroxylase was identified as a doublet of two closely-migrating radioactive spots. Treatment of intact ganglia with depolarizing agents, nicotinic and muscarinic agonists, phorbol esters, and agents that increase the content of cyclic adenosine 3':5'-monophosphate in the ganglion stimulated the incorporation of 32Pi into distinct but overlapping groups of phosphoproteins. All of these agents increased the phosphorylation of tyrosine hydroxylase. In contrast, only phorbol esters and muscarinic agonists increased the phosphorylation of the 83,000 ganglionic phosphoprotein. Our data are consistent with the idea that the various classes of agonists may activate distinct protein kinases in the ganglion.
对大鼠颈上神经节中蛋白质的磷酸化进行了研究。将神经节与³²Pᵢ一起孵育，神经节中³²P标记的蛋白质通过二维电泳分离，并通过放射自显影进行可视化。通过这些方法可观察到约40种不同的磷蛋白。标记最重的神经节蛋白是一种Mr约为83,000的酸性蛋白。酪氨酸羟化酶被鉴定为两个迁移紧密的放射性斑点组成的双重峰。用去极化剂、烟碱和毒蕈碱激动剂、佛波酯以及增加神经节中3':5'-环磷酸腺苷含量的试剂处理完整的神经节，可刺激³²Pᵢ掺入不同但有重叠的磷蛋白组中。所有这些试剂均增加了酪氨酸羟化酶的磷酸化。相比之下，只有佛波酯和毒蕈碱激动剂增加了83,000神经节磷蛋白的磷酸化。我们的数据与各类激动剂可能激活神经节中不同蛋白激酶的观点一致。
