钙依赖性4-氨基吡啶对鱿鱼视叶突触体中蛋白质磷酸化的刺激作用。
Calcium-dependent 4-aminopyridine stimulation of protein phosphorylation in squid optic lobe synaptosomes.
作者信息
Pant H C, Gallant P E, Cohen R, Neary J T, Gainer H
出版信息
Cell Mol Neurobiol. 1983 Sep;3(3):223-38. doi: 10.1007/BF00710949.
Abstract
When intact synaptosomes were incubated with [gamma-32P]ATP, maximal protein phosphorylation was attained 2 min after the start of incubation. Protein phosphorylation under basal conditions was dependent on external Ca2+, and the dominant peak of phosphorylation was a 50-kd protein. Incubation of intact synaptosomes in the presence of 3-6 mM 4-aminopyridine (4-AP) caused a markedly enhanced phosphorylation of high molecular weight proteins of 90, 100, 130, and 180 kd, with no increase in the 50 or 38 kd proteins. This effect of 4-AP was dependent on external calcium ions in the incubation medium. The 4-AP effect on the high molecular weight proteins was also found in synaptosomal plasma membranes isolated from the synaptosomes. Tetraethylammonium (TEA) ions did not produce this enhancement of phosphorylation.
摘要
当完整的突触体与[γ-32P]ATP一起孵育时，孵育开始2分钟后可达到最大蛋白质磷酸化。基础条件下的蛋白质磷酸化依赖于细胞外Ca2+，磷酸化的主要峰值是一种50-kd的蛋白质。在3-6 mM 4-氨基吡啶（4-AP）存在的情况下孵育完整的突触体，会导致90、100、130和180 kd的高分子量蛋白质的磷酸化显著增强，而50或38 kd的蛋白质没有增加。4-AP的这种作用依赖于孵育培养基中的细胞外钙离子。在从突触体分离的突触体质膜中也发现了4-AP对高分子量蛋白质的作用。四乙铵（TEA）离子不会产生这种磷酸化增强作用。
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