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纯胆碱能神经末梢中去极化刺激的蛋白磷酸化

Depolarization-stimulated protein phosphorylation in pure cholinergic nerve endings.

作者信息

Guitart X, Blasi J, Solsona C, Marsal J

机构信息

Departament de Biologia Cel.lular i Anatomia Patològica, Facultat de Medicina, Hospital de Bellvitge, Universitat de Barcelona, Spain.

出版信息

Neurosci Lett. 1988 May 3;87(3):297-301. doi: 10.1016/0304-3940(88)90465-x.

Abstract

Cholinergic synaptosomes obtained from the electric organ of Torpedo marmorata have been used to study chemical stimulation-stimulated protein phosphorylation. Cholinergic synaptosomes were exposed to elevated K+0 concentrations or other chemical depolarizing agents such as gramicidin or secretagogues as the calcium ionophore A23187. During depolarization several synaptosomal proteins increase their state of phosphorylation. This phenomenon depends on the presence of Ca2+ in the external medium. These results suggest that stimulation of protein phosphorylation may be implicated in the acetylcholine release process and could represent a modulation mechanism in the neurotransmitter release machinery at this cholinergic synapse.

摘要

从斑纹电鳐的电器官中获得的胆碱能突触体已被用于研究化学刺激引发的蛋白质磷酸化。胆碱能突触体暴露于升高的K⁺浓度或其他化学去极化剂,如短杆菌肽或作为钙离子载体的A23187等促分泌素中。在去极化过程中,几种突触体蛋白的磷酸化状态增加。这种现象取决于细胞外介质中Ca²⁺的存在。这些结果表明,蛋白质磷酸化的刺激可能与乙酰胆碱释放过程有关,并且可能代表了这种胆碱能突触处神经递质释放机制中的一种调节机制。

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