Robinson P J, Dunkley P R
Neurosci Lett. 1983 Dec 23;43(1):85-90. doi: 10.1016/0304-3940(83)90133-7.
Depolarization of synaptosomes increases the phosphorylation of a number of proteins in a calcium-dependent manner. The concentration of calcium required for optimum stimulation was 0.1 mM, with higher concentrations up to 2.5 mM being progressively less effective. Calcium was significantly better than strontium at increasing depolarization-dependent protein phosphorylation, while barium had no stimulating effect at concentrations above 0.1 mM. The order of potency of these ions is consistent with a calmodulin-stimulated protein kinase being activated on entry of calcium into synaptosomes, but is not consistent with the known efficacy of these ions in stimulating neurotransmitter release. The data show for the first time that phosphorylation of proteins may not be a prerequisite for neurotransmitter release.
突触体的去极化以钙依赖的方式增加多种蛋白质的磷酸化。最佳刺激所需的钙浓度为0.1 mM,浓度高达2.5 mM时效果逐渐降低。在增加依赖去极化的蛋白质磷酸化方面,钙明显优于锶,而钡在浓度高于0.1 mM时没有刺激作用。这些离子的效力顺序与钙调蛋白刺激的蛋白激酶在钙进入突触体时被激活一致,但与这些离子在刺激神经递质释放方面的已知效力不一致。数据首次表明蛋白质磷酸化可能不是神经递质释放的先决条件。