Zurgil N, Zisapel N
FEBS Lett. 1983 Jun 13;156(2):257-61. doi: 10.1016/0014-5793(83)80508-0.
Preincubation of intact fetal rat brain neurons in culture with 32Pi results in the incorporation of 32Pi into about 20 specific proteins. Upon stimulation by electrical field stimulation or by K+-induced depolarization, highly significant calcium-dependent increase in phosphorylation of a protein of app. Mr 43 000 and decrease in phosphorylation of an app. Mr 55 000 protein occur. These changes can be attributed to the entry of Ca2+ into the cellular cytoplasm since they can occur upon selective permeabilization of the cell membrane to Ca2+ by the Ca2+-ionophore A23187 and are not observed upon stimulation of the cells in the presence of the Ca2+ channel blocker D-600. These data suggest that these phosphoproteins may be involved in the regulation of processes underlying neurotransmitter release.
将培养的完整胎鼠脑神经元与³²P预先温育，结果³²P掺入约20种特定蛋白质中。在电场刺激或K⁺诱导的去极化刺激下，表观分子量约为43000的一种蛋白质的磷酸化出现高度显著的钙依赖性增加，而表观分子量约为55000的一种蛋白质的磷酸化则减少。这些变化可归因于Ca²⁺进入细胞质，因为它们可在细胞膜被Ca²⁺离子载体A23187选择性通透以允许Ca²⁺进入时发生，而在存在Ca²⁺通道阻滞剂D - 600的情况下刺激细胞时未观察到这些变化。这些数据表明，这些磷蛋白可能参与神经递质释放相关过程的调节。
