Inhibition of calcium flux and calcium channel antagonist binding in the PC12 neural cell line by phorbol esters and protein kinase C.
Inhibition of calcium flux and calcium channel antagonist binding in the PC12 neural cell line by phorbol esters and protein kinase C.
复制标题
佛波酯和蛋白激酶 C 抑制 PC12 神经细胞系中的钙流和钙通道拮抗剂结合。
DOI：
10.1016/0006-291x(86)90439-0
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发表时间：
1986
影响因子：
3.1
通讯作者：
Greenberg,DA
中科院分区：
文献类型：
--
作者：
Messing,RO;Carpenter,CL;Greenberg,DA
Ca2+和磷脂依赖性蛋白激酶（蛋白激酶C）已被证明可以改变多种细胞中受体介导的Ca2+反应。为了评估其在调节电压依赖性Ca2+反应中的可能作用，我们研究了肿瘤促进肽酯（激活蛋白激酶C）对PC12神经细胞系Ca2+通道功能的影响。Phorbol 12-肉豆蔻酸酯13-乙酸降低了K+-去极化引起的45ca摄取，并降低了Ca2+通道拮抗剂[3H](+)PN200-110与完整细胞的结合。结合抑制在PC12膜上明显降低，但通过重组具有蛋白激酶C活性的膜而恢复。因此，蛋白激酶C可能参与哺乳动物神经细胞中电压依赖性Ca2+通道的内源性调节。
Ca2+- and phospholipid-dependent protein kinase (protein kinase C) has been shown to modify receptor-mediated Ca2+responses in a variety of cells. To assess its possible role in modulating voltage-dependent Ca2+responses, we examined the effect of tumor-promoting phorbol esters, which activate protein kinase C, on Ca2+channel function in the PC12 neural cell line. Phorbol 12-myristate 13-acetate reduced K+-depolarization-evoked45Ca uptake and decreased binding of the Ca2+channel antagonist [3H](+)PN200-110 to intact cells. Inhibition of binding was markedly reduced in PC12 membranes, but was restored by reconstituting membranes with protein kinase C activity. Protein kinase C may therefore participate in endogenous regulation of voltage-dependent Ca2+channels in mammalian neural cells.