Yoshida K, Imaki J, Matsuda H, Hagiwara M
Department of Ophthalmology, Hokkaido University School of Medicine, Sapporo, Japan.
J Neurochem. 1995 Oct;65(4):1499-504. doi: 10.1046/j.1471-4159.1995.65041499.x.
The signal pathway for light-induced expression of c-fos and the neuropeptide somatostatin (SS) in rat retinal cells was investigated. Flashing light induced c-fos and SS mRNA in the inner nuclear layer and the ganglion cell layer. As both c-fos and SS genes have a cyclic AMP response element (CRE) in their promoters, CRE-binding protein (CREB) phosphorylation in retinal cells was examined with a phospho-CREB-specific antibody. Both flashing light and administration of the L-type Ca2+ channel activator Bay K 8644 induced phosphorylation of CREB in the nuclei of the amacrine cells and the ganglion cells where c-fos/SS mRNAs were expressed. These cells could be double-stained with anti-calmodulin kinase II (anti-CaM kinase II) monoclonal antibody and phospho-CREB-specific polyclonal antiserum after Bay K 8644 administration, indicating the colocalization of phosphorylated CREB at Ser133 and CaM kinase II in the neural retina.
研究了大鼠视网膜细胞中光诱导c-fos和神经肽生长抑素(SS)表达的信号通路。闪光在内核层和神经节细胞层诱导了c-fos和SS mRNA。由于c-fos和SS基因在其启动子中都有一个环磷酸腺苷反应元件(CRE),因此用磷酸化CREB特异性抗体检测了视网膜细胞中CRE结合蛋白(CREB)的磷酸化。闪光和施用L型Ca2+通道激活剂Bay K 8644均诱导了表达c-fos/SS mRNA的无长突细胞和神经节细胞核中CREB的磷酸化。施用Bay K 8644后,这些细胞可用抗钙调蛋白激酶II(抗CaM激酶II)单克隆抗体和磷酸化CREB特异性多克隆抗血清进行双重染色,表明在神经视网膜中Ser133处磷酸化的CREB与CaM激酶II共定位。