Study of neurofilament phosphorylation in long-term potentiation of hlppocampus

点击翻译按钮获取中文摘要

Long-term potentiation (LTP) is a cellular model of neuronal plasticity that is thought to involve the phosphorylation of various proteins. NF-L is considered a possible substrate for phosphorylation. First, we prepared site-specific phosphorylation-dependent antibodies (abNFL26) against the phosphorylation site Ser-26 of Rho-kinase. The in vitro specificity of those antibodies were appreciated by dot and western blot analyses. During LTP stimulation of mouse hippocampal slices, the series of the site-specific phosphorylation-dependent antibodies against the phosphorylation sites, Ser-26, -51, -55, -57, demonstrates the increase in the phosphorylation level of Ser57 in NF-L, and the visualization of the localized distribution of Ser57 phosphorylation in a subpopulation of apical dendrites of the pyramidal neurons. Furthermore, Ser57 phosphorylation during LTP is suggested to be mediated by CaMKII.We show that NF-L is phosphorylated by CaMKII in a subpopulation of the apical dendrites during LTP, indicating that Ser57 is a novel phosphorylation site of NF-L in vivo related to the neuronal signal transduction. And these data implies that the phosphorylation of NF-L by CaMKII might be influenced, resulting in memory dysfuctions.