Soulié C, Lépagnol J, Delacourte A, Caillet-Boudin M L
INSERM U 422, Lille, France.
Neurosci Lett. 1996 Mar 15;206(2-3):189-92. doi: 10.1016/s0304-3940(96)12472-1.
Recent data have shown that the microtubule-associated Tau proteins are phosphorylated but to a lesser extent than PHF-Tau proteins which are the major components of Alzheimer's disease paired helical filaments. These normal Tau proteins are highly sensitive to the endogenous phosphatase activity during post-mortem delay. In order to understand the basic equilibrium between phosphatase and kinase activities, phosphorylation and dephosphorylation mechanisms of Tau proteins were studied in neuroblastoma cells. The present results demonstrate that an endogenous phosphatase activity is present and directed on Tau proteins in the SKNSH-SY 5Y cell extracts. Interestingly, the okadaic acid-induced hyperphosphorylated Tau proteins are more resistant to the phosphatase activity than the control Tau proteins. Our data emphasize the value of this in vitro cellular model for the study of biological conditions that control Tau protein phosphorylation levels.
最近的数据表明，与微管相关的Tau蛋白发生了磷酸化，但程度低于阿尔茨海默病成对螺旋丝的主要成分PHF-Tau蛋白。这些正常的Tau蛋白在死后延迟期间对内源性磷酸酶活性高度敏感。为了理解磷酸酶和激酶活性之间的基本平衡，在神经母细胞瘤细胞中研究了Tau蛋白的磷酸化和去磷酸化机制。目前的结果表明，SKNSH-SY 5Y细胞提取物中存在针对Tau蛋白的内源性磷酸酶活性。有趣的是，冈田酸诱导的过度磷酸化Tau蛋白比对照Tau蛋白对磷酸酶活性更具抗性。我们的数据强调了这种体外细胞模型在研究控制Tau蛋白磷酸化水平的生物学条件方面的价值。
