中文摘要：

目的 探讨JNK／p38MAPK在p淀粉样蛋白多肽片段25-35（Aβ25-35）诱导的阿尔茨海默病（AD）样胎鼠皮层神经元Tau蛋白过度磷酸化中的作用。方法 应用蛋白免疫印迹和免疫细胞化学染色的方法，观察Tau蛋白磷酸化和JNK／p38丝裂原活化的蛋白激酶（JNK／p38MAPK）的表达情况。结果凝聚态Aβ25-35（20μmol／L）作用于皮层神经元12h，Tau蛋白sep396、Ser199/202、Thr205位点的磷酸化水平明显增高，同时JNK／p38MAPK的总量及其活性形式．磷酸化JNK／p38MAPK的蛋白表达水平也增加。结论 Aβ25-35可通过激活JNK／p38MAPK使Tau蛋白的磷酸化水平增高。

英文摘要：

Objective To investigate the effect and the molecular mechanism of aggregated beta-amyloid peptide 25-35 （Aβ25-35） on the level of Tau protein phosphorylation in rat embryo cortical neurons. Methods Western blotting and immunocytochemical stain were performed to observe the Tau protein phosphorylation and the expression of JNK/p38 MAPK. Results The level of Tau protein phosphorylation in the sites of Ser396 , Ser199/202 and Thr205 increased after Aβ25-35 of 20μmol/L was exposed to cortical neurons, meanwhile the level of JNK/p38 MAPK also increased after treatment with Aβ25-35 for 12 hours. Pretreatment with specific inhibitor of JNK/p38 MAPK markedly attenuated Tau protein hyperphosphorylation and the expression of JNK/p38 MAPK. Conclusion JNK/p38 MAPK activated by Aβ25-35 may lead to Tau phosphorylafion.