【摘要】 目的探讨JNK/p38 MAPK在β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/p38 MAPK)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Ser396、Ser199/202、Thr205位点的磷酸化水平明显增高,同时JNK/p38 MAPK的总量及其活性形式-磷酸化JNK/p38 MAPK的蛋白表达水平也增加。结论Aβ25~35可通过激活JNK/p38 MAPK使Tau蛋白的磷酸化水平增高。更多还原

【Abstract】 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 phosphorylation.更多还原