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自噬与β-淀粉样蛋白及Tau蛋白关系的研究进展
作者:彭翊倩  顾倩影  吕海芹 
单位:东南大学 医学院, 江苏 南京 210009
关键词:自噬 阿尔茨海默病 β-淀粉样蛋白 Tau蛋白 文献综述 
分类号:Q255;R749.16
出版年·卷·期(页码):2019·38·第三期(522-527)
摘要:

自噬是真核细胞通过溶酶体降解受损或异常折叠的蛋白质及衰老细胞器的重要途径,是细胞对抗退化、维持自身稳态和正常功能的保护性因素。自噬既负责清除及调节β-淀粉样蛋白(Aβ)和Tau蛋白,又受Aβ和过度磷酸化的Tau蛋白的影响。阿尔茨海默病(AD)患者的自噬功能异常,Aβ和Tau蛋白清除障碍,形成大量异常Tau蛋白和错误折叠的Aβ蛋白;Aβ和Tau蛋白相互协同,干扰自噬溶酶体的形成,导致轴突远端自噬体聚集、突触丢失、神经元凋亡及认知功能障碍。作者就自噬与Aβ及Tau蛋白关系的研究进展进行综述,以期有助于进一步了解AD的发病机制及发现新的防治药物靶点。

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