SUMO在阿尔茨海默症及其运动干预调节中的作用
张晨斐1,2,赵 娜2,夏 杰2,王 璟2,徐 波1,2*
(1 华东师范大学“青少年健康评价与运动干预”教育部重点实验室,上海 200241;2 华东师范大学体育与健康学院,上海 200241)

摘 要:摘 要:阿尔茨海默症(Alzheimer's diseases, AD) 是一种常见的神经退行性疾病,俗称老年性痴呆。脑内Aβ 过度聚集、Tau蛋白过度磷酸化和神经元凋亡是AD 的主要病理特征。小泛素样修饰蛋白(small ubiquitin-ike modifier, SUMO) 通过与底物蛋白结合参与蛋白质翻译后修饰,已被发现可通过以下方式参与AD 的病理过程,主要有:(1) SUMO 修饰BACE1,促进Aβ 产生;(2) SUMO 修饰Tau 蛋白,促进其磷酸化并抑制其被泛素蛋白酶系统降解;(3) AD 脑内SUMO 化异常导致神经元过度凋亡。运动已被证实可改善AD 病理特征,调节体内SUMO 化水平,这提示运动缓解AD 可能存在SUMO 化机制。现通过综述SUMO与AD,以及运动对SUMO 的影响,阐述SUMO 介导的运动抗AD 的可能机制。

The roles of SUMO in Alzheimer’s disease and regulation of exercise intervention
ZHANG Chen-Fei1,2, ZHAO Na2, XIA Jie2, WANG Jing2, XU Bo1,2*
(1 Key Laboratory of Aolescent Health Assessment and Exercise Interventin, Ministry of Enducation, East China Normal University, Shanghai 200241, China; 2 College of Physical Education and Health, East China Normal University, Shanghai 200241, China)

Abstract: Abstract: Alzheimer’s disease (AD) is a neurodegenerative disease commonly known as dementia, characterized by excessive aggregation of Aβ, hyperphosphorylation of Tau protein and neuronal apoptosis. The small ubiquitinlike modifier (SUMO) is mainly involved in post-translational modification of proteins via binding to the substrate protein. And SUMO proteins are involved in the pathological process of AD in the following ways: (1) SUMO modifies BACE1, promoting Aβ secretion; (2) SUMO modifies Tau, enhancing its phosphorylation and inhibiting its degradation by ubiquitin protease system; (3) aberrant level of SUMOylation in AD leads to excessive neuron apoptosis. In addition, it has widely been demonstrated that exercise can mitigate the symptom of AD and regulate the level of SUMOylation in vivo, which infers to that there may be a SUMOylation mechanism in exerciserelieving AD. Therefore, this article reviews the mechanism of SUMOylation in AD and the effect of exercise on SUMO, aiming to expound the possible mechanism of SUMO-mediated exercise-relieving AD.

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