Alteration of global protein SUMOylation in neurons and astrocytes in response to Alzheimer's disease-associated insults

被引:11
作者
Maruyama, Takuma [1 ]
Wada, Harmony [1 ]
Abe, Yoichiro [2 ]
Niikura, Takako [1 ]
机构
[1] Sophia Univ, Dept Informat & Commun Sci, Fac Sci & Technol, Tokyo, Japan
[2] Keio Univ, Dept Pharmacol, Sch Med, Tokyo, Japan
关键词
SUMO; Alzheimer's disease; Amyloid beta; Hydrogen peroxide; Glutamate; AMYLOID-BETA OLIGOMERS; OXIDATIVE STRESS; TOXICITY; CONJUGATION; ACTIVATION; RELEASE; SUMO;
D O I
10.1016/j.bbrc.2018.04.104
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
SUMOylation, a post-translational modification of lysine residues by small ubiquitin-like modifier (SUMO) proteins, has been implicated in the pathogenesis of neurodegenerative disorders including Alzheimer's disease (AD), and in neuron- and astrocyte-specific physiological functions. Global SUMOylation is increased in the AD mouse brain in the pre-plaque-forming stage but returns to wild type levels in the plaque-bearing stage. To clarify the reason for the transient change in SUMOylation, we analyzed the alteration of global SUMOylation induced by AD-associated cytotoxic stimuli in neurons and astrocytes individually. In neurons, amyloid beta 42 oligomers induced some but not significant increase in levels of SUMO1-modified proteins. Both hydrogen peroxide and glutamate significantly reduced SUMO1-modified protein levels. These changes were more prominent in neurons than in astrocytes. The opposite effect of A beta and oxidative/excitotoxic stimuli on SUMO1 modification may cause the pathological stage-associated change in the level of SUMO-modified proteins in the AD mouse brain. (C) 2018 Elsevier Inc. All rights reserved.
引用
收藏
页码:470 / 475
页数:6
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