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

Abstract:

: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 β42 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 Aβ 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.

authors

Maruyama T,Wada H,Abe Y,Niikura T

doi

10.1016/j.bbrc.2018.04.104

subject

Has Abstract

pub_date

2018-06-02 00:00:00

pages

470-475

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)30883-0

journal_volume

500

pub_type

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