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

Takuma Maruyama, Harmony Wada, Yoichiro Abe, Takako Niikura

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)470-475
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume500
Issue number2
DOIs
Publication statusPublished - 2018 Jun 2

Fingerprint

Sumoylation
Astrocytes
Neurons
Alzheimer Disease
Ubiquitin
Brain
Proteins
Bearings (structural)
Ubiquitins
Post Translational Protein Processing
Oligomers
Amyloid
Neurodegenerative Diseases
Hydrogen Peroxide
Lysine
Glutamic Acid

Keywords

  • Alzheimer's disease
  • Amyloid β
  • Glutamate
  • Hydrogen peroxide
  • SUMO

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Alteration of global protein SUMOylation in neurons and astrocytes in response to Alzheimer's disease-associated insults. / Maruyama, Takuma; Wada, Harmony; Abe, Yoichiro; Niikura, Takako.

In: Biochemical and Biophysical Research Communications, Vol. 500, No. 2, 02.06.2018, p. 470-475.

Research output: Contribution to journalArticle

@article{5fd3fcff86ae48c9830ecc9aae22e127,
title = "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.",
keywords = "Alzheimer's disease, Amyloid β, Glutamate, Hydrogen peroxide, SUMO",
author = "Takuma Maruyama and Harmony Wada and Yoichiro Abe and Takako Niikura",
year = "2018",
month = "6",
day = "2",
doi = "10.1016/j.bbrc.2018.04.104",
language = "English",
volume = "500",
pages = "470--475",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Alteration of global protein SUMOylation in neurons and astrocytes in response to Alzheimer's disease-associated insults

AU - Maruyama, Takuma

AU - Wada, Harmony

AU - Abe, Yoichiro

AU - Niikura, Takako

PY - 2018/6/2

Y1 - 2018/6/2

N2 - 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.

AB - 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.

KW - Alzheimer's disease

KW - Amyloid β

KW - Glutamate

KW - Hydrogen peroxide

KW - SUMO

UR - http://www.scopus.com/inward/record.url?scp=85045703911&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85045703911&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2018.04.104

DO - 10.1016/j.bbrc.2018.04.104

M3 - Article

VL - 500

SP - 470

EP - 475

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -