| First Author | Maruyama T | Year | 2018 |
| Journal | Biochem Biophys Res Commun | Volume | 500 |
| Issue | 2 | Pages | 470-475 |
| PubMed ID | 29660340 | Mgi Jnum | J:273337 |
| Mgi Id | MGI:6280900 | Doi | 10.1016/j.bbrc.2018.04.104 |
| Citation | Maruyama T, et al. (2018) Alteration of global protein SUMOylation in neurons and astrocytes in response to Alzheimer's disease-associated insults. Biochem Biophys Res Commun 500(2):470-475 |
| abstractText | 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 beta42 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 Abeta 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. |
