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Salubrinal attenuates β-amyloid-induced neuronal death and microglial activation by inhibition of the NF-κB pathway.

Abstract：

:Alzheimer's disease (AD) is characterized by the deposition of β-amyloid (Aβ) peptides in the brain, inducing neuronal cell death and microglial activation. Endoplasmic reticulum (ER) stress has been proposed to be a mediator of Aβ neurotoxicity. In this study, we test whether salubrinal, an ER stress inhibitor, can protect against Aβ-mediated neurotoxicity. We show in rat primary cortical neurons and mouse microglial BV-2 cells that short-term treatment with salubrinal attenuates Aβ-induced neuronal death and microglial activation. Remarkably, our results show that salubrinal's neuroprotective effects are not due to inhibition of ER stress. Rather, we demonstrate that salubrinal exerts its effects through the inhibition of IκB kinase (IKK) activation, IκB degradation, and the subsequent nuclear factor-kappa B (NF-κB) activation. These results elucidate inhibition of the NF-κB pathway as a new mechanism responsible for the protective effects of salubrinal against Aβ neurotoxicity. This study also suggests that modulation of Aβ-induced NF-κB activation could be a potential therapeutic strategy for Alzheimer's disease.

journal_name

Neurobiol Aging

journal_title

Neurobiology of aging

authors

Huang X,Chen Y,Zhang H,Ma Q,Zhang YW,Xu H

doi

10.1016/j.neurobiolaging.2011.10.007

subject

Has Abstract

pub_date

2012-05-01 00:00:00

pages

1007.e9-17

issue

5

eissn

0197-4580

issn

1558-1497

pii

S0197-4580(11)00401-5

journal_volume

33

pub_type

杂志文章

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