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Up-regulation of NSP3 by Oligomeric Aβ Accelerates Neuronal Death Through Cas-independent Rap1A Activation.
Neuroscience 2018 August 22
β-Amyloid (Aβ) plays an important role in the early pathogenesis of Alzheimer's disease (AD). In vitro studies have demonstrated that Aβ oligomers induce hippocampal and neocortical neuronal death. However the neurotoxic mechanisms by which soluble Aβ oligomers cause neuronal damage and death remain to be fully elucidated. To this end, we analyzed the gene expression profile of rat cerebral cortical neurons treated with Aβ oligomers in vitro. Aβ treatment induced the expression of novel SH2-containing protein 3 (NSP3), an adaptor molecule interacting with Cas family proteins. NSP3 expression was upregulated not only in oligomeric-Aβ-treated cultured neurons but also in the neocortex of aged Tg2576 mice. NSP3 overexpression in cultured cortical neurons accelerated neuronal death. The C-terminal region of NSP3 unbound to a Cas protein was necessary for the NSP3-induced acceleration of neuronal death, as was Cas-independent Rap1A activation downstream of NSP3. Moreover, NSP3 RNAi knockdown partially rescued Aβ-oligomer-treated neurons. These results indicate that NSP3 upregulation by soluble Aβ oligomers may accelerate neuronal death via Cas-independent Rap1A activation, implicating NSP3 in the pathogenesis of AD.
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