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Intracellular oligomeric amyloid-beta rapidly regulates GluA1 subunit of AMPA receptor in the hippocampus. | LitMetric

Intracellular oligomeric amyloid-beta rapidly regulates GluA1 subunit of AMPA receptor in the hippocampus.

Sci Rep

1] Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology (LINE) [2] Centre for Synaptic Plasticity, Faculty of Medicine and Dentistry, University of Bristol, Whitson Street, Bristol BS1 3NY, United Kingdom.

Published: June 2015

AI Article Synopsis

Article Abstract

The acute neurotoxicity of oligomeric forms of amyloid-β 1-42 (Aβ) is implicated in the pathogenesis of Alzheimer's disease (AD). However, how these oligomers might first impair neuronal function at the onset of pathology is poorly understood. Here we have examined the underlying toxic effects caused by an increase in levels of intracellular Aβ, an event that could be important during the early stages of the disease. We show that oligomerised Aβ induces a rapid enhancement of AMPA receptor-mediated synaptic transmission (EPSC(A)) when applied intracellularly. This effect is dependent on postsynaptic Ca(2+) and PKA. Knockdown of GluA1, but not GluA2, prevents the effect, as does expression of a S845-phosphomutant of GluA1. Significantly, an inhibitor of Ca(2+)-permeable AMPARs (CP-AMPARs), IEM 1460, reverses the increase in the amplitude of EPSC(A). These results suggest that a primary neuronal response to intracellular Aβ oligomers is the rapid synaptic insertion of CP-AMPARs.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4460729PMC
http://dx.doi.org/10.1038/srep10934DOI Listing

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