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Amyloid-β Oligomers Induce Only Mild Changes to Inhibitory Bouton Dynamics
Author(s) -
Marvin Ruiter,
Christine Lützkendorf,
Jian Liang,
Corette J. Wierenga
Publication year - 2021
Publication title -
journal of alzheimer's disease reports
Language(s) - English
Resource type - Journals
ISSN - 2542-4823
DOI - 10.3233/adr-200291
Subject(s) - inhibitory postsynaptic potential , hippocampal formation , hippocampus , neuroscience , amyloid (mycology) , chemistry , biology , microbiology and biotechnology , inorganic chemistry
The amyloid-β protein precursor is highly expressed in a subset of inhibitory neuron in the hippocampus, and inhibitory neurons have been suggested to play an important role in early Alzheimer’s disease plaque load. Here we investigated bouton dynamics in axons of hippocampal interneurons in two independent amyloidosis models. Short-term (24 h) amyloid-β (Aβ)-oligomer application to organotypic hippocampal slices slightly increased inhibitory bouton dynamics, but bouton density and dynamics were unchanged in hippocampus slices of young-adult AppNL - F - G-mice, in which Aβ levels are chronically elevated. These results indicate that loss or defective adaptation of inhibitory synapses are not a major contribution to Aβ-induced hyperexcitability.

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