Amyloid-beta mediates homeostatic synaptic plasticity
The physiological role of the amyloid-precursor protein (APP) is insufficiently understood. Recent work has implicated APP in the regulation of synaptic plasticity. Substantial evidence exists for a role of APP and its secreted ectodomain APPsα in Hebbian plasticity. Here, we addressed the relevance...
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| Main Authors: | , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
June 16, 2021
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| In: |
The journal of neuroscience
Year: 2021, Volume: 41, Issue: 24, Pages: 5157-5172 |
| ISSN: | 1529-2401 |
| DOI: | 10.1523/JNEUROSCI.1820-20.2021 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1523/JNEUROSCI.1820-20.2021 Verlag, lizenzpflichtig, Volltext: https://www.jneurosci.org/content/41/24/5157 
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| Author Notes: | Christos Galanis, Meike Fellenz, Denise Becker, Charlotte Bold, Stefan F. Lichtenthaler, Ulrike C. Müller, Thomas Deller, and Andreas Vlachos |
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| 520 | |a The physiological role of the amyloid-precursor protein (APP) is insufficiently understood. Recent work has implicated APP in the regulation of synaptic plasticity. Substantial evidence exists for a role of APP and its secreted ectodomain APPsα in Hebbian plasticity. Here, we addressed the relevance of APP in homeostatic synaptic plasticity using organotypic tissue cultures prepared from APP−/− mice of both sexes. In the absence of APP, dentate granule cells failed to strengthen their excitatory synapses homeostatically. Homeostatic plasticity is rescued by amyloid-β and not by APPsα, and it is neither observed in APP+/+ tissue treated with β- or γ-secretase inhibitors nor in synaptopodin-deficient cultures lacking the Ca2+-dependent molecular machinery of the spine apparatus. Together, these results suggest a role of APP processing via the amyloidogenic pathway in homeostatic synaptic plasticity, representing a function of relevance for brain physiology as well as for brain states associated with increased amyloid-β levels. | ||
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