A vicious cycle of β amyloid−dependent neuronal hyperactivation
Open accessAbstract
β-amyloid (Aβ)-dependent neuronal hyperactivity is believed to contribute to the circuit dysfunction that characterizes the early stages of Alzheimer's disease (AD). Although experimental evidence in support of this hypothesis continues to accrue, the underlying pathological mechanisms are not well understood. In this experiment, we used mouse models of Aβ-amyloidosis to show that hyperactivation is initiated by the suppression of glutamate reuptake. Hyperactivity occurred in neurons with preexisting baseline activity, whereas inactive neurons were generally resistant to Aβ-mediated hyperactivation. Aβ-containing AD brain extracts and purified Aβ dimers were able to sustain this vicious cycle. Our findings suggest a cellular mechanism of Aβ-dependent neuronal dysfunction that can be active before plaque formation.
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The early abnormal neuronal hyperactivity phenotype in AppNL-G-F mice has been shown to be dependent on soluble amyloid beta.
“which has been shown to be dependent on soluble Aβ [38–40]”
From Selective suppression of oligodendrocyte-derived amyloid beta rescues neuronal dysfunction in Alzheimer’s disease (2024) · cites this paper as [40]
The sections “Neuronal hyperactivity requires pre-existing baseline activity” and “Hyperactivation through an Aβ-dependent block of glutamate reuptake” support a role for soluble Aβ in neuronal hyperactivity. However, the mouse model studied for early hyperactivity was APP23 × PS45, not AppNL-G-F; the source does not establish that dependency in AppNL-G-F mice. Page numbers are unavailable in our copy. (LLM, conf=0.86)
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- Authors
- Zott, B., Simon, M. M., Hong, W., Unger, F., Chen-Engerer, H.-J., Frosch, M. P., Sakmann, B., Walsh, D. M., & Konnerth, A.
- Affiliations
- Munich Cluster for Systems Neurology (DE)
- Brigham and Women's Hospital (US)
- Massachusetts General Hospital (US)
- Technical University of Munich (DE)
- Corresponding author
- Konnerth, Arthur
- ORCID
- Venue
- Science
- Published
- 2019-08-09
- Volume
- 365
- Issue
- 6453
- Pages
- 559-565
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC6690382
- OpenAlex
- W2968840243
- Cited by
- 640
- References
- 48
- Citations by year
- 2026: 72 · 2025: 93 · 2024: 111 · 2023: 92 · 2022: 79 · 2021: 110 · 2020: 61 · 2019: 21 · 2018: 1
- FWCI
- 46.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Open access LMU (Ludwid Maxmilian's Universitat Munchen) (submittedVersion)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- Funders
- National Institutes of Health (AG046275)
- National Institute on Aging (AG005134)
- BrightFocus Foundation (A2013059S)
- Deutsche Forschungsgemeinschaft (SFB 870)
- Gemeinnützige Hertie-Stiftung (Senior Professorship)
- Alzheimer Association (ZEN-18-533290)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Alzheimer's disease, glutamate uptake, glutamate excitotoxicity
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Humans, Neurons, Amyloid beta-Peptides, Long-Term Potentiation, Glutamic Acid, Mice, Protein Multimerization, CA1 Region, Hippocampal, Plaque, Amyloid
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