Amyloid beta from axons and dendrites reduces local spine number and plasticity
Open accessAbstract
Excessive synaptic loss is thought to be one of the earliest events in Alzheimer's disease. Amyloid beta (Abeta), a peptide secreted in an activity-modulated manner by neurons, has been implicated in the pathogenesis of Alzheimer's disease by removing dendritic spines, sites of excitatory synaptic transmission. However, issues regarding the subcellular source of Abeta, as well as the mechanisms of its production and actions that lead to synaptic loss, remain poorly understood. In rat organotypic slices, we found that acute overproduction of either axonal or dendritic Abeta reduced spine density and plasticity at nearby ( approximately 5-10 mum) dendrites. The production of Abeta and its effects on spines were sensitive to blockade of action potentials or nicotinic receptors; the effects of Abeta (but not its production) were sensitive to NMDA receptor blockade. Notably, only 30-60 min blockade of Abeta overproduction permitted induction of plasticity. Our results indicate that continuous overproduction of Abeta at dendrites or axons acts locally to reduce the number and plasticity of synapses.
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An increase in the levels of Aβ secreted from axons and dendrites decreases spine number significantly in local dendrites.
“Recently, it was demonstrated that an increase in the levels of A secreted from axons and dendrites decreases spine number significantly in local dendrites (Wei et al., 2010).”
From Differential Effects of ApoE Isoforms on Dendritic Spines<i>In Vivo</i>: Linking an Alzheimer's Disease Risk Factor with Synaptic Alterations (2010) · cites this paper as Wei et al., 2010
Both Aβ and tau are released with normal network activity, so each protein most likely serves a physiological purpose.
“Both A and tau are released with normal network activity, so each protein most likely serves a physiological purpose (51,52).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [51]
Soluble oligomers isolated from AD brain inhibit long-term potentiation, enhance long-term depression, and reduce dendritic spine density in rodent hippocampal slice cultures.
“Soluble oligomers isolated from AD brain have been shown to potently inhibit long-term potentiation (LTP), enhance long-term depression (LTD) and reduce dendritic spine density in rodent hippocampal slice cultures”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Wei et al., 2010
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“Recently, it was demonstrated that an increase in the levels of A secreted from axons and dendrites decreases spine number significantly in local dendrites (Wei et al., 2010).”
Background
- Authors
- Wei, W., Nguyen, L. N., Kessels, H. W., Hagiwara, H., Sisodia, S., & Malinow, R.
- Affiliations
- Cold Spring Harbor Laboratory (US)
- University of California San Diego (US)
- University of Chicago (US)
- Corresponding author
- Malinow, Roberto
- Venue
- Nature Neuroscience
- Published
- 2009-12-27
- Volume
- 13
- Issue
- 2
- Pages
- 190-196
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC3310198
- OpenAlex
- W2014739744
- Cited by
- 357
- References
- 50
- Citations by year
- 2026: 12 · 2025: 15 · 2024: 19 · 2023: 16 · 2022: 22 · 2021: 20 · 2020: 24 · 2019: 15 · 2018: 21 · 2017: 17 · 2016: 22 · 2015: 11 · 2014: 28 · 2013: 34 · 2012: 37
- FWCI
- 17.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- National Institute on Aging (R01AG032132)
- National Institute of Mental Health (R01MH049159)
- National Institute of General Medical Sciences (T32GM008444)
- National Institute of Neurological Disorders and Stroke (R01NS032827)
- 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, dendritic spines, spine density, synaptic plasticity, synaptic loss, NMDA receptor, nicotinic acetylcholine receptors, action potential, excitatory synapses
- MeSH terms
- Action Potentials, Animals, Axons, Dendrites, Hippocampus, Neuronal Plasticity, Peptide Fragments, Receptors, Nicotinic, Synapses, Time Factors, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Pyramidal Cells, Dendritic Spines, Rats, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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