Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Open accessAbstract
Evidence for an ever-expanding variety of molecular mediators of amyloid β-protein neurotoxicity (membrane lipids, receptor proteins, channel proteins, second messengers and related signaling cascades, cytoskeletal proteins, inflammatory mediators, etc.) has led to the notion that the binding of hydrophobic Aβ assemblies to cellular membranes triggers multiple effects affecting diverse pathways. It appears unlikely that there are only one or two cognate receptors for neurotoxic forms of Aβ and also that there are just one or two assembly forms of the peptide that induce neuronal dysfunction. Rather, various soluble (diffusible) oligomers of Aβ that may be in dynamic equilibrium with insoluble, fibrillar deposits (amyloid plaques) and that can bind to different components of neuronal and non-neuronal plasma membranes appear to induce complex patterns of synaptic dysfunction and network disorganization that underlie the intermittent but gradually progressive cognitive manifestations of the clinical disorder. Modern analyses of this problem utilize electrophysiology coupled with synaptic biochemistry and behavioral phenotyping of animal models to elucidate the affected circuits and assess the effects of potential therapeutic interventions.
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Synaptic deficits occur in early Alzheimer's disease and mild cognitively impaired patients before onset of plaques and are some of the first signs of the neuronal degenerative process.
“Synaptic deficits occur in early AD and mild cognitively impaired patients before onset of plaques and are some of the first signs of the neuronal degenerative process (4, 23-25).”
From Complement and microglia mediate early synapse loss in Alzheimer mouse models (2016) · cites this paper as [4]
The “Early versus Late” section links synaptic alterations with cognitive impairment in AD subjects and reports that synaptic deficits precede plaques and substantial neuronal loss in hAPP mice. It does not establish that deficits precede plaques in human patients with early AD or mild cognitive impairment, so the claim extends the mouse finding to those patients. No page number is available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredIn Alzheimer's disease, plaque deposits, fibrils, and oligomers of Aβ are considered essential mediators in the pathophysiological cascade leading to cognitive decline.
“In AD, plaque deposits, fibrils, and oligomers of A are considered essential mediators in the pathophysiological cascade leading to cognitive decline (Mucke and Selkoe, 2012).”
From Early Alterations in Functional Connectivity and White Matter Structure in a Transgenic Mouse Model of Cerebral Amyloidosis (2014) · cites this paper as Mucke and Selkoe, 2012
In the section on monomers, oligomers, and fibrils (page not provided), the paper links Aβ accumulation and soluble oligomers to neuronal dysfunction relevant to cognitive decline, and allows that plaques may have local neurotoxic effects. It does not treat plaques, fibrils, and oligomers alike as essential mediators: it describes insoluble fibrils as potentially relatively inactive reservoirs and reports that washed plaque cores did not block synaptic plasticity unless dissolved to release oligomers. (LLM, conf=0.88)
Experimental — accuracy not yet measuredSynapse loss in Alzheimer's disease correlates with cognitive decline.
“Synapse loss in Alzheimer's disease (AD) correlates with cognitive decline.”
From Complement and microglia mediate early synapse loss in Alzheimer mouse models (2016) · cites this paper as [4]
Oligomeric Aβ, but not monomeric Aβ or vehicle, induced C1q deposition in wild-type mice.
“Oligomeric Aβ (oAβ), which is prefibrillar in nature and acts as a mediator of synapse loss and dysfunction in AD (4), but not the relatively innocuous monomeric Aβ or vehicle, induced C1q deposition (Fig. 2A and fig. S5).”
From Complement and microglia mediate early synapse loss in Alzheimer mouse models (2016) · cites this paper as [4]
Aβ can deteriorate synaptic functions and block LTP.
“Numerous in vitro and in vivo studies have demonstrated that Aβ can deteriorate synaptic functions and block long-term potentiation (LTP), which is the cellular basis of learning and memory (35).”
From Deletion of <i>Abi3</i> gene locus exacerbates neuropathological features of Alzheimer’s disease in a mouse model of Aβ amyloidosis (2021) · cites this paper as [35]
Aβ can induce neurotoxicity through various mediators, such as inflammatory molecules, membrane lipids, and cytoskeletal proteins.
“Last, Aβ can induce neurotoxicity through various mediators, such as inflammatory molecules, membrane lipids, and cytoskeletal proteins (35).”
From Deletion of <i>Abi3</i> gene locus exacerbates neuropathological features of Alzheimer’s disease in a mouse model of Aβ amyloidosis (2021) · cites this paper as [35]
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The Role of Amyloid-Beta and Tau in the Early Pathogenesis of Alzheimer’s Disease
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Pathogenesis, Animal Models, and Drug Discovery of Alzheimer’s Disease
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Amyloid-β Impairs Vesicular Secretion in Neuronal and Astrocyte Peptidergic Transmission
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Mouse models of neurodegenerative disease: preclinical imaging and neurovascular component
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“12,13 However, many additional genes on HSA21 modulate processes that could contribute to AD pathology in DS. 14–16 Importantly, it has been shown in preclinical models of DS-AD that triplication of HSA21 genes modulates A β aggregation and APP transgene - associated mortality independently of an…”
Hebbian plasticity: The elusive missing link at the heart of Alzheimer’s disease pathogenesis?
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- Authors
- Mucke, L., & Selkoe, D. J.
- Affiliations
- University of California, San Francisco (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Mucke, L.
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2012-03-13
- Volume
- 2
- Issue
- 7
- Pages
- a006338-a006338
- ISSN
- 2157-1422 (ISSN-L)
- PMC
- PMC3385944
- OpenAlex
- W2126402425
- Cited by
- 1,000
- References
- 109
- Citations by year
- 2026: 41 · 2025: 44 · 2024: 53 · 2023: 81 · 2022: 91 · 2021: 103 · 2020: 74 · 2019: 57 · 2018: 82 · 2017: 75 · 2016: 71 · 2015: 87 · 2014: 91 · 2013: 37 · 2012: 11
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- 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, neurotoxicity, synaptic dysfunction, neuronal network dysfunction, membrane binding, amyloid plaques, receptor binding, cognitive impairment, animal models of Alzheimer's disease, therapeutic interventions
- MeSH terms
- Alzheimer Disease, Animals, Extracellular Space, Humans, Nerve Net, Synaptic Transmission, Neurons, Synapses, Amyloid beta-Peptides
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.
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