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A mechanistic hypothesis for the impairment of synaptic plasticity by soluble Aβ oligomers from Alzheimer’s brain
Abstract
It is increasingly accepted that early cognitive impairment in Alzheimer's disease results in considerable part from synaptic dysfunction caused by the accumulation of a range of oligomeric assemblies of amyloid β‐protein (Aβ). Most studies have used synthetic Aβ peptides to explore the mechanisms of memory deficits in rodent models, but recent work suggests that Aβ assemblies isolated from human (AD) brain tissue are far more potent and disease‐relevant. Although reductionist experiments show Aβ oligomers to impair synaptic plasticity and neuronal viability, the responsible mechanisms are only partly understood. Glutamatergic receptors, GABAergic receptors, nicotinic receptors, insulin receptors, the cellular prion protein, inflammatory mediators, and diverse signaling pathways have all been suggested. Studies using AD brain‐derived soluble Aβ oligomers suggest that only certain bioactive forms (principally small, diffusible oligomers) can disrupt synaptic plasticity, including by binding to plasma membranes and changing excitatory–inhibitory balance, perturbing mGluR, PrP, and other neuronal surface proteins, down‐regulating glutamate transporters, causing glutamate spillover, and activating extrasynaptic GluN2B‐containing NMDA receptors. We synthesize these emerging data into a mechanistic hypothesis for synaptic failure in Alzheimer's disease that can be modified as new knowledge is added and specific therapeutics are developed. image
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Most binding partners have not been studied in human brain nor using human derived Aβ species.
“It is relevant to note that most binding partners have not been studied in human brain nor using human derived Aβ species [38, 63].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [38]
Most Aβ binding partners have not been validated in Alzheimer's cases nor using human derived Aβ species.
“An important outstanding question in the field is which of these potential partners binds Aβ in human synapses, as most binding partners have not been validated in Alzheimer’s cases nor using human derived Aβ species [38, 63].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [38]
Substantial evidence supports an important role for Aβ in synaptotoxicity early in the disease process in Alzheimer's.
“While it is clear that toxicity of tau and changes in non-neuronal cells are also important in disease pathogenesis [24], substantial evidence supports an important role for Aβ in synaptotoxicity early in the disease process in Alzheimer’s [38].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [38]
Due its hydrophobic nature, Aβ binds to lipid membranes interrupting membrane fluidity and destabilizing several membrane receptors.
“Due its hydrophobic nature, Aβ binds to lipid membranes interrupting membrane fluidity and destabilizing several membrane receptors [38].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [38]
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Metadata
- Authors
- Li, S., & Selkoe, D. J.
- Affiliations
- Ann Romney Center for Neurologic Diseases Brigham and Women’s Hospital and Harvard Medical School Boston MA USA
- ORCID
- Li, Shaomin
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2020-04-05
- Volume
- 154
- Issue
- 6
- Pages
- 583-597
- ISSN
- 0022-3042
- 1471-4159
- PMC
- PMC7487043
- Cited by
- 263
- References
- 42
- Language
- en
- Funders
- Foundation for the National Institutes of Health (AG 027443 and AG 036694)
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