Aβ Oligomers – a decade of discovery

Walsh, Dominic M.; Selkoe, Dennis J.

doi:10.1111/j.1471-4159.2006.04426.x

Cited by 1,938Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Aβ Oligomers – a decade of discovery

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Walsh, Dominic M., Selkoe, Dennis J.·2007·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2006.04426.x

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Abstract

Converging lines of evidence suggest that progressive accumulation of the amyloid β‐protein (Aβ) plays a central role in the genesis of Alzheimer’s disease, but it was long assumed that Aβ had to be assembled into extracellular amyloid fibrils to exert its cytotoxic effects. Over the past decade, data have emerged from the use of synthetic Aβ peptides, cell culture models, β‐amyloid precursor protein transgenic mice and human brain to suggest that pre‐fibrillar, diffusible assemblies of Aβ are also deleterious. Although the precise molecular identity of these soluble toxins remains unsettled, accumulating evidence suggests that soluble forms of Aβ are indeed the proximate effectors of synapse loss and neuronal injury. Here we review recent progress in understanding the role of soluble oligomers in Alzheimer’s disease.

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Soluble Aβ oligomers are more neurotoxic than insoluble aggregates both in vitro and in vivo.
“recent studies have shown that the soluble Aβ oligomers are more neurotoxic both in vitro and in vivo.5−8”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [5]
In “Detection and toxicity of non-fibrillar assemblies of synthetic Aβ” (page not provided), the review reports that oligomers caused substantially faster and greater neuronal death in culture than fibrillar Aβ. It also describes brain dysfunction caused by soluble oligomers in animals in “Aβ self-association is required for toxicity” (page not provided), but does not establish that they are more neurotoxic than insoluble aggregates in vivo. (LLM, conf=0.83)
Experimental — accuracy not yet measured
For preformed Aβ42 fibrils, no significant cell toxicity was observed in either the absence or presence of Cu2+.
“For the preformed Aβ42 fibrils, no significant cell toxicity was observed in either the absence or presence of Cu2+ (Figure 9, lanes 1 and 2), supporting the previously reported diminished toxicity of Aβ42 fibrils.5,7,54−56”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [5]
In “Detection and toxicity of non-fibrillar assemblies of synthetic Aβ” (page not provided), the review reports that fibrillar Aβ caused only modest cell death at a higher concentration and after a longer exposure than oligomers. This supports the cited background point that fibrils have diminished toxicity, but it does not report the citing paper’s specific finding of no significant toxicity from preformed Aβ42 fibrils with or without Cu2+. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Soluble Aβ oligomers are more neurotoxic than amyloid plaques and most likely responsible for synaptic dysfunction and memory loss in AD.
“However, recent in vivo studies have shown that soluble Aβ oligomers are more neurotoxic than amyloid plaques and most likely responsible for synaptic dysfunction and memory loss in AD.7–11”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [7]
Soluble Aβ oligomers are possibly more neurotoxic than amyloid plaques and are likely responsible for synaptic dysfunction and memory loss in AD patients and AD animal models.
“However, recent in vivo studies have shown that the soluble Aβ oligomers are possibly more neurotoxic than amyloid plaques,14–17 and are likely responsible for synaptic dysfunction and memory loss in AD patients and AD animal models.18–21”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [19]
Aβ42 peptide was shown to form neurotoxic soluble Aβ oligomers.
“which was also shown to form neurotoxic soluble Aβ oligomers.18–20”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [19]

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D. M. Walsh and D. J. Selkoe Journal Compilation Ó 2007 International Society for Neurochemistry, J. Neurochem. (2007) 101, 1172-1184
Ó 2007 The Authors 14714159, 2007, 5, · DOI
Ó 2007 The Authors Journal Compilation Ó 2007 International Society for Neurochemistry, J. Neurochem. (2007) 101, 1172-1184 14714159, 2007, 5, · DOI
D. M. Walsh and D. J. Selkoe Journal Compilation Ó 2007 International Society for Neurochemistry, J. Neurochem. (2007) 101, 1172-1184
Ó 2007 The Authors 14714159, 2007, 5, · DOI
Shankar G. M., Townsend M., Walsh D. M., Selkoe D. J. and Sabatini B. L. (2007) Natural oligomers of the Alzheimer amyloid beta- protein induce hippocampal synapse loss but can be neutralized by antibodies and small molecules. J. Neurosci. in press.
Westerman M. A., Cooper-Blacketer D., Mariash A., Kotilinek L., Kawarabayashi T., Younkin L. H., Carlson G. A., Younkin S. G. Ab Oligomers -a decade of discovery 1183 Ó 2007 The Authors Journal Compilation Ó 2007 International Society for Neurochemistry, J. Neurochem. (2007) 101, 1172-1184 14714159, 2007, 5, · DOI
D. M. Walsh and D. J. Selkoe Journal Compilation Ó 2007 International Society for Neurochemistry, J. Neurochem. (2007) 101, 1172-1184
Ó 2007 The Authors 14714159, 2007, 5, · DOI

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Authors: Walsh, D. M., & Selkoe, D. J.
Affiliations: University College Dublin (IE)
Brigham and Women's Hospital (US)
Corresponding author: Walsh, Dominic M.
Selkoe, Dennis J.
ORCID: Walsh, Dominic M.
Selkoe, Dennis J.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2007-01-04
Volume: 101
Issue: 5
Pages: 1172-1184
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2006.04426.x
OpenAlex: W1981458288
Cited by: 1,938
References: 147
Citations by year: 2026: 48 · 2025: 36 · 2024: 46 · 2023: 47 · 2022: 50 · 2021: 63 · 2020: 76 · 2019: 81 · 2018: 81 · 2017: 109 · 2016: 120 · 2015: 136 · 2014: 134 · 2013: 159 · 2012: 167
FWCI: 14.23
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: Foundation for Neurologic Diseases
Wellcome Trust (067660)
National Institutes of Health
National Institute on Aging (AG-06173)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta oligomers, Alzheimer's disease, soluble amyloid-beta, synaptic loss, neuronal injury, amyloid fibrils, amyloid precursor protein, transgenic mouse model
MeSH terms: Alzheimer Disease, Humans, Male, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Protein Structure, Secondary

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