Beta-amyloid oligomers: recent developments
Open accessAbstract
Recent studies point to a critical role of soluble β-amyloid oligomers in the pathogenesis of one of the most common neurodegenerative diseases, Alzheimer's disease (AD). Beta-amyloid peptides are cleavage products of a ubiquitously expressed protein, the amyloid precursor protein. Early studies suggested that accumulation of extracellular β-amyloid aggregates are the most toxic species causing synaptic dysfunction and neuronal loss in particular regions of the brain (neurobiological features underlying cognitive decline of the AD patients). In recent years, a shift of pardigm occurred, and now there is accumulating evidence that soluble oligomeric forms of the peptide are the most toxic to neuronal cells. In this review, we discuss recent findings on the toxic effects of amyloid-β oligomers, their physico-chemical properties and the possible pathways of their formation in vitro and in vivo.
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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 [9]
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 Aβ<sub>42</sub>Peptide (2012) · cites this paper as [21]
Oligomeric Aβ peptides are more destructive than Aβ monomers and fibrillar forms in the brain.
“it has been observed that oligomeric Aβ peptides are more destructive than Aβ monomers and fibrillar forms in the brain [132,133].”
From Beneficial Effects of Spirulina Consumption on Brain Health (2022) · cites this paper as [133]
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1 retracted
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Beneficial Effects of Spirulina Consumption on Brain Health
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Cognitive dysfunction in type 1 diabetes: role of TREM2 in microglial activation and Aβ pathology
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- Authors
- Borutaite, V., Morkuniene, R., & Valincius, G.
- Affiliations
- Institute for Biomedical Research, Lithuanian University of Health Sciences, Eiveniu Str. 4, LT-50009 Kaunas, Lithuania
- Institute of Biochemistry, Vilnius University, Mokslininku Str. 12, LT-08662 Vilnius, Lithuania
- Venue
- bmc
- Publisher
- Walter de Gruyter GmbH
- Published
- 2011-06-01
- Volume
- 2
- Issue
- 3
- Pages
- 211-222
- ISSN
- 1868-5021 (ISSN-L)
- 1868-503X
- OpenAlex
- W1978076524
- Cited by
- 9
- References
- 136
- Citations by year
- 2026: 1 · 2022: 1 · 2020: 1 · 2018: 1 · 2016: 2 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- BioMolecular Concepts (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Lithuanian University of Health Sciences (submittedVersion)
- 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, amyloid precursor protein, neurotoxicity, synaptic dysfunction, neuronal loss
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