Cited by 146Alzheimer's disease research and treatmentsNeuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Alzheimer's disease amyloid β-protein and synaptic function

Ondrejcak, Tomas, Klyubin, Igor, Hu, Neng-Wei, Barry, Andrew E., Cullen, William K., Rowan, Michael J.·2010·NeuroMolecular Medicine

DOI 10.1007/s12017-009-8091-0

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Abstract

Alzheimer's disease (AD) is characterized neuropathologically by the deposition of different forms of amyloid beta-protein (A beta) including variable amounts of soluble species that correlate with severity of dementia. The extent of synaptic loss in the brain provides the best morphological correlate of cognitive impairment in clinical AD. Animal research on the pathophysiology of AD has therefore focussed on how soluble A beta disrupts synaptic mechanisms in vulnerable brain regions such as the hippocampus. Synaptic plasticity in the form of persistent activity-dependent increases or decreases in synaptic strength provide a neurophysiological substrate for hippocampal-dependent learning and memory. Acute treatment with human-derived or chemically prepared soluble A beta that contains certain oligomeric assemblies, potently and selectively disrupts synaptic plasticity causing inhibition of long-term potentiation (LTP) and enhancement of long-term depression (LTD) of glutamatergic transmission. Over time these and related actions of A beta have been implicated in reducing synaptic integrity. This review addresses the involvement of neurotransmitter intercellular signaling in mediating or modulating the synaptic plasticity disrupting actions of soluble A beta, with particular emphasis on the different roles of glutamatergic and cholinergic mechanisms. There is growing evidence to support the view that NMDA and possibly nicotinic receptors are critically involved in mediating t…

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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Philosophical transactions of the Royal Society of London. B
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Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
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Authors: Ondrejcak, T., Klyubin, I., Hu, N.-W., Barry, A. E., Cullen, W. K., & Rowan, M. J.
Affiliations: Trinity College Dublin (IE)
Corresponding author: Rowan, Michael J.
ORCID: Klyubin, Igor
Hu, Neng-Wei
Rowan, Michael J.
Venue: NeuroMolecular Medicine
Publisher: Springer Science and Business Media LLC
Published: 2009-09-16
Volume: 12
Issue: 1
Pages: 13-26
ISSN: 1535-1084 (ISSN-L)
1559-1174
DOI: 10.1007/s12017-009-8091-0
OpenAlex: W2150302044
Cited by: 146
References: 189
Citations by year: 2026: 3 · 2025: 6 · 2024: 7 · 2023: 2 · 2022: 7 · 2021: 6 · 2020: 5 · 2019: 5 · 2018: 7 · 2017: 16 · 2016: 5 · 2015: 7 · 2014: 10 · 2013: 13 · 2012: 18
FWCI: 10.26
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: NeuroMolecular Medicine (publishedVersion)
PubMed (publishedVersion)
Funders: Health Research Board
Science Foundation Ireland
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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: Alzheimer's disease, amyloid-beta, soluble amyloid-beta oligomers, synaptic plasticity, long-term potentiation, long-term depression, glutamatergic neurotransmission, cholinergic mechanisms, NMDA receptor, nicotinic acetylcholine receptors, muscarinic receptors, hippocampus, synaptic loss, neurotransmitter signaling
MeSH terms: Acetylcholine, Alzheimer Disease, Animals, Humans, Synaptic Transmission, Receptors, Cholinergic, Synapses, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, Long-Term Potentiation, Glutamic Acid, Long-Term Synaptic Depression

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Alzheimer's disease amyloid β-protein and synaptic function

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