Alzheimer's disease, β‐amyloid, glutamate, NMDA receptors and memantine – searching for the connections

Danysz, Wojciech; Parsons, Chris G

doi:10.1111/j.1476-5381.2012.02057.x

Cited by 500Alzheimer's disease research and treatmentsNeuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration Mechanisms

Alzheimer's disease, β‐amyloid, glutamate, NMDA receptors and memantine – searching for the connections

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Danysz, Wojciech, Parsons, Chris G·2012·British Journal of Pharmacology

DOI 10.1111/j.1476-5381.2012.02057.xPMC PMC3481041

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Abstract

β‐amyloid (Aβ) is widely accepted to be one of the major pathomechanisms underlying Alzheimer's disease (AD), although there is presently lively debate regarding the relative roles of particular species/forms of this peptide. Most recent evidence indicates that soluble oligomers rather than plaques are the major cause of synaptic dysfunction and ultimately neurodegeneration. Soluble oligomeric Aβ has been shown to interact with several proteins, for example glutamatergic receptors of the NMDA type and proteins responsible for maintaining glutamate homeostasis such as uptake and release. As NMDA receptors are critically involved in neuronal plasticity including learning and memory, we felt that it would be valuable to provide an up to date review of the evidence connecting Aβ to these receptors and related neuronal plasticity. Strong support for the clinical relevance of such interactions is provided by the NMDA receptor antagonist memantine. This substance is the only NMDA receptor antagonist used clinically in the treatment of AD and therefore offers an excellent tool to facilitate translational extrapolations from in vitro studies through in vivo animal experiments to its ultimate clinical utility.

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Aβ deposition contributes to disturbed glutamatergic neurotransmission.
“previous studies showing that A β deposition contributes to disturbed glutamatergic neurotransmission”
From Genetic variants of phospholipase C-γ2 alter the phenotype and function of microglia and confer differential risk for Alzheimer’s disease (2023) · cites this paper as [38]
The section “Aβ influences glutamate concentrations in the synaptic cleft” says Aβ can disrupt glutamate uptake and homeostasis, supporting the link to disturbed glutamatergic neurotransmission. It discusses soluble Aβ and toxic peptide fragments, however, rather than establishing that Aβ deposition specifically causes the disturbance; it also cautions that many studies used high concentrations. (LLM, conf=0.84)
Experimental — accuracy not yet measured
oAβ impairs NMDAR-dependent synaptic LTP within hippocampal CA1 and dentate gyrus regions.
“oAβ has been reported to impair NMDAR-dependent synaptic LTP within hippocampal CA1 and dentate gyrus regions [65].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [65]

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BackgroundInfluential
Ionotropic Glutamate Receptors as Therapeutic Targets
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“…pathological changes (i.e. receptor down-regulation as an adaptive change), as well as blatant loss of neuronal cells and synapses expressing these receptors as a long term consequence of chronic excitotoxicity (Geddes et al., 1986; Procter et al., 1989; Ninomiya et al., 1991; Hynd et al., 2001).”
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Welcome to the Journal of Neuroinflammation!
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BJP Alzheimer's disease, b-amyloid, glutamate, NMDA receptors and memantine British Journal of Pharmacology (2012) 167 324-352 345
BJP Alzheimer's disease, b-amyloid, glutamate, NMDA receptors and memantine British Journal of Pharmacology (2012) 167 324-352 347
BJP Alzheimer's disease, b-amyloid, glutamate, NMDA receptors and memantine British Journal of Pharmacology (2012) 167 324-352 351

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Authors: Danysz, W., & Parsons, C. G.
Affiliations: Merz (Germany) (DE)
Corresponding author: Parsons, Chris G
ORCID: Danysz, Wojciech
Parsons, Chris G
Venue: British Journal of Pharmacology
Publisher: Wiley
Published: 2012-08-22
Volume: 167
Issue: 2
Pages: 324-352
ISSN: 0007-1188 (ISSN-L)
1476-5381
DOI: 10.1111/j.1476-5381.2012.02057.x
PMC: PMC3481041
OpenAlex: W1561114541
Cited by: 500
References: 260
Citations by year: 2026: 15 · 2025: 31 · 2024: 38 · 2023: 34 · 2022: 41 · 2021: 35 · 2020: 28 · 2019: 37 · 2018: 45 · 2017: 60 · 2016: 48 · 2015: 33 · 2014: 35 · 2013: 17 · 2012: 2
FWCI: 2.99
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: British Journal of Pharmacology (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: Alzheimer's disease, amyloid-beta, NMDA receptor, glutamate, glutamate homeostasis, synaptic dysfunction, neurodegeneration, neuroplasticity, learning and memory, memantine, NMDA receptor antagonists, amyloid plaques
MeSH terms: Alzheimer Disease, Humans, Memantine, Dopamine Agents, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, Glutamic Acid

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Alzheimer's disease, β‐amyloid, glutamate, NMDA receptors and memantine – searching for the connections

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