The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5
Open accessAbstract
Soluble oligomers of amyloid beta (Abeta) play a role in the memory impairment characteristic of Alzheimer's disease. Acting as pathogenic ligands, Abeta oligomers bind to particular synapses and perturb their function, morphology, and maintenance. Events that occur shortly after oligomer binding have been investigated here in live hippocampal neurons by single particle tracking of quantum dot-labeled oligomers and synaptic proteins. Membrane-attached oligomers initially move freely, but their diffusion is hindered markedly upon accumulation at synapses. Concomitantly, individual metabotropic glutamate receptors (mGluR5) manifest strikingly reduced lateral diffusion as they become aberrantly clustered. This clustering of mGluR5 elevates intracellular calcium and causes synapse deterioration, responses prevented by an mGluR5 antagonist. As expected, clustering by artificial crosslinking also promotes synaptotoxicity. These results reveal a mechanism whereby Abeta oligomers induce the abnormal accumulation and overstabilization of a glutamate receptor, thus providing a mechanistic and molecular basis for Abeta oligomer-induced early synaptic failure.
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“Aβ oligomers can drive additional vicious cycles by stimulating metabotropic glutamate receptor 5 (mGluR5)146,147, which activates feedforward Ca2+–cAMP signaling and drive tau phosphorylation (Fig. 5, brown).”
From Stress weakens prefrontal networks: molecular insults to higher cognition (2015) · cites this paper as [146]
In the citing paper
“Aβ binds to α7 nicotinic acetylcholine receptors (α7 nAChRs) and to metabotropic glutamate receptors, in particular mGluR5 [31–33].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [32]
In the citing paper
“ADDL binding to synapses displays saturable kinetics (Renner et al., 2010)”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“Double-labeling with synaptophysin or FM463 establishes this localization to be at functional synapses (Renner et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“single particle tracking of quantum dot-labeled Aβ oligomers has demonstrated the participation of metabotropic glutamate receptors (mGluR5) in oligomer binding and clustering at synapses (Renner et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“Initially, Aβ oligomers diffused as if bound to an untethered protein. Within minutes, however, movement slowed and oligomers became immobilized, typically at active synapses labeled with FM4-64. The synaptic trapping of oligomers was accompanied by co-clustering and immobilization of mGluR5 metabotropic glutamate receptors.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“protection also is afforded by antagonists of metabotropic mGluR5 receptors (Rammes et al., 2011; Renner et al., 2010; Wang et al., 2004).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
In the citing paper
“the recent finding that mGluR5 is implicated in the toxic clustering of Aβ oligomers at synapses and the ensuing aberrant calcium signaling (Renner et al., 2010) suggests that selective mGluR5 inhibitors may hold potential to block oligomer-induced synapse dysfunction.”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Renner et al., 2010
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Metadata
- Authors
- Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Northwestern University (US)
- Corresponding author
- Klein, William L.
- Triller, Antoine
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 66
- Issue
- 5
- Pages
- 739-754
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3111138
- OpenAlex
- W2003655335
- Cited by
- 468
- References
- 62
- Citations by year
- 2026: 18 · 2025: 22 · 2024: 23 · 2023: 14 · 2022: 26 · 2021: 34 · 2020: 38 · 2019: 25 · 2018: 29 · 2017: 26 · 2016: 32 · 2015: 38 · 2014: 31 · 2013: 30 · 2012: 44
- FWCI
- 24.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion, cc-by-nc)
- Funders
- National Institute on Aging (R01AG029460)
- National Institute of Neurological Disorders and Stroke (R01NS058894)
- 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
- amyloid-beta oligomers, mGluR5, metabotropic glutamate receptors, receptor clustering, synaptic dysfunction, synaptotoxicity, Alzheimer's disease, hippocampal neurons, single-particle tracking, quantum dots, intracellular calcium, receptor diffusion, receptor cross-linking
- MeSH terms
- Animals, Cells, Cultured, Extracellular Matrix, Neurons, Protein Binding, Synapses, Amyloid beta-Peptides, Rats, Sprague-Dawley, Receptors, Metabotropic Glutamate, Mice, Knockout, Mice, Rats, Protein Stability, Receptor, Metabotropic Glutamate 5
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