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Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Open accessAbstract
A pathological hallmark of Alzheimer's disease is an accumulation of insoluble plaque containing the amyloid-beta peptide of 40-42 amino acid residues. Prefibrillar, soluble oligomers of amyloid-beta have been recognized to be early and key intermediates in Alzheimer's-disease-related synaptic dysfunction. At nanomolar concentrations, soluble amyloid-beta oligomers block hippocampal long-term potentiation, cause dendritic spine retraction from pyramidal cells and impair rodent spatial memory. Soluble amyloid-beta oligomers have been prepared from chemical syntheses, transfected cell culture supernatants, transgenic mouse brain and human Alzheimer's disease brain. Together, these data imply a high-affinity cell-surface receptor for soluble amyloid-beta oligomers on neurons-one that is central to the pathophysiological process in Alzheimer's disease. Here we identify the cellular prion protein (PrP(C)) as an amyloid-beta-oligomer receptor by expression cloning. Amyloid-beta oligomers bind with nanomolar affinity to PrP(C), but the interaction does not require the infectious PrP(Sc) conformation. Synaptic responsiveness in hippocampal slices from young adult PrP null mice is normal, but the amyloid-beta oligomer blockade of long-term potentiation is absent. Anti-PrP antibodies prevent amyloid-beta-oligomer binding to PrP(C) and rescue synaptic plasticity in hippocampal slices from oligomeric amyloid-beta. Thus, PrP(C) is a mediator of amyloid-beta-oligomer-induced synaptic dysfunction, and PrP(C)-specific pharmaceuticals may have therapeutic potential for Alzheimer's disease.
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In the citing paper
“Among the Aβ binding candidates, cellular prion protein (PrPc) represents the most studied, either alone or through a complex with mGluR5 [37, 62, 72, 79].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [37]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The most studied binding partner is the PrPc, which through a cascade involving a complex with mGluR5 may lead to toxicity independently or via tau [37, 62, 72, 79].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [37]
Experimental — accuracy not yet measuredIn 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 [33]
In the citing paper
“A genome-wide association study (GWAS) identified PrPC as a potential high-affinity receptor for oAβ [87].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [87]
In the citing paper
“Subsequent studies showed that oAβ, especially high-molecular weight oligomers [88], preferentially bind to PrPC within an N-terminal 95-111aa segment [87].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [87]
In the citing paper
“oligomer binding is significantly reduced in PrPC knock-out cells (Lauren et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lauren et al., 2009
In the citing paper
“Aβ oligomers bind with nanomolar affinity to cellular prion protein (PrPC) and that anti-PrP antibodies reduce oligomer binding to neurons and rescue synaptic plasticity (Lauren et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lauren et al., 2009
In the citing paper
“explaining the finding that knocking-down these proteins or adding antibodies against their extracellular domains blocks the accumulation of ADDL clusters (“hotspots”) at synapses (De Felice et al., 2007; Decker et al., 2010a; Lauren et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lauren et al., 2009
In the citing paper
“PrPC binds synthetic Aβ oligomers with high affinity and plays a role in the oligomer-mediated inhibition of LTP (17).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [17]
In the citing paper
“In an elegant study Lauren et al. (17) reported that PrPC mediates the Aβ oligomer-induced hippocampal synaptic plasticity impairment.”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [17]
In the citing paper
“The 22 °C-Aβ oligomers impaired recognition memory in both Prnp +/+ and Prnp 0/0 mice (Fig. 4C).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [17]
In the citing paper
“When amyloid-β oligomers bind to PrPc, long-term potentiation and the formation of new memories are disrupted [129,130,131].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [130]
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Metadata
- Authors
- Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M.
- Affiliations
- Yale University (US)
- Corresponding author
- Strittmatter, Stephen M.
- Venue
- Nature
- Published
- 2009-02
- Volume
- 457
- Issue
- 7233
- Pages
- 1128-1132
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2748841
- OpenAlex
- W2171526610
- Cited by
- 1,560
- References
- 37
- Citations by year
- 2026: 46 · 2025: 45 · 2024: 50 · 2023: 52 · 2022: 87 · 2021: 82 · 2020: 85 · 2019: 71 · 2018: 108 · 2017: 117 · 2016: 103 · 2015: 98 · 2014: 104 · 2013: 116 · 2012: 119
- FWCI
- 87.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- U.S. Public Health Service (5T32GN07205)
- National Institute on Drug Abuse (P30DA018343)
- National Institute of Neurological Disorders and Stroke (R01NS042304, R01NS039962, R37NS033020)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- cellular prion protein, amyloid-beta oligomers, Alzheimer's disease, synaptic plasticity, long-term potentiation, cell surface receptors, lipid rafts, hippocampus, anti-PrP antibodies, prion disease, expression cloning, neurotoxicity, spatial memory, neuroprotection, neurodegeneration
- MeSH terms
- Alzheimer Disease, Amyloidosis, Animals, Chlorocebus aethiops, Hippocampus, Humans, Mice, Inbred C57BL, Neuronal Plasticity, Neurons, Peptide Fragments, Prions, Protein Binding, Receptors, Cell Surface, Synapses, Amyloid beta-Peptides, Long-Term Potentiation, COS Cells, Mice, Amyloid Precursor Protein Secretases, Protein Multimerization
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