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The prion protein as a receptor for amyloid-β
Open accessAbstract
Increased levels of brain amyloid-beta, a secreted peptide cleavage product of amyloid precursor protein (APP), is believed to be critical in the aetiology of Alzheimer's disease. Increased amyloid-beta can cause synaptic depression, reduce the number of spine protrusions (that is, sites of synaptic contacts) and block long-term synaptic potentiation (LTP), a form of synaptic plasticity; however, the receptor through which amyloid-beta produces these synaptic perturbations has remained elusive. Laurén et al. suggested that binding between oligomeric amyloid-beta (a form of amyloid-beta thought to be most active) and the cellular prion protein (PrP(C)) is necessary for synaptic perturbations. Here we show that PrP(C) is not required for amyloid-beta-induced synaptic depression, reduction in spine density, or blockade of LTP; our results indicate that amyloid-beta-mediated synaptic defects do not require PrP(c).
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“supporting the notion that, at least in part, the deleterious effects of Aβ oligomers on plasticity are independent of PrPC (Kessels et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Kessels et al., 2010
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Metadata
- Authors
- Kessels, H. W., Nguyen, L. N., Nabavi, S., & Malinow, R.
- Affiliations
- University of California San Diego (US)
- Venue
- Nature
- Published
- 2010-08-12
- Volume
- 466
- Issue
- 7308
- Pages
- E3-E4
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3057871
- OpenAlex
- W2009755157
- Cited by
- 253
- References
- 14
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2023: 3 · 2022: 6 · 2021: 13 · 2020: 13 · 2019: 9 · 2018: 12 · 2017: 27 · 2016: 14 · 2015: 21 · 2014: 16 · 2013: 39 · 2012: 30
- FWCI
- 24.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute on Aging (R01AG032132)
- National Institute of Mental Health (R01MH049159)
- National Institute of General Medical Sciences (T32GM008444)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amyloid-beta, cellular prion protein, Alzheimer's disease, synaptic depression, dendritic spine density, long-term potentiation, synaptic plasticity, amyloid-beta oligomers, amyloid precursor protein, receptor binding
- MeSH terms
- Alzheimer Disease, Animals, Learning, Mice, Inbred C57BL, Mice, Transgenic, Synaptic Transmission, Serotonin, Synapses, Reproducibility of Results, Amyloid beta-Peptides, PrPC Proteins, Mice
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