Cited by 253Alzheimer's disease research and treatmentsNeuroscience and Neuropharmacology ResearchPrion Diseases and Protein Misfolding

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The prion protein as a receptor for amyloid-β

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Kessels, Helmut W., Nguyen, Louis N., Nabavi, Sadegh, Malinow, Roberto·2010·Nature

DOI 10.1038/nature09217PMC PMC3057871

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Abstract

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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1 retracted

RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
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Self-citation
Natural Oligomers of the Alzheimer Amyloid-β Protein Induce Reversible Synapse Loss by Modulating an NMDA-Type Glutamate Receptor-Dependent Signaling Pathway
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Authors: Kessels, H. W., Nguyen, L. N., Nabavi, S., & Malinow, R.
Affiliations: University of California San Diego (US)
ORCID: Kessels, Helmut W.
Nabavi, Sadegh
Malinow, Roberto
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2010-08-12
Volume: 466
Issue: 7308
Pages: E3-E4
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature09217
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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The prion protein as a receptor for amyloid-β

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