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

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

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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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
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
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
  • Health Sciences › Medicine › Physiology › 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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