Memory Impairment in Transgenic Alzheimer Mice Requires Cellular Prion Protein
Open accessAbstract
Soluble oligomers of the amyloid-β (Aβ) peptide are thought to play a key role in the pathophysiology of Alzheimer's disease (AD). Recently, we reported that synthetic Aβ oligomers bind to cellular prion protein (PrP C ) and that this interaction is required for suppression of synaptic plasticity in hippocampal slices by oligomeric Aβ peptide. We hypothesized that PrP C is essential for the ability of brain-derived Aβ to suppress cognitive function. Here, we crossed familial AD transgenes encoding APPswe and PSen1ΔE9 into Prnp −/− mice to examine the necessity of PrP C for AD-related phenotypes. Neither APP expression nor Aβ level is altered by PrP C absence in this transgenic AD model, and astrogliosis is unchanged. However, deletion of PrP C expression rescues 5-HT axonal degeneration, loss of synaptic markers, and early death in APPswe/PSen1ΔE9 transgenic mice. The AD transgenic mice with intact PrP C expression exhibit deficits in spatial learning and memory. Mice lacking PrP C , but containing Aβ plaque derived from APPswe/PSen1ΔE9 transgenes, show no detectable impairment of spatial learning and memory. Thus, deletion of PrP C expression dissociates Aβ accumulation from behavioral impairment in these AD mice, with the cognitive deficits selectively requiring PrP C .
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oAβ interactions with PrPC have little effect on Aβ plaque deposition and glial activation.
“However, oAβ interactions with PrPC have little effect on Aβ plaque deposition and glial activation [89].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [89]
Neurons lacking PrPC are refractory to dendritic spine loss triggered by oAβ.
“Interestingly, neurons lacking PrPC are refractory to dendritic spine loss triggered by oAβ.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [89]
PrPC deletion functionally restored synaptic LTP deficits induced by oAβ in different AD mouse models.
“PrPC deletion functionally restored synaptic LTP deficits induced by oAβ in different AD mouse models, such as APP/PS1 (APPswe /PSEN1△E9) [89].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [89]
PrPC is involved in synaptic binding and synaptotoxicity of Aβ oligomers.
“These findings suggest that PrPC is involved in synaptic binding and synaptotoxicity of Aβ oligomers (Gimbel et al., 2010).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Gimbel et al., 2010
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Amyloid-<i>β</i>-Induced Dysregulation of AMPA Receptor Trafficking
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Hippocampal Deficits in Amyloid-β-Related Rodent Models of Alzheimer’s Disease
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BMP9 ameliorates amyloidosis and the cholinergic defect in a mouse model of Alzheimer’s disease
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- Authors
- Gimbel, D. A., Nygaard, H. B., Coffey, E. E., Gunther, E. C., Laurén, J., Gimbel, Z. A., & Strittmatter, S. M.
- Affiliations
- Yale University (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2010-05-05
- Volume
- 30
- Issue
- 18
- Pages
- 6367-6374
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3323924
- OpenAlex
- W2121948289
- Cited by
- 418
- References
- 62
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 15 · 2023: 18 · 2022: 17 · 2021: 19 · 2020: 28 · 2019: 20 · 2018: 16 · 2017: 36 · 2016: 28 · 2015: 36 · 2014: 28 · 2013: 48 · 2012: 46
- FWCI
- 31.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- Yale University
- Cure Alzheimer's Fund
- Dr. Ralph and Marian Falk Medical Research Trust
- National Institutes of Health
- National Institute on Aging (R01AG034924)
- National Institute on Drug Abuse (P30DA018343)
- National Institute of Neurological Disorders and Stroke (R01NS042304, R01NS039962, R37NS033020, R01NS056485)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, cellular prion protein, amyloid-beta oligomers, APPswe, Prnp knockout mice, spatial learning and memory, synaptic plasticity, astrocyte activation, cognitive impairment, amyloid plaques
- MeSH terms
- Alzheimer Disease, Animals, Avoidance Learning, Brain, Disease Models, Animal, Memory, Mice, Inbred C57BL, Mice, Transgenic, Nerve Degeneration, Random Allocation, Serotonin, Survival Analysis, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, PrPC Proteins, Maze Learning, Mice, Presenilin-1
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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