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Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins
Open accessAbstract
Missense mutations in two related genes, termed presenilin 1 (PS1) and presenilin 2 (PS2), cause dementia in a subset of early-onset familial Alzheimer's disease (FAD) pedigrees. In a variety of experimental in vitro and in vivo settings, FAD-linked presenilin variants influence the processing of the amyloid precursor protein (APP), leading to elevated levels of the highly fibrillogenic Abeta1-42 peptides that are preferentially deposited in the brains of Alzheimer Disease (AD) patients. In this report, we demonstrate that transgenic animals that coexpress a FAD-linked human PS1 variant (A246E) and a chimeric mouse/human APP harboring mutations linked to Swedish FAD kindreds (APP swe) develop numerous amyloid deposits much earlier than age-matched mice expressing APP swe and wild-type Hu PS1 or APP swe alone. These results provide evidence for the view that one pathogenic mechanism by which FAD-linked mutant PS1 causes AD is to accelerate the rate of beta-amyloid deposition in brain.
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In the citing paper
“However, APP mice develop dystrophic neurites immediately around plaques (50), suggesting that this neuronal pathology is independent of cell death.”
From Attenuating astrocyte activation accelerates plaque pathogenesis in APP/PS1 mice (2013) · cites this paper as [50]
In the citing paper
“However, such studies have not definitively identified which Aβ species are responsible for seeding amyloid deposition in either the parenchyma or vasculature.”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Borchelt et al., 1997
In the citing paper
“Increasing relative Aβ42 levels lowers the age when deposition first occurs, increases the amount of diffuse Aβ, and promotes parenchymal versus cerebrovascular deposition.”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Borchelt et al., 1997
In the citing paper
“These genetic findings led to several transgenic mouse models that successfully recapitulated Aβ plaque formation, increasing support for the hypothesis (Table 1) [23–29].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [24]
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Metadata
- Authors
- Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S.
- Affiliations
- Johns Hopkins University (US)
- Frederick National Laboratory for Cancer Research (US)
- Corresponding author
- Borchelt, David R
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1997-10
- Volume
- 19
- Issue
- 4
- Pages
- 939-945
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2062214806
- Cited by
- 1,023
- References
- 52
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 16 · 2023: 17 · 2022: 18 · 2021: 36 · 2020: 35 · 2019: 25 · 2018: 30 · 2017: 38 · 2016: 29 · 2015: 38 · 2014: 33 · 2013: 44 · 2012: 46
- FWCI
- 17.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuron (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG 14248, P50AG005146, P01AG014248, AG 05146)
- National Institute of Neurological Disorders and Stroke (NS-20471)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- presenilin 1, presenilin 2, amyloid precursor protein, familial Alzheimer's disease, amyloid-beta deposition, transgenic mice, amyloid-beta 42, amyloidosis, Alzheimer's disease pathogenesis
- MeSH terms
- Aging, Alzheimer Disease, Amyloid, Animals, Brain, Family, Humans, Membrane Proteins, Mice, Transgenic, Pedigree, Recombinant Fusion Proteins, Sweden, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Mice, Presenilin-1
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