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Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
Abstract
Familial Alzheimer disease mutations of presenilin 1 (PS-1) enhance the generation of A beta1-42, indicating that PS-1 is involved in amyloidogenesis. However, PS-1 transgenic mice have failed to show amyloid plaques in their brains. Because PS-1 mutations facilitate apoptotic neuronal death in vitro, we did careful quantitative studies in PS-1 transgenic mice and found that neurodegeneration was significantly accelerated in mice older than 13 months (aged mice) with familial Alzheimer disease mutant PS-1, without amyloid plaque formation. However, there were significantly more neurons containing intracellularly deposited A beta42 in aged mutant transgenic mice. Our data indicate that the pathogenic role of the PS-1 mutation is upstream of the amyloid cascade.
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“Apart from extracellular deposition, early increases in intracellular Aβ levels have been observed in vulnerable neurons of AD human patients [41, 78] and animal models [22, 87, 110], preceding the appearance of Aβ plaques.”
From Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology (2023) · cites this paper as [22]
In the citing paper
“Additionally, it has been shown that intraneuronal Aβ accumulation in specific AD-vulnerable neurons precedes the formation of extracellular Aβ plaques both in AD patients [41, 78] and mouse models [22, 87, 110].”
From Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology (2023) · cites this paper as [22]
In the citing paper
“lack of plaque formation in intraneuronal Aβ42 accumulating transgenic mice with concomitant neurodegeneration [36, 93] limited conclusions that could be drawn to the human disease, since pathological diagnosis of AD requires Aβ plaques.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [36]
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Metadata
- Authors
- Chui, D.-H., Tanahashi, H., Ozawa, K., Ikeda, S., Checler, F., Ueda, O., Suzuki, H., Araki, W., Inoue, H., Shirotani, K., Takahashi, K., Gallyas, F., & Tabira, T.
- Affiliations
- National Center of Neurology and Psychiatry (JP)
- Chugai Pharmaceutical Co., Ltd. (Japan) (JP)
- Centre National de la Recherche Scientifique (FR)
- University of Pecs (HU)
- Corresponding author
- Tabira, Takeshi
- Venue
- Nature Medicine
- Published
- 1999-05
- Volume
- 5
- Issue
- 5
- Pages
- 560-564
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- DOI
- 10.1038/8438
- OpenAlex
- W58149416
- Cited by
- 364
- References
- 31
- Citations by year
- 2025: 3 · 2024: 4 · 2023: 4 · 2022: 6 · 2021: 2 · 2020: 6 · 2019: 16 · 2018: 8 · 2017: 6 · 2016: 9 · 2015: 9 · 2014: 4 · 2013: 6 · 2012: 19
- FWCI
- 16.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Human Health Foundation
- Chugai Pharmaceutical
- 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, familial Alzheimer's disease, transgenic mice, neurodegeneration, amyloid-beta 42, amyloid plaques, amyloidogenesis, neuronal apoptosis, aging
- MeSH terms
- Age Factors, Alzheimer Disease, Animals, Cell Count, Humans, Membrane Proteins, Mice, Transgenic, Neurons, Peptide Fragments, Amyloid beta-Peptides, Apoptosis, Mutation, Missense, Mice, Presenilin-1, Plaque, Amyloid
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