Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation

Chui, De-Hua; Tanahashi, Hiroshi; Ozawa, Kazuharu; Ikeda, Sachiya; Checler, Frédéric; Ueda, Otoya; Suzuki, Hiroshi; Araki, Wataru; Inoue, Haruhisa; Shirotani, Keiro; Takahashi, Keikichi; Gallyas, Ferenc; Tabira, Takeshi

doi:10.1038/8438

Cited by 364Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation

Chui, De-Hua, Tanahashi, Hiroshi, Ozawa, Kazuharu, Ikeda, Sachiya, Checler, Frédéric, Ueda, Otoya, Suzuki, Hiroshi, Araki, Wataru +5 more·1999·Nature Medicine

DOI 10.1038/8438

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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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Early increases in intracellular amyloid-β levels have been observed in vulnerable neurons of Alzheimer's disease human patients and animal models, preceding the appearance of amyloid-β plaques.
“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]
Intraneuronal amyloid-β accumulation in specific Alzheimer's disease-vulnerable neurons precedes the formation of extracellular amyloid-β plaques both in Alzheimer's disease patients and mouse models.
“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]
Lack of plaque formation in intraneuronal Aβ42 accumulating transgenic mice with concomitant neurodegeneration limited conclusions that could be drawn to human disease, since pathological diagnosis of AD requires Aβ plaques.
“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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Editorial Expression of Concern: Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
Chui, D., Tanahashi, H., Ozawa, K., Ikeda, S., Checler, F., Ueda, O., Suzuki, H., Araki, W., Inoue, H., Shirotani, K., et al. (2025) · Nature Medicine · doi:10.1038/s41591-025-03903-4
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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
ORCID: Checler, Frédéric
Araki, Wataru
Inoue, Haruhisa
Shirotani, Keiro
Gallyas, Ferenc
Venue: Nature Medicine
Publisher: Springer Science and Business Media LLC
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
Update notices: expression_of_concern (2025-07-25)
expression_of_concern (2025-07-25)
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Nature Medicine (publishedVersion)
PubMed (publishedVersion)
Funders: Human Health Foundation
Chugai Pharmaceutical
Topics: Health Sciences › Medicine › Physiology › 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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Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation

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