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Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Abstract
Alzheimer's disease (AD) is the most common cause of progressive intellectual failure in aged humans. AD brains contain numerous amyloid plaques surrounded by dystrophic neurites, and show profound synaptic loss, neurofibrillary tangle formation and gliosis. The amyloid plaques are composed of amyloid beta-peptide (A beta), a 40-42-amino-acid fragment of the beta-amyloid precursor protein (APP). A primary pathogenic role for APP/A beta is suggested by missense mutations in APP that are tightly linked to autosomal dominant forms of AD. A major obstacle to elucidating and treating AD has been the lack of an animal model. Animals transgenic for APP have previously failed to show extensive AD-type neuropathology, but we now report the production of transgenic mice that express high levels of human mutant APP (with valine at residue 717 substituted by phenylalanine) and which progressively develop many of the pathological hallmarks of AD, including numerous extracellular thioflavin S-positive A beta deposits, neuritic plaques, synaptic loss, astrocytosis and microgliosis. These mice support a primary role for APP/A beta in the genesis of AD and could provide a preclinical model for testing therapeutic drugs.
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In the citing paper
“Mouse models that overexpress amyloid precursor protein (APP) develop plaques remarkably similar to those observed in AD but do not recapitulate neurofibrillary pathology or widespread neuronal loss (Games et al., 1995;Hsiao et al., 1996;Irizarry et al., 1997a;Urbanc et al., 2002), allowing interpretation of results in the context of amyloid-related pathologies.”
From Dendritic Spine Abnormalities in Amyloid Precursor Protein Transgenic Mice Demonstrated by Gene Transfer and Intravital Multiphoton Microscopy (2005) · cites this paper as Games et al., 1995
In the citing paper
“Similar to AD, APP transgenic mouse models have elevated inflammation markers and gliosis associated with amyloid deposits (Games et al., 1995; Hsiao et al., 1996; Sturchler-Pierrat et al., 1997).”
From Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006) · cites this paper as Games et al., 1995
In the citing paper
“The first successful mouse models reproducing Aβ pathologies overexpressed human APP with either a single Swedish [25, 26] or Indiana [27] mutation.”
From Amyloid-β plaque formation and reactive gliosis are required for induction of cognitive deficits in App knock-in mouse models of Alzheimer’s disease (2019) · cites this paper as [27]
In the citing paper
“The hAPP tg line J9 selected for this study expresses an alternatively spliced minigene, hA PP, bearing the amyloidogenic V717F and K670M / N671L mutations that have been linked to familial AD (Games et al., 1995).”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Games et al., 1995
In the citing paper
“The J9 model utilizes a mini-APP gene that can produce all three isoforms of APP: APP695, APP751 and APP770 [41].”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [41]
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 [25]
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Metadata
- Authors
- Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., Guido, T., Hagopian, S., Johnson-Wood, K., Khan, K., Lee, M., Leibowitz, P., Lieberburg, I., Little, S., Masliah, E., McConlogue, L., Montoya-Zavala, M., Mucke, L., Paganini, L., Penniman, E., Power, M., Schenk, D., Seubert, P., Snyder, B., Soriano, F., Tan, H., Vitale, J., Wadsworth, S., Wolozin, B., & Zhao, J.
- Affiliations
- Worcester Polytechnic Institute (US)
- University of Massachusetts Chan Medical School (US)
- Eli Lilly (United States) (US)
- Boston Children's Hospital (US)
- University of California San Diego (US)
- Scripps Research Institute (US)
- ORCID
- Venue
- Nature
- Published
- 1995-02
- Volume
- 373
- Issue
- 6514
- Pages
- 523-527
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2126800086
- Cited by
- 2,516
- References
- 28
- Citations by year
- 2026: 17 · 2025: 34 · 2024: 55 · 2023: 38 · 2022: 42 · 2021: 52 · 2020: 55 · 2019: 42 · 2018: 35 · 2017: 54 · 2016: 69 · 2015: 64 · 2014: 58 · 2013: 75 · 2012: 73
- FWCI
- 101.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid precursor protein, transgenic mice, amyloid-beta, amyloid plaques, neuritic plaques, synaptic loss, astrocyte activation, microglial activation, animal models of Alzheimer's disease, thioflavin S staining
- MeSH terms
- Alzheimer Disease, Animals, Base Sequence, Brain, Humans, Immunoenzyme Techniques, Mice, Transgenic, Molecular Sequence Data, Mutation, Platelet-Derived Growth Factor, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, DNA Primers, Microscopy, Confocal, Mice
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