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β-Amyloid peptides enhance α-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
Open accessAbstract
Alzheimer's disease and Parkinson's disease are associated with the cerebral accumulation of β-amyloid and α-synuclein, respectively. Some patients have clinical and pathological features of both diseases, raising the possibility of overlapping pathogenetic pathways. We generated transgenic (tg) mice with neuronal expression of human β-amyloid peptides, α-synuclein, or both. The functional and morphological alterations in doubly tg mice resembled the Lewy-body variant of Alzheimer's disease. These mice had severe deficits in learning and memory, developed motor deficits before α-synuclein singly tg mice, and showed prominent age-dependent degeneration of cholinergic neurons and presynaptic terminals. They also had more α-synuclein-immunoreactive neuronal inclusions than α-synuclein singly tg mice. Ultrastructurally, some of these inclusions were fibrillar in doubly tg mice, whereas all inclusions were amorphous in α-synuclein singly tg mice. β-Amyloid peptides promoted aggregation of α-synuclein in a cell-free system and intraneuronal accumulation of α-synuclein in cell culture. β-Amyloid peptides may contribute to the development of Lewy-body diseases by promoting the aggregation of α-synuclein and exacerbating α-synuclein-dependent neuronal pathologies. Therefore, treatments that block the production or accumulation of β-amyloid peptides could benefit a broader spectrum of disorders than previously anticipated.
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In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“The hαSyn/hAPP model recapitulated many of the clinical symptoms and pathology of AD-LBV.”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Further evidence of a link between αSyn and Aβ pathology was offered from studies using mice expressing wt human αSyn (hαSyn) and human APP (hAPP) (hαSyn/hAPP).”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
In the citing paper
“Compared to animals expressing only hαSyn or hAPP, the hαSyn/hAPP animals had marked cholinergic neuron loss, intraneuronal LRP, florid Aβ plaques, exhibited marked motor dysfunction and had significant learning and memory deficits [198].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [198]
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Metadata
- Authors
- Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., & Mucke, L.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-09-25
- Volume
- 98
- Issue
- 21
- Pages
- 12245-12250
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC59799
- OpenAlex
- W2131710583
- Cited by
- 607
- References
- 56
- Citations by year
- 2026: 8 · 2025: 26 · 2024: 17 · 2023: 23 · 2022: 17 · 2021: 17 · 2020: 39 · 2019: 26 · 2018: 25 · 2017: 23 · 2016: 24 · 2015: 26 · 2014: 44 · 2013: 29 · 2012: 24
- FWCI
- 15.14
- Type
- journal article
- Language
- en
- Update notices
- correction (2025-05-22)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association
- National Institutes of Health (AG5131, 5r29ag010869-05, AG‐18440, AG11385, AG10869)
- National Institute on Aging (AG-11385, R37AG018440, R37AG011385, R01AG018440, P50AG005131, AG-5131, AG 18440, AG10869, R01AG011385)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, alpha-synuclein, Alzheimer's disease, Parkinson's disease, Lewy body disease, transgenic mice, neuronal inclusions, alpha-synuclein aggregation, cholinergic neuron degeneration, motor impairment, learning and memory impairment, presynaptic terminals
- MeSH terms
- Age Factors, Alzheimer Disease, Animals, Cell Line, Disease Models, Animal, Female, Humans, Learning Disabilities, Male, Memory Disorders, Mice, Transgenic, Nerve Tissue Proteins, Neurons, Parkinson Disease, Gene Expression, Amyloid beta-Peptides, Mice, Synucleins, alpha-Synuclein
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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