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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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“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
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