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Spread of aggregates after olfactory bulb injection of α-synuclein fibrils is associated with early neuronal loss and is reduced long term
Open accessAbstract
Parkinson's disease is characterized by degeneration of substantia nigra dopamine neurons and by intraneuronal aggregates, primarily composed of misfolded α-synuclein. The α-synuclein aggregates in Parkinson's patients are suggested to first appear in the olfactory bulb and enteric nerves and then propagate, following a stereotypic pattern, via neural pathways to numerous regions across the brain. We recently demonstrated that after injection of either mouse or human α-synuclein fibrils into the olfactory bulb of wild-type mice, α-synuclein fibrils recruited endogenous α-synuclein into pathological aggregates that spread transneuronally to over 40 other brain regions and subregions, over 12 months. We previously reported the progressive spreading of α-synuclein aggregates, between 1 and 12 months following α-synuclein fibril injections, and now report how far the pathology has spread 18- and 23-month post-injection in this model. Our data show that between 12 and 18 months, there is a further increase in the number of brain regions exhibiting pathology after human, and to a lesser extent mouse, α-synuclein fibril injections. At both 18 and 23 months after injection of mouse and human α-synuclein fibrils, we observed a reduction in the density of α-synuclein aggregates in some brain regions compared to others at 12 months. At 23 months, no additional brain regions exhibited α-synuclein aggregates compared to earlier time points. In addition, we also demonstrate that the induced α-synucleinopathy triggered a significant early neuron loss in the anterior olfactory nucleus. By contrast, there was no loss of mitral neurons in the olfactory bulb, even at 18 month post-injection. We speculate that the lack of continued progression of α-synuclein pathology is due to compromise of the neural circuitry, consequential to neuron loss and possibly to the activation of proteolytic mechanisms in resilient neurons of wild-type mice that counterbalances the spread and seeding by degrading pathogenic α-synuclein.
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Metadata
- Authors
- Rey, N. L., George, S., Steiner, J. A., Madaj, Z., Luk, K. C., Trojanowski, J. Q., Lee, V. M.-Y., & Brundin, P.
- Affiliations
- Van Andel Institute (US)
- University of Pennsylvania (US)
- Corresponding author
- Rey, Nolwen L.
- ORCID
- Venue
- Acta Neuropathologica
- Published
- 2017-12-05
- Volume
- 135
- Issue
- 1
- Pages
- 65-83
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC5756266
- OpenAlex
- W2774883898
- Cited by
- 215
- References
- 77
- Citations by year
- 2026: 13 · 2025: 20 · 2024: 17 · 2023: 18 · 2022: 25 · 2021: 41 · 2020: 39 · 2019: 29 · 2018: 10 · 2017: 2
- FWCI
- 15.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Acta Neuropathologica (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Van Andel Research Institute
- Peter C. and Emajean Cook Foundation
- National Institutes of Health (1R01DC016519-01, 5R21NS093993-02)
- Penn Morris K. Udall Parkinson's disease Research Center of Excellence (P50 NS053488)
- Penn Morris K. Undall Parkinson's Research Center of Excellence (P50 NS053488)
- Penn AD Core center (P30 AG10124, P01 AG17586)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- alpha-synuclein fibrils, Parkinson's disease, olfactory bulb, transneuronal spread, synucleinopathies, neuronal loss, anterior olfactory nucleus, mitral cells, substantia nigra, neurodegeneration
- MeSH terms
- Animals, Biological Transport, Brain, Disease Models, Animal, DNA-Binding Proteins, Female, Humans, Mice, Inbred C57BL, Neurons, Olfactory Bulb, Recombinant Proteins, tau Proteins, Cell Death, Disease Progression, Neurodegenerative Diseases, alpha-Synuclein, Protein Aggregation, Pathological
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