Fatty Acid-Binding Protein 3 is Critical for α-Synuclein Uptake and MPP+-Induced Mitochondrial Dysfunction in Cultured Dopaminergic Neurons
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α-Synuclein is an abundant neuronal protein that accumulates in insoluble inclusions in Parkinson′s disease and other synucleinopathies. Fatty acids partially regulate α-Synuclein accumulation, and mesencephalic dopaminergic neurons highly express fatty acid-binding protein 3 (FABP3). We previously demonstrated that FABP3 knockout mice show decreased α-Synuclein oligomerization and neuronal degeneration of tyrosine hydroxylase (TH)-positive neurons in vivo. In this study, we newly investigated the importance of FABP3 in α-Synuclein uptake, 1-methyl-4-phenylpyridinium (MPP+)-induced axodendritic retraction, and mitochondrial dysfunction. To disclose the issues, we employed cultured mesencephalic neurons derived from wild type or FABP3−/− C57BL6 mice and performed immunocytochemical analysis. We demonstrated that TH+ neurons from FABP3+/+ mice take up α-Synuclein monomers while FABP3−/− TH+ neurons do not. The formation of filamentous α-Synuclein inclusions following treatment with MPP+ was observed only in FABP3+/+, and not in FABP3−/− neurons. Notably, detailed morphological analysis revealed that FABP−/− neurons did not exhibit MPP+-induced axodendritic retraction. Moreover, FABP3 was also critical for MPP+-induced reduction of mitochondrial activity and the production of reactive oxygen species. These data indicate that FABP3 is critical for α-Synuclein uptake in dopaminergic neurons, thereby preventing synucleinopathies, including Parkinson′s disease.
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FABP3 is essential in MPP+-induced morphological abnormality, mitochondrial dysfunction and neurotoxicity.
“FABP3 is also essential in 1-methyl-4-phenylpyridinium (MPP+)-induced morphological abnormality, mitochondrial dysfunction and neurotoxicity [144].”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [144]
FABP3 is critical for α-synuclein uptake into dopaminergic neurons and enhances α-synuclein spreading.
“Very recently, we showed that fatty acid-binding protein 3 (FABP3) is critical for α-synuclein uptake into dopaminergic neurons [144] and enhancement of α-synuclein spreading [145].”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [144]
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- Authors
- Kawahata, I., Bousset, L., Melki, R., & Fukunaga, K.
- Affiliations
- Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan
- Centre National de la Recherche Scientifique (FR)
- Tohoku University (JP)
- Corresponding author
- Fukunaga, Kohji
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2019-10-28
- Volume
- 20
- Issue
- 21
- Pages
- 5358
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6862506
- OpenAlex
- W2982145395
- Cited by
- 56
- References
- 47
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 10 · 2023: 8 · 2022: 7 · 2021: 13 · 2020: 7 · 2019: 1
- FWCI
- 4.74
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Japan Agency for Medical Research and Development (JP19dm0107071, JP18dm0107071)
- Agence Nationale de la Recherche (ANR-17-JPCD-0002)
- Japan Society for the Promotion of Science (19K07097)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- fatty acid binding protein 3, MPP+, mitochondrial dysfunction, dopaminergic neurons, Parkinson's disease, synucleinopathies, reactive oxygen species, alpha-synuclein oligomerization, tyrosine hydroxylase neurons
- MeSH terms
- Fatty Acid Binding Protein 3, Animals, Biological Transport, Cells, Cultured, Dopamine, Mesencephalon, Mice, Inbred C57BL, Mitochondria, Parkinson Disease, Tyrosine 3-Monooxygenase, 1-Methyl-4-phenylpyridinium, Reactive Oxygen Species, Mice, Knockout, Mice, alpha-Synuclein, Dopaminergic Neurons
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