Inhibition of MPTP-induced α-synuclein oligomerization by fatty acid-binding protein 3 ligand in MPTP-treated mice
Abstract
Accumulation and aggregation of α-synuclein (αSyn) triggers dopaminergic (DAergic) neuronal loss in Parkinson's disease (PD). This pathological event is partly facilitated by the presence of long-chain polyunsaturated fatty acids (LC-PUFAs), including arachidonic acid. The intracellular transport and metabolism of LC-PUFAs are mediated by fatty acid-binding proteins (FABPs). We previously reported that heart-type FABP (FABP3) interacts with αSyn, thereby promoting αSyn oligomerization in DAergic neurons in the substantia nigra pars compacta (SNpc) following 1-methyl-1,2,3,6-tetrahydropyridine (MPTP) treatment. This αSyn oligomerization is prevented in Fabp3 gene knock out mice. We document a novel FABP3 ligand, MF1 (4-(2-(1-(2-chlorophenyl)-5-phenyl-1H-pyrazol-3-yl)phenoxy)butanoic acid), that inhibits αSyn accumulation in DA neurons, thereby inhibiting the oligomerization of αSyn, loss of DAergic neurons, and PD-like motor deficits in MPTP-treated mice. Chronic oral administration of MF1 (0.3 or 1.0 mg/kg/day) significantly improved motor impairments and inhibited MPTP-induced accumulation and oligomerization of αSyn in the SNpc, and in turn prevented loss of tyrosine hydroxylase (TH)-positive cells in the SNpc. MF1 administration (0.1, 0.3, or 1.0 mg/kg/day) also restored MPTP-induced cognitive impairments. Although chronic administration of l-DOPA (3,4-dihydroxl-l-phenylalanine; 25 mg/kg/day, i.p.) also improved motor deficits, it failed to improve the cognitive impairments. In addition, l-DOPA failed to inhibit DAergic neuronal loss and αSyn pathologies in the SNpc. In summary, the novel FABP3 ligand MF1 rescues MPTP-induced behavioural and neuropathological features, suggesting that MF1 may be a disease-modifying drug candidate for synucleinopathies.
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FABP3 ligand inhibits α-synuclein oligomerization in PD mouse models.
“Intriguingly, FABP3 ligand, which we have recently synthesized, inhibits α-synuclein oligomerization in PD mouse models [150,151].”
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 [150]
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Self-citationWang, H., Fukunaga, K., Cheng, A., Wang, Y., Arimura, N., Yoshino, H., Sasaki, T., & Kawahata, K. (2023) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2023.02.008 · Cited by 9 · see citing works
Self-citationFABP2 is Involved in Intestinal α-Synuclein Pathologies
Sekimori, T., Fukunaga, K., Oizumi, H., Baba, T., Totsune, T., Takeda, A., Sasaki, T., & Kawahata, K. (2024) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2302044 · Cited by 8 · see citing works
Self-citationWang, Z., Cui, Y., Li, D., Yan, L., Zhu, S., Ma, X., Lu, Z., Li, C., Feng, J., Yuan, W., et al. (2025) · npj Biofilms and Microbiomes · doi:10.1038/s41522-025-00855-y · Cited by 8 · see citing works
Yabuki, Y., Liu, J., Kawahata, K., Izumi, H., Shinoda, Y., Koga, K., Ueno, S., Shioda, N., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155525 · Cited by 9 · see citing works
Self-citationα‐Synuclein decoy peptide protects mice against α‐synuclein‐induced memory loss
Guo, Q., Kawahata, K., Jia, W., Wang, H., Cheng, A., Yabuki, Y., Shioda, N., & Fukunaga, K. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14120 · Cited by 7 · see citing works
Self-citationWidyarti, S., Wibowo, S., Sabarudin, A., Abhirama, I., & Sumitro, S. B. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e18123 · Cited by 6 · see citing works
Truxillic acid monoamides as fatty acid binding protein 5 inhibitors
Zhu, C., Schutz, L., Jayanetti, K., Takemura, K., Doswell, F., Wang, L., Ojima, I., & Kaczocha, M. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117464 · Cited by 6 · see citing works
The Role of Fatty Acid Binding Proteins in Neuropsychiatric Diseases: A Narrative Review
Powell, A., Yamaguchi, N., Lu, H., Pareek, O., Elman, I., Gold, M. S., Pinhasov, A., Blum, K., & Thanos, P. K. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl26812 · Cited by 5 · see citing works
Matsuo, K., Yabuki, Y., Melki, R., Bousset, L., Owada, Y., & Fukunaga, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010400 · Cited by 5 · see citing works
Self-citationAssociations among blood biomarkers, clinical subtypes, and prognosis in Parkinson’s disease
Oizumi, H., Hasegawa, T., Kawahata, K., Sekimori, T., Totsune, T., Sugimura, Y., Baba, T., Fukunaga, K., & Takeda, A. (2025) · Clinical Parkinsonism & Related Disorders · doi:10.1016/j.prdoa.2025.100313 · Cited by 3 · see citing works
Self-citationJia, W., He, X., Cheng, A., He, Y., Zhao, F., Fukunaga, K., & Zhao, W. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05963-0 · Cited by 1 · see citing works
Self-citationDiscovery of disease-modifying drug inhibiting alpha-synuclein aggregation in Lewy body dementia
Fukunaga, K., Matsuo, K., Cheng, A., & Shinoda, Y. (2019) · IBRO Reports · doi:10.1016/j.ibror.2019.07.1153
Self-citationAlpha-Synuclein in the Blood of Mice in a Neurotoxic Model of Parkinson’s Disease
Blokhin, V. E., & Ugryumov, M. V. (2021) · Neurochemical Journal · doi:10.1134/s1819712421010025
Fatty Acid-Binding Proteins and Substance Use Disorders: From Lipid Signaling to Therapeutic Targets
Powell, A., Yamaguchi, N., Delgado, M., Blum, K., Pinhasov, A., Elman, I., & Thanos, P. K. (2026) · Genes · doi:10.3390/genes17091000
BindingDB Entry 50020331: Truxillic acid monoamides as fatty acid binding protein 5 inhibitors.
BindingDB (2024) · UC San Diego · doi:10.7270/q2668jnq
- Authors
- Matsuo, K., Cheng, A., Yabuki, Y., Takahata, I., Miyachi, H., & Fukunaga, K.
- Affiliations
- Tohoku University (JP)
- The University of Tokyo (JP)
- Corresponding author
- Fukunaga, Kohji
- Venue
- Neuropharmacology
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 150
- Pages
- 164-174
- ISSN
- 0028-3908 (ISSN-L)
- OpenAlex
- W2927509112
- Cited by
- 43
- References
- 63
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 3 · 2023: 7 · 2022: 2 · 2021: 13 · 2020: 8 · 2019: 3
- FWCI
- 4.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuropharmacology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Agency for Medical Research and Development (JP17dm0107071, JP18dm0107071)
- Ministry of Education, Culture, Sports, Science and Technology (18J20651)
- 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
- alpha-synuclein oligomerization, fatty acid binding protein 3, MPTP-induced neurotoxicity, Parkinson's disease, dopaminergic neuron loss, substantia nigra pars compacta, long-chain polyunsaturated fatty acids, arachidonic acid, tyrosine hydroxylase, cognitive impairment, L-DOPA, synucleinopathies
- MeSH terms
- Fatty Acid Binding Protein 3, Animals, Male, Motor Skills, MPTP Poisoning, Mice, alpha-Synuclein, Dopaminergic Neurons
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