Abstract
Background: αSyn toxicity is triggered by oligomerization of αSyn, and its formation is partly regulated by PUFAs. Results: MPTP-induced neurotoxicity and αSyn oligomerization are attenuated in Fabp3-/- mice. Conclusion: FABP3 is implicated in arachidonic acid-induced αSyn oligomerization and promotes dopaminergic cell death. Significance: FABP3 aggravates MPTP-induced neuronal toxicity and αSyn accumulation.
| Original language | English |
|---|---|
| Pages (from-to) | 18957-18965 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 289 |
| Issue number | 27 |
| DOIs | |
| Publication status | Published - 2014 Jul 4 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Shioda, N., Yabuki, Y., Kobayashi, Y., Onozato, M., Owada, Y., & Fukunaga, K. (2014). FABP3 protein promotes α-synuclein oligomerization associated with 1-Methyl-1,2,3,6-tetrahydropiridine-induced neurotoxicity. Journal of Biological Chemistry, 289(27), 18957-18965. https://doi.org/10.1074/jbc.M113.527341