| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Outline of Final Research Achievements |
α-Synuclein is a 140-amino acid protein and abundant in presynaptic terminals of neurons. Intracellular aggregation of α-synuclein is a pathological feature of neurodegenerative diseases, such as Parkinson’s disease (PD). Lysosomal dysfunction and α-synuclein accumulation are considered as the major pathogenic features in PD. For instance, mutations in β-glucocerebrosidase (GBA) gene, responsible for Gaucher disease, are known as a risk factor for PD. Recent studies demonstrate that deficiency of lysosomal enzymes causes lysosomal dysfunction and α-synuclein accumulation; however, the molecular mechanism of α-synuclein accumulation remains unclear. In this study, we investigated the effects of reduced activity of lysosomal enzymes GBA and cathepsins B and D on α-synuclein accumulation. Our study suggested that dysfunctions of cathepsins B and D are more critical role in accumulation and insolubilization of α-synuclein than the GBA dysfunction.
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