Analysis of protein aggregation in amyotrophic lateral sclerosis.
| Project/Area Number |
21790275
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Osaka University |
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Principal Investigator |
MATSUMOTO Ayako Osaka University, 産業科学研究所, 特任助教(常勤) (60444519)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2010: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2009: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | スーパーオキシドジスムターゼ / 筋萎縮性側索硬化症 / 凝集体 / 筋萎縮性硬化症 / SOD / オリゴマー / 酵素 / 蛋白質 / 脳神経疾患 |
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| Research Abstract |
We have explored a mechanism of protein aggregation in amyotrophic lateral sclerosis and found that apo SOD1 and FALS mutant SODs become a substrate for transglutaminase. We could detect soluble oligomeric SODls by high-resolution clear native polyacrylamide gel electrophoresis (hrCN-PAGE). Moreover, hrCN-PAGE can be followed by in-gel activity assay, which revealed enzymatic activities on some oligomeric SODIs from both wild type and FALS mutants.
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Report
(3 results)
Research Products
(5 results)
