A molecular mechanism regulating pathological aggregation of SOD1 proteins
| Project/Area Number |
20770130
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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 |
Biophysics
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
FURUKAWA Yoshiaki The Institute of Physical and Chemical Research, 構造神経病理研究チーム, 基礎科学特別研究員 (40415287)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2008: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | タンパク質凝集 / SOD1 / 神経変性疾患 / 筋萎縮性側索硬化症 / アミロイド / フォールディング / 蛋白質凝集 / 翻訳後修飾 / 金属シャペロン蛋白質 |
|---|
| Research Abstract |
ALS-causing mutations facilitate aggregation of SOD1, upon which significant structural changes of SOD1 have been assumed; however, a structure of protein aggregate remains obscure. Here, by utilizing mass spectrometry, I have identified a protease-resistant core in wild-type as well as ALS-causing mutant SOD1 aggregates. SOD1 aggregates exhibit mutation-dependent structural polymorphism, which further regulates biochemical properties of aggregates such as solubility. Based upon these results, I propose a new pathomechanism of fALS in which mutation-dependent structural polymorphism of SOD1 aggregates can affect disease phenotypes.
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Report
(3 results)
Research Products
(24 results)
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[Journal Article] RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells2008
Author(s)
Hiroshi Doi, Kazumasa Okamura, Peter O. Bauer, Yoshiaki Furukawa, Hideaki Shimizu, Masaru Kurosawa, Yoko Machida, Haruko Miyazaki, Kenichi Mitsui, Yoshiyuki Kuroiwa, Nobuyuki Nukina
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Journal Title
The Journal of Biological Chemistry 283
Pages: 6489-6500
Related Report
Peer Reviewed
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