Participation in ALS pathology of ALS linked mutant SOD1 proteins accumulated in MAM
Project/Area Number |
24700391
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Neurochemistry/Neuropharmacology
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Research Institution | Doshisha University |
Principal Investigator |
WATANABE Shoji 同志社大学, 高等研究教育機構, 助教 (80462745)
|
Project Period (FY) |
2012 – 2013
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | SOD1 / ALS / MAM / Kv2.1 / 変異SOD1 / Sigma-1レセプター |
Research Abstract |
SOD1 is a major causative protein of familial amyotrophic lateral screosis (fALS). I found that fALS linked mutant SOD1 proteins are specifically accumulated in mitochondria-ER associated membrane (MAM) fraction. The toxic mechanisms by this event, however, are still unknown. I hypothesized that Sigma-1 receptor (SigR1), which is a major MAM protein was inhibited by the accumulation of mutant SOD1 proteins in MAM. In this study, I found two novel finding (1) SigR1 was directly interacted with Kv2.1 and Kv4.2 (2) SigR1 was related with the localization of Kv2.1. Although I need to investigate these results more, these findings might be contributed to elucidation of the pathomechanism of fALS.
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Report
(3 results)
Research Products
(4 results)
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[Journal Article] Specific sorting and post-Golgi trafficking of dendric potassium channels in living neuron.2014
Author(s)
Jensen C. S., Watanabe, S., Rasmussen H. B., Schmitt, N., Olsen S. P., Frost N. A., Blanpied T.A., Misonou, H.
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Journal Title
Journal of Biological chemistry
Volume: vol.289(15)
Pages: 10566-10581
Related Report
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[Journal Article] Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis2014
Author(s)
Nomura, T., Watanabe, S., Kaneko, K., Yamanaka, K., Nukina, N., Furukawa, Y.
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Journal Title
Journal of Biological chemistry
Volume: vol.289(2)
Pages: 1192-1202
Related Report
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