An analysis of relation between MENb and nuclear foci in Huntington's disease
Project/Area Number |
25871169
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Neurology
Nerve anatomy/Neuropathology
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Research Institution | The University of Tokyo (2014-2015) 独立行政法人国立精神・神経医療研究センター (2013) |
Principal Investigator |
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2015: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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Keywords | non-coding RNA / 神経変性疾患 / ハンチントン病 / 凝集体形成 / R6/2マウス / microRNA / ノンコーディングRNA / Huntington's disease |
Outline of Final Research Achievements |
MEN beta (MENb) long non-coding RNA have been identified as an essential factor for structural integrity of nuclear body paraspeckle involved in stress responses. The ability of MENb to retain several nuclear proteins in paraspeckle seems likely to contribute to formation of abnormal nuclear foci observed in neurodegenerative disorders such as Huntington’s disease; however, it remains to be elucidated. In this study, we evaluated whether MENb influences organization of nuclear foci in Huntington’s disease using model mice and stable cell lines expressing the mutant Huntingtin (mHTT) gene. The expression analysis of MENb and the localization analysis of nuclear foci derived from mHTT in vitro and in vivo suggested a poor relation between MENb and mHTT aggregations.
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Report
(4 results)
Research Products
(15 results)
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[Journal Article] A functional involvement of ABCE1, eukaryotic ribosome recycling factor, in nonstop mRNA decay in Drosophila melanogaster cells2014
Author(s)
(206)Kashima, I., Takahashi, M., Hashimoto, Y., Sakota, E., Nakamura, Y., Inada, T.
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Journal Title
Biochimie
Volume: 106
Pages: 10-16
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] Ubiquitin C-terminal hydrolase L1 (UCH-L1) act as a novel potentiator of cyclin-dependent kinases to enhance cell proliferation, independent of its hydrolase activity2013
Author(s)
Kabuta, T., Mitsui, T., Takahashi, M., Fujiwara, Y., Kabuta, C., Konya, C., Tsuchiya, Y., Hatanaka, Y., Uchida, K., Hohjoh, H., Wada, K
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Journal Title
J. Biol. Chem
Volume: 288
Issue: 18
Pages: 12615-12626
DOI
Related Report
Peer Reviewed
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