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Increase in α-tubulin modifications in the neuronal processes of hippocampal neurons in both kainic acid-induced epileptic seizure and Alzheimer's disease

https://hiroshima.repo.nii.ac.jp/records/2008802
https://hiroshima.repo.nii.ac.jp/records/2008802
93d03dc3-4bae-40a5-be9b-e3c177aee371
名前 / ファイル ライセンス アクション
SciRep_7_40205.pdf SciRep_7_40205.pdf (8.0 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Increase in α-tubulin modifications in the neuronal processes of hippocampal neurons in both kainic acid-induced epileptic seizure and Alzheimer's disease
言語 en
作成者 Thi Vu, Hang

× Thi Vu, Hang

en Thi Vu, Hang

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Akatsu, Hiroyasu

× Akatsu, Hiroyasu

en Akatsu, Hiroyasu

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Hashizume, Yoshio

× Hashizume, Yoshio

en Hashizume, Yoshio

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Setou, Mitsutoshi

× Setou, Mitsutoshi

en Setou, Mitsutoshi

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Ikegami, Koji

× Ikegami, Koji

en Ikegami, Koji

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 © The Author(s) 2017. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
内容記述
内容記述 Neurodegeneration includes acute changes and slow-developing alterations, both of which partly involve common cellular machinery. During neurodegeneration, neuronal processes are impaired along with dysregulated post-translational modifications (PTMs) of cytoskeletal proteins. In neuronal processes, tubulin undergoes unique PTMs including a branched form of modification called glutamylation and loss of the C-terminal tyrosine residue and the penultimate glutamic acid residue forming Δ2-tubulin. Here, we investigated the state of two PTMs, glutamylation and Δ2 form, in both acute and slow-developing neurodegenerations, using a newly generated monoclonal antibody, DTE41, which had 2-fold higher affinity to glutamylated Δ2-tubulin, than to unmodified Δ2-tubulin. DTE41 recognised glutamylated Δ2-tubulin preferentially in immunostaining than in enzyme-linked immunosorbent assay and immunoblotting. In normal mouse brain, DTE41 stained molecular layer of the cerebellum as well as synapse-rich regions in pyramidal neurons of the cerebral cortex. In kainic acid-induced epileptic seizure, DTE41-labelled signals were increased in the hippocampal CA3 region, especially in the stratum lucidum. In the hippocampi of post-mortem patients with Alzheimer’s disease, intensities of DTE41 staining were increased in mossy fibres in the CA3 region as well as in apical dendrites of the pyramidal neurons. Our findings indicate that glutamylation on Δ2-tubulin is increased in both acute and slow-developing neurodegeneration.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported in part by grants-in-aid for Challenging Exploratory Research (26670091) and for Scientific Research on Innovative Areas (23117517) to K.I., and by grants-in-aid for Scientific Research on Innovative Areas (Comprehensive Brain Science Network, 221S0003) and for Platform of Supporting Cohort Study and Biospecimen Analysis (JSPS KAKENHI JP 16H06277). H.T.V. is receiving a scholarship from MEXT and formerly from Shizuoka Bank.
出版者
出版者 Nature Research
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1038/srep40205
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1038/srep40205
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 2045-2322
開始ページ
開始ページ 40205
書誌情報 Scientific Reports
Scientific Reports

巻 7, p. 40205, 発行日 2017-01-09
旧ID 48731
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