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  1. 学部学科区分一覧
  2. 工学部・工学研究科
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  2. 学術雑誌論文

An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3

https://repository.lib.tottori-u.ac.jp/records/7245
https://repository.lib.tottori-u.ac.jp/records/7245
c2e3d82c-3a9f-4c8c-815d-aafbcf3ca273
名前 / ファイル ライセンス アクション
jbc296_j.jbc.2021.100663.pdf jbc296_j.jbc.2021.100663.pdf (5.0 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2022-06-30
タイトル
タイトル An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3
言語 en
言語
言語 eng
資源タイプ
資源タイプ journal article
著者 フクイ, ナオヤ

× フクイ, ナオヤ

WEKO 26875

ja-Kana フクイ, ナオヤ

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本郷, 邦広

× 本郷, 邦広

WEKO 779
e-Rad 80335504
研究者総覧鳥取大学 100000563

本郷, 邦広

ja-Kana ホンゴウ, クニヒロ

en Hongo, Kunihiro

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溝端, 知宏

× 溝端, 知宏

WEKO 2225
e-Rad 50263489
研究者総覧鳥取大学 100000572

溝端, 知宏

ja-Kana ミゾバタ, トモヒロ

en Mizobata, Tomohiro

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河田, 康志

× 河田, 康志

WEKO 1457
e-Rad 40177697
研究者総覧鳥取大学 100000496

河田, 康志

ja-Kana カワタ, ヤスシ

en Kawata, Yasushi

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Fukui, Naoya

× Fukui, Naoya

WEKO 26876

en Fukui, Naoya

ja-Kana フクイ, ナオヤ

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Yamamoto, Hanae

× Yamamoto, Hanae

WEKO 26877

en Yamamoto, Hanae

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Miyabe, Moe

× Miyabe, Moe

WEKO 26878

en Miyabe, Moe

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Aoyama, Yuki

× Aoyama, Yuki

WEKO 26879

en Aoyama, Yuki

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Kawahata, Ichiro

× Kawahata, Ichiro

WEKO 26880

en Kawahata, Ichiro

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Yabuki, Yasushi

× Yabuki, Yasushi

WEKO 26881

en Yabuki, Yasushi

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Shinoda, Yasuharu

× Shinoda, Yasuharu

WEKO 26882

en Shinoda, Yasuharu

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Fukunaga, Kohji

× Fukunaga, Kohji

WEKO 26883

en Fukunaga, Kohji

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著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University
著者所属(英)
言語 en
値 Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University
著者所属(英)
言語 en
値 Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University
著者所属(英)
言語 en
値 Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University
著者所属(英)
言語 en
値 Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Faculty of Engineering/Graduate School of Engineering, Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University
抄録
内容記述タイプ Other
内容記述 α-synuclein (αSyn) is a protein known to form intracellular aggregates during the manifestation of Parkinson’s disease. Previously, it was shown that αSyn aggregation was strongly suppressed in the midbrain region of mice that did not possess the gene encoding the lipid transport protein fatty acid binding protein 3 (FABP3). An interaction between these two proteins was detected in vitro, suggesting that FABP3 may play a role in the aggregation and deposition of αSyn in neurons. In order to characterize the molecular mechanisms that underlie the interactions between FABP3 and αSyn that modulate the cellular accumulation of the latter, in this report, we used in vitro fluorescence assays combined with fluorescence microscopy, transmission electron microscopy, and quartz crystal microbalance assays to characterize in detail the process and consequences of FABP3-αSyn interaction. We demonstrated that binding of FABP3 to αSyn results in changes in the aggregation mechanism of the latter; specifically, a suppression of fibrillar forms of αSyn, and also the production of aggregates with an enhanced cytotoxicity toward mice neuro2A cells. Since this interaction involved the C-terminal sequence region of αSyn, we tested a peptide derived from this region of αSyn (αSynP130-140) as a decoy to prevent the FABP3-αSyn interaction. We observed that the peptide competitively inhibited binding of αSyn to FABP3 in vitro and in cultured cells. We propose that administration of αSynP130-140 might be used to prevent the accumulation of toxic FABP3-αSyn oligomers in cells, thereby preventing the progression of Parkinson’s disease.
書誌情報 Journal of Biological Chemistry
en : Journal of Biological Chemistry

巻 296, 発行日 2021-04-20
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 00219258
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA1202441X
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 10.1016/j.jbc.2021.100663
権利
権利情報 © 2021 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. http://creativecommons.org/licenses/by/4.0/
情報源
関連名称 Fukui, Naoya. Yamamoto, Hanae. Miyabe, Moe. et al. An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3. Journal of Biological Chemistry. 296, 100663. 2021-04-20.
関連サイト
識別子タイプ URI
関連識別子 https://www.sciencedirect.com/science/article/pii/S0021925821004518
関連名称 https://www.sciencedirect.com/science/article/pii/S0021925821004518
著者版フラグ
出版タイプ VoR
EISSN
値 1083351X
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