| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2022-06-30 |
| タイトル |
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タイトル |
Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein |
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言語 |
en |
| 言語 |
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言語 |
eng |
| キーワード |
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主題Scheme |
Other |
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主題 |
molecular chaperone |
| キーワード |
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主題Scheme |
Other |
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主題 |
human Hsp60 |
| キーワード |
|
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主題Scheme |
Other |
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主題 |
apical domain |
| キーワード |
|
|
主題Scheme |
Other |
|
主題 |
α-synuclein |
| キーワード |
|
|
主題Scheme |
Other |
|
主題 |
amyloid fibril suppression |
| キーワード |
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|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
molecular chaperone |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
human Hsp60 |
| キーワード |
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|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
apical domain |
| キーワード |
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|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
α-synuclein |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
amyloid fibril suppression |
| 資源タイプ |
|
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資源タイプ |
journal article |
| 著者 |
フクイ, ナオヤ
本郷, 邦広
溝端, 知宏
河田, 康志
Yamamoto, Hanae
Fukui, Naoya
Adachi, Mayuka
Saiki, Eiichi
Yamasaki, Anna
Matsumura, Rio
Kuroyanagi, Daichi
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| 著者所属（英） |
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言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University |
| 著者所属（英） |
|
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言語 |
en |
|
値 |
Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Faculty of Engineering, Tottori University |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University / Department of Chemistry and Biotechnology, Faculty of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University / Department of Chemistry and Biotechnology, Faculty of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry |
| 著者所属（英） |
|
|
言語 |
en |
|
値 |
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University / Department of Chemistry and Biotechnology, Faculty of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry |
| 抄録 |
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内容記述タイプ |
Other |
|
内容記述 |
Heat shock proteins play roles in assisting other proteins to fold correctly and in preventing the aggregation and accumulation of proteins in misfolded conformations. However, the process of aging significantly degrades this ability to maintain protein homeostasis. Consequently, proteins with incorrect conformations are prone to aggregate and accumulate in cells, and this aberrant aggregation of misfolded proteins may trigger various neurodegenerative diseases, such as Parkinson’s disease. Here, we investigated the possibilities of suppressing α-synuclein aggregation by using a mutant form of human chaperonin Hsp60, and a derivative of the isolated apical domain of Hsp60 (Hsp60 AD(Cys)). In vitro measurements were used to detect the effects of chaperonin on amyloid fibril formation, and interactions between Hsp60 proteins and α-synuclein were probed by quartz crystal microbalance analysis. The ability of Hsp60 AD(Cys) to suppress α-synuclein intracellular aggregation and cytotoxicity was also demonstrated. We show that Hsp60 mutant and Hsp60 AD(Cys) both effectively suppress α-synuclein amyloid fibril formation, and also demonstrate for the first time the ability of Hsp60 AD(Cys) to function as a mini-chaperone inside cells. These results highlight the possibility of using Hsp60 AD as a method of prevention and treatment of neurodegenerative diseases. |
| 書誌情報 |
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
en : INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
巻 21,
号 1,
発行日 2020-01-01
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| 出版者 |
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出版者 |
MDPI |
| DOI |
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関連タイプ |
isIdenticalTo |
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識別子タイプ |
DOI |
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関連識別子 |
10.3390/ijms21010047 |
| 権利 |
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権利情報 |
(C) 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
| 情報源 |
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関連名称 |
Yamamoto Hanae, Fukui Naoya, Adachi Mayuka, et al. Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of alpha-Synuclein. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2020. 21(1). doi:10.3390/ijms21010047 |
| 関連サイト |
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識別子タイプ |
URI |
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関連識別子 |
https://www.mdpi.com/1422-0067/21/1/47 |
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関連名称 |
https://www.mdpi.com/1422-0067/21/1/47 |
| 著者版フラグ |
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出版タイプ |
VoR |
| EISSN |
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値 |
14220067 |
ijms21(1)_ijms21010047.pdf (1.6 MB)
