{"created":"2023-08-02T03:58:05.208507+00:00","id":7228,"links":{},"metadata":{"_buckets":{"deposit":"2fb7d33a-b44a-47f0-9874-579356d60150"},"_deposit":{"created_by":10,"id":"7228","owners":[10],"pid":{"revision_id":0,"type":"depid","value":"7228"},"status":"published"},"_oai":{"id":"oai:repository.lib.tottori-u.ac.jp:00007228","sets":["1:10","2:12"]},"author_link":["26773","779","2225","1457","26774","26775","26776","26777","26778","26779","26780"],"item_10001_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2020-01-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"1","bibliographicVolumeNumber":"21","bibliographic_titles":[{"bibliographic_title":"INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES"},{"bibliographic_title":"INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES","bibliographic_titleLang":"en"}]}]},"item_10001_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"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.","subitem_description_type":"Other"}]},"item_10001_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"MDPI"}]},"item_10001_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.3390/ijms21010047","subitem_relation_type_select":"DOI"}}]},"item_10001_relation_16":{"attribute_name":"情報源","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"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"}]}]},"item_10001_relation_17":{"attribute_name":"関連サイト","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"https://www.mdpi.com/1422-0067/21/1/47"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://www.mdpi.com/1422-0067/21/1/47","subitem_relation_type_select":"URI"}}]},"item_10001_rights_15":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"(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/)."}]},"item_10001_text_26":{"attribute_name":"EISSN","attribute_value_mlt":[{"subitem_text_value":"14220067"}]},"item_10001_text_33":{"attribute_name":"著者所属(英)","attribute_value_mlt":[{"subitem_text_language":"en","subitem_text_value":"Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Chemistry and Biotechnology, Faculty of Engineering, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"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"},{"subitem_text_language":"en","subitem_text_value":"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"},{"subitem_text_language":"en","subitem_text_value":"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"}]},"item_10001_version_type_20":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"フクイ, ナオヤ","creatorNameLang":"ja-Kana"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"本郷, 邦広"},{"creatorName":"ホンゴ, クニヒロ","creatorNameLang":"ja-Kana"},{"creatorName":"Hongo, Kunihiro","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"溝端, 知宏"},{"creatorName":"ミゾバタ, トモヒロ","creatorNameLang":"ja-Kana"},{"creatorName":"Mizobata, Tomohiro","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"河田, 康志"},{"creatorName":"カワタ, ヤスシ","creatorNameLang":"ja-Kana"},{"creatorName":"Kawata, Yasushi","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"Yamamoto, Hanae","creatorNameLang":"en"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Fukui, Naoya","creatorNameLang":"en"},{"creatorName":"フクイ, ナオヤ","creatorNameLang":"ja-Kana"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Adachi, Mayuka","creatorNameLang":"en"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Saiki, Eiichi","creatorNameLang":"en"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Yamasaki, Anna","creatorNameLang":"en"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Matsumura, Rio","creatorNameLang":"en"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Kuroyanagi, Daichi","creatorNameLang":"en"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2023-03-17"}],"displaytype":"detail","filename":"ijms21(1)_ijms21010047.pdf","filesize":[{"value":"1.6 MB"}],"format":"application/pdf","licensefree":"(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/).","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"ijms21(1)_ijms21010047.pdf","url":"https://repository.lib.tottori-u.ac.jp/record/7228/files/ijms21(1)_ijms21010047.pdf"},"version_id":"0d466177-e932-4f54-9c45-815a555f29cb"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"molecular chaperone","subitem_subject_scheme":"Other"},{"subitem_subject":"human Hsp60","subitem_subject_scheme":"Other"},{"subitem_subject":"apical domain","subitem_subject_scheme":"Other"},{"subitem_subject":"α-synuclein","subitem_subject_scheme":"Other"},{"subitem_subject":"amyloid fibril suppression","subitem_subject_scheme":"Other"},{"subitem_subject":"molecular chaperone","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"human Hsp60","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"apical domain","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"α-synuclein","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"amyloid fibril suppression","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article"}]},"item_title":"Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein","subitem_title_language":"en"}]},"item_type_id":"10001","owner":"10","path":["12","10"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2022-06-30"},"publish_date":"2022-06-30","publish_status":"0","recid":"7228","relation_version_is_last":true,"title":["Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein"],"weko_creator_id":"10","weko_shared_id":-1},"updated":"2023-09-29T00:40:18.317717+00:00"}