A small-angle X-ray scattering study of alpha-synuclein from human red blood cells

Araki, Katsuya; Yagi, Naoto; Nakatani, Rie; Sekiguchi, Hiroshi; So, Masatomo; Yagi, Hisashi; Ohta, Noboru; Nagai, Yoshitaka; Goto, Yuji; Mochizuki, Hideki

doi:info:doi/10.1038/srep30473

このアイテムのアクセス数:105件（2020-11-01 07:42 集計）

このアイテムへのリンクには次のURLをご利用ください:https://doi.org/10.1038/srep30473

このアイテムへのリンクには次のURLをご利用ください:http://hdl.handle.net/11094/71266

閲覧可能ファイル

ファイル	フォーマット	サイズ	閲覧回数	説明
SR_6_30473	pdf	1.27 MB	113

論文情報

タイトル	A small-angle X-ray scattering study of alpha-synuclein from human red blood cells
著者	Araki, Katsuya Araki, Katsuya
	Yagi, Naoto Yagi, Naoto
	Nakatani, Rie Nakatani, Rie
	Sekiguchi, Hiroshi Sekiguchi, Hiroshi
	So, Masatomo So, Masatomo
	Yagi, Hisashi Yagi, Hisashi
	Ohta, Noboru Ohta, Noboru
	Nagai, Yoshitaka Nagai, Yoshitaka
	Goto, Yuji Goto, Yuji
	Mochizuki, Hideki Mochizuki, Hideki
内容	Katsuya Araki, Naoto Yagi, Rie Nakatani, Hiroshi Sekiguchi, Masatomo So, Hisashi Yagi, Noboru Ohta, Yoshitaka Nagai, Yuji Goto & Hideki Mochizuki "A small-angle X-ray scattering study of alpha-synuclein from human red blood cells", Scientific Reports, volume 6, Article number: 30473, Springer Nature, 2016
抄録	α-synuclein (α-syn) is the main component of Lewy bodies, which are neuropathological hallmarks of patients with Parkinson’s disease. As it has been controversial whether human α-syn from erythrocytes exists as a tetramer under physiological conditions, we tried solving this issue by the small-angle X-ray solution scattering method. Under two different conditions (high ionic strength with a Tris buffer and low ionic strength with an ammonium acetate buffer), no evidence was found for the presence of tetramer. When comparing erythrocyte and recombinant α-syn molecules, we found no significant difference of the molecular weight and the secondary structure although the buffer conditions strongly affect the radius of gyration of the protein. The results indicate that, even though a stable tetramer may not be formed, conformation of α-syn depends much on its environment, which may be the reason for its tendency to aggregate in cells.
公開者	Springer Nature
掲載誌名	Scientific Reports
巻	6
開始ページ	30473
刊行年月	2016-07
ISSN	20452322
DOI	info:doi/10.1038/srep30473
URL	http://hdl.handle.net/11094/71266
権利情報	This article is licensed under a Creative Commons Attribution 4.0 International License.
言語	英語
カテゴリ	学術雑誌論文 Journal Article

著者版フラグ	publisher
NII資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
dcmi資源タイプ	text
DCTERMS.bibliographicCitation	Scientific Reports.6 P.30473
DC.title	A small-angle X-ray scattering study of alpha-synuclein from human red blood cells
DC.creator	Araki, Katsuya
	Yagi, Naoto
	Nakatani, Rie
	Sekiguchi, Hiroshi
	So, Masatomo
	Yagi, Hisashi
	Ohta, Noboru
	Nagai, Yoshitaka
	Goto, Yuji
	Mochizuki, Hideki
DC.publisher	Springer Nature
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2016-07
DC.identifier	info:doi/10.1038/srep30473
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71266
DC.description	Katsuya Araki, Naoto Yagi, Rie Nakatani, Hiroshi Sekiguchi, Masatomo So, Hisashi Yagi, Noboru Ohta, Yoshitaka Nagai, Yuji Goto & Hideki Mochizuki "A small-angle X-ray scattering study of alpha-synuclein from human red blood cells", Scientific Reports, volume 6, Article number: 30473, Springer Nature, 2016
DCTERMS.abstract	α-synuclein (α-syn) is the main component of Lewy bodies, which are neuropathological hallmarks of patients with Parkinson’s disease. As it has been controversial whether human α-syn from erythrocytes exists as a tetramer under physiological conditions, we tried solving this issue by the small-angle X-ray solution scattering method. Under two different conditions (high ionic strength with a Tris buffer and low ionic strength with an ammonium acetate buffer), no evidence was found for the presence of tetramer. When comparing erythrocyte and recombinant α-syn molecules, we found no significant difference of the molecular weight and the secondary structure although the buffer conditions strongly affect the radius of gyration of the protein. The results indicate that, even though a stable tetramer may not be formed, conformation of α-syn depends much on its environment, which may be the reason for its tendency to aggregate in cells.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
citation_title	A small-angle X-ray scattering study of alpha-synuclein from human red blood cells
citation_author	Araki, Katsuya
	Yagi, Naoto
	Nakatani, Rie
	Sekiguchi, Hiroshi
	So, Masatomo
	Yagi, Hisashi
	Ohta, Noboru
	Nagai, Yoshitaka
	Goto, Yuji
	Mochizuki, Hideki
citation_publisher	Springer Nature
citation_language	英語
citation_date	2016-07
citation_journal_title	Scientific Reports
citation_volume	6
citation_firstpage	30473
citation_issn	20452322
citation_doi	info:doi/10.1038/srep30473
citation_public_url	http://hdl.handle.net/11094/71266

閲覧可能ファイル

論文情報

論文詳細を表示