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:https://doi.org/10.1038/srep30473

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

Araki, Katsuya; Yagi, Naoto; Nakatani, Rie et al.

Scientific Reports, 2016, 6, 30473

アクセス数:1,250件（2025-07-12 00:12 集計）

固定URL: https://hdl.handle.net/11094/71266

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タイトル	A small-angle X-ray scattering study of alpha-synuclein from human red blood cells
著者	NRID 1000050649431 1000050649431 著者名 Araki, Katsuya
	NRID 1000080133940 1000080133940 著者名 Yagi, Naoto
	著者名 Nakatani, Rie
	NRID 1000000401563 1000000401563 著者名 Sekiguchi, Hiroshi
	著者名 So, Masatomo
	NRID 1000010432494 1000010432494 著者名 Yagi, Hisashi
	NRID 1000090353507 1000090353507 著者名 Ohta, Noboru
	NRID 1000060335354 1000060335354 著者名 Nagai, Yoshitaka
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
	NRID 1000090230044 1000090230044 ORCID 0000-0002-0874-7542 0000-0002-0874-7542 researchmap permalink read0207787 read0207787 Scopus Author ID 7202006099 7202006099 著者名 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.
出版者	Springer Nature
収録物名	Scientific Reports
巻(号)	6
ページ	30473
刊行年月	2016-07
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71266
eISSN	20452322
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1038/srep30473
アクセス権	open access
権利情報	© 2016 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

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. 2016, 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
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2016-07
DC.identifier	https://doi.org/10.1038/srep30473
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	© 2016 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	71266
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_doi	https://doi.org/10.1038/srep30473
citation_public_url	https://hdl.handle.net/11094/71266

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

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