Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin

Ohhashi, Yumiko; Kihara, Miho; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M506501200

Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin

Ohhashi, Yumiko; Kihara, Miho; Naiki, Hironobu et al.

Journal of Biological Chemistry, 2005, 280(38), 32843-32848

アクセス数:567件（2025-07-08 11:40 集計）

固定URL: https://hdl.handle.net/11094/71293

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タイトル	Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin
著者	NRID 1000010422669 1000010422669 著者名 Ohhashi, Yumiko
	著者名 Kihara, Miho
	NRID 1000010227704 1000010227704 著者名 Naiki, Hironobu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Miho Kihara, Hironobu Naiki and Yuji Goto. Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin. J. Biol. Chem. 2005; 280, 32843-32848. © the American Society for Biochemistry and Molecular Biology
抄録	To obtain insight into the mechanism of fibril formation, we examined the effects of ultrasonication, a strong agitator, on β2 -microglobulin (β2-m), a protein responsible for dialysis-related amyloidosis. Upon sonication of an acid-unfolded β2-m solution at pH 2.5, thioflavin T fluorescence increased markedly after a lag time of 1–2 h with a simultaneous increase of light scattering. Atomic force microscopy images showed the formation of a large number of short fibrils 3 nm in diameter. When the sonication-induced fibrils were used as seeds in the next seeding experiment at pH 2.5, a rapid and intense formation of long fibrils 3 nm in diameter was observed demonstrating seed-dependent fibril growth. We then examined the effects of sonication on the native β2-m at neutral pH, conditions under which amyloid deposits occur in patients. In the presence of 0.5 mm sodium dodecyl sulfate, a model compound of potential trigger and stabilizer of amyloid fibrils in patients, a marked increase of thioflavin T fluorescence was observed after 1 day of sonication at pH 7.0. The products of sonication caused the accelerated fibril formation at pH 7.0. Atomic force microscopy images showed that the fibrils formed at pH 7.0 have a diameter of more than 7 nm, thicker than those prepared at pH 2.5. These results indicate that ultrasonication is one form of agitation triggering the formation of amyloid fibrils of β2-m, producing fibrils adapted to the respective pH.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	280(38)
ページ	32843-32848
刊行年月	2005-09
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71293
eISSN	1083351X
NCID	AA1202462X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M506501200
アクセス権	open access
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	Journal of Biological Chemistry. 2005, 280(38), p. 32843-32848
DC.title	Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin
DC.creator	Ohhashi, Yumiko
	Kihara, Miho
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2005-09
DC.identifier	https://doi.org/10.1074/jbc.M506501200
DC.description	This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Miho Kihara, Hironobu Naiki and Yuji Goto. Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin. J. Biol. Chem. 2005; 280, 32843-32848. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	To obtain insight into the mechanism of fibril formation, we examined the effects of ultrasonication, a strong agitator, on β2 -microglobulin (β2-m), a protein responsible for dialysis-related amyloidosis. Upon sonication of an acid-unfolded β2-m solution at pH 2.5, thioflavin T fluorescence increased markedly after a lag time of 1–2 h with a simultaneous increase of light scattering. Atomic force microscopy images showed the formation of a large number of short fibrils 3 nm in diameter. When the sonication-induced fibrils were used as seeds in the next seeding experiment at pH 2.5, a rapid and intense formation of long fibrils 3 nm in diameter was observed demonstrating seed-dependent fibril growth. We then examined the effects of sonication on the native β2-m at neutral pH, conditions under which amyloid deposits occur in patients. In the presence of 0.5 mm sodium dodecyl sulfate, a model compound of potential trigger and stabilizer of amyloid fibrils in patients, a marked increase of thioflavin T fluorescence was observed after 1 day of sonication at pH 7.0. The products of sonication caused the accelerated fibril formation at pH 7.0. Atomic force microscopy images showed that the fibrils formed at pH 7.0 have a diameter of more than 7 nm, thicker than those prepared at pH 2.5. These results indicate that ultrasonication is one form of agitation triggering the formation of amyloid fibrils of β2-m, producing fibrils adapted to the respective pH.
DC.format	71293
citation_title	Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin
citation_author	Ohhashi, Yumiko
	Kihara, Miho
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2005-09
citation_journal_title	Journal of Biological Chemistry
citation_volume	280
citation_issue	38
citation_firstpage	32843
citation_lastpage	32848
citation_doi	https://doi.org/10.1074/jbc.M506501200
citation_public_url	https://hdl.handle.net/11094/71293

Ultrasonication-induced Amyloid Fibril Formation of β2-Microglobulin

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