Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH

Kihara, Miho; Chatani, Eri; Sakai, Miyo; Hasegawa, Kazuhiro; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M411949200

Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH

Kihara, Miho; Chatani, Eri; Sakai, Miyo et al.

Journal of Biological Chemistry, 2005, 280(12), 12012-12018

アクセス数:518件（2025-07-19 10:55 集計）

固定URL: https://hdl.handle.net/11094/71295

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タイトル	Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH
著者	著者名 Kihara, Miho
	NRID 1000000432493 1000000432493 著者名 Chatani, Eri
	著者名 Sakai, Miyo
	NRID 1000060324159 1000060324159 著者名 Hasegawa, Kazuhiro
	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. Miho Kihara, Eri Chatani, Miyo Sakai, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH. J. Biol. Chem. 2005; 280, 12012-12018. © the American Society for Biochemistry and Molecular Biology
抄録	β2-Microglobulin (β2-m) is a major component of amyloid fibrils deposited in patients with dialysis-related amyloidosis. Recent studies have focused on the mechanism by which amyloid fibrils are formed under physiological conditions, which had been difficult to reproduce quantitatively. Yamamoto et al. (Yamamoto, S., Hasegawa, K., Yamaguchi, I., Tsutsumi, S., Kardos, J., Goto, Y., Gejyo, F. & Naiki, H. (2004) Biochemistry 43, 11075-11082) showed that a combination of seed fibrils prepared under acidic conditions and a low concentration of sodium dodecyl sulfate below its critical micelle concentration enabled extensive fibril formation at pH 7.0. Here, we found that repeated self-seeding at pH 7.0 with fibrils formed at the same pH causes a marked acceleration of growth, indicating the maturation of fibrils. The observed maturation can be simulated by assuming the existence of two types of fibrils with different growth rates. Importantly, some mutations of β2-m or the addition of a low concentration of urea, both destabilizing the native conformation, were not enough to extend the fibrils at pH 7.0, and a low concentration of sodium dodecyl sulfate (i.e. 0.5 mm) was essential. Thus, even though the first stage fibrils in patients are unstable and require stabilizing factors to remain at neutral pH, they can adapt to a neutral pH with repeated self-seeding, implying a mechanism of development of amyloid deposition after a long latent period in patients.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	280(12)
ページ	12012-12018
刊行年月	2005-03
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71295
eISSN	1083351X
NCID	AA1202464X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M411949200
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(12), p. 12012-12018
DC.title	Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH
DC.creator	Kihara, Miho
	Chatani, Eri
	Sakai, Miyo
	Hasegawa, Kazuhiro
	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	2005-03
DC.identifier	https://doi.org/10.1074/jbc.M411949200
DC.description	This research was originally published in the Journal of Biological Chemistry. Miho Kihara, Eri Chatani, Miyo Sakai, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH. J. Biol. Chem. 2005; 280, 12012-12018. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	β2-Microglobulin (β2-m) is a major component of amyloid fibrils deposited in patients with dialysis-related amyloidosis. Recent studies have focused on the mechanism by which amyloid fibrils are formed under physiological conditions, which had been difficult to reproduce quantitatively. Yamamoto et al. (Yamamoto, S., Hasegawa, K., Yamaguchi, I., Tsutsumi, S., Kardos, J., Goto, Y., Gejyo, F. & Naiki, H. (2004) Biochemistry 43, 11075-11082) showed that a combination of seed fibrils prepared under acidic conditions and a low concentration of sodium dodecyl sulfate below its critical micelle concentration enabled extensive fibril formation at pH 7.0. Here, we found that repeated self-seeding at pH 7.0 with fibrils formed at the same pH causes a marked acceleration of growth, indicating the maturation of fibrils. The observed maturation can be simulated by assuming the existence of two types of fibrils with different growth rates. Importantly, some mutations of β2-m or the addition of a low concentration of urea, both destabilizing the native conformation, were not enough to extend the fibrils at pH 7.0, and a low concentration of sodium dodecyl sulfate (i.e. 0.5 mm) was essential. Thus, even though the first stage fibrils in patients are unstable and require stabilizing factors to remain at neutral pH, they can adapt to a neutral pH with repeated self-seeding, implying a mechanism of development of amyloid deposition after a long latent period in patients.
DC.format	71295
citation_title	Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH
citation_author	Kihara, Miho
	Chatani, Eri
	Sakai, Miyo
	Hasegawa, Kazuhiro
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2005-03
citation_journal_title	Journal of Biological Chemistry
citation_volume	280
citation_issue	12
citation_firstpage	12012
citation_lastpage	12018
citation_doi	https://doi.org/10.1074/jbc.M411949200
citation_public_url	https://hdl.handle.net/11094/71295

Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH

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