Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond

Hong, Dong-Pyo; Gozu, Masayo; Hasegawa, Kazuhiro; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M200188200

Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond

Hong, Dong-Pyo; Gozu, Masayo; Hasegawa, Kazuhiro et al.

Journal of Biological Chemistry, 2002, 277(24), 21554-21560

Number of Access:545（2025-08-30 01:43 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71302

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Title	Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond
Creator	CreatorName Hong, Dong-Pyo
	CreatorName Gozu, Masayo
	NRID 1000060324159 1000060324159 CreatorName Hasegawa, Kazuhiro
	NRID 1000010227704 1000010227704 CreatorName Naiki, Hironobu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
Description	This research was originally published in the Journal of Biological Chemistry. Dong-Pyo Hong, Masayo Gozu, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond. J. Biol. Chem. 2002; 277, 21554-21560. © the American Society for Biochemistry and Molecular Biology
Abstract	β2-Microglobulin (β2-m), a major component of dialysis-related amyloid fibrils, has an intrachain disulfide bond buried inside the native structure. We examined the conformation of β2-m amyloid fibrils by analyzing the reactivity of the disulfide bond to a reducing reagent, dithiothreitol. Although the disulfide bond in the native structure was highly protected from reduction, the disulfide bonds in the amyloid fibrils prepared at pH 2.5 were progressively reduced at pH 8.5 by 50 mmdithiothreitol. Because β2-m amyloid fibrils prepared under acidic conditions have been known to depolymerize at a neutral pH, we examined the relation between depolymerization and reduction of the disulfide bond. The results indicate that the disulfide bonds in the amyloid fibrils were protected from reduction, and the reduction occurred during depolymerization. On the other hand, the disulfide bonds of immature filaments, the thin and flexible filaments prepared under conditions of high salt at pH 2.5, were reduced at pH 8.5 more readily than those of amyloid fibrils, suggesting that the disulfide bonds are exposed to the solvent. Taken together, the disulfide bond once exposed to the solvent upon acid denaturation may be progressively buried in the interior of the amyloid fibrils during its formation.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	277(24)
Page	21554-21560
Date of Issued	2002-06
Language	English
Handle URL	https://hdl.handle.net/11094/71302
eISSN	1083351X
NCID	AA1202471X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M200188200
Access Rights	open access
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2002, 277(24), p. 21554-21560
DC.title	Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond
DC.creator	Hong, Dong-Pyo
	Gozu, Masayo
	Hasegawa, Kazuhiro
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2002-06
DC.identifier	https://doi.org/10.1074/jbc.M200188200
DC.description	This research was originally published in the Journal of Biological Chemistry. Dong-Pyo Hong, Masayo Gozu, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond. J. Biol. Chem. 2002; 277, 21554-21560. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	β2-Microglobulin (β2-m), a major component of dialysis-related amyloid fibrils, has an intrachain disulfide bond buried inside the native structure. We examined the conformation of β2-m amyloid fibrils by analyzing the reactivity of the disulfide bond to a reducing reagent, dithiothreitol. Although the disulfide bond in the native structure was highly protected from reduction, the disulfide bonds in the amyloid fibrils prepared at pH 2.5 were progressively reduced at pH 8.5 by 50 mmdithiothreitol. Because β2-m amyloid fibrils prepared under acidic conditions have been known to depolymerize at a neutral pH, we examined the relation between depolymerization and reduction of the disulfide bond. The results indicate that the disulfide bonds in the amyloid fibrils were protected from reduction, and the reduction occurred during depolymerization. On the other hand, the disulfide bonds of immature filaments, the thin and flexible filaments prepared under conditions of high salt at pH 2.5, were reduced at pH 8.5 more readily than those of amyloid fibrils, suggesting that the disulfide bonds are exposed to the solvent. Taken together, the disulfide bond once exposed to the solvent upon acid denaturation may be progressively buried in the interior of the amyloid fibrils during its formation.
DC.format	71302
citation_title	Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond
citation_author	Hong, Dong-Pyo
	Gozu, Masayo
	Hasegawa, Kazuhiro
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2002-06
citation_journal_title	Journal of Biological Chemistry
citation_volume	277
citation_issue	24
citation_firstpage	21554
citation_lastpage	21560
citation_doi	https://doi.org/10.1074/jbc.M200188200
citation_public_url	https://hdl.handle.net/11094/71302

Conformation of β2-Microglobulin Amyloid Fibrils Analyzed by Reduction of the Disulfide Bond

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