Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures

Ban, Tadato; Morigaki, Kenichi; Yagi, Hisashi; Kawasaki, Takashi; Kobayashi, Atsuko; Yuba, Shunsuke; Naiki, Hironobu; Goto, Yuji

doi:info:doi/10.1074/jbc.M606072200

このアイテムのアクセス数:99件（2020-10-23 15:22 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/10.1074/jbc.M606072200

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/11094/71291

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
JBC_33677-83	pdf	918 KB	115

論文情報

タイトル	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
著者	Ban, Tadato Ban, Tadato
	Morigaki, Kenichi Morigaki, Kenichi
	Yagi, Hisashi Yagi, Hisashi
	Kawasaki, Takashi Kawasaki, Takashi
	Kobayashi, Atsuko Kobayashi, Atsuko
	Yuba, Shunsuke Yuba, Shunsuke
	Naiki, Hironobu Naiki, Hironobu
	Goto, Yuji Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Tadato Ban, Kenichi Morigaki, Hisashi Yagi, Takashi Kawasaki, Atsuko Kobayashi, Shunsuke Yuba, Hironobu Naiki and Yuji Goto. Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures. J. Biol. Chem. 2006; 281, 33677–33683. © the American Society for Biochemistry and Molecular Biology
抄録	In Alzheimer disease, amyloid β, a 39-43-residue peptide produced by cleavage from a large amyloid precursor protein, undergoes conformational change to form amyloid fibrils and deposits as senile amyloid plaques in the extracellular cerebral cortices of the brain. However, the mechanism of how the intrinsically linear amyloid fibrils form spherical senile plaques is unknown. With total internal reflection fluorescence microscopy combined with the use of thioflavin T, an amyloid-specific fluorescence dye, we succeeded in observing the formation of the senile plaque-like spherulitic structures with diameters of around 15 μm on the chemically modified quartz surface. Real-time observation at a single fibrillar level revealed that, in the absence of tight contact with the surface, the cooperative and radial growth of amyloid fibrils from the core leads to a huge spherulitic structure. The results suggest the underlying physicochemical mechanism of senile plaque formation, essential for obtaining insight into prevention of Alzheimer disease.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	281
号	44
開始ページ	33677
終了ページ	33683
刊行年月	2006-11
ISSN	1083351X
NCID	AA1202460X
DOI	info:doi/10.1074/jbc.M606072200
URL	http://hdl.handle.net/11094/71291
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	Journal of Biological Chemistry.281(44) P.33677-P.33683
DC.title	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
DC.creator	Ban, Tadato
	Morigaki, Kenichi
	Yagi, Hisashi
	Kawasaki, Takashi
	Kobayashi, Atsuko
	Yuba, Shunsuke
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2006-11
DC.identifier	info:doi/10.1074/jbc.M606072200
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71291
DC.description	This research was originally published in the Journal of Biological Chemistry. Tadato Ban, Kenichi Morigaki, Hisashi Yagi, Takashi Kawasaki, Atsuko Kobayashi, Shunsuke Yuba, Hironobu Naiki and Yuji Goto. Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures. J. Biol. Chem. 2006; 281, 33677–33683. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	In Alzheimer disease, amyloid β, a 39-43-residue peptide produced by cleavage from a large amyloid precursor protein, undergoes conformational change to form amyloid fibrils and deposits as senile amyloid plaques in the extracellular cerebral cortices of the brain. However, the mechanism of how the intrinsically linear amyloid fibrils form spherical senile plaques is unknown. With total internal reflection fluorescence microscopy combined with the use of thioflavin T, an amyloid-specific fluorescence dye, we succeeded in observing the formation of the senile plaque-like spherulitic structures with diameters of around 15 μm on the chemically modified quartz surface. Real-time observation at a single fibrillar level revealed that, in the absence of tight contact with the surface, the cooperative and radial growth of amyloid fibrils from the core leads to a huge spherulitic structure. The results suggest the underlying physicochemical mechanism of senile plaque formation, essential for obtaining insight into prevention of Alzheimer disease.
citation_title	Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures
citation_author	Ban, Tadato
	Morigaki, Kenichi
	Yagi, Hisashi
	Kawasaki, Takashi
	Kobayashi, Atsuko
	Yuba, Shunsuke
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2006-11
citation_journal_title	Journal of Biological Chemistry
citation_volume	281
citation_issue	44
citation_firstpage	33677
citation_lastpage	33683
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M606072200
citation_public_url	http://hdl.handle.net/11094/71291

閲覧可能ファイル

論文情報

論文詳細を表示