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  1. 050 医学部, 大学院医学系研究科
  2. 0501 学術論文

Amyloid fibrils formed by selective N-, C-terminal sequences of mouse apolipoprotein A-II

http://hdl.handle.net/10091/10791
http://hdl.handle.net/10091/10791
6fc50a02-43bb-4114-b51c-e9e703c4e124
名前 / ファイル ライセンス アクション
Amyloid_fibrils_formed_selective_N-C-terminal.pdf Amyloid_fibrils_formed_selective_N-C-terminal.pdf (901.5 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2010-11-18
タイトル
タイトル Amyloid fibrils formed by selective N-, C-terminal sequences of mouse apolipoprotein A-II
言語
言語 eng
DOI
関連識別子 https://doi.org/10.1016/j.bbapap.2009.06.028
関連名称 10.1016/j.bbapap.2009.06.028
キーワード
主題 Apolipoprotein A-II, Mouse senile amyloidosis, Fibril conformation
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
著者 Sawashita, Jinko

× Sawashita, Jinko

en Sawashita, Jinko

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Kametani, Fuyuki

× Kametani, Fuyuki

en Kametani, Fuyuki

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Hasegawa, Kazuhiro

× Hasegawa, Kazuhiro

en Hasegawa, Kazuhiro

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Tsutsumi-Yasuhara, Shinobu

× Tsutsumi-Yasuhara, Shinobu

en Tsutsumi-Yasuhara, Shinobu

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Zhang, Beiru

× Zhang, Beiru

en Zhang, Beiru

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Yan, Jingmin

× Yan, Jingmin

en Yan, Jingmin

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Mori, Masayuki

× Mori, Masayuki

en Mori, Masayuki

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Naiki, Hironobu

× Naiki, Hironobu

en Naiki, Hironobu

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Higuchi, Keiichi

× Higuchi, Keiichi

en Higuchi, Keiichi

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信州大学研究者総覧へのリンク
氏名 Mori, Masayuki
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.OpSCZafV.html
信州大学研究者総覧へのリンク
氏名 Higuchi, Keiichi
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.gCfUPmAh.html
出版者
出版者 ELSEVIER SCIENCE BV
引用
内容記述 BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. 1794(10):1517-1529 (2009)
書誌情報 BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

巻 1794, 号 10, p. 1517-1529, 発行日 2009-10
抄録
内容記述 In mice, amyloidogenic type C apolipoprotein A-II (apoA-II) forms amyloid fibrils in age-associated amyloidosis. To understand the mechanism of amyloid fibril formation by apoA-II, we examined the polymerization of synthetic partial peptides of apoA-II in vitro. None of the partial apoA-II peptides polymerized into amyloid fibrils when tested as a single species mixture. We found a unique mechanism in which N- and C-terminal peptides associated into amyloid fibrils in a 1:1 ratio at pH 2.5. The 11-residue amino acid sequence (6-16), which is a common sequence of type B apoA-II and type C apoA-II proteins in amyloidosis-resistant mice and amyloidosis-susceptible mice, respectively, was critical for polymerization into amyloid fibrils. The 18-residue-long amino acid sequence (48-65) is also necessary for nucleation, but not for the extension phase. These findings suggest that there may be different mechanisms underlying the nucleation and extension phases of apoA-II amyloid fibril formation. We also found that amino acid substitutions between type B apoA-II (Pro5, Val38) and type C apoA-II (Gln5, Ala38) did not affect either phase. The strategy of using synthetic partial peptides of amyloidogenic proteins in vitro is a useful system for understanding amyloid fibril formation and for the development of novel therapies.
資源タイプ(コンテンツの種類)
ISSN
収録物識別子タイプ PISSN
収録物識別子 1570-9639
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA11685085
PubMed
識別子タイプ PMID
関連識別子 https://pubmed.ncbi.nlm.nih.gov/19596087
関連名称 19596087
権利
権利情報 Copyright (c) 2009 Elsevier B.V.
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
WoS
URL http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000270259000017
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