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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. (C) 2009 Elsevier B.V. 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Amyloid fibrils formed by selective N-, C-terminal sequences of mouse apolipoprotein A-II
http://hdl.handle.net/10091/10791
http://hdl.handle.net/10091/107916fc50a02-43bb-4114-b51c-e9e703c4e124
名前 / ファイル | ライセンス | アクション |
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2010-11-18 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Amyloid fibrils formed by selective N-, C-terminal sequences of mouse apolipoprotein A-II | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Apolipoprotein A-II | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Mouse senile amyloidosis | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | 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× Kametani, Fuyuki× Hasegawa, Kazuhiro× Tsutsumi-Yasuhara, Shinobu× Zhang, Beiru× Yan, Jingmin× Mori, Masayuki× Naiki, Hironobu× 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 | ||||||
内容記述タイプ | Other | |||||
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 |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
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) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Article | |||||
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 | |||||
DOI | ||||||
識別子タイプ | 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 | |||||
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 | ||||||
表示名 | Web of Science | |||||
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