| Item type |
学術雑誌論文 / Journal Article.(1) |
| 公開日 |
2021-03-09 |
| 書誌情報 |
en : INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
巻 22,
号 3,
発行日 2021
|
| タイトル |
|
|
タイトル |
Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
amyloid A amyloidosis |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
amyloid enhancing factor |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
homology |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
serum amyloid A |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
quantum-dot |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| アクセス権 |
|
|
アクセス権 |
open access |
|
アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 著者 |
リン, シュウグアン
WATANABE, Kenichi
倉賀野, 正弘
徳樂, 清孝
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| 室蘭工業大学研究者データベースへのリンク |
|
|
表示名 |
徳樂 清孝（TOKURAKU Kiyotaka） |
|
URL |
http://rdsoran.muroran-it.ac.jp/html/100000137_ja.html |
| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-beta structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species. Serum amyloid A (SAA) is one of the most important precursor amyloid proteins and plays a vital step in AA amyloidosis. Amyloid enhancing factor (AEF) serves as a seed for fibril formation and shortens the onset of AA amyloidosis sharply. In this study, we examined whether AEFs extracted and purified from five animal species (camel, cat, cattle, goat, and mouse) could promote mouse SAA (mSAA) protein aggregation in vitro using quantum-dot (QD) nanoprobes to visualize the aggregation. The results showed that AEFs shortened and promoted mSAA aggregation. In addition, mouse and cat AEFs showed higher mSAA aggregation-promoting activity than the camel, cattle, and goat AEFs. Interestingly, homology analysis of SAA in these five animal species revealed a more similar amino acid sequence homology between mouse and cat than between other animal species. Furthermore, a detailed comparison of amino acid sequences suggested that it was important to mSAA aggregation-promoting activity that the 48th amino acid was a basic residue (Lys) and the 125th amino acid was an acidic residue (Asp or Glu). These data imply that AA amyloidosis exhibits higher transmission activity among animals carrying genetically homologous SAA gene, and may provide a new understanding of the pathogenesis of amyloidosis. |
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言語 |
en |
| 出版者 |
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出版者 |
MDPI |
|
言語 |
en |
| 出版者版へのリンク |
|
|
表示名 |
10.3390/ijms22031036 |
|
URL |
https://doi.org/10.3390/ijms22031036 |
| DOI |
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|
関連タイプ |
isIdenticalTo |
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|
識別子タイプ |
DOI |
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関連識別子 |
10.3390/ijms22031036 |
| 日本十進分類法 |
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|
主題Scheme |
NDC |
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主題 |
499 |
| 権利 |
|
|
言語 |
en |
|
権利情報 |
©2021 by the authors; licensee MDPI AG, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution License(http://creativecommons.org/licenses/by/4.0/) |
| 著者版フラグ |
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|
出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| フォーマット |
|
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内容記述タイプ |
Other |
|
内容記述 |
application/pdf |
IJMS_22_1036 (3.6 MB)
