Item type |
学術雑誌論文 / Journal Article(1) |
公開日 |
2012-09-11 |
タイトル |
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タイトル |
Mouse Senile Amyloid Fibrils Deposited in Skeletal Muscle Exhibit Amyloidosis-Enhancing Activity |
言語 |
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言語 |
eng |
DOI |
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関連識別子 |
https://doi.org/10.1371/journal.ppat.1000914 |
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関連名称 |
10.1371/journal.ppat.1000914 |
キーワード |
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主題 |
APOLIPOPROTEIN-A-II, PATHOLOGICAL PRION PROTEIN, CREUTZFELDT-JAKOB-DISEASE, SENESCENCE-ACCELERATED MOUSE, INCLUSION-BODY MYOSITIS, AAPOAII AMYLOIDOSIS, PRPSC ACCUMULATION, TRANSGENIC MICE, INBRED STRAINS, APOA-II |
資源タイプ |
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資源 |
http://purl.org/coar/resource_type/c_6501 |
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タイプ |
journal article |
著者 |
Qian, Jinze
Yan, Jingmin
Ge, Fengxia
Zhang, Beiru
Fu, Xiaoying
Tomozawa, Hiroshi
Sawashita, Jinko
Mori, Masayuki
Higuchi, Keiichi
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信州大学研究者総覧へのリンク |
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氏名 |
Mori, Masayuki |
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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 |
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氏名 |
Higuchi, Keiichi |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.gCfUPmAh.html |
出版者 |
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出版者 |
PUBLIC LIBRARY SCIENCE |
引用 |
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内容記述 |
PLOS PATHOGENS. 6(5):e1000914 (2010) |
書誌情報 |
PLOS PATHOGENS
巻 6,
号 5,
発行日 2010-05
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抄録 |
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内容記述 |
Amyloidosis describes a group of protein folding diseases in which amyloid proteins are abnormally deposited in organs and/or tissues as fine fibrils. Mouse senile amyloidosis is a disorder in which apolipoprotein A-II (apoA-II) deposits as amyloid fibrils (AApoAII) and can be transmitted from one animal to another both by the feces and milk excreted by mice with amyloidosis. Thus, mouse AApoAII amyloidosis has been demonstrated to be a "transmissible disease". In this study, to further characterize the transmissibility of amyloidosis, AApoAII amyloid fibrils were injected into transgenic Apoa2(c)Tg(+/-) and normal R1.P1-Apoa2(c) mice to induce AApoAII systemic amyloidosis. Two months later, AApoAII amyloid deposits were found in the skeletal muscles of amyloid-affected mice, primarily in the blood vessels and in the interstitial tissues surrounding muscle fibers. When amyloid fibrils extracted from the skeletal muscles were subjected to Western blot analysis, apoA-II was detected. Amyloid fibril fractions isolated from the muscles not only demonstrated the structure of amyloid fibrils but could also induce amyloidosis in young mice depending on its fibril conformation. These findings present a possible pathogenesis of amyloidosis: transmission of amyloid fibril conformation through muscle, and shed new light on the etiology involved in amyloid disorders. |
資源タイプ(コンテンツの種類) |
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内容記述 |
Article |
ISSN |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
1553-7366 |
書誌レコードID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA12072310 |
PubMed |
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関連識別子 |
https://pubmed.ncbi.nlm.nih.gov/20502680 |
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関連名称 |
20502680 |
権利 |
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権利情報 |
Copyright © 2010 Qian et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
出版タイプ |
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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 |
WoS |
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URL |
http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000278759900033 |