Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity.
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 a...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2010-05-01
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| Series: | PLoS Pathogens |
| Online Access: | http://europepmc.org/articles/PMC2873911?pdf=render |
| _version_ | 1811284229853544448 |
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| author | Jinze Qian Jingmin Yan Fengxia Ge Beiru Zhang Xiaoying Fu Hiroshi Tomozawa Jinko Sawashita Masayuki Mori Keiichi Higuchi |
| author_facet | Jinze Qian Jingmin Yan Fengxia Ge Beiru Zhang Xiaoying Fu Hiroshi Tomozawa Jinko Sawashita Masayuki Mori Keiichi Higuchi |
| author_sort | Jinze Qian |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T02:26:24Z |
| format | Article |
| id | doaj.art-390f4c7cc74341289ee402d1d9fce148 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-04-13T02:26:24Z |
| publishDate | 2010-05-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-390f4c7cc74341289ee402d1d9fce1482022-12-22T03:06:46ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742010-05-0165e100091410.1371/journal.ppat.1000914Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity.Jinze QianJingmin YanFengxia GeBeiru ZhangXiaoying FuHiroshi TomozawaJinko SawashitaMasayuki MoriKeiichi HiguchiAmyloidosis 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.http://europepmc.org/articles/PMC2873911?pdf=render |
| spellingShingle | Jinze Qian Jingmin Yan Fengxia Ge Beiru Zhang Xiaoying Fu Hiroshi Tomozawa Jinko Sawashita Masayuki Mori Keiichi Higuchi Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. PLoS Pathogens |
| title | Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. |
| title_full | Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. |
| title_fullStr | Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. |
| title_full_unstemmed | Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. |
| title_short | Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. |
| title_sort | mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis enhancing activity |
| url | http://europepmc.org/articles/PMC2873911?pdf=render |
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