Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils

被引:35
作者
Fu, XY
Korenaga, T
Fu, L
Xing, YM
Guo, ZJ
Matsushita, T
Hosokawa, M
Naiki, H
Baba, S
Kawata, Y
Ikeda, S
Ishihara, T
Mori, M
Higuchi, K
机构
[1] Shinshu Univ, Inst Aging & Adapt, Dept Aging Biol, Grad Sch Med, Matsumoto, Nagano 3908621, Japan
[2] Kyoto Univ, Inst Frontier Med Sci, Field Regenerat Control, Kyoto 6068507, Japan
[3] Aichi Human Serv Ctr, Inst Dev Res, Dept Pathol, Kasugai, Aichi 4800392, Japan
[4] Fukui Med Univ, Dept Pathol, Matsuoka, Fukui 9101193, Japan
[5] Hamamatsu Univ Sch Med, Dept Pathol 2, Hamamatsu, Shizuoka 4313192, Japan
[6] Tottori Univ, Fac Engn, Dept Biotechnol, Tottori 6808552, Japan
[7] Shinshu Univ, Sch Med, Dept Med 3, Matsumoto, Nagano 3908621, Japan
[8] Yamaguchi Univ, Sch Med, Dept Pathol 1, Ube, Yamaguchi 7558505, Japan
关键词
amyloid fibril; AApoAII amyloidosis; induction; common structure;
D O I
10.1016/S0014-5793(04)00295-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Preformed amyloid fibrils accelerate conformational changes of amyloid precursor proteins and result in rapid extension of amyloid fibrils in vitro. We injected various kinds of amyloid fibrils into mice with amyloidogenic apoAII gene (Apoa2(C)). The most severe amyloid depositions were detected in the tissues of mice injected with mouse AApoAII(C) amyloid fibrils. Mild amyloid depositions were also detected in the tissues of mice that were injected with other types of fibrils, including synthetic peptides and recombinant proteins. However, no amyloid depositions were found in mice that were injected with non-amyloid fibril proteins. These results demonstrated that a common structure of amyloid fibrils could serve as a seed for amyloid fibril formation in vivo. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:179 / 184
页数:6
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