| Literature DB >> 15063745 |
Xiaoying Fu1, Tatsumi Korenaga, Li Fu, Yanming Xing, Zhanjun Guo, Takatoshi Matsushita, Masanori Hosokawa, Hironobu Naiki, Satoshi Baba, Yasushi Kawata, Shu-Ichi Ikeda, Tokuhiro Ishihara, Masayuki Mori, Keiichi Higuchi.
Abstract
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.Entities:
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Year: 2004 PMID: 15063745 DOI: 10.1016/S0014-5793(04)00295-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124