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Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils
Author(s) -
Fu Xiaoying,
Korenaga Tatsumi,
Fu Li,
Xing Yanming,
Guo Zhanjun,
Matsushita Takatoshi,
Hosokawa Masanori,
Naiki Hironobu,
Baba Satoshi,
Kawata Yasushi,
Ikeda Shu-ichi,
Ishihara Tokuhiro,
Mori Masayuki,
Higuchi Keiichi
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00295-9
Subject(s) - fibril , amyloid (mycology) , amyloidosis , amyloid fibril , chemistry , in vitro , amyloid disease , in vivo , biophysics , p3 peptide , biochemistry , biochemistry of alzheimer's disease , amyloid β , amyloid precursor protein , pathology , biology , alzheimer's disease , medicine , inorganic chemistry , microbiology and biotechnology , disease
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.