Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils.
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.
Fu
Xiaoying
X
Department of Aging Biology, Institute on Aging and Adaptation, Shinshu University Graduate School of Medicine, Asahi 3-1-1, Matsumoto 390-8621, Japan.
Korenaga
Tatsumi
T
Fu
Li
L
Xing
Yanming
Y
Guo
Zhanjun
Z
Matsushita
Takatoshi
T
Hosokawa
Masanori
M
Naiki
Hironobu
H
Baba
Satoshi
S
Kawata
Yasushi
Y
Ikeda
Shu-Ichi
S
Ishihara
Tokuhiro
T
Mori
Masayuki
M
Higuchi
Keiichi
K
D000682:Amyloid / Q000378:metabolism* / Q000648:ultrastructure; D000686:Amyloidosis / Q000235:genetics* / Q000473:pathology*; D000818:Animals; D016633:Apolipoprotein A-II / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D005260:Female; D006801:Humans; D007267:Injections; D051379:Mice; D008817:Mice, Mutant Strains; D010455:Peptides / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000378:metabolism
D000682:Amyloid; D016633:Apolipoprotein A-II; D010455:Peptides; D011994:Recombinant Proteins