Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils
Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils
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DOI：
10.1016/s0014-5793(04)00295-9
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发表时间：
2004-04-09
期刊：
影响因子：
3.5
通讯作者：
Higuchi, K
中科院分区：
文献类型：
--
作者：
Fu, XY;Korenaga, T;Higuchi, K
预形成的淀粉样纤维加速淀粉样前体蛋白的构象变化，并导致淀粉样纤维在体外快速延伸。我们将各种淀粉样纤维注射到具有淀粉样蛋白生成apoAII基因（Apoa2（C））的小鼠中。在注射小鼠AApoAII（C）淀粉样蛋白原纤维的小鼠组织中检测到最严重的淀粉样蛋白沉积。在注射了其他类型的原纤维（包括合成肽和重组蛋白）的小鼠组织中也检测到轻度淀粉样蛋白沉积。然而，在注射非淀粉样蛋白原纤维蛋白的小鼠中没有发现淀粉样蛋白沉积。这些结果表明，淀粉样蛋白原纤维的共同结构可以作为体内淀粉样蛋白原纤维形成的种子。(C)2004年由Elsevier B.V.代表欧洲生物化学学会联合会出版。
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.