期刊
FEBS LETTERS
卷 579, 期 22, 页码 5029-5034出版社
WILEY
DOI: 10.1016/j.febslet.2005.08.010
关键词
p62; protein aggregation; Alzheimer's disease; sequestosome
资金
- NINDS NIH HHS [NS 33661] Funding Source: Medline
The polyubiquitin-binding protein p62 has been shown to localize in aggregates common to several types of diseases. Here, we report that p62 forms independent fibrillar aggregates in vitro in a time- and concentration-dependent manner. FTIR spectra and ThT fluorescence assay of p62 reveals increased beta-sheet content as aggregates form compared to the native protein. The fibrillar nature of the aggregates was observed by transmission electron microscopy. Overexpression of p62 in HEK cells results in aggregate formation that may protect cells from apoptosis. Altogether, these results suggest that p62 fibrils may influence cell viability and indicates an important role for p62 in aggresome formation. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据