期刊
FEBS LETTERS
卷 578, 期 3, 页码 217-223出版社
WILEY
DOI: 10.1016/j.febslet.2004.11.003
关键词
20S proteasome; 4-hydroxynonenal; chymotrypsin-like activity; proteasome inhibition; MALDI-TOF mass spectrometry
资金
- NEI NIH HHS [EY013623] Funding Source: Medline
The proteasome is responsible for most intracellular protein degradation and is essential for cell survival. Previous research has shown that the proteasome can be inhibited by a number of oxidants, including 4-hydroxynonenal (HNE). The present study demonstrates that HNE rapidly inhibits the chymotrypsin-like activity of the 20S proteasome purified from liver. Subunits containing HNE-adducts were identified following 2D gel electrophoresis, Western immunoblotting, and analysis by MALDI-TOF MS. At a time when only the chymotrypsin-like activity was inhibited, the alpha6/C2 subunit was uniquely modified. These results provide important molecular details regarding the catalytic site-specific inhibition of proteasome by HNE. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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