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FEBS Lett. 2004 Dec 17;578(3):217-23.

Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.

Author information

1
Department of Ophthalmology, University of Minnesota, Minneapolis, MN 55455, USA. ferri013@umn.edu

Abstract

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 alpha 6/C2 subunit was uniquely modified. These results provide important molecular details regarding the catalytic site-specific inhibition of proteasome by HNE.

PMID:
15589823
DOI:
10.1016/j.febslet.2004.11.003
[Indexed for MEDLINE]
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