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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
578
Issue
3
Identifiers
DOI: 10.1016/j.febslet.2004.11.003
Keywords
  • 20S Proteasome
  • 4-Hydroxynonenal
  • Chymotrypsin-Like Activity
  • Proteasome Inhibition
  • Maldi-Tof Mass Spectrometry
Disciplines
  • Biology

Abstract

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 α6/C2 subunit was uniquely modified. These results provide important molecular details regarding the catalytic site-specific inhibition of proteasome by HNE.

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