Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal |
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Authors: | Ferrington Deborah A Kapphahn Rebecca J |
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Affiliation: | Department of Ophthalmology, University of Minnesota, Minneapolis, MN 55455, USA. ferri013@umn.edu |
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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. |
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Keywords: | 20S proteasome 4-Hydroxynonenal Chymotrypsin-like activity Proteasome inhibition MALDI-TOF mass spectrometry |
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