AI Article Synopsis
- The degradation of oxidized proteins is vital for cell antioxidant defenses, with 4-hydroxy-2-nonenal being a harmful byproduct of lipid peroxidation.
- Research shows that this modified protein can be broken down by both the ubiquitin-proteasome pathway and lysosomal pathway, but previous studies indicated cathepsin G specifically degrades it in U937 cells.
- In this study, cathepsin G was confirmed as the enzyme responsible for degrading 4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase, highlighting its significant role in managing cellular damage.
Article Abstract
Degradation of oxidized or oxidatively modified proteins is an essential part of the antioxidant defenses of cells. 4-Hydroxy-2-nonenal, a major reactive aldehyde formed by lipid peroxidation, causes many types of cellular damage. It has been reported that 4-hydroxy-2-nonenal-modified proteins are degraded by the ubiquitin-proteasome pathway or, in some cases, by the lysosomal pathway. However, our previous studies using U937 cells showed that 4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G. In the present study, we isolated the 4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase-degrading enzyme from rat neutrophils to an active protein fraction of 28 kDa. Using the specific antibody, the 28 kDa protein was identified as cathepsin G. Moreover, the degradation activity was inhibited by cathepsin G inhibitors. These results suggest that cathepsin G plays a crucial role in the degradation of 4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166769 | PMC |
| http://dx.doi.org/10.1155/2011/213686 | DOI Listing |
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