Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050237 | FEBS Letters | 2008 | 6 Pages |
Abstract
The resistance of secreted cysteine cathepsins to peroxide inactivation was evaluated using as model THP-1 cells. Differentiated cells released mostly cathepsin B, but also cathepsins H, K, and L, with a maximum of endopeptidase activity at day 6. Addition of non-cytotoxic concentrations of H2O2 did not affect mRNA expression levels and activity of cathepsins, while the catalase activity remained also unchanged, consistently with RT-PCR analysis. Conversely inhibition of extracellular catalase led to a striking inactivation of secreted cysteine cathepsins by H2O2. This report suggests that catalase may participate in the protection of extracellular cysteine proteases against peroxidation.
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Authors
Virginie Hervé-Grépinet, Florian Veillard, Emmanuel Godat, Nathalie Heuzé-Vourc’h, Fabien Lecaille, Gilles Lalmanach,