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Regulation of cathepsin K activity by hydrogen (...)

Biol Chem. 2008 Aug ;389(8):1123-6
Regulation of cathepsin K activity by hydrogen peroxide.
Godat E, Herve-Grvepinet V, Veillard F, Lecaille F, Belghazi M, Bromme D, Lalmanach G.

Although cysteine cathepsins, including cathepsin K, are sensitive to oxidation, proteolytically active forms are found at inflammatory sites. Regulation of cathepsin K activity was analyzed in the presence of H2O2 to gain an insight into these puzzling observations. H2O2 impaired processing of procathepsin K and inactivated its mature form in a time- and dose-dependent mode. However, as a result of the formation of a sulfenic acid, as confirmed by trapping in the presence of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazol, approximately one-third of its initial activity was restored by dithiothreitol. This incomplete inactivation may partially explain why active cysteine cathepsins are still found during acute lung inflammation.


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