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

Biol Chem. 2008 Aug ; [Epub ahead of print]
Regulation of cathepsin K activity by hydrogen peroxide.
Godat E, Herve-Grepinet V, Veillard F, Lecaille F, Belghazi M, Bromme D, Lalmanach G.

Abstract 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 H(2)O(2) to tentatively understand these puzzling observations. H(2)O(2) 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, about 1/3 of its initial activity was restored by dithiothreitol. This incomplete inactivation may partially explain why active cysteine cathepsins are still found during acute lung inflammations.


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