期刊
BIOLOGICAL CHEMISTRY
卷 389, 期 8, 页码 1123-1126出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2008.109
关键词
cysteine cathepsin; inflammation; oxidation; protease; proteolysis; sulfenic acid
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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