IndraLab

Statements

Hypochlorous acid inhibits CTSB. 5 / 5
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"Thus, the data indicate that HOCl modified LDL inactivates cathepsin B by a chloramine dependent mechanism, most likely via oxidation of the enzyme 's critical cysteine residue."
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"Thus, inactivation of cathepsin B by HOCl modified LDL can be inhibited by ascorbic and lipoic acids, likely via elimination of LDL associated chloramines.DISCUSSIONThis study shows for the first time that HOCl modified LDL can inactivate the lysosomal protease cathepsin B and that LDL associated chloramines are likely involved in this process."
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"Inactivation of cathepsin B by HOCl modified LDL was very rapid, occurring within 1 min of incubation at ambient temperature (data not shown)."
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"Ascorbic and lipoic acids protect against inactivation of cathepsin B by HOCl modified LDL."
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"Finally, it is of interest to note that epitopes to MPO and HOCl modified LDL colocalize within monocyte and macrophages in vivo.13,14,43 CONCLUSIONSThe results of this study show that HOCl modified LDL can inactivate the lysosomal cysteine protease cathepsin B by a chloramine dependent mechanism."
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