IndraLab

Statements

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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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"AA = ascorbic acid, LA = lipoic acid, Lys = lysine, LysCA = Nαacetyl-lysine chloramine. HOCl-modified LDL inactivates the lysosomal protease cathepsin B 347 Cathepsin B (% control) RNHCl (µM) 100 60 75 45 50 30 25 15 00 0 50 100 150 200 AA or LA (µM) Fig. 4."
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"31 The mechanism by which HOCl-modified LDL inactivates cathepsin B differs from that of copper-oxidized LDL."
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"16–19 However, direct inactivation of cathepsin B by oxidized LDL has also been proposed."
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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."
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"HOCl-modified LDL inactivates cathepsin B. LDL (0.5 mg protein/ml PBS, ~1 µM) was incubated for 10 min at ambient temperature with 25–200 µM HOCl."
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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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"The data show that HOCl-modified LDL inactivates cathepsin B by a chloramine-dependent mechanism, most likely via oxidation of the enzyme’s critical cysteine residue, and that ascorbic and lipoic acids may be able to inhibit this potentially pro-atherogenic process by scavenging LDL-associated chloramines."
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"37 LDL-associated chloramines, rather than secondary products of lipid oxidation, were implicated in inactivation of this enzyme,37 in agreement with inactivation of cathepsin B by HOCl-modified LDL in the present study."
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"Elimination of LDL-associated chloramines by the small molecule antioxidants ascorbic and lipoic acids protected against cathepsin B inactivation by HOClmodified LDL."
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"Inactivation of cathepsin B by oxidized LDL involves complex formation induced by binding of putative reactive sites exposed at low pH to thiols on the enzyme."
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"Ascorbic and lipoic acids protect against inactivation of cathepsin B by HOCl-modified LDL."
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"33–35 Since specific aldehydes, such as 4-hydroxynonenal, also inactivated LCAT,36 the mechanism of LCAT inactivation appears analogous to that for inactivation of cathepsin B by copper-oxidized LDL."
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"J Clin Invest 1994; 94: 1506–1512. HOCl-modified LDL inactivates the lysosomal protease cathepsin B 349 21."
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"DISCUSSION This 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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