Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues

Oxidation of plasma low‐density lipoprotein (oxLDL) generates the lipid peroxidation product 4‐hydroxy‐2 nonenal (HNE) and also reduces proteolytic degradation of oxLDL and other proteins internalized by mouse peritoneal macrophages in culture. This leads to accumulation of undegraded material in ly...

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Veröffentlicht in:	Protein science 2002-04, Vol.11 (4), p.831-840
Hauptverfasser:	Crabb, John W., O'Neil, June, Miyagi, Masaru, West, Karen, Hoff, Henry F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldehydes - pharmacology Amino Acids - metabolism Animals BHT, butylated hydroxytoluene Binding Sites Blotting, Western BSA, bovine serum albumin cathepsin B Cathepsin B - antagonists & inhibitors Cathepsin B - metabolism Cattle CLN, Nα‐CBZ‐l‐lysine p‐nitrophenyl ester Cysteine Proteinase Inhibitors - pharmacology DTT, dithiothreitol ESMS, electrospray mass spectrometry Gas Chromatography-Mass Spectrometry HNE, 4‐hydroxy‐2‐nonenal hydroxynonenal LC ESMS, liquid chromatography electrospray mass spectrometry LDL, low‐density lipoprotein Lipid Peroxidation Macrophages - drug effects Macrophages - enzymology Macrophages - metabolism mass spectrometry Mice Michael adducts Oxidation-Reduction Oxidative damage Oxidative Stress ox‐LDL, oxidized LDL PBS, phosphate‐buffered saline Protein Conformation Spleen - drug effects Spleen - enzymology TCA, trichloroacetic acid
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