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Apolipoprotein oxidation in the absence of lipid peroxidation enhances LDL uptake by macrophages
Author(s) -
Hunt James V.,
Bailey James R.,
Schultz Donna L.,
McKay Alan G.,
Mitchinson Malcolm J.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00706-3
Subject(s) - probucol , chemistry , apolipoprotein b , lipid peroxidation , hydrogen peroxide , lipid oxidation , malondialdehyde , lipoprotein , biochemistry , antioxidant , low density lipoprotein , fragmentation (computing) , cholesterol , medicine , endocrinology , biology , ecology
A characteristic of the antioxidant, probucol, is its inability to inhibit apolipoprotein B fragmentation in low density lipoprotein (LDL), despite a pronounced ability to inhibit lipid oxidation on relatively lengthy exposure to Cu(II). Here we show that a short exposure of LDL to hydrogen peroxide and Cu(II) leads to 125 I‐labelled apolipoprotein B fragmentation, the production of malondialdehyde and hydroperoxides and leads to increased uptake by macrophages on subsequent culture. However, pre‐loading LDL with probucol protects LDL from lipid oxidation but not protein fragmentation or macrophage uptake. The use of probucol to conduct studies on apolipoprotein B oxidation without extensive lipid oxidation may prove useful when studying LDL apolipoprotein damage on exposure to an aqueous free radical insult.