Apolipoprotein oxidation in the absence of lipid peroxidation enhances LDL uptake by macrophages

FEBS Lett. 1994 Aug 8;349(3):375-9. doi: 10.1016/0014-5793(94)00706-3.

Abstract

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 125I-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apolipoproteins B / drug effects
  • Apolipoproteins B / metabolism*
  • Biological Transport
  • Cell Line
  • Copper / pharmacology
  • Humans
  • Hydrogen Peroxide / pharmacology
  • Lipid Peroxidation
  • Lipoproteins, LDL / metabolism*
  • Macrophages / metabolism*
  • Oxidation-Reduction
  • Probucol / pharmacology

Substances

  • Apolipoproteins B
  • Lipoproteins, LDL
  • Copper
  • Hydrogen Peroxide
  • Probucol