Copper- and malondialdehyde-induced modification of high density lipoprotein and parallel loss of lecithin cholesterol acyltransferase activation

Atherosclerosis. 1993 Dec;104(1-2):213-9. doi: 10.1016/0021-9150(93)90192-w.

Abstract

Incubation of high density lipoproteins (HDL) with 0.1-10 microM copper ions resulted in a decrease in tryptophan residues and a moderate diminution of lysine residues. Polymerization of apolipoprotein AI (apo A-I) was only observed for the highest concentration of Cu2+. A dose-dependent loss in lecithin cholesterol acyl-transferase (LCAT) activity was noted. Following incubation with 10 mM malondialdehyde, the physicochemical properties of HDL were more pronouncedly affected, in terms of lipid peroxidation products, relative electrophoretic mobility and percentages of intact tryptophan and lysine residues. Polymerization of apo A-I occurred after 40 min incubation, and a time-dependent loss of LCAT activation was noted. Since the deficiency in LCAT activation was observed in relatively mild conditions, when no perturbation of the physico-chemical properties of the particle could be shown, the determination of LCAT activity appears to be a sensitive test for HDL discrete modification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apolipoprotein A-I / chemistry
  • Chemical Phenomena
  • Chemistry, Physical
  • Copper / pharmacology*
  • Electrophoresis
  • Enzyme Activation / drug effects
  • Humans
  • In Vitro Techniques
  • Lipid Peroxidation / drug effects
  • Lipoproteins, HDL / chemistry*
  • Lipoproteins, HDL / metabolism
  • Malondialdehyde / pharmacology*
  • Phosphatidylcholine-Sterol O-Acyltransferase / chemistry*
  • Phosphatidylcholine-Sterol O-Acyltransferase / metabolism
  • Tryptophan / chemistry

Substances

  • Apolipoprotein A-I
  • Lipoproteins, HDL
  • Malondialdehyde
  • Copper
  • Tryptophan
  • Phosphatidylcholine-Sterol O-Acyltransferase