Different susceptibility to oxidation of proline and arginine residues of apolipoprotein B-100 among subspecies of low density lipoproteins

FEBS Lett. 2001 Feb 23;491(1-2):123-6. doi: 10.1016/s0014-5793(01)02181-0.

Abstract

gamma-Glutamyl semialdehyde is a primary oxidation product of apolipoprotein (apo) B-100 proline (Pro) and arginine (Arg) side chain residues. By reduction gamma-glutamyl semialdehyde forms 5-hydroxy-2-aminovaleric acid (HAVA). Here we describe the application of sensitive and specific HAVA measurement to characterize the formation of gamma-glutamyl semialdehyde in several domains of apoB-100 in LDL(1) (S(f) 7-12) and LDL(2) (S(f) 0-7) subfractions subjected to oxidative damage in the presence of iron in vitro. Results suggest that susceptibility of apoB-100 Pro and Arg residues toward oxygen radicals drastically changes along the lipoprotein metabolic cascade.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Amino Acids / chemistry
  • Apolipoprotein B-100
  • Apolipoproteins B / blood
  • Apolipoproteins B / chemistry*
  • Arginine / chemistry*
  • Gas Chromatography-Mass Spectrometry
  • Glutamates / chemistry
  • Humans
  • Lipoproteins, LDL / blood
  • Lipoproteins, LDL / chemistry*
  • Male
  • Oxidation-Reduction
  • Proline / chemistry*
  • Reactive Oxygen Species

Substances

  • Amino Acids
  • Apolipoprotein B-100
  • Apolipoproteins B
  • Glutamates
  • Lipoproteins, LDL
  • Reactive Oxygen Species
  • glutamic acid gamma-semialdehyde
  • 2-amino-5-hydroxyvaleric acid
  • Arginine
  • Proline