Activation of NAD(P)H oxidase by lipid hydroperoxides: mechanism of oxidant-mediated smooth muscle cytotoxicity

Free Radic Biol Med. 2003 Apr 1;34(7):937-46. doi: 10.1016/s0891-5849(03)00032-7.

Abstract

Oxidized lipids, such as 13-hydroperoxyoctadecadienoic acid (13-HPODE), have been implicated in the pathogenesis of atherosclerosis. 13-HPODE, a constituent of oxidized low-density lipoproteins, can induce cytotoxicity of vascular smooth muscle cells (SMC), which may facilitate plaque destabilization and/or rupture. 13-HPODE-induced cytotoxicity has been linked to oxidative stress, although the mechanisms by which this occurs are unknown. In the present study, we show that 13-HPODE and 9-HPODE (10-30 microM) increased superoxide (O2*-) production and induced cytotoxicity in SMC. The 13-HPODE-induced increase in O2*- was blocked by transfecting the cells with antisense oligonucleotides against p22phox, suggesting that the O2*- was produced by NAD(P)H oxidase. Similar concentrations of the corresponding HPODE reduction products, 13-hydroxyoctadecadienoic acid (13-HODE) and 9-HODE, neither increased O2*- production nor induced cytotoxicity, while 4-hydroxy nonenal (4-HNE), an unsaturated aldehyde lipid peroxidation product, induced cytotoxicity without increasing O2*- production. Treatment with superoxide dismutase or Tiron to scavenge O2*-, or transfection with p22phox antisense oligonucleotides to inhibit O2*- production, attenuated 13-HPODE-induced cytotoxicity, but not that induced by 4-HNE. These findings suggest that activation of NAD(P)H oxidase, and production of O2*-, play an important role in lipid hydroperoxide-induced smooth muscle cytotoxicity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Arteriosclerosis
  • Cell Survival
  • Cells, Cultured
  • Enzyme Activation
  • Free Radicals
  • Imidazoles*
  • Linoleic Acids / pharmacology
  • Lipid Peroxides / metabolism*
  • Lipid Peroxides / pharmacology
  • Male
  • Membrane Transport Proteins*
  • Microscopy, Confocal
  • Muscle, Smooth / cytology
  • Muscle, Smooth / metabolism
  • NADPH Dehydrogenase / metabolism
  • NADPH Oxidases / metabolism*
  • Oligonucleotides, Antisense / pharmacology
  • Oxidants / metabolism
  • Oxidative Stress
  • Oxygen / metabolism
  • Phosphoproteins / metabolism
  • Pyrazines / pharmacology
  • RNA, Messenger / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Reverse Transcriptase Polymerase Chain Reaction
  • Superoxides / metabolism
  • Transfection

Substances

  • Free Radicals
  • Imidazoles
  • Linoleic Acids
  • Lipid Peroxides
  • Membrane Transport Proteins
  • Oligonucleotides, Antisense
  • Oxidants
  • Phosphoproteins
  • Pyrazines
  • RNA, Messenger
  • Superoxides
  • 13-hydroperoxy-9,11-octadecadienoic acid
  • coelenterazine
  • 9-hydroperoxy-11,12-octadecadienoic acid
  • NADPH Oxidases
  • CYBA protein, human
  • NADPH Dehydrogenase
  • Oxygen