Remnant lipoprotein particles induce apoptosis in endothelial cells by NAD(P)H oxidase-mediated production of superoxide and cytokines via lectin-like oxidized low-density lipoprotein receptor-1 activation: prevention by cilostazol

Circulation. 2004 Mar 2;109(8):1022-8. doi: 10.1161/01.CIR.0000117403.64398.53. Epub 2004 Feb 16.

Abstract

Background: Remnant lipoprotein particles (RLPs), products of lipolytic degradation of triglyceride-rich lipoprotein derived from VLDL, exert atherogenesis. In this study, we observed how RLPs induced cytotoxicity in human umbilical vein endothelial cells (HUVECs) and cilostazol prevented cell death.

Methods and results: RLPs were isolated from the plasma of hyperlipidemic patients by use of an immunoaffinity gel mixture of anti-apolipoprotein A-1 and anti-apolipoprotein B-100 monoclonal antibodies. RLPs (50 microg/mL) significantly increased superoxide formation in HUVECs associated with elevated gp91phox mRNA and protein expression and Rac1 translocation, accompanied by increased production of tumor necrosis factor (TNF)-alpha and interleukin-1beta, DNA fragmentation, and cell death. Cilostazol (1 to 100 micromol/L) significantly suppressed not only NAD(P)H oxidase-dependent superoxide production but also TNF-alpha and interleukin-1beta release and restored viability. RLPs activated a lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1), which was not inhibited by cilostazol. Treatment of HUVECs with monoclonal antibody for LOX-1 attenuated RLP-mediated production of superoxide, TNF-alpha, and interleukin-1beta and DNA fragmentation.

Conclusions: RLPs stimulated NAD(P)H oxidase-dependent superoxide formation and induction of cytokines in HUVECs via activation of LOX-1, consequently leading to reduction in cell viability with DNA fragmentation, and cilostazol exerts a cell-protective effect by suppressing these variables.

MeSH terms

  • Adult
  • Apoptosis / drug effects*
  • Arteriosclerosis / etiology
  • Arteriosclerosis / metabolism
  • Cells, Cultured / cytology
  • Cells, Cultured / drug effects
  • Chylomicron Remnants
  • Chylomicrons / pharmacology
  • Cilostazol
  • Cytokines / biosynthesis*
  • Endothelial Cells / drug effects
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / drug effects*
  • Enzyme Induction / drug effects
  • Enzyme Inhibitors / pharmacology
  • Female
  • Genistein / pharmacology
  • Humans
  • Interleukin-1 / biosynthesis
  • Interleukin-1 / genetics
  • Lipoproteins / pharmacology*
  • Lipoproteins, LDL / pharmacology
  • Male
  • Membrane Glycoproteins / biosynthesis
  • Membrane Glycoproteins / genetics
  • Membrane Transport Proteins / biosynthesis
  • Membrane Transport Proteins / genetics
  • Middle Aged
  • NADPH Dehydrogenase / biosynthesis
  • NADPH Dehydrogenase / genetics
  • NADPH Oxidase 2
  • NADPH Oxidases / biosynthesis
  • NADPH Oxidases / genetics
  • NADPH Oxidases / physiology*
  • Phosphoproteins / biosynthesis
  • Phosphoproteins / genetics
  • Receptors, LDL / drug effects*
  • Receptors, LDL / physiology
  • Signal Transduction / drug effects
  • Superoxides / metabolism*
  • Tetrazoles / pharmacology
  • Tumor Necrosis Factor-alpha / biosynthesis
  • Tumor Necrosis Factor-alpha / genetics
  • rac1 GTP-Binding Protein / metabolism

Substances

  • Chylomicron Remnants
  • Chylomicrons
  • Cytokines
  • Enzyme Inhibitors
  • Interleukin-1
  • Lipoproteins
  • Lipoproteins, LDL
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Phosphoproteins
  • Receptors, LDL
  • Tetrazoles
  • Tumor Necrosis Factor-alpha
  • oxidized low density lipoprotein
  • Superoxides
  • Genistein
  • CYBB protein, human
  • NADPH Oxidase 2
  • NADPH Oxidases
  • CYBA protein, human
  • NADPH Dehydrogenase
  • rac1 GTP-Binding Protein
  • Cilostazol