• Title of article

    High-density lipoprotein increases the abundance of eNOS protein in human vascular endothelial cells by increasing its half-life

  • Author/Authors

    Maria E. R?met، نويسنده , , Mika R?met، نويسنده , , Qing Lu، نويسنده , , Moriah Nickerson، نويسنده , , Markku J. Savolainen، نويسنده , , Amy Malzone، نويسنده , , Richard H. Karas، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2003
  • Pages
    10
  • From page
    2288
  • To page
    2297
  • Abstract
    Objectives Given the importance of endothelial nitric oxide synthase (eNOS) in regulating endothelium-dependent vasorelaxation, we investigated the effects of high-density lipoprotein in (HDL) on eNOS protein abundance in cultured human vascular endothelial cells. Background Endothelial dysfunction, characterized by decreased nitric oxide production, is one of the early features in the development of atherosclerosis. We have recently shown in vivo that niacin therapy increases plasma HDL concentration and improves endothelium-dependent vasorelaxation in patients with coronary artery disease. Methods Human vascular endothelial cells were cultured in the presence or absence of HDL or apolipoprotein (apo)A-I. The eNOS protein abundance was assessed by immunoblotting, and protein half-life was assessed by pulse-chase techniques. The eNOS messenger ribonucleic acid (mRNA) abundance was measured using real-time quantitative polymerase chain reaction. Results High density lipoprotein, or apoA-I alone, increased eNOS protein abundance by 3.5 ± 0.7 and 2.7 ± 0.5-fold, respectively (p < 0.05 for both). However, neither HDL nor apoA-I increased eNOS mRNA abundance. It was shown that HDL increased eNOS protein half-life up to 3.3 ± 0.2-fold (p = 0.001). Both HDL and apoA-I activated mitogen-actived protein-kinase and phosphatidylinositol 3-kinase (PI3K) Akt-pathways in human arterial endothelial cells, and inhibition of either of these pathways by specific pharmacologic inhibitors abolished the effect of HDL on eNOS. Conclusions We demonstrate that HDL activates both extracellular signal-regulated kinase 1/2 (ERK1/2) and Akt, resulting in enhanced eNOS protein stability and subsequent accumulation of eNOS protein. This posttranslational regulation represents a previously unrecognized mechanism for regulating eNOS.
  • Keywords
    phosphatidylinositol 3-kinase , RT–PCR , real-time quantitative polymerase chain reaction , apo , apolipoprotein , CAD , coronary artery disease , endothelial nitric oxide synthase , ERK1/2 , extracellular signal-regulated kinase 1/2 , HDL , high-density lipoprotein , PI3K , eNOS
  • Journal title
    JACC (Journal of the American College of Cardiology)
  • Serial Year
    2003
  • Journal title
    JACC (Journal of the American College of Cardiology)
  • Record number

    598079