Statins control oxidized LDL-mediated histone modifications and gene expression in cultured human endothelial cells

Arterioscler Thromb Vasc Biol. 2009 Mar;29(3):380-6. doi: 10.1161/ATVBAHA.108.178319. Epub 2009 Jan 2.

Abstract

Objective: Activation of the endothelium by oxidized low-density lipoprotein (oxLDL) has been implicated in the development of atherosclerosis. Histone modifications impact on the transcriptional activity state of genes. We tested the hypothesis that oxLDL-induced inflammatory gene expression is regulated by histone modifications and experienced the effect of statins on these alterations.

Methods and results: OxLDL-related interleukin-8 (IL-8) and monocyte-chemoattractant protein-1 (MCP-1) secretion in endothelial cells was reduced by statins but enhanced by histone deacetylase inhibitors. OxLDL induced lectin-like oxidized LDL receptor-1 (LOX-1) and extracellular regulated kinases (ERK1/2)-dependent acetylation of histone H3 and H4 as well as phosphorylation of histone H3, both globally and on the promoters of il8 and mcp1. Pretreatment of oxLDL-exposed cells with statins reduced the above mentioned histone modification, as well as recruitment of CREB binding protein (CBP) 300, NF-kappaB, and of RNA polymerase II but prevented loss of binding of histone deacetylase (HDAC)-1 and -2 at the il8 and mcp1 gene promoters. OxLDL reduced HDAC1 and 2 expression, and statins partly restored global HDAC-activity. Statin-related effects were reverted with mevalonate. In situ experiments indicated decreased expression of HDAC2 in endothelial cells in atherosclerotic plaques of human coronary arteries.

Conclusions: Histone modifications seem to play an important role in atherosclerosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • Chemokine CCL2 / metabolism
  • Coronary Vessels / enzymology
  • Cytokines / genetics
  • Cytokines / metabolism*
  • Endothelial Cells / drug effects*
  • Endothelial Cells / enzymology
  • Endothelial Cells / immunology
  • Fatty Acids, Monounsaturated / pharmacology
  • Fluvastatin
  • Gene Expression Regulation / drug effects
  • Histone Deacetylase 1
  • Histone Deacetylase 2
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases / metabolism
  • Histones / metabolism*
  • Humans
  • Hydroxamic Acids / pharmacology
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors / pharmacology*
  • Indoles / pharmacology
  • Inflammation Mediators / metabolism*
  • Interleukin-8 / metabolism
  • Lipoproteins, LDL / metabolism*
  • Mevalonic Acid / pharmacology
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3 / metabolism
  • Promoter Regions, Genetic / drug effects
  • RNA Interference
  • RNA, Small Interfering / metabolism
  • Repressor Proteins / antagonists & inhibitors
  • Repressor Proteins / metabolism
  • Scavenger Receptors, Class E / metabolism
  • Signal Transduction / drug effects
  • Simvastatin / pharmacology
  • Vorinostat

Substances

  • CCL2 protein, human
  • CXCL8 protein, human
  • Chemokine CCL2
  • Cytokines
  • Fatty Acids, Monounsaturated
  • Histone Deacetylase Inhibitors
  • Histones
  • Hydroxamic Acids
  • Hydroxymethylglutaryl-CoA Reductase Inhibitors
  • Indoles
  • Inflammation Mediators
  • Interleukin-8
  • Lipoproteins, LDL
  • OLR1 protein, human
  • RNA, Small Interfering
  • Repressor Proteins
  • Scavenger Receptors, Class E
  • oxidized low density lipoprotein
  • trichostatin A
  • Fluvastatin
  • Vorinostat
  • Simvastatin
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • HDAC1 protein, human
  • Histone Deacetylase 1
  • Histone Deacetylase 2
  • Histone Deacetylases
  • Mevalonic Acid