Homocysteine-induced caspase-3 activation by endoplasmic reticulum stress in endothelial progenitor cells from patients with coronary heart disease and healthy donors

Biosci Biotechnol Biochem. 2011;75(7):1300-5. doi: 10.1271/bbb.110074. Epub 2011 Jul 7.

Abstract

Previous studies have suggested an association of hyperhomocysteinemia-induced vascular pathology with enhanced apoptotic potential of endothelial progenitor cells in patients with coronary heart disease. Our results indicate that 500 µmol/L homocysteine induced endothelial progenitor cell apoptosis and activation of caspase-3, both of which were abolished by 100 µmol/L and 200 µmol/L salubrinal, an agent that prevents endoplasmic reticulum stress-induced apoptosis. The addition of 500 µmol/L homocysteine caused a release of Ca(2+) from intracellular stores, and enhanced phosphor-eukaryotic initiation factor 2α phosphorylation at Ser51 and the expression of a glucose-regulated protein of 78 kDa and a C/EBP homologous protein independently of extracellular Ca(2+). These effects of homocysteine on endothelial progenitor cells were significantly greater in patients with coronary heart disease than in healthy donors. These findings suggest that homocysteine induces endoplasmic reticulum stress-mediated activation of caspase-3 in endothelial progenitor cells, an event that is enhanced in patients with coronary heart disease. Furthermore, enhanced endoplasmic reticulum stress-mediated activation of caspase-3 in endothelial progenitor cells might be involved in hyperhomocysteinemia-associated vascular pathology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / drug effects
  • Blood Donors
  • Calcium Signaling / drug effects
  • Caspase 3 / drug effects
  • Caspase 3 / metabolism
  • Cell Line
  • Cinnamates / antagonists & inhibitors
  • Cinnamates / pharmacology
  • Coronary Disease / metabolism*
  • Endoplasmic Reticulum / drug effects
  • Endoplasmic Reticulum / metabolism*
  • Endothelial Cells / drug effects
  • Endothelial Cells / metabolism*
  • HSP70 Heat-Shock Proteins / drug effects
  • Homocysteine / metabolism*
  • Humans
  • Male
  • Membrane Proteins / drug effects
  • Oxidative Stress / drug effects
  • Phosphorylation / drug effects
  • Stem Cells / drug effects
  • Stem Cells / metabolism*
  • Thiourea / analogs & derivatives
  • Thiourea / antagonists & inhibitors
  • Thiourea / pharmacology

Substances

  • Cinnamates
  • HSP70 Heat-Shock Proteins
  • Membrane Proteins
  • glucose-regulated proteins
  • salubrinal
  • Homocysteine
  • Caspase 3
  • Thiourea