Anandamide induces apoptosis in human endothelial cells: its regulation system and clinical implications

Thromb Haemost. 2003 May;89(5):875-84.

Abstract

Anandamide (AEA), an endogenous cannabinoid, is generated by macrophages during shock conditions, and is thought to be a causative mediator of septic shock. Thus, we hypothesized that AEA plays a crucial role in endothelial cell (EC) injury. Here, we demonstrate that AEA induces apoptosis in a time-and dose-dependent manner in human umbilical vein endothelial cells (HUVECs). AEA triggered phosphorylation of c-Jun NH(2)-terminal kinase (JNK) and p38 mitogen activated protein kinase. AEA also showed a marked increase of interleukin Ibeta- converting enzyme (ICE)CED-3 family protease (caspase-3) activity. AEA-induced EC death was inhibited by a selective vanilloid receptor 1 (VR1) antagonist, capsazepine, and was enhanced by a VR1 agonist, capsaicin, indicating that AEA induces apoptosis in ECs via VR1. In conclusion, we propose that AEA may play a crucial role in EC injury under conditions of shock, and that the use of inhibitors of the AEA regulation system may have a therapeutic effect under these conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / drug effects*
  • Arachidonic Acids / pharmacology*
  • Caspase 3
  • Caspases / metabolism
  • Cells, Cultured
  • Endocannabinoids
  • Endothelial Cells / drug effects*
  • Endothelial Cells / pathology
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / pathology
  • Humans
  • JNK Mitogen-Activated Protein Kinases
  • Kinetics
  • Mitogen-Activated Protein Kinases / metabolism
  • Phosphorylation / drug effects
  • Polyunsaturated Alkamides
  • Receptors, Drug / physiology
  • Shock, Septic / pathology
  • Umbilical Veins / cytology
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Arachidonic Acids
  • Endocannabinoids
  • Polyunsaturated Alkamides
  • Receptors, Drug
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • CASP3 protein, human
  • Caspase 3
  • Caspases
  • anandamide