Artemisinin inhibits monocyte adhesion to HUVECs through the NF-κB and MAPK pathways in vitro

Int J Mol Med. 2016 Jun;37(6):1567-75. doi: 10.3892/ijmm.2016.2579. Epub 2016 Apr 26.

Abstract

The adhesion of monocytes to human umbilical vein endothelial cells (HUVECs) plays a crucial role in the initiation of atherosclerosis. Intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1) are two important molecules involved in the adhesion of monocytes to HUVECs. Previous studies have suggested that artemisinin, apart from an anti-malarial agent, also has other effects. In the present study, we found that artemisinin significantly decreased the adhesion of monocytes to tumor necrosis factor-α (TNF-α)-stimulated HUVECs in a dose-dependent manner and suppressed the mRNA and protein level of ICAM-1 and VCAM-1 in the TNF-α-stimulated HUVECs. In addition, the nuclear factor-κB (NF-κB) inhibitor, Bay 11-7082, and mitogen-activated protein kinase (MAPK) inhibitors (SB203580 and U0126) respectively reduced the adhesion of monocytes to TNF-α-stimulated HUVECs, and suppressed ICAM-1 and VCAM-1 expression in TNF-α stimulated HUVECs. Moreover, artemisinin impeded the activation of the NF-κB and MAPK signaling pathways. Furthermore, Bay 11-7082 significantly decreased the phosphorylation of levels extracellular signal-regulated protein kinase (ERK)1/2, p38 and c-Jun N-terminal kinase (JNK). Taken together, the findings of our study indicated that artemisinin blocked monocyte adhesion to TNF-α-stimulated to HUVECs by downregulating ICAM-1 and VCAM-1 expression in the TNF-α-stimulated HUVECs. Artemisinin may thus have potential for use in the protection against the early development of atherosclerotic lesions.

MeSH terms

  • Anti-Inflammatory Agents / pharmacology*
  • Artemisinins / pharmacology*
  • Butadienes / pharmacology
  • Cell Adhesion / drug effects
  • Cell Line
  • Coculture Techniques
  • Gene Expression Regulation
  • Human Umbilical Vein Endothelial Cells
  • Humans
  • Imidazoles / pharmacology
  • Intercellular Adhesion Molecule-1 / genetics
  • Intercellular Adhesion Molecule-1 / metabolism
  • JNK Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • JNK Mitogen-Activated Protein Kinases / genetics*
  • JNK Mitogen-Activated Protein Kinases / metabolism
  • Mitogen-Activated Protein Kinase 1 / antagonists & inhibitors
  • Mitogen-Activated Protein Kinase 1 / genetics*
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3 / antagonists & inhibitors
  • Mitogen-Activated Protein Kinase 3 / genetics*
  • Mitogen-Activated Protein Kinase 3 / metabolism
  • Monocytes / cytology
  • Monocytes / drug effects*
  • Monocytes / metabolism
  • NF-kappa B / genetics*
  • NF-kappa B / metabolism
  • Nitriles / pharmacology
  • Phosphorylation / drug effects
  • Protein Kinase Inhibitors / pharmacology
  • Pyridines / pharmacology
  • Signal Transduction
  • Sulfones / pharmacology
  • Tumor Necrosis Factor-alpha / antagonists & inhibitors
  • Tumor Necrosis Factor-alpha / pharmacology
  • Vascular Cell Adhesion Molecule-1 / genetics
  • Vascular Cell Adhesion Molecule-1 / metabolism

Substances

  • 3-(4-methylphenylsulfonyl)-2-propenenitrile
  • Anti-Inflammatory Agents
  • Artemisinins
  • Butadienes
  • ICAM1 protein, human
  • Imidazoles
  • NF-kappa B
  • Nitriles
  • Protein Kinase Inhibitors
  • Pyridines
  • Sulfones
  • Tumor Necrosis Factor-alpha
  • U 0126
  • Vascular Cell Adhesion Molecule-1
  • Intercellular Adhesion Molecule-1
  • artemisinin
  • JNK Mitogen-Activated Protein Kinases
  • MAPK1 protein, human
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • SB 203580