Activation of formyl peptide receptor like-1 by serum amyloid A induces CCL2 production in human umbilical vein endothelial cells

Biochem Biophys Res Commun. 2009 Mar 6;380(2):313-7. doi: 10.1016/j.bbrc.2009.01.068. Epub 2009 Jan 22.

Abstract

We investigated the effects of serum amyloid A (SAA) on the production of C-C chemokine motif ligand 2 (CCL2) and the mechanism underlying SAA action in human umbilical vein endothelial cells (HUVECs). Stimulation of HUVECs by SAA elicited CCL2 production in a concentration-dependent manner. SAA induced the activations of NF-kappaB and AP-1, which were essential for CCL2 production after SAA stimulation. HUVECs expressed formyl peptide receptor-like 1 (FPRL1), and short interfering RNA knockdown of FPRL1 nearly completely blocked SAA-induced CCL2 production in HUVECs. We suggest that SAA stimulates CCL2 production via FPRL1 and, thus, contributes to atherosclerosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Atherosclerosis / metabolism*
  • Cells, Cultured
  • Chemokine CCL2 / biosynthesis*
  • Endothelial Cells / drug effects
  • Endothelial Cells / metabolism
  • Humans
  • Receptors, Formyl Peptide / agonists*
  • Receptors, Formyl Peptide / genetics
  • Receptors, Formyl Peptide / metabolism
  • Serum Amyloid A Protein / metabolism*
  • Serum Amyloid A Protein / pharmacology
  • Umbilical Veins / cytology
  • Umbilical Veins / drug effects
  • Umbilical Veins / metabolism

Substances

  • CCL2 protein, human
  • Chemokine CCL2
  • FPR1 protein, human
  • Receptors, Formyl Peptide
  • Serum Amyloid A Protein