Activation of ICAM-1 promoter by lysophosphatidylcholine: possible involvement of protein tyrosine kinases

Biochim Biophys Acta. 1997 Mar 10;1345(1):93-8. doi: 10.1016/s0005-2760(96)00169-5.


Lysophosphatidylcholine (lyso-PC) selectively upregulates the mRNA level of intercellular adhesion molecule-1 (ICAM-1) but not that of vascular cell adhesion molecule-1 (VCAM-1) in cultured human umbilical vein endothelial cells. Transfection studies show that lyso-PC activates the ICAM-1 promoter but not the VCAM-1 promoter. Gel mobility shift assays document an increase in NF-kappa B binding in cells treated with lyso-PC. The increases of ICAM-1 mRNA and NF-kappa B binding were inhibited by the protein tyrosine kinase inhibitors, genistein and lavendustin A, but not by inhibitors for cyclic AMP-dependent protein kinases or protein kinase C. Our results suggest that lyso-PC induces ICAM-1 expression most likely by activating NF-kappa B, and that the effect appears to be protein tyrosine kinase-dependent.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cell Line
  • Endothelium, Vascular / drug effects
  • Humans
  • Intercellular Adhesion Molecule-1 / genetics*
  • Lysophosphatidylcholines / pharmacology*
  • NF-kappa B / metabolism
  • Promoter Regions, Genetic / drug effects
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / metabolism*
  • RNA, Messenger / analysis
  • Transfection
  • Up-Regulation
  • Vascular Cell Adhesion Molecule-1 / genetics


  • Lysophosphatidylcholines
  • NF-kappa B
  • RNA, Messenger
  • Vascular Cell Adhesion Molecule-1
  • Intercellular Adhesion Molecule-1
  • Protein-Tyrosine Kinases