Y. Zhu et al., ACTIVATION OF ICAM-1 PROMOTER BY LYSOPHOSPHATIDYLCHOLINE - POSSIBLE INVOLVEMENT OF PROTEIN-TYROSINE KINASES, Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1345(1), 1997, pp. 93-98
Lysophosphatidylcholine (lyse-PC) selectively upregulates the mRNA lev
el of intercellular adhesion molecule-1 (ICAM-1) but not that of vascu
lar cell adhesion molecule-1 (VCAM-1) in cultured human umbilical vein
endothelial cells. Transfection studies show that lyse-PC activates t
he ICAM-1 promoter but not the VCAM-1 promoter. Gel mobility shift ass
ays document an increase in NF-kappa B binding in cells treated with l
yse-PC. The increases of ICAM-1 mRNA and NF-kappa B binding were inhib
ited by the protein tyrosine kinase inhibitors, genistein and lavendus
tin A, but not by inhibitors for cyclic AMP-dependent protein kinases
or protein kinase C. Our results suggest that lyse-PC induces ICAM-1 e
xpression most likely by activating NF-kappa B, and that the effect ap
pears to be protein tyrosine kinase-dependent.