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Epidermal growth factor [EGF] mediated stimulation of its receptor in endothelial cell [EC] is accompanied by phosphorylation of the EGF-receptor [EGFR] and activation of phospholipase C- γ , resulting in the breakdown of phosphatidylinositol(4,5)-bisphosphate and generating inositol (1,4,5)-trisphosphate [IP 3 ] and diacylglycerol. IP 3 thus formed can be further converted to inositol (1,3,4,5)-tetrakisphosphate [IP 4 ] by an enzyme called IP 3 -kinase [IP 3 K]. In this study we have investigated the effect of modulation of intracellular IP 3 K activity by the use of an inhibitor, 2-trifluoromethyl [6-(4-nitrobenzyl)-purine] [IP 3 KI] and siRNA against IP 3 KB on EGF-induced ERK-phosphorylation and cell motility. EGF stimulated ERK-phosphorylation that has been implicated in EGF-stimulated cell migration was inhibited by both IP 3 KI and siRNA against IP 3 KB. Inhibition of ERK-phosphorylation was accompanied by decreased cell migration in the presence of IP 3 KI.

Modulation of Epidermal Growth Factor Stimulated ERK Phosphorylation and Cell Motility by Inositol Trisphosphate Kinase