IndraLab

Statements


Kinase-active EGFR leads to the phosphorylation of MET on tyrosine. 2 / 2
2 |

"Treatment of Caco-2 and LoVo cells with PGE2 (10 micromolar, 5 mins) significantly increased c-met-R phosphorylation. when these cells were treated with a specific inhibitor Tryphostin AG 1478 of EGFR, PGE2 almost completely inhibited PGE2-induced c-met-R phosphorylation, indicating that functional EGFR is required for PGE2-induced c-Met-R activation."

"Inhibitors of Src (PP2, SU6656) or EGFR (AG99), but not p145(met) (K252a), effectively blocked tyrosine phosphorylation of p145(met) and promoted cell death accompanied by activation of caspase-like proteases."