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P38 mitogen-activated protein kinase mediates transactivation of epidermal growth factor receptor by oxidative stress in renal epithelial cells


, : P38 mitogen-activated protein kinase mediates transactivation of epidermal growth factor receptor by oxidative stress in renal epithelial cells. FASEB Journal 18(4-5): Abst 400 10

Epidermal growth factor receptor (EGFR) is activated in response to oxidative stress in a variety of cell types. H2O2-stimulated EGFR activation has been proposed to occur through inhibition of EGFR dephosphorylation, activation of Src and/or induction of metalloprotease-dependent cleavage of heparin-binding EGF. In this study, we examined the mechanism of oxidant-induced EGFR transactivation in renal proximal tubular cells (RPTC). H2O2 induced p38 and EGFR phosphorylation in a concentration- and time-dependent manner. Pretreatment with SB 203580, a specific p38 inhibitor, attenuated EGFR phosphorylation (Try 1068) induced by H2O2, but not by EGF, suggesting that this response is independent of typical EGFR ligands. In support of this hypothesis, p38 inhibition attenuated ultraviolet C- and osmotic stress-induced EGFR phosphorylation. PP1, a selective Src inhibitor, inhibited H2O2-induced p38 and EGFR phosphorylation whereas SB 203580 did not inhibit Src phosphorylation. Although H2O2 exposure also induced phosphoinositide-3-kinase/Akt and extracellular signal-regulated kinases 1/2 activation in RPTC, blockade of these two pathways did not affect H2O2-induced EGFR phosphorylation. These data suggest the following novel sequence of EGFR transactivation following oxidative stress: H2O2 > Src > p38 > EGFR. (Supported by NIH ES-04410).

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