| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2114147 | Cancer Letters | 2010 | 6 Pages |
Abstract
TGFβ is known to transactivate EGFR. However, the signaling component involved in this crosstalk has yet to be revealed. Here, we found that TGFβ1 phosphorylated EGFR in a dose-dependent manner in SCC13 and A431 cells, and it was not blocked by EGF-neutralizing antibody. H2O2 was increased by TGFβ1 treatment in the same time-kinetics as EGFR activation. Pretreatment of N-acetyl cysteine abolished TGFβ1-induced H2O2 induction and EGFR activation. Direct treatment of H2O2 phosphorylated EGFR and catalase inhibitor prolonged TGFβ1-induced EGFR activation. These results show that TGFβ1 activates EGFR via an H2O2-dependent mechanism, which subsequently leads to the activation of Erk1/2.
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Authors
EunAh Lee, Jae Youn Yi, Eunkyung Chung, Youngsook Son,