Journal
CANCER LETTERS
Volume 290, Issue 1, Pages 43-48Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.canlet.2009.08.022
Keywords
EGFR; TGF beta; H2O2; Crosstalk; Transactivation
Categories
Funding
- Korean Ministry of Education, Science and Technology
- Musculoskeletal Bioorgan Center [A040003]
- Korean Ministry of Health and Welfare
- Korea Science and Engineering Foundation (KOSEF) [M2070600005-08B0600-00510]
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TGF beta is known to transactivate EGFR. However, the signaling component involved in this crosstalk has yet to be revealed. Here, we found that TGF beta(1) 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 TGF beta(1), treatment in the same time-kinetics as EGFR activation. Pretreatment of N-acetyl cysteine abolished TGF beta(1)-induced H2O2 induction and EGFR activation. Direct treatment of H2O2 phosphorylated EGFR and catalase inhibitor prolonged TGF beta(1)-induced EGFR activation. These results show that TGF beta(1) activates EGFR via an H2O2-dependent mechanism, which subsequently leads to the activation of Erk(1/2). (C) 2009 Elsevier Ireland Ltd. All rights reserved.
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