Abstract
The present report provides evidence that, in A431 cells, interferon gamma (IFNgamma) induces the rapid (within 5 min), and reversible, tyrosine phosphorylation of the epidermal growth factor receptor (EGFR). IFNgamma-induced EGFR transactivation requires EGFR kinase activity, as well as activity of the Src-family tyrosine kinases and JAK2. Here, we show that IFNgamma-induced STAT1 activation in A431 and HeLa cells partially depends on the kinase activity of both EGFR and Src. Furthermore, in these cells, EGFR kinase activity is essential for IFNgamma-induced ERK1,2 activation. This study is the first to demonstrate that EGFR is implicated in IFNgamma-dependent signaling pathways.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Enzyme Activation
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ErbB Receptors / genetics
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ErbB Receptors / metabolism*
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HeLa Cells
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Humans
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Interferon-gamma / pharmacology*
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Janus Kinase 2 / antagonists & inhibitors
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Mitogen-Activated Protein Kinase 1 / antagonists & inhibitors
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Mitogen-Activated Protein Kinase 1 / metabolism
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Mitogen-Activated Protein Kinase 3 / antagonists & inhibitors
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Mitogen-Activated Protein Kinase 3 / metabolism
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Phosphorylation
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Protein Kinase Inhibitors / pharmacology
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STAT1 Transcription Factor / metabolism*
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Signal Transduction
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Transcriptional Activation* / drug effects
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src-Family Kinases / antagonists & inhibitors
Substances
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Protein Kinase Inhibitors
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STAT1 Transcription Factor
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STAT1 protein, human
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Interferon-gamma
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ErbB Receptors
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Janus Kinase 2
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src-Family Kinases
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Mitogen-Activated Protein Kinase 1
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Mitogen-Activated Protein Kinase 3