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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 392, Issue 10

Issues

Ligand-independent activation of the arylhydrocarbon receptor by ETK (Bmx) tyrosine kinase helps MCF10AT1 breast cancer cells to survive in an apoptosis-inducing environment

Yasuko Fujisawa
  • Department of Environmental Toxicology, University of California Davis, One Shields Avenue, Davis, CA 95616, USA
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/ Wen Li
  • Department of Environmental Toxicology, University of California Davis, One Shields Avenue, Davis, CA 95616, USA
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/ Dalei Wu
  • Department of Environmental Toxicology, University of California Davis, One Shields Avenue, Davis, CA 95616, USA
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/ Patrick Wong
  • Department of Environmental Toxicology, University of California Davis, One Shields Avenue, Davis, CA 95616, USA
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/ Christoph Vogel
  • Department of Environmental Toxicology, University of California Davis, One Shields Avenue, Davis, CA 95616, USA
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/ Bin Dong
  • Department of Environmental Toxicology, University of California Davis, One Shields Avenue, Davis, CA 95616, USA
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/ Hsing-Jien Kung
  • Cancer Research Center, UCD Medical Center, University of California Davis, Sacramento, CA 95817, USA
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/ Fumio Matsumura
Published Online: 2011-08-24 | DOI: https://doi.org/10.1515/BC.2011.087

Abstract

It has been reported that the arylhydrocarbon receptor (AHR) is overexpressed in certain types of breast tumors. However, so far no concrete evidence has been provided yet as to why and how the overexpressed AHR in those cancer cells is functionally activated without exogenous ligands. Here we show that the AHR was functionally activated when estrogen receptor-negative, AHR overexpressing MCF10AT1 human breast cancer cells (designated P20E) were subjected to serum starvation. Transfection of cells with ETK-KQ, a plasmid for kinase-dead epithelial and endothelial tyrosine kinase (ETK), attenuated this AHR activation. Artificial over-expression of ETK in P20E cells through transfection with wild-type ETK plasmid (ETK-wt) caused up-regulation of cytochrome P4501a1 (CYP1A1; a marker of functional activation of AHR). Furthermore, ablation of ETK expression by a specific antisense oligonucleotide or AG879, a specific inhibitor of ETK kinase suppressed activation of AHR induced by omeprazole, a strong ligand-independent activator of AHR. Activation of ETK in those cells conferred them resistance to UVB- as well as doxorubicin-induced apoptosis, both of which were reversed by ETK-KQ. Together, these findings support our conclusion that ETK is the tyrosine kinase responsible for the functional activation of the AHR in these mammary epithelial cells.

Keywords: arylhydrocarbon receptor; breast cancer; endothelial tyrosine kinase; ligand-independent activation

About the article

Corresponding author


Received: 2011-03-18

Accepted: 2011-06-30

Published Online: 2011-08-24

Published in Print: 2011-10-01


Citation Information: Biological Chemistry, Volume 392, Issue 10, Pages 897–908, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2011.087.

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