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. 2016 Jun 18;21(6):792. doi: 10.3390/molecules21060792

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© 2016 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).

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Inhibition of EGFR phosphorylation in A431 cells. A431 cells were treated for 15 min with PE4 at a concentration of 12.5 and 50 µg/mL or with the EGFR tyrosine kinase inhibitor (EGFR-I) AG1478 (5 µM). Untreated cells served as control. Subsequently the cells were stimulated for 5 min with 50 ng/mL EGF. (A) Afterwards the cells were lysed and prepared for western blotting with anti-EGFR, anti-phosphoEGFR (pEGFR) and anti-β actin antibodies; (B) The graph shows the band intensity of the western blot. The pEGFR/tubulin quotient was equaled to 100%. Data are expressed as means ± SD of three independent experiments and the statistical significance was determined compared to the untreated control (** p < 0.01).

Inhibition of EGFR phosphorylation in A431 cells. A431 cells were treated for 15 min with PE4 at a concentration of 12.5 and 50 µg/mL or with the EGFR tyrosine kinase inhibitor (EGFR-I) AG1478 (5 µM). Untreated cells served as control. Subsequently the cells were stimulated for 5 min with 50 ng/mL EGF. (A) Afterwards the cells were lysed and prepared for western blotting with anti-EGFR, anti-phosphoEGFR (pEGFR) and anti-β actin antibodies; (B) The graph shows the band intensity of the western blot. The pEGFR/tubulin quotient was equaled to 100%. Data are expressed as means ± SD of three independent experiments and the statistical significance was determined compared to the untreated control (** p < 0.01).