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. 2014 Dec 5;14:135. doi: 10.1186/s12935-014-0135-3

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© Duan et al.; licensee BioMed Central Ltd. 2014

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Both M. hyorhinis and p37 activate PI3K-AKT signaling. (A) M. hyorhinis upregulates EGFR, PI3K and AKT phosphorylations in gastric cancer cell MGC803 and BGC823. Cells were serum starved for 24 hours and then infected with M. hyorhinis for another 2 hours. Protein lysates were analyzed by Western blot with indicated antibodies. (B) Purified p37 protein upregulates PI3K and AKT phosphorylations in gastric cancer cell MGC803. Cells were serum starved for 24 hours and then treated with p37 for another 2 hours. Protein lysates were analyzed by Western blot with indicated antibodies. Optical densities of protein bands were quantified by Image J software and relative expression levels of indicated protein to loading control were shown in graph. Values represented the mean ± SD from three to four independent experiments.