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Aim. To study a possible involvement of NADPH oxidases in the control of cell motility and Akt signaling in the human breast adenocarcinoma MCF-7 cells that stably overexpress the full-length form of adaptor protein Ruk/CIN85. Methods. Cell motility was studied by a transwell migration assay. The dynamics of EGF-induced Akt activation was investigated by Western blot analysis. Results. It has been shown that apocynin, an inhibitor of the assembly of plasma membrane NADPH oxidases, substantially attenuates the motility of Ruk/CIN85 overexpressing MCF-7 cells (subclone G10) in comparison with control cells. In addition, apocynin induced the transition from sustained to transient EGF-dependent Akt activation in G10 cells and did not influence transient Akt activation in control cells. Conclusions. The data obtained can suggest that ROS produced by NADPH oxidases are signaling components, upstream to Akt kinase, that mediate the increased migratory potential of Ruk/CIN85 overexpressing MCF-7 cells.\u

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Apocynin attenuates motility and induces transition from sustained to transient EGF-dependent Akt activation in MCF-7 cells that overexpress adaptor protein Ruk/CIN85