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. 2017 Dec 19;15(3):2889–2898. doi: 10.3892/ol.2017.7654

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Copyright: © Zou et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 6. — Ginsenoside Rg3 increases the phosphorylation level of EEF2 on Thr57. (A) Representative MS/MS spectra of the identified phosphopeptide AGETRFpTDTR (left) and the non-phosphopeptide DLEEDHACIPIKK (right) from EEF2. Inset presents the relative intensities of the TMT reporter tags following treatment with Rg3 at different time points in biological duplicates. (B) Time course of Rg3-induced EEF2 phosphorylation in MDA-MB-231 and HCC1143 cells. Following treatment with Rg3 for the indicated times, cells were subjected to lysis and resolved by SDS-PAGE. Threonine phosphorylation of EEF2 was probed by Western blotting with antibodies against phospho-EEF2 (Thr57). The amount of total EEF2 was determined by Western blotting with anti-EEF2 antibodies. The amount of total GAPDH was determined by Western blotting with antibodies against GAPDH as the loading control. TMT, tandem mass tag; EEF2, elongation factor 2; MS, mass spectrum; phospho, phosphorylated.