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. 2012 Oct;32(20):4237–4244. doi: 10.1128/MCB.00443-12

Fig 3.

Fig 3

Silencing of hnRNPC increases the stability of PDCD4 protein by inhibiting the Akt and p70S6K pathways. (A) T98G cells were transfected with control (CTRL) or hnRNPC siRNAs; 48 h later, whole-cell lysates were prepared and the levels of hnRNPC, PDCD4, phosphorylated Akt (p-Akt), Akt, p-p70S6K, and p-S6 were determined by Western blot analysis. (B) T98G cells were treated with various concentrations of PI3K inhibitor wortmannin; 24 h later, whole-cell lysates were prepared and the levels of PDCD4 and p-Akt were determined by Western blot analysis. (C) To check whether hnRNPC influenced the protein stability of PDCD4, T98G cells were transfected with control (CTRL) or hnRNPC siRNAs; 24 h later, cells were transferred into 6-well plates, treated with cycloheximide (CHX; 10 μg/ml), and harvested at the indicated times. The levels of PDCD4 and GAPDH were determined by Western blot analysis. Data are means and standard deviations from three different experiments.

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