Fig. 4

ALDOA inhibited the phosphorylation of extracellular signal-regulated kinase 1/2 (ERK1/2) in NSCLC. Key proteins in the mitogen-activated protein kinase, phosphoinositide-3-kinase/protein kinase B (PI3K/AKT) and Wnt/β-catenin pathways that are involved in cyclin D1 transcription were evaluated by western blotting. The results revealed that ALDOA knockdown promoted the phosphorylation of ERK1/2 instead of AKT and β-catenin in a H520 and b H1299 cells. In contrast, ALDOA overexpression inhibited the phosphorylation of ERK1/2 instead of AKT and β-catenin in c H157 and d H1299 cells. Black arrows indicated exogenous ALDOA. Data are shown as mean ± SD. β-actin served as loading control. *P < 0.05 versus shNC