Fig. 1

High level of Aurora-A promotes glycolysis in malignant cancer cells. a In human cancer cell lines A549, MCF-7, RKO, DLD1, U251, and 293 T, the expressions and activity of Aurora-A kinase were examined. The status of p53 (WT: wild-type, Mut: mutation, -: inactivation) was labelled at the bottom of each lane. b The glycolytic rates were analyzed by standard Seahorse assay. The extracellular acidification rate (ECAR) over time (left panel) and ECAR in different stages of the measurement (right panel) were shown. c Aurora-A kinase activity was inhibited by selective inhibitor MLN8237 (200 nM, for 1, 2, and 4 h) in DLD1 cells. The kinase activity of Aurora-A was tested. d The glycolytic flux was investigated by seahorse assay in control and Aurora-A inhibition cells in c. The ECAR over time (left panel) and ECAR in different stages of the measurement (right panel) were shown. e Empty Vector (EV) and kinase-dead (KD, D274A) Aurora-A were transfected in DLD1 cells, then the levels of Aurora-A and p-Aurora-A were examined. f The ECAR of cells in e were measured by seahorse assay. g Empty Vector (EV) and p53 R273H mutant were transfected in A549 cells, the levels of Aurora-A, p-Aurora-A and p53 were examined. h The ECAR of cells in g were measured by seahorse assay. Cells were treated with DMSO or MLN8237 for 4 h before assay. The error bar in panels b, d, f, h represents the standard error of mean (SEM), n = 3 independent experiments. Source data are provided as a Source Data files. (Student’s t-test *p < 0.05, **p < 0.01, ***p < 0.001, ns not significant).