Fig 1: Effects of Fbp1 on oxidative stress and the Nrf2 pathway in vitro. A, ROS levels detected by fluorescence microscopy after knock‐down or overexpression of Fbp1 (magnification ×200). B, C, ROS levels detected by Multi‐Mode Microplate Reader. D, E, malondialdehyde (MDA) content, (F, G) glutathione (GSH) content, and (H, I) superoxide dismutase (SOD) activity in the different groups. J‐O, Protein expression levels of nuclear Nrf2, Keap1, total‐Nrf2, p‐Nrf2 and HO‐1 in the different groups. *P < .05, **P < .01, ***P < .001 as compared to the Si‐nc group; # P < .05, ## P < .01, ### P < .001 as compared to the P‐nc group
Fig 2: Methylation status of FBP1 promoter detected in lung cancer and normal tissues and its relationship with overall survival. (a) FBP1 methylation was assessed in 107 pair lung cancer and normal tissues using methylation assay. (b) Statistical analysis was performed to confirm the correlation between FBP1 methylation and overall survival rate of lung cancer patients.
Fig 3: Effect of FBP1 expression on cell invasiveness of A549 and H460 cells. (a) Western blot result shows the overexpression of FBP1 protein in A549 cells; (b and c) representative images showing the engineered FBP1 expression in A549 cells (b) and SiRNA-knockdown of FBP1 expression in H460 cells (c) on cell invasiveness. Graphs showing the changes of cell invasiveness of A549 cells (b) and H460 cells (c). The data represents the average of the results from three independent experiments. Error bar indicates the standard deviation. “∗” indicates P<0.01.
Fig 4: miR-18a-5p can target and inhibit FBP1 expression in liver cancer cells. (a) Schematic diagram of binding sequence between miR-18a-5p and FBP1-wt and FBP1-mut. (b) Luciferase activity of FBP1 in liver cancer cell line HepG2 in different treatment groups detected by dual-luciferase assay. (c) The expression of FBP1 mRNA in liver cancer cell line HepG2 detected by qRT-PCR. (d) The expression of FBP1 protein in liver cancer cell line HepG2 detected by western blot; * represents p < 0.05.
Fig 5: FBP1 promotes c-Myc degradation in pancreatic cancer cells. a and b, western blot analysis of whole cell lysate of PANC-1 cells transfected with the indicated constructs. Cells were treated with or without 20 µM of MG132 for 8 h before harvest (a). The c-Myc protein was quantified and normalized to the quantified value of ß-Tubulin (b). c and d, PANC-1 cells were infected with indicated constructs. After 72 h, cells were treated with 50 µg/µl cycloheximide (CHX). At different time points, cells were harvested for western blot analysis. At each time point, the intensity of FBP1 was normalized to the intensity of ß-Tubulin (loading control) first and then to the value at the 0-h time point. e, PANC-1 and SW1990 cells infected with indicated constructs. Western blot analysis of whole cell lysate of PANC-1 and SW1990 cells after 72 h infection. Cells were treated with or without 20 µM of MG132 for 8 h before harvest. f-i, PANC-1 cells were transfected with indicated constructs. 24 h post transfection, cells were harvested for western blot analysis (f and g), RT-qPCR (h) and glucose consumption measurement (i). Data are shown as means ± SD (n = 3). n.s., not significant; ***, P < 0.001. j, western blot analysis of whole cell lysate of PANC-1 cells transfected with indicated constructs. Cells were treated with or without 20 µM of MG132 for 8 h before harvest. k, western blot analysis of whole cell lysate of PANC-1 cells transfected with indicated constructs. l, western blot analysis of whole cell lysate of PANC-1 cells transfected with indicated constructs. m, western blot analysis of whole cell lysate of PANC-1 cells transfected with indicated constructs. Cells were treated with or without 20 µM of MG132 for 8 h before harvest
Supplier Page from Abcam for Anti-FBP1 antibody [EPR4620]