Fig. 3: PFTK1 enhanced Wnt/β-catenin signaling to modulate gefitinib resistance in NSCLC.

a The proteomics analysis was carried out from HCC827/Vec and HCC827/PFTK1 cells. The scatter plot showed the log2 fold-change of the proteome dataset. Red dots represented significantly upregulated proteins, while green dots represented significantly downregulated proteins. b The subcellular localization of the above proteins was exhibited. c Through GO analysis, we displayed the differently expressed proteins in Wnt/β-catenin signaling. d In HCC827 and PC9 cells with increasing PFTK1, HCC827/GR and PC9/GR cells with PFTK1 knockdown, the protein levels of p-LRP6 and β-catenin were determined (n = 3). **p < 0.01. e IF assays were performed to measure the distribution of β-catenin. Scale bars: 40 μm. f PFTK1-flag overexpression plasmid was transfected into HCC827 cells, and CO-IP assays were accomplished. Since p-LRP6 and LRP6 were almost the same molecular weight, p-LRP6 was shown in a different gel. g TOPFlash and FOPFlash plasmids were transfected into HCC827 and PC9 cells with overexpression PFTK1, respectively. Ada (Adavivint), an effective classical Wnt signaling pathway inhibitor, was used in the PFTK1 group. Luciferase activity was detected in mentioned cells (n = 3). **p < 0.01. h HCC827 and PC9 cells with restored PFTK1 and control group, together with Ada treatment group were all applied to gefitinib at the indicated concentration for 72 h, and the cell viability of each group was evaluated by MTS assays (n = 3). **p < 0.01. i The workflow was shown. The elements of this image were created from icofont website (https://www.iconfont.cn). HCC827/Luc with PFTK1 and control cells were subcutaneously injected into BALB/c nude mice to establish a xenograft tumor model. In addition, half of the HCC827/PFTK1/Luc group was treated with Ada. All the animals were treated with gefitinib. Luciferase activity was imaged and measured by In Vivo Xtreme from Bruker (n = 2). **p < 0.01.