Fig 1: TM4SF1 overexpression inhibits the growth of MCF-7 xenografts. (A) Tumor growth curve of MCF-7 cells transfected with pLenti-CMV TM4SF1 or pLenti-CMV vectors (upper panel). Tumor images (lower panel). (B) Representative Ki-67 immunohistochemical staining image (left). Frequency of Ki-67+ cells (right, mean ± SD). * p < 0.05 compared with the pLenti-vector transfected group by t-test analysis. (C) TM4SF1 overexpression induces apoptosis in MCF-7 xenografts. Representative TUNEL staining images of apoptotic cancer cells are shown. (D) Effect of the TM4SF1 overexpression on the mTOR pathway, apoptosis, and autophagy in MCF-7 cells. GAPDH was used as a loading control. Data shown are representative of at least two independent experiments. TM4SF1, transmembrane 4 L six family 1.
Fig 2: BCYRN1 overexpression enhances BATF-mediated TM4SF1 upregulation to modulate HCC proliferation, migration, and invasion. (a) Proliferation was examined via colony formation assay. (b) HCC cell migration and invasion were evaluated in a Transwell assay (×200). (c) BATF, TM4SF1, E-cadherin, and MMP2 levels in HCC cells were assessed by Western blotting, with GAPDH for normalization. (d) Immunofluorescent staining of E-cadherin levels. Data are means ± SD from triplicate experiments.
Fig 3: pLenti-CMV TM4SF1 transfection-mediated upregulation of TM4SF1 reduces cell viability. (A) TM4SF1 overexpression efficiency was evaluated using real-time quantitative PCR (normalized to GAPDH). Data are presented as fold changes relative to the TM4SF1 levels in control cells (mean ± SD, n = 3). ** p < 0.01 compared with the pLenti-vector transfected group by t-test analysis. (B) TM4SF1 protein levels were significantly upregulated following with the TM4SF1 plasmid. GAPDH was used a loading control. (C, D) MTT assays were performed to detect the MCF-7 and ZR-75-1 cell viability (mean ± SD), * p < 0.05, ** p < 0.01 compared with the pLenti-vector transfected group by t-test analysis. Data shown are representative of at least two independent experiments. TM4SF1, transmembrane 4 L six family 1.
Fig 4: BCYRN1 recruits BATF to drive TM4SF1 expression. (a) The impact of BCYRN1 on TM4SF1 promoter activity was examined via the luciferase reporter assay. (b) Interactions between BATF and BCYRN1 were confirmed through a RIP assay, ∗∗P < 0.01 vs. IgG. (c) Putative BATF binding sites within the TM4SF1 promoter. (d) HCCLM3 cells were transfected with BATF expression vectors and truncated TM4SF1 luciferase reporter constructs or (e) mutant TM4SF1 luciferase reporter constructs in a luciferase reporter assay, ∗∗P < 0.01 vs. the OV-NC group. (f) BATF binding to TM4SF1 promoter site 2 was assessed via ChIP assay, ∗∗P < 0.01 vs. IgG. (g) BATF-mediated upregulation of TM4SF1 by BATF following BCYRN1 silencing within HCCLM3 cells. (h) TM4SF1 and BATF levels were assessed by Western blotting, with GAPDH for normalization. Data are means ± SD from triplicate experiments and were compared via paired t-tests when normally distributed.
Fig 5: TM4SF1 knockdown in breast cancer cells. (A–C) TM4SF1 knockdown efficiency was evaluated using quantitative PCR (normalized to GAPDH). Data are presented as fold changes relative to the TM4SF1 levels in control cells, mean ± SD. ** p < 0.01 compared with the negative control siRNA-transfected group by t-test analysis. (B–E) TM4SF1 protein levels were significantly downregulated following transfection with TM4SF1 siRNA. GAPDH was used as a loading control. (D–F) Effect of TM4SF1 siRNA transfection on cell proliferation, mean ± SD, * p < 0.05, ** p < 0.01 compared with the negative control siRNA-transfected group by t-test analysis. Data shown are representative of at least two independent experiments. TM4SF1, transmembrane 4 L six family one; siRNA, small interfering RNA.
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