Fig. 6

HBP1 inhibits the functions of PTEN and caspase-3 through suppressing AFP in hepatoma cells. a AFP rescues the effect of HBP1 on PTEN, caspase-3, and MMP9 protein levels. HepG2 cells were co-transfected HBP1 with or without AFP expression plasmid. The protein levels of HBP1, AFP, PTEN, phospho-AKT, AKT, pro-caspase-3, cleaved-caspase-3 and MMP9 were measured by Western blotting. b AFPshRNA rescues the effect of HBP1shRNA on PTEN, caspase-3, and MMP9 protein levels. HepG2 cells were co-transfected HBP1shRNA with or without AFPshRNA expression plasmid. The protein levels of HBP1, AFP, PTEN, phospho-AKT, AKT, pro-caspase-3, cleaved-caspase-3 and MMP9 were measured by Western blotting. c HBx rescues the effect of HBP1 on PTEN, caspase-3, and MMP9 protein levels. HepG2 cells were co-transfected HBP1 with or without HBx expression plasmid. The protein levels of HBP1, AFP, PTEN, phospho-AKT, AKT, pro-caspase-3, cleaved-caspase-3 and MMP9 were measured by Western blotting. d Icaritin enhances the effect of HBP1 on PTEN, caspase-3, and MMP9 protein levels. HepG2 cells transfected with HBP1 were treated with or without Icaritin. The protein levels of HBP1, AFP, PTEN, phospho-AKT, AKT, pro-caspase-3, cleaved-caspase-3 and MMP9 were measured by Western blotting. e HBP1 acetylation at K419 is required for the effect of HBP1 on PTEN, caspase-3, and MMP9 protein levels. HepG2 cells were transfected HBP1 or K419R expression plasmid. The protein levels of HBP1, AFP, PTEN, phospho-AKT, AKT, pro-caspase-3, cleaved-caspase-3 and MMP9 were measured by Western blotting