Cells were harvested and lysed in RIPA buffer (150 mM NaCl, 50 mM Tris Base, 50 mM EDTA, 1% NP40) supplemented with protease inhibitor. Protein quantification was performed using the Coomassie brilliant blue G-250 method. Proteins were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis through 8% to 10% gels and transferred to 0.45‐µm polyvinylidene fluoride membranes (Millipore Corp., Bedford, MA, USA), which were incubated with 5% skim milk for 1 hour to block nonspecific binding sites. The membranes were then incubated overnight at 4°C with the following primary antibodies: anti-LSD1 (1:1000, Cell Signaling Technology, Danvers, MA, USA, cat. 2184), anti–β-catenin (1:1000, ProteinTech, Rosemont, IL, USA, cat. 51067-2-AP), anti-H3K4me2 (1:1000, Cell Signaling Technology, Danvers, MA, USA, cat. 9725), anti–β-actin (1:1000, Servicebio, cat. GB12001), anti–c-MYC (1:1000, ProteinTech, cat. 10828-1-AP), anti–cyclin D3 (1:1000, Cell Signaling Technology, Danvers, MA, USA, cat. 2936), anti–caspase 3 (1:1000, Cell Signaling Technology, Danvers, MA, USA, cat. 14220T), anti–cleaved caspase 3 (1:1000, Cell Signaling Technology, Danvers, MA, USA, cat. 9664T), and anti-poly(ADP-ribose)polymerase (PARP) (1:1000, Cell Signaling Technology, Danvers, MA, USA, cat. 9532). The membranes were washed three times in PBST (PBS containing 0.1% Tween) and incubated with the appropriate secondary antibody (anti-mouse IgG, 1:15,000, Promega, Madison, WI, USA, cat. W4021 or anti-rabbit IgG, 1:15,000, Promega, cat. W4011) at room temperature for 1 hour before the protein bands were visualized with chemiluminescence (Thermo Scientific, Waltham, MA, USA).