Liver tissues were lysed using RIPA lysis buffer and centrifuged at 16,000g for 15 min. LX-2 cells were lysed in RIPA buffer (Cell Signaling Technology, Beverly, MA, USA) containing a cocktail of protease inhibitors (Calbiochem part of Merck KGaA, Darmstadt, Germany) on ice. The supernatants were then obtained after centrifugation at 16,200g for 15 min at 4℃. The protein concentrations of the cell lysates or liver tissues were measured by Bradford assay (Pro-Measure, iNtRON Biotechnology, Seoul, Korea) and the proteins were dissolved in the SDS sample buffer. Western blot analysis was conducted as previously described (Song et al. 2016 (link)). Samples were separated using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE). The separated proteins were transferred to nitrocellulose membranes (GE Healthcare, Madison, WI, USA) and blocked with 5% skim milk. The proteins on the membrane were incubated with the primary antibodies (Supplementary Table 1) overnight. Horseradish peroxidase-conjugated IgG antibodies (Cell Signaling Technology, Beverly, MA, USA) were used as the secondary antibodies. After 2 h incubation with the secondary antibody, immune complexes were detected using the Immobilon Western Chemiluminescent HRP Substrate (Merck Millipore, Billerica, MA, USA).