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. 2023 Jun 6;11:goad032. doi: 10.1093/gastro/goad032

Figure 8.

Figure 8.

SIRT1 deacetylates CPT1A to suppress its ubiquitination degradation. (A) SIRT1 and CPT1A protein expression levels in HepG2 cells transfected with normal control (NC), SIRT1-WT, or mutant plasmids (SIRT1-H363Y). (B) co-IP experiments in HepG2 cells exposed to vehicle or PA with or without BBR treatment, using an anti-CPT1A antibody for IP and anti-acetyl-lysine antibody or anti-ubiquitin antibody for immunoblotting. (C) co-IP experiments in SIRT1 knock-down or SIRT1 overexpression HepG2 cells, utilizing an anti-CPT1A antibody for IP and an anti-acetyl-lysine antibody or anti-ubiquitin antibody for immunoblotting. (D) Quantitative analysis of CPT1A acetylation levels in HepG2 cells exposed to vehicle or PA with or without BBR treatment. (E) and (F) Quantitative analysis of CPT1A acetylation levels in (E) SIRT1 knock-down or (F) SIRT1 overexpression HepG2 cells. (G) CPT1A acetylation levels in livers of C57BL/6J mice fed a chow diet or HFD with or without BBR treatment. (H) Quantitative analysis of CPT1A acetylation levels in livers of C57BL/6J mice. (I) co-IP experiments in HEK293T cells co-transfected with HA-CPT1A-WT and SIRT1-WT or catalytic mutant plasmids (SIRT1-H363Y), employing an anti-HA antibody for IP and anti-acetyl-lysine antibodies and anti-ubiquitin antibodies for immunoblotting. All results are representative of three independent experiments. Values are presented as means ± SD; *P < 0.05 (compared with the control group or chow diet group); #P < 0.05 (compared with the PA group or HFD group). WT, wild-type; NC, normal control; sh, short hairpin; Lv, lentivirus; co-IP, co-immunoprecipitation; IP, immunoprecipitation; PA, palmitate; BBR, berberine; HFD, high-fat diet; HEK, human embryonic kidney; Ac, acetylation; Ub, ubiquitin.