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. 2021 Jul 25;17(12):3173–3187. doi: 10.7150/ijbs.62556

Figure 5.

Figure 5

BBR increases the deacetylated level of PPARγ by SIRT1 activation. The levels of PPARγ acetylation were measured in fully differentiated (A, B) 3T3-L1 and (C, D) HIB1b cells treated with BBR (5 μM) for 24 h. The levels of PPARγ acetylation were examined via immunoprecipitation (IP) with anti-acetylated lysine antibody and anti-PPARγ antibody. The effects of BBR on PPARγ acetylation were determined in WT and SIRT1 knockout (E) 3T3-L1 and (F) HIB1b cells, respectively. (G) WT and Sirt1-/- mouse embryonic fibroblasts (MEFs) were treated with or without BBR (5 μM) for 24 h. (H) Flag-SIRT1 plasmid or catalytically inactive mutant 363 HY plasmid was transfected into stably SIRT1 knockdown 3T3-L1 cells. WT and SIRT1 knockdown 3T3-L1 cells were treated with BBR (5 μM) for 24 h. The levels of PPARγ acetylation were examined by IP with anti-acetylated lysine antibody.