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. 2018 Mar 14;9(3):398. doi: 10.1038/s41419-018-0428-x

Fig. 3. The HDAC3 deficiency inhibited STAT3(Y705) phosphorylation and enhanced STAT3 acetylation in hepatocytes.

Fig. 3

a Immunofluorescence demonstrates that p-STAT3(Y705) is not activated in the HDAC3△ hepatocytes (scale bar: 50 μm). b Western blot analysis shows that p-STAT3(Y705) and c-myc are reduced in the HDAC3△ mice during the early phase of liver regeneration. GAPDH was used as the loading control. c Western blot analysis shows that p-STAT3 remains inhibited in the mutant hepatocytes after the LPS/PH treatment. d Co-immunoprecipitation shows that STAT3 is associated with p300 in both the control and HDAC3△ liver. e Immunoprecipitation confirms that the protein complex overwhelmingly consists of ac-STAT3 with extremely low p-STAT3(Y705) in the HDAC3△ liver. f Western blot analysis shows that the HDAC3 deficiency leads to prolonged acetylation of STAT3 in the cytoplasm during liver regeneration. β-Actin and histone H3 were used as the loading controls. g Immunofluorescence demonstrates that ac-STAT3 significantly accumulates in the cytoplasm of the HDAC3△ hepatocytes (scale bar: 50 μm). n = 3–5; ***p < 0.001