Fig. 4

JMJD2C enhances HES1 expression by interacting with HIF1α to remove H3K9 methylation modification at the HES1 promoter region in cells. a Representative Western blots of HES1 protein and its quantitation in MG-63 and SaOS-2 cells treated with si-HIF1α, relative to β-actin. * p < 0.05 vs. cells treated with si-NC by unpaired t-test. b Representative Western blots of JMJD2C, HIF1α and HES1 proteins and their quantitation in MG-63 and SaOS-2 cells treated with si-HIF1α, relative to β-actin. * p < 0.05 vs. cells treated with oe-NC + LV-shNC. c The quantity of the HES1 promoter in the immune complexes was determined by ChIP-qPCR assay in MG-63 and SaOS-2 cells treated with oe-JMJD2C or in combination with shHIF1α. * p < 0.05 vs. cells treated with oe-NC + LV-shNC. d Representative Western blots of JMJD2C, HIF1α, and HES1 proteins and their quantitation in MG-63 and SaOS-2 cells treated with oe-JMJD2C or in combination with shHIF1α, relative to β-actin. * p < 0.05 vs. cells treated with LV-shNC + oe-NC. e The quantity of the HES1 promoter in the immune complexes was determined by ChIP-qPCR assay in MG-63 and SaOS-2 cells treated with shJMJD2C or in combination with oe-HIF1α. f, g The quantity of HES1 promoter in the immune complexes with anti-H3K9me2 (f) and anti-H3 (g) in MG-63 and SaOS-2 cells treated with shJMJD2C or in combination with oe-HIF1α. * p < 0.05 vs. cells treated with LV-shNC + oe-NC. Data in panel (c-h) were performed using one-way ANOVA with Tukey’s test. Data are shown as mean ± standard deviation of three technical replicates