Fig. 3: LncCIRBIL binds to Bclaf1 and inhibits its nuclear translocation. | Nature Communications

Fig. 3: LncCIRBIL binds to Bclaf1 and inhibits its nuclear translocation.

From: The long noncoding RNA lncCIRBIL disrupts the nuclear translocation of Bclaf1 alleviating cardiac ischemia–reperfusion injury

Fig. 3

A Upper panel: silver staining of proteins pulled down by lncCIRBIL; lower panel: western blot analysis of Bclaf1 pulled down by lncCIRBIL. The data have been reproduced in 3 independent experiments. B RNA immunoprecipitation (RIP) of lncCIRBIL by Bclaf1 antibody in mice heart tissue. N = 9 from 3 mice. *P < 0.05 versus IgG group. P values were determined by unpaired t test. C LncCIRBIL distribution by in situ hybridization and Bclaf1 by immunofluorescence staining in isolated adult cardiomyocytes from WT, lncCIRBIL-TG, and lncCIRBIL-KO mice (scale bar: 20 μm). D, E Bclaf1 protein levels in subcellular fractions determined by western blot. Lamin is the loading control for nuclear extracts. N = 3 for total protein; N = 18 for TG, 12 for KO in nuclear protein; N = 17 for TG, 10 for KO in cytoplasmic protein. *P < 0.05 versus WT group. P values were determined by unpaired t test. F Distribution of lncCIRBIL and Bclaf1 in isolated cardiomyocytes after ischemia–reperfusion injury (scale bar: 20 μm). G Detection of Bclaf1 in subcellular fractions by Western blotting after I/R injury. N = 6. *P < 0.05 versus WT-IR group, #P < 0.05 versus WT-IR group. P values were determined by one-way ANOVA test followed by Bonferroni post hoc analysis. Data are expressed as mean ± SEM.

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