Fig. 4: Protein stability of KDM5B isoforms. | Cancer Gene Therapy

Fig. 4: Protein stability of KDM5B isoforms.

From: A truncated and catalytically inactive isoform of KDM5B histone demethylase accumulates in breast cancer cells and regulates H3K4 tri-methylation and gene expression

Fig. 4

A After CHX treatment, the KDM5B-NTT results more stable than KDM5B-PLU-1 in both MCF7 and MDA-MB-231, as shown from the blots using the anti-C-terminal KDM5B (upper panel) and the anti-exon-6 KDM5B (lower panel) antibodies. B Degradation kinetics of KDM5B isoforms in a time course in MCF7 cells (n = 3 for each time point). C Degradation kinetics of KDM5B isoforms in a time course in MDA-MB-231 cells (n = 3 for each time point). D Comparing the degradation curves of PLU-1 isoform in the two analyzed breast cancer cell lines, it was found a different rate of degradation, that is significantly faster in MDA-MB-231, where the mean half-life-time of the PLU-1 is of about 2 h, versus MCF7, where instead it is around 4 h (n = 3 for each time point). E The cycloheximide (CHX) treatment highlights the PLU-1 instability, which is rescued by MG132 treatment, demonstrating that the proteasomal activity regulates the turnover of PLU-1 isoform in MCF7 and MDA-MB-231. ns: p > 0.05, *p < = 0.05, **p < = 0.01, ***p < = 0.001; Statistics by unpaired Welch’s t-test.

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