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. Author manuscript; available in PMC: 2020 Feb 4.
Published in final edited form as: Sci Transl Med. 2019 May 29;11(494):eaau9087. doi: 10.1126/scitranslmed.aau9087

Fig. 4. Up-regulation of histone methylation in the PPARγ gene in myeloma-associated adipocytes.

Fig. 4.

(A and B) Western blots showing the expression of H3K27me3 in adipocytes isolated from normal BM (n = 4), the BM of patients in complete remission (CR Pt; n = 5), and the BM of patients with newly diagnosed myeloma (New Pt; n = 2) (A) and in normal adipocytes and adipocytes exposed to ARP-1, RPMI8226, or patient-derived myeloma cells (Pt MM; n = 3) (B). The expression of H3 protein served as loading controls. (C) Binding profile of ChIP-seq results for H3K27me3 in normal adipocytes and adipocytes exposed to myeloma cells in the PPARγ gene located in chromosome 3. Lower panel, enlarged view. R1 to R4, subregions covering promoter region and transcriptional starting site of the PPARγ gene. (D) ChIP assay showing the enrichment of EZH2, SUZ12, and H3K27me3 in normal adipocytes and adipocytes exposed to myeloma cells. (E) Western blots showing the expression of EZH2, SUZ12, PPARγ, and H3K27me3 in adipocytes exposed to myeloma cells with or without 1 μM 3-deazaneplanocin A (DZNep) treatment. β-Actin served as a loading control. (F) ChIP assay showing EZH2, SUZ12, and H3K27me3 enrichment in adipocytes exposed to Pt MM (n = 5), ARP-1, or RPMI8226 cells with or without DZNep. Data are averages ± SD. Each experiment was repeated three times. **P < 0.01; ***P < 0.001. All P values were determined using one-way ANOVA.