Xenoestrogen-induced Regulation of EZH2 and Histone Methylation via Non-Genomic Estrogen
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1 Xenoestrogen-induced Regulation of EZH2 and Histone Methylation via Non-Genomic Estrogen Receptor Signaling to PI3K/AKT Tiffany G. Bredfeldt, Kristen L. Greathouse, Stephen H. Safe, Mien-Chie Hung, Mark T. Bedford, Cheryl L. Walker SUPPLEMENTAL FIGURE LEGENDS Figure S1. E2-BSA does not activate the genomic ER pathway. RNA was extracted from MCF-7 cells treated with E2-BSA (25 nm), DES (50 nm), or VEH for 6 h. DNase treated RNA was then reversed transcribed into cdna. cdna was then subjected to qpcr analysis. The calibrator for this qpcr experiment was a VEH sample. Fold change was calculated for each sample in comparison to the calibrator. Graph bars represent mean ± SEM. Statistical significance (p 0.05) was determined by student s t-test. Figure S2. MCF-7 cells stably transfected with CA-AKT have increased P-EZH2 and reduced H3K27Me3 levels. A. Lysates were collected from MCF-7 cells or MCF-7 cells stably transfected with CA-AKT and analyzed by western blot to determine activity of AKT pathway. Increases in phospho-tsc2 and phospho-s6k demonstrate elevated AKT activity. B. Increased AKT activity induces EZH2 phosphorylation. P-EZH2 was immunoprecipitated from MCF-7 cells or MCF-7 cells stably transfected with CA-AKT. Immunoprecipitates were resolved by SDS-PAGE and blotted for EZH2. EZH2 and AKT inputs are used as a loading control.
2 C. Constitutively active AKT (CA-AKT) causes reduction in H3K27Me3 levels in an estrogenresponsive cell line. Histone proteins were collected from MCF-7 or MCF-7 CA-AKT cells and analyzed by western blot. Graphs show densitometry analysis of western blot data as represented by change in phosphorylation (P-EZH2/total EZH2) or methylation (H3K27Me3/total H3) relative to MCF-7 cells. Statistical significance was given to data with p 0.05 as determined by student s t-test. Figure S3. Growth factor-induced activation of the PI3K/AKT pathway and downstream EZH2 phosphorylation. A. MCF-7 cells were starved for 48 h and then treated with IGF (20 ng/ml), which activated the PI3K/AKT pathway. B. Serum deprived MCF-7 cells were treated with 20% serum for indicated times. Activation of the PI3K/AKT pathway was detected by western blot analysis. C. Immunoprecipitation of phospho-ezh2 from MCF-7 cells treated with 20% serum demonstrates growth factor-induced EZH2 phosphorylation as determined by immunoprecipitation of phospho- EZH2. Each panel displays a representative western blot from three independent experiments. Graphs display the increase in phospho-akt relative to loading control (mean ± SEM), which has been normalized to VEH treated cells as determined by densitometry. Figure S4. Xenoestrogen-induced activation of non-genomic signaling causes phosphorylation of EZH2. MCF-7 cells were transfected using 6 μg of plasmid DNA (for a 10 cm plate), Opti-MEM, and Lipofectamine 2000 according to manufacturer s specifications (Invitrogen, Carlsbad, CA). Cells were
3 transfected with myc-ezh2 or mock in complete media h after transfection, complete media was replaced with phenol red-free, serum-free media for an additional 24 h prior to treatment. Following transfection and subsequent starvation, MCF-7 cells were treated with DES (50 nm) for indicated times and cell lysates were collected and subjected to immunoprecipitation followed by western blot analysis. Figure S5. A low concentration of xenoestrogen activates the PI3K/AKT pathway to phosphorylate EZH2. A. Lysates were collected from MCF-7 cells treated with 5 nm DES or VEH (ethanol) and analyzed by western blot for activation of the PI3K/AKT pathway, as detected by increases in phospho- AKT, phospho-s6k, and phospho-s6. B. Immunoprecipitation of phospho-ezh2 from MCF-7 cells treated with 5 nm DES indicates that activation of rapid ER signaling by this treatment causes EZH2 phosphorylation. Graphs display densitometry analysis of western blots of phospho-akt or phospho-ezh2 from independent experiments relative to VEH treated cells. Statistical significance (p 0.05) was determined by student s t-test. Figure S6. Scheme demonstrating estrogen-induced reprogramming of gene expression in uterine myometrial cells. 1. Cells are depleted of hormone and growth factors for 48 h. 2. Non-genomic signaling and EZH2 phosphorylation is stimulated by daily treatment with E2-BSA or DES to modulate H3K27Me3 levels and promote chromatin remodeling. 3. Priming estrogen treatments are removed and cells are washed with PBS to remove estrogen and maintained in serum- and hormone-free media for 48 h. 4. Cells are challenged with DES and the expression of estrogen-responsive genes is analyzed by qpcr.
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DOI:.38/ncb2822 a MTC02 FAO cells EEA1 b +/+ MEFs /DAPI -/- MEFs /DAPI -/- MEFs //DAPI c HEK 293 cells WCE N M C P AKT TBC1D7 Lamin A/C EEA1 VDAC d HeLa cells WCE N M C P AKT Lamin A/C EEA1 VDAC Figure
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Supplementary Figure 1 IL-27 IL
Tim-3 Supplementary Figure 1 Tc0 49.5 0.6 Tc1 63.5 0.84 Un 49.8 0.16 35.5 0.16 10 4 61.2 5.53 10 3 64.5 5.66 10 2 10 1 10 0 31 2.22 10 0 10 1 10 2 10 3 10 4 IL-10 28.2 1.69 IL-27 Supplementary Figure 1.
(A) Dose response curves of HMLE_shGFP (blue circle), HMLE_shEcad (red square),
Supplementary Figures and Tables Figure S1. Validation of EMT-selective small molecules (A) Dose response curves of HMLE_shGFP (blue circle), HMLE_shEcad (red square), and HMLE_Twist (black diamond) cells
Supplementary Figure 1. mir124 does not change neuron morphology and synaptic
Supplementary Figure 1. mir124 does not change neuron morphology and synaptic density. Hippocampal neurons were transfected with mir124 (containing DsRed) or DsRed as a control. 2 d after transfection,
LPS LPS P6 - + Supplementary Fig. 1.
P6 LPS - - - + + + - LPS + + - - P6 + Supplementary Fig. 1. Pharmacological inhibition of the JAK/STAT blocks LPS-induced HMGB1 nuclear translocation. RAW 267.4 cells were stimulated with LPS in the absence
(A) SW480, DLD1, RKO and HCT116 cells were treated with DMSO or XAV939 (5 µm)
Supplementary Figure Legends Figure S1. Tankyrase inhibition suppresses cell proliferation in an axin/β-catenin independent manner. (A) SW480, DLD1, RKO and HCT116 cells were treated with DMSO or XAV939
TITLE: Characterization of the Mechanisms of IGF-I-Mediated Stress-Activated Protein Kinase Activation in Human Breast Cancer Cell MCF-7
AD Award Number DAMD17-98-1-8066 TITLE: Characterization of the Mechanisms of IGF-I-Mediated Stress-Activated Protein Kinase Activation in Human Breast Cancer Cell MCF-7 PRINCIPAL INVESTIGATOR: Wei Liu,
Figure S1. Generation of inducible PTEN deficient mice and the BMMCs (A) B6.129 Pten loxp/loxp mice were mated with B6.
Figure S1. Generation of inducible PTEN deficient mice and the BMMCs (A) B6.129 Pten loxp/loxp mice were mated with B6.129-Gt(ROSA)26Sor tm1(cre/ert2)tyj /J mice. To induce deletion of the Pten locus,