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Results: 4

1.
Figure 4

Figure 4. From: Bisphenol A Diglycidyl Ether Induces Adipogenic Differentiation of Multipotent Stromal Stem Cells through a Peroxisome Proliferator-Activated Receptor Gamma-Independent Mechanism.

Effect of the PPARγ antagonist T0070907 in BADGE- or BPA-induced adipogenic abilities of MSCs. Adipogenesis was induced in hMSCs (A) or mMSCs (B) by the addition of an adipogenic cocktail for 14 days with DMSO, 500 nM ROSI, 100 nM BADGE, or 100 nM BPA in the presence of DMSO or 100 nM T0070907 (PPARγ antagonist). All data are expressed as mean ± SE lipid accumulation in six replicates. *p < 0.05, and **p < 0.01 relative to vehicle (DMSO) controls.

Raquel Chamorro-García, et al. Environ Health Perspect. 2012 July;120(7):984-989.
2.
Figure 1

Figure 1. From: Bisphenol A Diglycidyl Ether Induces Adipogenic Differentiation of Multipotent Stromal Stem Cells through a Peroxisome Proliferator-Activated Receptor Gamma-Independent Mechanism.

Dose response of MSCs adipogenic capacities to in vitro exposure to BADGE and BPA. Adipogenesis was induced in hMSCs (A) and mMSCs (B) by the addition of an adipogenic cocktail for 14 days in the absence (DMSO) or presence of ROSI 500 nM or increasing doses of BADGE and BPA. All data are expressed as mean ± SE lipid accumulation in six replicates. *p < 0.05, **p < 0.01, and #p < 0.001 relative to vehicle (DMSO) controls.

Raquel Chamorro-García, et al. Environ Health Perspect. 2012 July;120(7):984-989.
3.
Figure 3

Figure 3. From: Bisphenol A Diglycidyl Ether Induces Adipogenic Differentiation of Multipotent Stromal Stem Cells through a Peroxisome Proliferator-Activated Receptor Gamma-Independent Mechanism.

Neither BADGE nor BPA affects PPARγ or RXR activity in transient transfection assays. The ability of a graded dose series of BADGE or BPA to activate or antagonize GAL4-hPPARγ and GAL-hRXRα was tested in transiently transfected COS7 cells. (A,B) Activation assays: BADGE and BPA (10–10 M through 10–4 M) were tested with 10–4 M producing noticeable cytotoxicity as judged by β-galactosidase activity. The control compounds ROSI (PPARγ agonist) and LG-268 (RXR agonist) were also tested (10–10 through 10–5 M). Neither BADGE nor BPA activated PPARγ or RXR. (C,D) Antagonism assays: BADGE, BPA, GW9662 (PPARγ antagonist), and HX-531 (RXR antagonist) were tested (10–10 through 10–5 M) against 10–7 M ROSI (PPARγ; C) or 10–7 M LG-268 (RXRα; D). Although GW9662 effectively antagonized PPARγ activity, BADGE and BPA did not. HX-531 antagonized RXRα at 10–5 M, whereas BADGE and BPA were inactive. Data are presented as fold induction over vehicle (0.1% DMSO) controls for activation assays or as fold reduction over 10–7 M ROSI or 10–7 M LG-268 for antagonism assays.

Raquel Chamorro-García, et al. Environ Health Perspect. 2012 July;120(7):984-989.
4.
Figure 2

Figure 2. From: Bisphenol A Diglycidyl Ether Induces Adipogenic Differentiation of Multipotent Stromal Stem Cells through a Peroxisome Proliferator-Activated Receptor Gamma-Independent Mechanism.

In vitro effect of BADGE exposure on the adipogenic capacities of hMSCs and mMSCs. Lipid accumulation in hMSCs (A) and mMSCs (B) (left). Adipogenesis was induced in MSCs by the addition of an adipogenic cocktail for 14 days with DMSO, 500 nM ROSI, 100 nM BADGE, or 100 nM BPA. Gene expression profile in hMSCs and mMSCs was assayed by QPCR (right) [early adipogenesis markers: PPARγ2, Pref-1, and FABP4; late adipogenesis markers: LEP, LPL, and ADIPOQ]. Expression was normalized to β-actin. (C) FABP4 protein levels were assayed by flow cytometry. Median fluorescence intensities (MFI) are represented relative to vehicle (DMSO) controls. ADIPOQ, adiponectin. All data are expressed as mean fold change ± SE in six replicates. *p < 0.05, **p < 0.01, and #p < 0.001 relative to vehicle (DMSO) controls.

Raquel Chamorro-García, et al. Environ Health Perspect. 2012 July;120(7):984-989.

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