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1.
Figure 6

Figure 6. Schema summarizing the paradoxical regulation of human FGF21.. From: Paradoxical Regulation of Human FGF21 by Both Fasting and Feeding Signals: Is FGF21 a Nutritional Adaptation Factor?.

A: Both fasting (PPARα and glucagon) and over feeding (glucose) signals activate human FGF21 gene transcription. B: Human FGF21 gene expression responds to nutritional crisis including fasting, starvation, over feeding and obesity.

Takashi Uebanso, et al. PLoS One. 2011;6(8):e22976.
2.
Figure 5

Figure 5. ChREBP is needed to induce FGF21 gene transcription by glucose.. From: Paradoxical Regulation of Human FGF21 by Both Fasting and Feeding Signals: Is FGF21 a Nutritional Adaptation Factor?.

A, B: Changes in relative ChREBP gene expression and protein abundance at 48 h after transfection of either shLacZ or shChREBP vector in mouse primary hepatocytes. C: Changes in relative luciferase activity of the human −1.6 kb FGF21 reporter vector stimulated by 20 mM glucose 48 h after transfection of either shLacZ or shChREBP vector in mouse primary hepatocytes. The relative mRNA expression and protein abundance of ChREBP transfected with shLacZ vector was set as 1.0. The relative luciferase activity of NT (non-treatment) was 1.0. Data represent mean ± SE (n = 3). * p<0.05 as compared to shLacZ or NT.

Takashi Uebanso, et al. PLoS One. 2011;6(8):e22976.
3.
Figure 4

Figure 4. The human FGF21 promoter has a putative carbohydrate-responsive element.. From: Paradoxical Regulation of Human FGF21 by Both Fasting and Feeding Signals: Is FGF21 a Nutritional Adaptation Factor?.

A, B: Changes in ChREBP protein abundance in cytosolic and nuclear fractions from mouse primary hepatocytes stimulated by 10 mM xylitol for 6 h. C: Putative carbohydrate responsive element (ChoRE) in the human FGF21 promoter. D: An electrophoretic mobility shift assay was performed with the mouse primary hepatocyte nuclear fraction stimulated by xylitol (X) or not (NT). We used a putative ChoRE (−380 to −366 bp; lanes 1–5). Factor C is a competitor (L-pk; −142 to −124 bp) and Ab is ChREBP antibody. Arrow indicates DNA and protein complex. Data represent mean ± SE (n = 3). *: p<0.05 as compared to NT (non-treatment).

Takashi Uebanso, et al. PLoS One. 2011;6(8):e22976.
4.
Figure 1

Figure 1. Glucose and xylitol induced FGF21 gene expression in HepG2 and mouse primary hepatocytes.. From: Paradoxical Regulation of Human FGF21 by Both Fasting and Feeding Signals: Is FGF21 a Nutritional Adaptation Factor?.

A: Changes in FGF21 gene expression stimulated by the indicated dose of glucose for 6 h in HepG2. B: Changes in FGF21 protein abundance in HepG2 cells stimulated by indicated dose of glucose for 24 h. C: Changes in FGF21, L-pk, and Fasn gene expression stimulated by 10 mM glucose (Glu), xylitol (Xyl) or mannitol (Man) for 6 h in mouse primary hepatocytes. The relative mRNA amount for each gene treated with 5 mM of glucose (A), or NT (non-treatment) (C) was set as 1.0. D: Changes in FGF21 concentration in the cultured media of mouse primary hepatocytes stimulated by 3 mM glucose (G3) or 25 mM glucose (G25) for indicated time. Data represent mean ± SE (n = 3). †: Concentration-dependent effects were observed by regression analysis, p<0.05. *: p<0.05 as compared to NT, mannitol and G3 stimulation.

Takashi Uebanso, et al. PLoS One. 2011;6(8):e22976.
5.
Figure 2

Figure 2. Wy-14643, glucagon and forskolin induced FGF21 gene transcription in mouse primary hepatocytes.. From: Paradoxical Regulation of Human FGF21 by Both Fasting and Feeding Signals: Is FGF21 a Nutritional Adaptation Factor?.

A: Changes in relative luciferase activity of a pFGF21-1.6k reporter vector containing the −1672 to +230 bp region of the human FGF21 promoter simulated by indicated dose of wy-14643 for 6 h in mouse primary hepatocytes. B: Schematic representation of 5′-deletion mutants of the human FGF21 promoter and changes in relative luciferase activity after stimulation with or without 10 µM wy-14643 for 6 h. C: Changes in relative luciferase activity of the pFGF21-1.6k reporter vector stimulated by 10−7 M glucagon or 10−6 M forskolin (FSK) for 6 h in mouse primary hepatocytes. D: Schematic representation of 5′-deletion mutants of the human FGF21 promoter and changes in relative luciferase activity after stimulation with or without 10−7 M glucagon. The relative luciferase activity treated with DMSO (A), or NT (non-treatment) (C) was set as 1.0. For deletion experiments (B and D), the relative luciferase activity of each deletion constructs treated with DMSO (B) or control (D) was set as 1.0. Data represent mean ± SE (n = 3). †: Concentration-dependent effects were observed by regression analysis, p<0.05. *: p<0.05 as compared to DMSO or NT.

Takashi Uebanso, et al. PLoS One. 2011;6(8):e22976.
6.
Figure 3

Figure 3. Glucose and xylitol induced human FGF21 gene transcription in mouse primary hepatocytes and HepG2 cells.. From: Paradoxical Regulation of Human FGF21 by Both Fasting and Feeding Signals: Is FGF21 a Nutritional Adaptation Factor?.

A: Changes in relative luciferase activity of the pFGF21-1.6k reporter vector stimulated by indicated dose of glucose for 24 h in HepG2 cells. B: Basal luciferase activity of the pFGF21-1.6k reporter vector in mouse primary hepatocytes (Mpl) and HepG2 cells. C: Changes in relative luciferase activity of the pFGF21-1.6k reporter vector stimulated by 10 mM glucose (Glu), xylitol (Xyl) or mannitol (Man) for 6 h in mouse primary hepatocytes. D: Changes in relative luciferase activity of the pFGF21-1.6k reporter vector stimulated by the indicated dose of xylitol for 6 h in mouse primary hepatocytes. E, F: Schematic representation of 5′-deletion mutants of the human FGF21 promoter and changes in relative luciferase activity after stimulation with or without 20 mM xylitol (E) or 20 mM glucose (F). G, H: Basal luciferase activities of 5′-deletion mutants of the human FGF21 promoter in mouse primary hepatocytes (G) and HepG2 cells (H). The relative luciferase activity for C through F was expressed as described in the Figure 2. For basal luciferase activity analysis (G and H), the relative luciferase activity of -1672 bp was set as 1.0. Data represent mean ± SE (n = 3). †: Concentration-dependent effects were observed by regression analysis, p<0.05. *: p<0.05 as compared to the control.

Takashi Uebanso, et al. PLoS One. 2011;6(8):e22976.

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