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R&D Systems human gdf15 enzyme linked immunosorbent assay kit
Human Gdf15 Enzyme Linked Immunosorbent Assay Kit, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 282 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+gdf15+enzyme+linked+immunosorbent+assay+kit/Human+GDF-15+Quantikine+ELISA+Kit/pm41898219-59-9-17
Average 96 stars, based on 282 article reviews

human gdf15 enzyme linked immunosorbent assay kit - by Bioz Stars, 2026-09

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Article Title: Circulating GDF15 and HbA1c Response to Add-On Exenatide Therapy in Type 2 Diabetes: A Post Hoc Analysis from a Multicenter Trial.
Article Snippet: The serum GDF15 levels were detected by using a human GDF15 enzyme-linked immunosorbent assay kit (Cat: DGD150, R&D Systems, Minneapolis, MN, USA).

Article Title: Circulating GDF15 and HbA1c Response to Add-On Exenatide Therapy in Type 2 Diabetes: A Post Hoc Analysis from a Multicenter Trial
Article Snippet: The serum GDF15 levels were detected by using a human GDF15 enzyme-linked immunosorbent assay kit (Cat: DGD150, R&D Systems, Minneapolis, MN, USA).

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Fig. 1 Gene expression of GDF 15 in human bladder cells. The mRNA levels of GDF15 (A) and a-SMA (B) in bladder smooth muscle cells (HBdSMC), ﬁbroblast cells (HBdSF), normal epithelial cells (HBdEC), and carcinoma cell lines (RT-4, HT1376, T24, and TSGH-8301) were determined by RT-qPCR assays. Data are expressed as the mean ratio of mRNA in relation to HJBdEC cells (n ¼ 3). (C) The protein levels of a-SMA, UPK2, and b-actin in bladder cells as indicated were determined by immunoblot assays. (D) GDF15 secretions from bladder cells as determined by ELISA (n ¼ 4).

Journal: Biomedical journal

Article Title: Caffeic acid phenethyl ester inhibits the growth of bladder carcinoma cells by upregulating growth differentiation factor 15.

doi: 10.1016/j.bj.2021.10.006

Figure Lengend Snippet: Fig. 1 Gene expression of GDF 15 in human bladder cells. The mRNA levels of GDF15 (A) and a-SMA (B) in bladder smooth muscle cells (HBdSMC), ﬁbroblast cells (HBdSF), normal epithelial cells (HBdEC), and carcinoma cell lines (RT-4, HT1376, T24, and TSGH-8301) were determined by RT-qPCR assays. Data are expressed as the mean ratio of mRNA in relation to HJBdEC cells (n ¼ 3). (C) The protein levels of a-SMA, UPK2, and b-actin in bladder cells as indicated were determined by immunoblot assays. (D) GDF15 secretions from bladder cells as determined by ELISA (n ¼ 4).

Article Snippet: The protein levels of the cell supernatants were measured by GDF15 enzyme-linked immunosorbent assay kit (Catalog #: DY957; R&D Systems, Inc., Minneapolis, MN, USA) per the r inhibits the growth of bladder carcinoma cells by upregulating 0.1016/j.bj.2021.10.006 manufacturer's protocol.

Techniques: Gene Expression, Quantitative RT-PCR, Western Blot, Enzyme-linked Immunosorbent Assay

Fig. 2 Effects of CAPE on GDF15 expression and proliferation of bladder carcinoma cells. (A) HT1376 and T24 cells were treated with various concentrations of CAPE as indicated for 24 h, then lysed, and the mRNA levels of GDF15 and b-actin were determined by RT-qPCR assays. Data are expressed as the mean ratio of mRNA relative to the control group (n ¼ 3). (B) GDF15 protein levels in conditional media were determined by ELISA (n ¼ 4). (C) T24 cells were treated with various concentrations of CAPE as indicated for 24 h and protein levels of GDF15 were determined by immunoblots. (D) The reporter activity of the GDF15 reporter vector in HT1376 cells treated with various dosages of CAPE for 24 h. Data are expressed as the mean percentage of luciferase activity relative to the mock-transfected group (n ¼ 6). The mRNA (E) and protein (F) levels of target genes as indicated were determined by RT-qPCR and immunoblots. Data are expressed as the mean ratio of mRNA relative to the control group (n ¼ 3). (G) Cell proliferation of T24 cells was determined by EdU assays after CAPE (30 mM) treatment for 24 h (n ¼ 4). **P < 0.01, *P < 0.05.

Journal: Biomedical journal

Article Title: Caffeic acid phenethyl ester inhibits the growth of bladder carcinoma cells by upregulating growth differentiation factor 15.

doi: 10.1016/j.bj.2021.10.006

Figure Lengend Snippet: Fig. 2 Effects of CAPE on GDF15 expression and proliferation of bladder carcinoma cells. (A) HT1376 and T24 cells were treated with various concentrations of CAPE as indicated for 24 h, then lysed, and the mRNA levels of GDF15 and b-actin were determined by RT-qPCR assays. Data are expressed as the mean ratio of mRNA relative to the control group (n ¼ 3). (B) GDF15 protein levels in conditional media were determined by ELISA (n ¼ 4). (C) T24 cells were treated with various concentrations of CAPE as indicated for 24 h and protein levels of GDF15 were determined by immunoblots. (D) The reporter activity of the GDF15 reporter vector in HT1376 cells treated with various dosages of CAPE for 24 h. Data are expressed as the mean percentage of luciferase activity relative to the mock-transfected group (n ¼ 6). The mRNA (E) and protein (F) levels of target genes as indicated were determined by RT-qPCR and immunoblots. Data are expressed as the mean ratio of mRNA relative to the control group (n ¼ 3). (G) Cell proliferation of T24 cells was determined by EdU assays after CAPE (30 mM) treatment for 24 h (n ¼ 4). **P < 0.01, *P < 0.05.

Techniques: Expressing, Quantitative RT-PCR, Control, Enzyme-linked Immunosorbent Assay, Western Blot, Activity Assay, Plasmid Preparation, Luciferase, Transfection

Fig. 3 Downregulation of cell proliferation and invasion by CAPE is GDF15-dependent in bladder carcinoma HT1376 cells. (A) HT_shCOL and HT_shGDF15 cells were treated with (þ) or without () CAPE (30 mM) for 24 h. The protein levels of target genes, as indicated, were determined via immunoblotting. (B) HT_shCOL and HT_shGDF15 cells were treated with (þ) or without () CAPE (30 mM) for 24 h and GDF15 secretions in the supernatants of culture media were determined by ELISA (n ¼ 4). (C) HT_shCOL and HT_shGDF15 cells were treated with (þ) or without () CAPE (30 mM) for 24 h, then the relative mRNA levels of GDF15, NDRG1, and maspin were determined by RT-qPCR assays (n ¼ 3). (D) Cell proliferation of HT_shCOL and HT_shGDF15 cells after treated with CAPE (30 mM) for 48 h was determined by EdU assays (n ¼ 4). (E) The quantitative result of EdU assays. (F) HT_shCOL and HT_shGDF15 cells were treated with 30 mM CAPE for 48 h and cell proliferation was determined by the CyQuant assay. The data were presented as the mean percentage compared with the control group (DMSO-treated, n ¼ 8). (G) HT_shCOL and HT_shGDF15 cells were treated with CAPE (30 mM) for 24 h and the cell invasive ability was measured by the Matrigel invasion assay after 24 h of incubation (H) The quantitative result of invasion assays. The data were presented as the mean percentage compared with the control group (DMSO-treated, n ¼ 3). **P < 0.01, *P < 0.05.

Journal: Biomedical journal

Article Title: Caffeic acid phenethyl ester inhibits the growth of bladder carcinoma cells by upregulating growth differentiation factor 15.

doi: 10.1016/j.bj.2021.10.006

Figure Lengend Snippet: Fig. 3 Downregulation of cell proliferation and invasion by CAPE is GDF15-dependent in bladder carcinoma HT1376 cells. (A) HT_shCOL and HT_shGDF15 cells were treated with (þ) or without () CAPE (30 mM) for 24 h. The protein levels of target genes, as indicated, were determined via immunoblotting. (B) HT_shCOL and HT_shGDF15 cells were treated with (þ) or without () CAPE (30 mM) for 24 h and GDF15 secretions in the supernatants of culture media were determined by ELISA (n ¼ 4). (C) HT_shCOL and HT_shGDF15 cells were treated with (þ) or without () CAPE (30 mM) for 24 h, then the relative mRNA levels of GDF15, NDRG1, and maspin were determined by RT-qPCR assays (n ¼ 3). (D) Cell proliferation of HT_shCOL and HT_shGDF15 cells after treated with CAPE (30 mM) for 48 h was determined by EdU assays (n ¼ 4). (E) The quantitative result of EdU assays. (F) HT_shCOL and HT_shGDF15 cells were treated with 30 mM CAPE for 48 h and cell proliferation was determined by the CyQuant assay. The data were presented as the mean percentage compared with the control group (DMSO-treated, n ¼ 8). (G) HT_shCOL and HT_shGDF15 cells were treated with CAPE (30 mM) for 24 h and the cell invasive ability was measured by the Matrigel invasion assay after 24 h of incubation (H) The quantitative result of invasion assays. The data were presented as the mean percentage compared with the control group (DMSO-treated, n ¼ 3). **P < 0.01, *P < 0.05.

Techniques: Western Blot, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR, CyQUANT Assay, Control, Invasion Assay, Incubation

Fig. 4 CAPE induces the phosphorylation of ERK, JNK, and p38 to modulate the expressions of GDF15, NDRG1, and maspin in bladder carcinoma HT1376 cells. (A) HT1376 cells were treated with various concentrations of CAPE as indicated for 24 h and the mRNA levels of target genes as indicated were determined by RT-qPCR assays. (B) Protein levels of target genes, as indicated, were determined by immunoblot assays after treatment with various concentrations of CAPE as indicated for 16 h in HT1376 cells. The quantitative data were expressed as the intensity of protein bands of the target genes/b-actin relative to the control solvent-treated group (n ¼ 3). The expressions of ERK, p-ERK (C, top), JNK, p-JNK (D, top), p38, and p-p38 (E, top) were determined by the immunoblots after 20 min of 30 mM CAPE treatment with (þ) or without () pretreatment of the indicated MAPK inhibitors for 1 h in HT1376 cells. The protein level of GDF15, NDRG1, maspin, and b-actin of HT1376 cells after CAPE treatment with (þ) or without () pretreatment with PD0325901 (C, bottom), SP600125 (D, bottom), or SB202190 (E, bottom). The quantitative data were expressed as the intensity of protein bands of the p-target gene/target gene or target genes/b-actin relative to the control solvent-treated group (n ¼ 3). **P < 0.01, *P < 0.05.

Journal: Biomedical journal

Article Title: Caffeic acid phenethyl ester inhibits the growth of bladder carcinoma cells by upregulating growth differentiation factor 15.

doi: 10.1016/j.bj.2021.10.006

Figure Lengend Snippet: Fig. 4 CAPE induces the phosphorylation of ERK, JNK, and p38 to modulate the expressions of GDF15, NDRG1, and maspin in bladder carcinoma HT1376 cells. (A) HT1376 cells were treated with various concentrations of CAPE as indicated for 24 h and the mRNA levels of target genes as indicated were determined by RT-qPCR assays. (B) Protein levels of target genes, as indicated, were determined by immunoblot assays after treatment with various concentrations of CAPE as indicated for 16 h in HT1376 cells. The quantitative data were expressed as the intensity of protein bands of the target genes/b-actin relative to the control solvent-treated group (n ¼ 3). The expressions of ERK, p-ERK (C, top), JNK, p-JNK (D, top), p38, and p-p38 (E, top) were determined by the immunoblots after 20 min of 30 mM CAPE treatment with (þ) or without () pretreatment of the indicated MAPK inhibitors for 1 h in HT1376 cells. The protein level of GDF15, NDRG1, maspin, and b-actin of HT1376 cells after CAPE treatment with (þ) or without () pretreatment with PD0325901 (C, bottom), SP600125 (D, bottom), or SB202190 (E, bottom). The quantitative data were expressed as the intensity of protein bands of the p-target gene/target gene or target genes/b-actin relative to the control solvent-treated group (n ¼ 3). **P < 0.01, *P < 0.05.

Techniques: Phospho-proteomics, Quantitative RT-PCR, Western Blot, Control, Solvent

Fig. 6 CAPE upregulates the activities of the AMPKa1/2 signaling pathway in bladder carcinoma cells. (A) HT1376 cells were treated with various concentrations of CAPE for 24 h, and the protein levels of the AMPKa1/2 and p-AMPKa1/2 were determined using immunoblot assays. (B) The expression of AMPKa1 and AMPKa2 was determined by RT-qPCR in HT_shCOL and HT_shAMPKa1/2 cells (n ¼ 3). (C) The expression of AMPKa1/2 and b-actin was determined by immunoblotting in HT_shCOL and HT_shAMPKa1/2 cells. The protein level of AMPKa1/2 and b-actin was determined by immunoblot assays (D) and the mRNA level of GDF15 was determined by RT-qPCR assays (E; n ¼ 3) in HT_shCOL and HT_shAMPKa1/2 cells after (þ) or without () 30 mM CAPE treatment. (F) The proliferation of HT_shCOL and HT_shAMPKa1/2 cells was determined by the EdU assays after (þ) or without () 30 mM CAPE treatment for 24 h (n ¼ 4). **P < 0.01, *P < 0.05.

Journal: Biomedical journal

Article Title: Caffeic acid phenethyl ester inhibits the growth of bladder carcinoma cells by upregulating growth differentiation factor 15.

doi: 10.1016/j.bj.2021.10.006

Figure Lengend Snippet: Fig. 6 CAPE upregulates the activities of the AMPKa1/2 signaling pathway in bladder carcinoma cells. (A) HT1376 cells were treated with various concentrations of CAPE for 24 h, and the protein levels of the AMPKa1/2 and p-AMPKa1/2 were determined using immunoblot assays. (B) The expression of AMPKa1 and AMPKa2 was determined by RT-qPCR in HT_shCOL and HT_shAMPKa1/2 cells (n ¼ 3). (C) The expression of AMPKa1/2 and b-actin was determined by immunoblotting in HT_shCOL and HT_shAMPKa1/2 cells. The protein level of AMPKa1/2 and b-actin was determined by immunoblot assays (D) and the mRNA level of GDF15 was determined by RT-qPCR assays (E; n ¼ 3) in HT_shCOL and HT_shAMPKa1/2 cells after (þ) or without () 30 mM CAPE treatment. (F) The proliferation of HT_shCOL and HT_shAMPKa1/2 cells was determined by the EdU assays after (þ) or without () 30 mM CAPE treatment for 24 h (n ¼ 4). **P < 0.01, *P < 0.05.

Techniques: Western Blot, Expressing, Quantitative RT-PCR

Fig. 2. NAG-1/GDF15 overexpression ameliorates HFD-induced hepatic steatosis and regulates lipid homeostasis in C57BL/6 mice. Mice were fed with LFD or HFD for 12 weeks. (A) Serum level of NAG-1/GDF15 as determined by ELISA. (B) Body weight changes. (C) Caloric intake adjusted for body weight. (D) Liver weight. (E) Representative H&E staining of liver tissues. Scale bar, 100 μm. (F) Hepatic TG and NEFA levels. (G–H) The expression of SREBP1c, SCD-1, CD36, and FASN at the mRNA level (G) or protein level (H) in the liver tissues as determined using qRT-PCR or Western blotting analysis. The relative intensities of proteins were normalized against β-actin. Data are shown as means ± SEM from three independent experiments, except for animal feeding study. Statistical analysis was performed using two-way ANOVA with post hoc Bonferroni’s correction in B-D (n = 6 mice/group). Two-way ANOVA followed by the Benjamini-Hochberg method for the FDR correction was used for multiple measurements in A, F-G (n = 6 mice/group), and H (n = 3 mice/group). *P < 0.05, **P < 0.01, ***P < 0.001 vs WT LFD- fed mice, #P < 0.05, ##P < 0.01, ###P < 0.001 vs WT HFD-fed mice. FDR: false discovery rate.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 2. NAG-1/GDF15 overexpression ameliorates HFD-induced hepatic steatosis and regulates lipid homeostasis in C57BL/6 mice. Mice were fed with LFD or HFD for 12 weeks. (A) Serum level of NAG-1/GDF15 as determined by ELISA. (B) Body weight changes. (C) Caloric intake adjusted for body weight. (D) Liver weight. (E) Representative H&E staining of liver tissues. Scale bar, 100 μm. (F) Hepatic TG and NEFA levels. (G–H) The expression of SREBP1c, SCD-1, CD36, and FASN at the mRNA level (G) or protein level (H) in the liver tissues as determined using qRT-PCR or Western blotting analysis. The relative intensities of proteins were normalized against β-actin. Data are shown as means ± SEM from three independent experiments, except for animal feeding study. Statistical analysis was performed using two-way ANOVA with post hoc Bonferroni’s correction in B-D (n = 6 mice/group). Two-way ANOVA followed by the Benjamini-Hochberg method for the FDR correction was used for multiple measurements in A, F-G (n = 6 mice/group), and H (n = 3 mice/group). *P < 0.05, **P < 0.01, ***P < 0.001 vs WT LFD- fed mice, #P < 0.05, ##P < 0.01, ###P < 0.001 vs WT HFD-fed mice. FDR: false discovery rate.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Over Expression, Enzyme-linked Immunosorbent Assay, Staining, Expressing, Quantitative RT-PCR, Western Blot

Fig. 3. NAG-1/GDF15 overexpression increases the expressions of the key genes and protein related to β-oxidation and lipolysis in mice upon both diets. Mice were fed with LFD or HFD for 12 weeks. (A–B) Expression of the key genes related to β-oxidation (A) and lipolysis (B) at the mRNA level in the liver tissues as determined using qRT-PCR. (C) Western blotting and densitometry analysis of the expressions of PPARα, HSL, and ATGL in liver tissues. The relative intensities of proteins were normalized against β-actin. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using two-way ANOVA followed by the Benjamini-Hochberg method for the FDR correction in Figure A–B (n = 6 mice/group), and C (n = 3 mice/group). *P < 0.05, **P < 0.01, ***P < 0.001 vs WT LFD-fed mice, #P < 0.05, ##P < 0.01, ###P < 0.001 vs WT HFD-fed mice.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 3. NAG-1/GDF15 overexpression increases the expressions of the key genes and protein related to β-oxidation and lipolysis in mice upon both diets. Mice were fed with LFD or HFD for 12 weeks. (A–B) Expression of the key genes related to β-oxidation (A) and lipolysis (B) at the mRNA level in the liver tissues as determined using qRT-PCR. (C) Western blotting and densitometry analysis of the expressions of PPARα, HSL, and ATGL in liver tissues. The relative intensities of proteins were normalized against β-actin. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using two-way ANOVA followed by the Benjamini-Hochberg method for the FDR correction in Figure A–B (n = 6 mice/group), and C (n = 3 mice/group). *P < 0.05, **P < 0.01, ***P < 0.001 vs WT LFD-fed mice, #P < 0.05, ##P < 0.01, ###P < 0.001 vs WT HFD-fed mice.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Over Expression, Expressing, Quantitative RT-PCR, Western Blot

Fig. 4. NAG-1/GDF15 overexpression inhibits HFD-induced AIM2 inflammasome activation in mice. (A) Heatmap indicating differential mRNA expression of the components of AIM2 inflammasome (AIM2, ASC, Caspase-1, IL-1β, and IL-18) in liver tissues upon HFD treatment from the GEO database GSE119441. (B–C) The expression of AIM2 inflammasome components (AIM2, ASC, Caspase-1, IL-1β, and IL-18) at the mRNA level (B) and protein level (C) in the liver of the WT and NAG-1 Tg mice upon LFD and HFD as determined using qRT-PCR or Western blotting analysis. The relative intensities of proteins were normalized against β-actin. (D) Serum levels of IL-1β and IL-18 in mice upon both diets. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using two- way ANOVA followed by the Benjamini-Hochberg method for the FDR correction in B and D (n = 6 mice/group), and C (n = 3 mice/group). *P < 0.05, **P < 0.01, ***P < 0.001 vs WT LFD-fed mice, #P < 0.05, ##P < 0.01, ###P < 0.001 vs WT HFD-fed mice.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 4. NAG-1/GDF15 overexpression inhibits HFD-induced AIM2 inflammasome activation in mice. (A) Heatmap indicating differential mRNA expression of the components of AIM2 inflammasome (AIM2, ASC, Caspase-1, IL-1β, and IL-18) in liver tissues upon HFD treatment from the GEO database GSE119441. (B–C) The expression of AIM2 inflammasome components (AIM2, ASC, Caspase-1, IL-1β, and IL-18) at the mRNA level (B) and protein level (C) in the liver of the WT and NAG-1 Tg mice upon LFD and HFD as determined using qRT-PCR or Western blotting analysis. The relative intensities of proteins were normalized against β-actin. (D) Serum levels of IL-1β and IL-18 in mice upon both diets. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using two- way ANOVA followed by the Benjamini-Hochberg method for the FDR correction in B and D (n = 6 mice/group), and C (n = 3 mice/group). *P < 0.05, **P < 0.01, ***P < 0.001 vs WT LFD-fed mice, #P < 0.05, ##P < 0.01, ###P < 0.001 vs WT HFD-fed mice.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Over Expression, Activation Assay, Expressing, Quantitative RT-PCR, Western Blot

Fig. 6. NAG-1/GDF15 regulates lipid metabolism-related gene and protein expressions in the FFA-induced hepatocellular steatosis model. (A–B) Expression of lipogenesis- and lipid uptake-related molecules at the mRNA level (A) and protein level (B) in HepG2 and Huh-7 cells transfected with pcDNA3.1-NAG-1 plasmid as determined using qRT-PCR or Western blotting analysis. (C–D) Expression of lipogenesis- and lipid uptake-related molecules at the mRNA level (C) and protein level (D) in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA. (E) Expression of the key genes related with fatty acid β oxidation and lipolysis at the mRNA level in HepG2 and Huh-7 cells as transfected with pcDNA3.1-NAG-1 plasmid. (F) Western blotting analysis of PPARα, ATGL, and HSL at the protein level in HepG2 and Huh- 7 cells as transfected with pcDNA3.1-NAG-1 plasmid. (G) Expression of the key genes related with fatty acid β oxidation and lipolysis at the mRNA level in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA. (H) Western blotting analysis of PPARα, ATGL, and HSL at the protein level in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA followed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01, ***P < 0.001 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 6. NAG-1/GDF15 regulates lipid metabolism-related gene and protein expressions in the FFA-induced hepatocellular steatosis model. (A–B) Expression of lipogenesis- and lipid uptake-related molecules at the mRNA level (A) and protein level (B) in HepG2 and Huh-7 cells transfected with pcDNA3.1-NAG-1 plasmid as determined using qRT-PCR or Western blotting analysis. (C–D) Expression of lipogenesis- and lipid uptake-related molecules at the mRNA level (C) and protein level (D) in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA. (E) Expression of the key genes related with fatty acid β oxidation and lipolysis at the mRNA level in HepG2 and Huh-7 cells as transfected with pcDNA3.1-NAG-1 plasmid. (F) Western blotting analysis of PPARα, ATGL, and HSL at the protein level in HepG2 and Huh- 7 cells as transfected with pcDNA3.1-NAG-1 plasmid. (G) Expression of the key genes related with fatty acid β oxidation and lipolysis at the mRNA level in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA. (H) Western blotting analysis of PPARα, ATGL, and HSL at the protein level in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA followed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01, ***P < 0.001 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing, Transfection, Plasmid Preparation, Quantitative RT-PCR, Western Blot, Negative Control

Fig. 7. NAG-1/GDF15 inhibits AIM2 inflammasome activation in the FFA-induced hepatocellular steatosis model. (A–B) The expression of AIM2 inflam masome (AIM2, ASC, Caspase-1, IL-1β, and IL-18) at the mRNA (A) and protein level (B) in HepG2 and Huh-7 cells upon treatment with FFA for 24 h as determined using qRT-PCR or Western blotting. (C–D) The mRNA (C) and protein (D) expression of AIM2 inflammasome components in HepG2 and Huh-7 cells as transfected with pcDNA3.1-NAG-1 plasmid with or without FFA treatment. (E, F) The expression of AIM2 inflammasome components at the mRNA (E) and protein level (F) in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA with or without FFA treatment. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA followed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01, ***P < 0.001 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P < 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 7. NAG-1/GDF15 inhibits AIM2 inflammasome activation in the FFA-induced hepatocellular steatosis model. (A–B) The expression of AIM2 inflam masome (AIM2, ASC, Caspase-1, IL-1β, and IL-18) at the mRNA (A) and protein level (B) in HepG2 and Huh-7 cells upon treatment with FFA for 24 h as determined using qRT-PCR or Western blotting. (C–D) The mRNA (C) and protein (D) expression of AIM2 inflammasome components in HepG2 and Huh-7 cells as transfected with pcDNA3.1-NAG-1 plasmid with or without FFA treatment. (E, F) The expression of AIM2 inflammasome components at the mRNA (E) and protein level (F) in HepG2 and Huh-7 cells as transfected with NAG-1 siRNA with or without FFA treatment. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA followed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01, ***P < 0.001 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P < 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Activation Assay, Expressing, Quantitative RT-PCR, Western Blot, Transfection, Plasmid Preparation, Negative Control

Fig. 8. NAG-1/GDF15 inhibits FFA-induced oxidative stress in HepG2 cells. (A–B) Representative DCFH-DA staining of intracellular ROS and quantitative analysis in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid (A) or NAG-1 siRNA (B) with or without FFA treatment. Scale bar, 20 μm. (C–D) Intracellular ROS levels as determined using flow cytometry in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid (C) or NAG-1 siRNA (D) with or without FFA treatment. (E–H) Hepatic activities of SOD and CAT, and level of MDA in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid (E, G) or NAG-1 siRNA (F, H). Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA followed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P < 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 8. NAG-1/GDF15 inhibits FFA-induced oxidative stress in HepG2 cells. (A–B) Representative DCFH-DA staining of intracellular ROS and quantitative analysis in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid (A) or NAG-1 siRNA (B) with or without FFA treatment. Scale bar, 20 μm. (C–D) Intracellular ROS levels as determined using flow cytometry in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid (C) or NAG-1 siRNA (D) with or without FFA treatment. (E–H) Hepatic activities of SOD and CAT, and level of MDA in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid (E, G) or NAG-1 siRNA (F, H). Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA followed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P < 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Staining, Transfection, Plasmid Preparation, Flow Cytometry, Negative Control

Fig. 9. NAG-1/GDF15 alleviates FFA-induced mitochondrial damage and suppresses FFA-induced mtDNA release from mitochondria in HepG2 cells. (A) The copy number of mtDNA as determined using qRT-PCR in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid or NAG-1 siRNA with or without FFA treatment. (B) The release of dsDNA into the cytosol as determined using PicoGreen (dsDNA staining), Mito-tracker (mitochondrial staining), and DAPI (nuclear staining) in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid or NAG-1 siRNA. Scale bar, 10 μm. White arrow points to cytosolic dsDNA (mtDNA release into the cytosol). (C) The content of dsDNA in the medium as determined using the PicoGreen fluorescent probe in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid or NAG-1 siRNA. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA fol lowed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P < 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Journal: Redox biology

Article Title: Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation.

doi: 10.1016/j.redox.2022.102322

Figure Lengend Snippet: Fig. 9. NAG-1/GDF15 alleviates FFA-induced mitochondrial damage and suppresses FFA-induced mtDNA release from mitochondria in HepG2 cells. (A) The copy number of mtDNA as determined using qRT-PCR in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid or NAG-1 siRNA with or without FFA treatment. (B) The release of dsDNA into the cytosol as determined using PicoGreen (dsDNA staining), Mito-tracker (mitochondrial staining), and DAPI (nuclear staining) in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid or NAG-1 siRNA. Scale bar, 10 μm. White arrow points to cytosolic dsDNA (mtDNA release into the cytosol). (C) The content of dsDNA in the medium as determined using the PicoGreen fluorescent probe in HepG2 cells as transfected with pcDNA3.1-NAG-1 plasmid or NAG-1 siRNA. Data are shown as means ± SEM from three independent experiments. Statistical analysis was performed using one-way ANOVA fol lowed by Bonferroni’s post hoc test (n = 3). *P < 0.05, **P < 0.01 vs empty vector or negative control of siRNA, without FFA treatment, #P < 0.05, ##P < 0.01 vs empty vector or negative control of siRNA, with FFA treatment.

Article Snippet: The enzyme-linked immunosorbent assay (ELISA) kits (human GDF15 (#DGD150), mIL-1β (#MLB00C), and mIL18 (#7625)) were obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Quantitative RT-PCR, Transfection, Plasmid Preparation, Staining, Negative Control

Elevated levels of GDF15 in aqueous humor and serum samples of POAG patients. Aqueous humor ( n = 40) and serum ( n = 41) samples derived from POAG patients revealed significantly elevated levels of growth/differentiation factor-15 (GDF15) (by >9-fold and 50%, respectively) compared to age- and gender-matched cataract patient samples ( n = 32). The box and whisker plots represent median and the interquartile range in the distribution. p -values were based on the Wilcoxon rank sum test of difference between medians. Abbreviations: GDF15, growth/differentiation factor-15; POAG, primary open-angle glaucoma.

Journal: Journal of Clinical Medicine

Article Title: Elevated Levels of Growth/Differentiation Factor-15 in the Aqueous Humor and Serum of Glaucoma Patients

doi: 10.3390/jcm11030744

Figure Lengend Snippet: Elevated levels of GDF15 in aqueous humor and serum samples of POAG patients. Aqueous humor ( n = 40) and serum ( n = 41) samples derived from POAG patients revealed significantly elevated levels of growth/differentiation factor-15 (GDF15) (by >9-fold and 50%, respectively) compared to age- and gender-matched cataract patient samples ( n = 32). The box and whisker plots represent median and the interquartile range in the distribution. p -values were based on the Wilcoxon rank sum test of difference between medians. Abbreviations: GDF15, growth/differentiation factor-15; POAG, primary open-angle glaucoma.

Article Snippet: Detection of GDF15: A human GDF15 enzyme-linked immunosorbent assay kit (Human GDF15 DuoSet ELISA, R&D Systems, Inc., Minneapolis, MN, USA) was used to determine the levels of GDF15 in both AH and serum samples.

Techniques: Derivative Assay, Whisker Assay

Elevated levels of GDF15 in aqueous humor samples from POAG patients. Aqueous humor samples derived from POAG patients ( n = 105) showed significantly increased levels of GDF15 (by 7.4-fold) compared to age- and gender-matched non-glaucoma cataract patient samples ( n = 117). The box and whisker plots represent median and the interquartile range in the distribution. p -values were based on Wilcoxon rank sum test of difference between medians. Abbreviations: GDF15, growth/differentiation factor-15; POAG, primary open-angle glaucoma.

Journal: Journal of Clinical Medicine

Article Title: Elevated Levels of Growth/Differentiation Factor-15 in the Aqueous Humor and Serum of Glaucoma Patients

doi: 10.3390/jcm11030744

Figure Lengend Snippet: Elevated levels of GDF15 in aqueous humor samples from POAG patients. Aqueous humor samples derived from POAG patients ( n = 105) showed significantly increased levels of GDF15 (by 7.4-fold) compared to age- and gender-matched non-glaucoma cataract patient samples ( n = 117). The box and whisker plots represent median and the interquartile range in the distribution. p -values were based on Wilcoxon rank sum test of difference between medians. Abbreviations: GDF15, growth/differentiation factor-15; POAG, primary open-angle glaucoma.

Techniques: Derivative Assay, Whisker Assay

GDF15 levels in the aqueous humor of male and female POAG and cataract patients.

Journal: Journal of Clinical Medicine

Article Title: Elevated Levels of Growth/Differentiation Factor-15 in the Aqueous Humor and Serum of Glaucoma Patients

doi: 10.3390/jcm11030744

Figure Lengend Snippet: GDF15 levels in the aqueous humor of male and female POAG and cataract patients.

Techniques:

GDF15 levels in the aqueous humor of Caucasian and African American POAG and cataract patients.

Journal: Journal of Clinical Medicine

Article Title: Elevated Levels of Growth/Differentiation Factor-15 in the Aqueous Humor and Serum of Glaucoma Patients

doi: 10.3390/jcm11030744

Figure Lengend Snippet: GDF15 levels in the aqueous humor of Caucasian and African American POAG and cataract patients.

Techniques:

Relationship between aqueous humor and serum GDF15 levels and disease severity of POAG. To determine whether elevated levels of GDF15 either in the AH or serum reveal a positive association with disease severity of glaucoma, POAG patients from a small cohort study were divided into mild, moderate, and severe glaucoma based on median deviation of visual field loss and GDF15 levels from the categories analyzed. ( A ) Overall, there was a significant difference in median deviation of visual field loss among the three groups, based on the Kruskal–Wallis test ( p < 0.001). Though the median deviation was not found to be significant between mild and moderate POAG, it was significant between mild to severe, and moderate to severe POAG based on the Wilcoxon rank sum test. ( B ) Cup-to-disk ratio showed a significant difference between cataract patients versus mild, moderate, and severe POAG, and between mild to moderate, and mild to severe POAG based on the Wilcoxon rank sum test. ( C ) AH GDF15 levels were significantly elevated between cataract and mild, moderate, and severe POAG, but not different between mild and moderate, and mild and severe POAG, based on the Wilcoxon rank sum test. ( D ) Serum GDF15 levels were also significantly elevated in moderate and severe POAG samples compared to cataract samples, but not different between mild and severe POAG, although there was a significant difference between mild and moderate POAG based on the Wilcoxon rank sum test. In all panels, the box and whisker plots represent median and the interquartile range in the distribution. Abbreviations: GDF15, growth/differentiation factor-15; POAG, primary open-angle glaucoma.

Journal: Journal of Clinical Medicine

Article Title: Elevated Levels of Growth/Differentiation Factor-15 in the Aqueous Humor and Serum of Glaucoma Patients

doi: 10.3390/jcm11030744

Figure Lengend Snippet: Relationship between aqueous humor and serum GDF15 levels and disease severity of POAG. To determine whether elevated levels of GDF15 either in the AH or serum reveal a positive association with disease severity of glaucoma, POAG patients from a small cohort study were divided into mild, moderate, and severe glaucoma based on median deviation of visual field loss and GDF15 levels from the categories analyzed. ( A ) Overall, there was a significant difference in median deviation of visual field loss among the three groups, based on the Kruskal–Wallis test ( p < 0.001). Though the median deviation was not found to be significant between mild and moderate POAG, it was significant between mild to severe, and moderate to severe POAG based on the Wilcoxon rank sum test. ( B ) Cup-to-disk ratio showed a significant difference between cataract patients versus mild, moderate, and severe POAG, and between mild to moderate, and mild to severe POAG based on the Wilcoxon rank sum test. ( C ) AH GDF15 levels were significantly elevated between cataract and mild, moderate, and severe POAG, but not different between mild and moderate, and mild and severe POAG, based on the Wilcoxon rank sum test. ( D ) Serum GDF15 levels were also significantly elevated in moderate and severe POAG samples compared to cataract samples, but not different between mild and severe POAG, although there was a significant difference between mild and moderate POAG based on the Wilcoxon rank sum test. In all panels, the box and whisker plots represent median and the interquartile range in the distribution. Abbreviations: GDF15, growth/differentiation factor-15; POAG, primary open-angle glaucoma.

Techniques: Whisker Assay

Differentially expressed genes identified by microarray analysis in wild-type p53 A2780 ovarian cancer cell line treated with cisplatin: ( a ) Heat map of genes with differential expression in the A2780 ovarian cancer cell line induced by treatment with cisplatin. The expression of these genes in the p53 mutant OVCA420 cell line was also shown. The color bar at the bottom indicates the fold change in reference to the expression value at zero hour on log2 scale; * indicated the genes validated in ( b ); ( b ) Validation of the up-regulation of the four genes by semi-quantitative RT-PCR analysis performed using total RNA extracted from A2780 cells treated with cisplatin at increasing doses (2.5, 4.5, 5.75, and 25 μM) for 16 h or a single dose at IC90 for different times (in triplicate); ( c ) Western blot showing expression of GDF15 in A2780 cells that were treated by cisplatin as indicated.

Journal: Cancers

Article Title: The Role of GDF15 in Regulating the Canonical Pathways of the Tumor Microenvironment in Wild-Type p53 Ovarian Tumor and Its Response to Chemotherapy

doi: 10.3390/cancers12103043

Figure Lengend Snippet: Differentially expressed genes identified by microarray analysis in wild-type p53 A2780 ovarian cancer cell line treated with cisplatin: ( a ) Heat map of genes with differential expression in the A2780 ovarian cancer cell line induced by treatment with cisplatin. The expression of these genes in the p53 mutant OVCA420 cell line was also shown. The color bar at the bottom indicates the fold change in reference to the expression value at zero hour on log2 scale; * indicated the genes validated in ( b ); ( b ) Validation of the up-regulation of the four genes by semi-quantitative RT-PCR analysis performed using total RNA extracted from A2780 cells treated with cisplatin at increasing doses (2.5, 4.5, 5.75, and 25 μM) for 16 h or a single dose at IC90 for different times (in triplicate); ( c ) Western blot showing expression of GDF15 in A2780 cells that were treated by cisplatin as indicated.

Article Snippet: A human GDF15 Quantikine enzyme-linked immunosorbent assay kit (R&D Systems, Minneapolis, MN, USA) was used to measure GDF15 levels in the sera of mice according to the manufacturers’ protocol.

Techniques: Microarray, Quantitative Proteomics, Expressing, Mutagenesis, Biomarker Discovery, Quantitative RT-PCR, Western Blot

Induction of GDF15 expression in ovarian cancer cell lines after treatment with cisplatin depends on the presence and induction of wild-type p53. Cell lines with wild-type p53 or mutant p53 were treated with cisplatin at IC90 dose for 24 h (2.5 μM: A2780, OVCA432; 5 μM: ALST, OVCAR3, OVCA420, TOV21G, SMOV2; 10 μM: ES2, HEYA8, KOC7C, OVCAR5, RMG1, SKOV3): ( a ) Semiquantitative RT-PCR analysis of GDF15 expression using total RNA extracted from a panel of ovarian cancer cell lines with wild-type p53 or mutant p53 confirmed by PCR-Sanger sequencing (in triplicate); ( b ) Western blots of GDF15 and p53 protein expression in ovarian cancer cell lines after treatment with cisplatin; ( c ) GDF15 was induced when SKOV3 ovarian cancer cells (p53-null) were transduced with an adenovirus carrying the wild-type p53 gene; ( d ) Knockdown of p53 (p53 KD) expression in A2780 ovarian cancer cells by p53 small interfering RNA suppressed the induction of GDF15 protein expression by treatment with cisplatin.

Journal: Cancers

Article Title: The Role of GDF15 in Regulating the Canonical Pathways of the Tumor Microenvironment in Wild-Type p53 Ovarian Tumor and Its Response to Chemotherapy

doi: 10.3390/cancers12103043

Figure Lengend Snippet: Induction of GDF15 expression in ovarian cancer cell lines after treatment with cisplatin depends on the presence and induction of wild-type p53. Cell lines with wild-type p53 or mutant p53 were treated with cisplatin at IC90 dose for 24 h (2.5 μM: A2780, OVCA432; 5 μM: ALST, OVCAR3, OVCA420, TOV21G, SMOV2; 10 μM: ES2, HEYA8, KOC7C, OVCAR5, RMG1, SKOV3): ( a ) Semiquantitative RT-PCR analysis of GDF15 expression using total RNA extracted from a panel of ovarian cancer cell lines with wild-type p53 or mutant p53 confirmed by PCR-Sanger sequencing (in triplicate); ( b ) Western blots of GDF15 and p53 protein expression in ovarian cancer cell lines after treatment with cisplatin; ( c ) GDF15 was induced when SKOV3 ovarian cancer cells (p53-null) were transduced with an adenovirus carrying the wild-type p53 gene; ( d ) Knockdown of p53 (p53 KD) expression in A2780 ovarian cancer cells by p53 small interfering RNA suppressed the induction of GDF15 protein expression by treatment with cisplatin.

Techniques: Expressing, Mutagenesis, Reverse Transcription Polymerase Chain Reaction, Sequencing, Western Blot, Transduction, Knockdown, Small Interfering RNA

GDF15 expression in ovarian cancer cell lines after treatment with carboplatin or paclitaxel. Cell lines with wild-type p53 (A2780, SMOV2, KOC7C) or mutant p53 (OVCA432, OVCA420, SKOV3) were treated with varying doses of carboplatin or paclitaxel for 24 h.

Journal: Cancers

Article Title: The Role of GDF15 in Regulating the Canonical Pathways of the Tumor Microenvironment in Wild-Type p53 Ovarian Tumor and Its Response to Chemotherapy

doi: 10.3390/cancers12103043

Figure Lengend Snippet: GDF15 expression in ovarian cancer cell lines after treatment with carboplatin or paclitaxel. Cell lines with wild-type p53 (A2780, SMOV2, KOC7C) or mutant p53 (OVCA432, OVCA420, SKOV3) were treated with varying doses of carboplatin or paclitaxel for 24 h.

Techniques: Expressing, Mutagenesis

Induction of GDF15 expression in mouse ovarian tumors and sera by cisplatin treatment in vivo: ( a ) Semiquantitative RT-PCR analysis of GDF15 expression performed using total RNA extracted from mouse A2780 (cisplatin-sensitive) and RMG1 (cisplatin-resistant) tumors after treatment with cisplatin (2.5 or 5 mg/kg) for 24 or 48 h. ** p = 0.004; *** p = 0.0007; **** p < 0.0001; ( b ) Enzyme-linked immunosorbent assay of GDF15 sera levels in mice. * p = 0.03; *** p = 0.0002.

Journal: Cancers

Article Title: The Role of GDF15 in Regulating the Canonical Pathways of the Tumor Microenvironment in Wild-Type p53 Ovarian Tumor and Its Response to Chemotherapy

doi: 10.3390/cancers12103043

Figure Lengend Snippet: Induction of GDF15 expression in mouse ovarian tumors and sera by cisplatin treatment in vivo: ( a ) Semiquantitative RT-PCR analysis of GDF15 expression performed using total RNA extracted from mouse A2780 (cisplatin-sensitive) and RMG1 (cisplatin-resistant) tumors after treatment with cisplatin (2.5 or 5 mg/kg) for 24 or 48 h. ** p = 0.004; *** p = 0.0007; **** p < 0.0001; ( b ) Enzyme-linked immunosorbent assay of GDF15 sera levels in mice. * p = 0.03; *** p = 0.0002.

Techniques: Expressing, In Vivo, Reverse Transcription Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay

The impact of GDF15 KD on ovarian tumor growth, cisplatin response and tumor composition; ( a ) Tumor weights in mice after treatment with PBS or cisplatin. * p = 0.0079; ** p = 0.0046; ( b ) Fold decrease in tumor weights after treatment with cisplatin normalized to control tumors treated with PBS; ( c ) Percentage of Ki67-positive ovarian tumor cells in the tumor. N.S., not significant; ( d ) RPPA analysis results showing induction of higher expression of the apoptotic proteins Bim, cleaved caspase-7, and phosphorylated Chk1 after treatment with cisplatin in GDF15-KD A2780 tumors compared to normal A2780 tumors; ( e ) Percentage of tumor and stromal cells in mouse A2780 and GDF15-KD A2780 tumors after treatment with PBS; ( f ) Percentage of tumor and stromal cells in mouse A2780 and GDF15-KD A2780 tumors after treatment with cisplatin.

Journal: Cancers

Article Title: The Role of GDF15 in Regulating the Canonical Pathways of the Tumor Microenvironment in Wild-Type p53 Ovarian Tumor and Its Response to Chemotherapy

doi: 10.3390/cancers12103043

Figure Lengend Snippet: The impact of GDF15 KD on ovarian tumor growth, cisplatin response and tumor composition; ( a ) Tumor weights in mice after treatment with PBS or cisplatin. * p = 0.0079; ** p = 0.0046; ( b ) Fold decrease in tumor weights after treatment with cisplatin normalized to control tumors treated with PBS; ( c ) Percentage of Ki67-positive ovarian tumor cells in the tumor. N.S., not significant; ( d ) RPPA analysis results showing induction of higher expression of the apoptotic proteins Bim, cleaved caspase-7, and phosphorylated Chk1 after treatment with cisplatin in GDF15-KD A2780 tumors compared to normal A2780 tumors; ( e ) Percentage of tumor and stromal cells in mouse A2780 and GDF15-KD A2780 tumors after treatment with PBS; ( f ) Percentage of tumor and stromal cells in mouse A2780 and GDF15-KD A2780 tumors after treatment with cisplatin.

Techniques: Control, Expressing

Activation or inhibition of canonical pathways in the tumor cell and stromal cell components of tumors formed by A2780 GDF15-NT control cells or A2780 GDF15-KD cells by cisplatin treatment. Z-score is a statistical measure of the match between expected relationship direction and observed gene expression changes after cisplatin treatment. z-score > 2 (activation) or z-score < 2 (inhibition) are considered significant.

Journal: Cancers

Article Title: The Role of GDF15 in Regulating the Canonical Pathways of the Tumor Microenvironment in Wild-Type p53 Ovarian Tumor and Its Response to Chemotherapy

doi: 10.3390/cancers12103043

Figure Lengend Snippet: Activation or inhibition of canonical pathways in the tumor cell and stromal cell components of tumors formed by A2780 GDF15-NT control cells or A2780 GDF15-KD cells by cisplatin treatment. Z-score is a statistical measure of the match between expected relationship direction and observed gene expression changes after cisplatin treatment. z-score > 2 (activation) or z-score < 2 (inhibition) are considered significant.

Techniques: Activation Assay, Inhibition, Control, Gene Expression

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