Journal: Neural Regeneration Research

Article Title: Ruxolitinib improves the inflammatory microenvironment, restores glutamate homeostasis, and promotes functional recovery after spinal cord injury

doi: 10.4103/NRR.NRR-D-23-01863

Figure Lengend Snippet: RUX restores EAAT2 loss in astrocytes by inhibiting the activation of STAT3 in vitro. (A) Representative western blotting of p-JAK2, JAK2, p-STAT3 and STAT3 expression of astrocytes in each group pre-treated with RUX (0.2, 0.5 and 1 µM) ( n = 3 per group). (B) Quantitative analysis of p-JAK2/JAK2 and p-STAT3/STAT3 level in each group. (C) Immunocytochemistry of GFAP (green, Alexa Fluor 488) and p-STAT3 (red, Alexa Fluor 594) in primary mouse astrocytes. DAPI (blue) was used to stain nuclei. The A1IM group exhibited higher nuclear p-STAT3 expression compared with the Control group, whereas the RUX group displayed decreased nuclear p-STAT3 expression compared with the A1IM group. Scale bar: 40 µm. (D) Quantitative results of relative p-STAT3 intensity. (E) Representative western blotting of STAT3 expression of astrocytes pre-treated with S3I-201 or vehicle. (F) Quantitative results of relative STAT3 expression level. (G) Primary mouse astrocytes were pretreated with S3I-201 (50 μM) or RUX for 1 hour and then exposed to LPS (1 µg/mL) or PBS for 5 hours. Western blotting was conducted to assess EAAT2 expression level, followed by quantitative analysis of EAAT2 protein expression (H). (I) Glutamate (100 nM) was introduced into each culture medium, and the relative glutamate uptake of astrocytes in each group was measured. Data are normalized to the control group. Data are presented as the mean ± SD ( n = 3 per group). ## P < 0.01, vs. control group; * P < 0.05, ** P < 0.01, vs. A1IM group (one-way analysis of variance followed by Tukey’s post hoc test). A1IM: A1-like astrocyte induction medium; Ctrl: control; DAPI: 4′,6-diamidino-2-phenylindole; EAAT2: excitatory amino acid transporter 2; GFAP: glial fibrillary acidic protein; JAK2: Janus kinase 2; ns: not significant; p-JAK2: phosphorylated JAK2; p-STAT3: phosphorylated STAT3; RUX: ruxolitinib; S3I-201: a STAT3 inhibitor; STAT3: signal transducer and activator of transcription 3.

Article Snippet: In experiments, cells were starved in DMEM for 1 hour before being treated with RUX (0.2, 0.5, and 1 µM), S3I-201 (50 µm; Selleck, Houston, TX, USA), or solvent (dimethyl sulfoxide, DMSO).

Techniques: Activation Assay, In Vitro, Western Blot, Expressing, Immunocytochemistry, Staining

Journal: Frontiers in Immunology

Article Title: The dual role of glucocorticoid regeneration in inflammation at parturition

doi: 10.3389/fimmu.2024.1459489

Figure Lengend Snippet: Role of STAT3 in the induction of COX-2 by cortisol in the presence or absence of LPS in human amnion fibroblasts. (A) Effect of STAT3 inhibitor S3I-201 (50 μM; 24 hours; n=5) on the induction of COX-2 by cortisol (1 μM; 24 hours) and LPS (10 ng/mL; 24 hours). (B) Effect of cortisol (1 μM; 3 hours) on STAT3 phosphorylation at Tyr705 (p-STAT3) (n=4). Data are mean ± SEM. Statistical analysis was performed with one-way ANOVA test followed by Newman-Keuls test (A) or paired Student’s t-test (B) . *p<0.05, vs. control (without treatment), ^p<0.05, $p<0.05 between lined groups, N.S., none significance vs. control.

Article Snippet: The cells were treated with cortisol and LPS with or without STAT3 antagonist S3I-201 (50 μM; Selleck, Houston, TX) or toll-like receptor-4 (TLR-4) antagonist TAK-242 (10 μM; R&D systems, Minneapolis, MN) or small interference RNA (siRNA)-mediated knockdown of p65 for 24 hours to examine their role in the induction of COX-2 by cortisol and LPS.

Techniques: Control

Journal: Frontiers in Immunology

Article Title: The dual role of glucocorticoid regeneration in inflammation at parturition

doi: 10.3389/fimmu.2024.1459489

Figure Lengend Snippet: Effect of LPS and corticosterone injection on the abundance of pro-inflammatory cytokines, COX-2, 11β-HSD1, p-p65 and p-STAT3 in mouse intrauterine tissues. (A) Effect of LPS (20 μg per dam) and corticosterone (1 μg per dam) injection on IL-1β and IL-6 abundance in the amnion fluid and fetal membranes (n = 7 each group). (B–F) Effect of LPS (20 μg per dam) and corticosterone (1 μg per dam) injection on 11β-HSD1, COX-2, p65 phosphorylation at Ser536 (p-p65) and STAT3 phosphorylation at Tyr705 (p-STAT3) in the fetal membranes (n=7 each group). Data are mean ± SEM. Statistical analysis was performed with one-way ANOVA test followed by Newman-Keuls test. *p<0.05, **p<0.01, ***P<0.001 vs. control (without treatment), #p<0.05, ##p<0.01 vs. LPS.

Article Snippet: The cells were treated with cortisol and LPS with or without STAT3 antagonist S3I-201 (50 μM; Selleck, Houston, TX) or toll-like receptor-4 (TLR-4) antagonist TAK-242 (10 μM; R&D systems, Minneapolis, MN) or small interference RNA (siRNA)-mediated knockdown of p65 for 24 hours to examine their role in the induction of COX-2 by cortisol and LPS.

Techniques: Injection, Control

Journal: Frontiers in Immunology

Article Title: The dual role of glucocorticoid regeneration in inflammation at parturition

doi: 10.3389/fimmu.2024.1459489

Figure Lengend Snippet: Diagram illustrating the role of glucocorticoid regeneration of the fetal membranes in parturition with infection-induced chorioamnionitis. When intrauterine infection is present in pregnancy, LPS from Gram-negative bacteria activates NF-κB via the TLR4 receptor, which subsequently induces the expression of pro-inflammatory cytokines such as IL-1β and IL-6, and COX-2, the rate-limiting enzyme in prostaglandin synthesis. Although prostaglandins synthesized by COX-2 are pro-parturition, excessive pro-inflammatory cytokines may harm the fetus and lead to fetal inflammatory response syndrome (FIRS). Meanwhile, LPS also induces 11β-HSD1 expression either by itself or in synergy with glucocorticoids, resulting in increased conversion of biologically inactive cortisone to bioactive cortisol. Cortisol not only suppresses LPS-induced pro-inflammatory cytokine and COX-2 expression via inhibition of NF-κB, but also induces COX-2 expression on its own through NF-κB-independent pathways such as activation of STAT3, thereby minimizing the fetus-hazardous effects of pro-inflammatory cytokines at parturition and helping the fetus escape from the in-utero environment affluent in pro-inflammatory cytokines at the same time. Black arrows indicate stimulation and the red arrow indicates inhibition.

Article Snippet: The cells were treated with cortisol and LPS with or without STAT3 antagonist S3I-201 (50 μM; Selleck, Houston, TX) or toll-like receptor-4 (TLR-4) antagonist TAK-242 (10 μM; R&D systems, Minneapolis, MN) or small interference RNA (siRNA)-mediated knockdown of p65 for 24 hours to examine their role in the induction of COX-2 by cortisol and LPS.

Techniques: Infection, Bacteria, Expressing, Synthesized, Inhibition, Activation Assay, In Utero

Journal: iScience

Article Title: Influenza A virus infection activates STAT3 to enhance SREBP2 expression, cholesterol biosynthesis, and virus replication

doi: 10.1016/j.isci.2024.110424

Figure Lengend Snippet: STAT3 promotes IAV replication through SREBP2 NL20 (A) and 293T (C) cells were pretreated with the indicated concentrations of S3I-201 (S3I) for 8 h. Untreated control cells were treated with 0.5% DMSO. After infection with 0.01 MOI H5N1 or H1N1 viruses, the cells were incubated for 24 h in the absence or presence of the same concentration of S3I-201. Viral proteins were detected with their specific antibody by western blot. NL20 (B) and 293T (D) cells seeded in a 96-well plate (3.5×10 4 cells/well) were incubated in the absence or presence of the indicated concentrations of S3I-201 in triplicate for 48 h. Cell viability was measured by using the CellTiter-Glo kit. The CC 50 values were calculated based on the mean ± SD of three experiments. To determine the EC 50 values, NL20 cells seeded in a 24-well plate were pretreated with the indicated concentrations of S3I-201 for 8 h. After infection with 0.01 MOI H5N1 or H1N1, the cells were incubated in the absence or presence of the same concentrations of S3I-201 for 24 h. The conditioned media were collected and analyzed for virus titers by measuring TCID 50 values. The results represent the mean ± SD of three experiments. The S.I. values were calculated by dividing the CC 50 values with the EC 50 values. (E) Control and STAT3-deficient 293T cells infected with the indicated MOI of H5N1 (SY) virus were incubated for 16 h. Cell lysates were prepared and analyzed for cholesterol biosynthesis-related and viral protein levels. WT, wild type; ΔSTAT3, STAT3 deficiency. (F) 293T cells were transfected with the empty vector or the vector encoding STAT3. After incubation for 48 h, the cells were infected with the indicated MOI of H5N1 (SY) virus and then incubated for 16 h. Cell lysates were analyzed for the indicated proteins by Western blot. (G and H) Conditioned media from control or STAT3-deficient or overexpression 293T cells were collected and analyzed for virus titers by measuring the TCID 50 values. Data are the mean ± SD of three experiments. ∗ p < 0.05, ∗∗ p < 0.01.

Article Snippet: To determine the cytotoxicity of Fatostatin and S3I-201, NL20 cells seeded in 96-well plates (3.5×10 4 cells/well) were incubated with various concentrations of Fatostatin or S3I-201 and then incubated for 48 h. Cell viability was measured by using a CellTiter-Glo kit (Promega, Madison, WI, USA).

Techniques: Control, Infection, Incubation, Concentration Assay, Western Blot, Virus, Transfection, Plasmid Preparation, Over Expression

Journal: iScience

Article Title: Influenza A virus infection activates STAT3 to enhance SREBP2 expression, cholesterol biosynthesis, and virus replication

doi: 10.1016/j.isci.2024.110424

Figure Lengend Snippet: STAT3 activation increases SREBP2 expression and cholesterol levels (A) NL20 cells were first infected with 0.1 MOI H5N1 (SY) virus. After incubation for 4 h, cells were treated with the indicated concentration of S3I-201 and then incubated for 20 h. Untreated control cells were treated with 0.5% DMSO. (B) Conditioned media were collected and analyzed for virus titers. Data are the mean ± SD of three experiments. ns, not significant. (C) Control and STAT3-deficient NL20 cells infected with the indicated MOI of H5N1 (SY) virus were incubated for 16 h. Cell lysates were prepared and analyzed for cholesterol biosynthesis-related and viral proteins. (D) Conditioned media were collected and analyzed for virus titers. Data are the mean ± SD of three experiments. ns, not significant. (E) Total cellular RNAs from control and STAT3-deficient NL20 cells were extracted and analyzed for SREBP2 and HMGCR mRNA levels by RT-qPCR. The results represent the mean ± SD of three experiments. ∗∗ p < 0.01. (F) Control and STAT3-deficient NL20 cells seeded on coverslips were stained with Filipin III and visualized under a confocal microscope. Scale bar, 10 μm. (G) The monolayers of control and STAT3-deficient NL20 cells in a 96-well plate (3.5×10 4 cells/well) were incubated in serum-free medium for 8 h. Filipin and Sytox Green fluorescent intensity was quantified in a plate reader. The arbitrary units of Filipin fluorescence intensity were normalized with that of Sytox Green intensity. The results represent the mean ± SD of three experiments. ∗ p < 0.05. (H) NL20 cells transiently transfected with the pcDNA empty vector or the vector encoding the STAT3 gene. After incubation for 48 h, the cells were infected with the indicated MOI of H5N1 (SY) and then incubated for 16 h. Cell lysates were prepared and analyzed for the expression of indicated proteins. (I) Total cellular RNAs from NL20 cells transfected with the empty vector or the vector encoding STAT3 were extracted and analyzed for SREBP2 and HMGCR mRNA levels by RT-qPCR. The results represent the mean ± SD of three experiments. ∗∗ p < 0.01. (J) NL20 cells seeded on coverslips were transiently transfected with the empty vector or the STAT3 expression vector. After incubation for 40 h, the cells were replenished with serum-free medium and then incubated for 8 h. The cells were stained with Filipin III and visualized under a confocal microscope. Scale bar, 10 μm. (K) NL20 cells seeded in a 96-well plate (3.5×10 4 cells/well) were transiently transfected with the empty vector or the STAT3 expression vector. After incubation for 40 h, the cells were replenished with serum-free medium and then incubated for 8 h. Filipin and Sytox Green fluorescent intensity was quantified in a plate reader. The arbitrary units of Filipin intensity were normalized with that of Sytox Green. The results represent the mean ± SD of three experiments. ∗ p < 0.05.

Article Snippet: To determine the cytotoxicity of Fatostatin and S3I-201, NL20 cells seeded in 96-well plates (3.5×10 4 cells/well) were incubated with various concentrations of Fatostatin or S3I-201 and then incubated for 48 h. Cell viability was measured by using a CellTiter-Glo kit (Promega, Madison, WI, USA).

Techniques: Activation Assay, Expressing, Infection, Virus, Incubation, Concentration Assay, Control, Quantitative RT-PCR, Staining, Microscopy, Fluorescence, Transfection, Plasmid Preparation

Journal: iScience

Article Title: Influenza A virus infection activates STAT3 to enhance SREBP2 expression, cholesterol biosynthesis, and virus replication

doi: 10.1016/j.isci.2024.110424

Figure Lengend Snippet: STAT3 enhances IAV replication by increasing cholesterol biosynthesis (A–C) NL20 cells were pretreated without or with cholesterol (5 or 10 μg/mL) minus or plus S3I-201 (25 μM) for 8 h and then infected with 0.01 MOI of H5N1 (SY) virus and incubated for 24 h. Cell lysates were prepared and analyzed for the PB2 and NP proteins (A). The relative viral protein levels were analyzed by quantifying the density of the protein bands using NIH ImageJ software and normalized to the density of the GAPDH band as a loading control. Data are the mean ± SD of three experiments. ∗ p < 0.05, ∗∗ p < 0.01, ns, not significant, compared to the untreated control; ## p < 0.01, compared to H5N1 virus infection (B). (C) Conditioned media were collected and analyzed for virus titers. Data are the mean ± SD of three experiments. ∗∗ p < 0.01, compared to the untreated control; ## p < 0.01, compared to H5N1 virus infection. (D–F) Control and STAT3-deficient NL20 cells were infected with the indicated MOIs of H5N1 (SY) virus and then incubated in the absence or presence of cholesterol (5 μg/mL) for 16 h. Cell lysates were prepared and analyzed for viral proteins (D). The relative viral protein levels were analyzed by quantifying the density of the protein bands using NIH ImageJ software and normalized to the density of the GAPDH band as a loading control. Data are the mean ± SD of three experiments. ∗ p < 0.05, ∗∗ p < 0.01 (E). Conditioned media were collected and analyzed for virus titers. Data are the mean ± SD of three experiments. ∗ p < 0.05 (F). (G) NL20 cells were pretreated in serum-free media containing S3I-201 for 8 h. Cells were then infected with 2.5 MOI H5N1 (SY) virus and incubated at 4°C for 1 h. After removing unattached viruses, total cellular RNAs were extracted and analyzed for viral RNAs by RT-qPCR. Data are the mean ± SD of three experiments. ∗∗ p < 0.01. (H) Wild-type and STAT3-deficient NL20 cells were starved in serum-free media for 8 h. Cells were then infected with 2.5 MOI of H5N1 (SY) virus and incubated at 4°C for 1 h. After removing unattached viruses, total cellular RNAs were extracted and analyzed for viral RNAs by RT-qPCR. Data are the mean ± SD of three experiments. ∗∗ p < 0.01. (I–K) NL20 cells were treated with SI3-201 (25 μM) for the indicated time points before or after H5N1 (SY) virus infection (0.01 MOI). Cell lysates were prepared and analyzed for viral proteins (I). The relative protein levels were analyzed by quantifying the density of the protein bands using NIH ImageJ software and normalized to the density of the β-actin band as a loading control (E and J). The results were presented as bar graphs. Data are the mean ± SD of three experiments. ∗ p < 0.05, ∗∗ p < 0.01, ns, not significant (J). Conditioned media were collected 24 h post infection and analyzed for virus titers. Data are the mean ± SD of three experiments. ∗ p < 0.05, ∗∗ p < 0.01, ns, not significant (K).

Article Snippet: To determine the cytotoxicity of Fatostatin and S3I-201, NL20 cells seeded in 96-well plates (3.5×10 4 cells/well) were incubated with various concentrations of Fatostatin or S3I-201 and then incubated for 48 h. Cell viability was measured by using a CellTiter-Glo kit (Promega, Madison, WI, USA).

Techniques: Infection, Virus, Incubation, Software, Control, Quantitative RT-PCR

Journal: iScience

Article Title: Influenza A virus infection activates STAT3 to enhance SREBP2 expression, cholesterol biosynthesis, and virus replication

doi: 10.1016/j.isci.2024.110424

Figure Lengend Snippet:

Article Snippet: To determine the cytotoxicity of Fatostatin and S3I-201, NL20 cells seeded in 96-well plates (3.5×10 4 cells/well) were incubated with various concentrations of Fatostatin or S3I-201 and then incubated for 48 h. Cell viability was measured by using a CellTiter-Glo kit (Promega, Madison, WI, USA).

Techniques: Virus, Recombinant, Staining, RNA Extraction, Transfection, Clone Assay, Cell Viability Assay, Software, CRISPR

Journal: International Journal of Molecular Sciences

Article Title: STAT3 Pathways Contribute to β-HCH Interference with Anticancer Tyrosine Kinase Inhibitors

doi: 10.3390/ijms25116181

Figure Lengend Snippet: CCK-8 assay performed on MCF-7, H358, LNCaP, and HepG2. Cells were incubated with 10 µM of β-HCH, TKIs, and S3I-201, as shown in . Cellular viability decreased after treatment with β-HCH + TKIs + S3I-201 compared with samples treated only with β-HCH + TKIs. The values reported in the histograms represent the averages of three independent experiments and are presented as the means and standard deviation. Statistical analysis was performed with the GraphPad Prisma software using ANOVA followed by Tukey’s post hoc test. Statistically significant differences referring to the CTRL or TKIs are marked with asterisks (ns: not statistically significant, * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001).

Article Snippet: For the experiments, the following inhibitors ( ) were used at the specified concentrations: 0.8 μM lapatinib (Sigma-Aldrich, Milan, Italy, Cat. No. CDS022971), 15 µM gefitinib (Sigma-Aldrich, SLM1657), 70 nM dasatinib (Selleckchem, Roma, Italy, Cat. No. S1021), 6 μM AZD1480 (Sigma-Aldrich, Milan, Italy, Cat. No. SML1505), and 100 μM S3I-201 (Sigma-Aldrich, Milan, Italy, Cat. No. SML0330).

Techniques: CCK-8 Assay, Incubation, Standard Deviation, Software

Journal: International Journal of Molecular Sciences

Article Title: STAT3 Pathways Contribute to β-HCH Interference with Anticancer Tyrosine Kinase Inhibitors

doi: 10.3390/ijms25116181

Figure Lengend Snippet: Immunoblotting evaluating the activation of STAT3 and HER2 in MCF-7 ( A ), STAT3 and EGFR in H358 ( B ), STAT3 and SRC in LNCAP ( C ), and STAT3 and JACK2 in HepG2 ( D ). Total protein extracts were subjected to immunoblot analysis. Immunoblot evidenced that STAT3 phosphorylation (pY705-STAT3), HER2 phosphorylation (pY1248-HER2), JACK2 phosphorylation (pY1007/1008-JAK2), and Src phosphorylation (pY416-Src) increased upon treatment with 10 µM of β-HCH. The increase in STAT3 phosphorylation was upheld even with the combined treatment β-HCH+ TKIs, whereas a decrease in the band intensity occurred in the sample with triple treatment (β-HCH+ TKI+ S3I-201), as evident in the relative densitometry. β-actin was used for housekeeping. Phosphorylation levels referred to the amount of total STAT3, HER2, EGFR, Src, or JAK2 present in each sample and were compared with the control. These images are representative of three independent experiments with similar results. Statistical analysis was performed with the GraphPad Prisma software using ANOVA followed by Tukey’s post hoc test. Statistically significant differences referring to the CTRL or TKIs are marked with asterisks (ns: not statistically significant, ** p < 0.01; *** p < 0.001; **** p < 0.0001).

Article Snippet: For the experiments, the following inhibitors ( ) were used at the specified concentrations: 0.8 μM lapatinib (Sigma-Aldrich, Milan, Italy, Cat. No. CDS022971), 15 µM gefitinib (Sigma-Aldrich, SLM1657), 70 nM dasatinib (Selleckchem, Roma, Italy, Cat. No. S1021), 6 μM AZD1480 (Sigma-Aldrich, Milan, Italy, Cat. No. SML1505), and 100 μM S3I-201 (Sigma-Aldrich, Milan, Italy, Cat. No. SML0330).

Techniques: Western Blot, Activation Assay, Software

Journal: International Journal of Molecular Sciences

Article Title: STAT3 Pathways Contribute to β-HCH Interference with Anticancer Tyrosine Kinase Inhibitors

doi: 10.3390/ijms25116181

Figure Lengend Snippet: Wound-healing assay conducted on MCF-7 ( A ), H358 ( B ), LNCaP ( C ), and HePG2 ( D ) cell lines. Images were collected immediately after scratching the cell monolayer (T0) and 48 h post-treatment with TKIs. The results show that after 48 h of incubation with specific TKIs +10 µM of β-HCH, the pollutant affected the drug efficacy. Conversely, in the triple treatment (β-HCH+ TKI+ S3I-201), by inhibiting the STAT3 protein, there was a reduction in the cellular migratory capability. These images, representative of three independent experiments with similar results, were captured with a Leica AF6000 Modular System microscope.

Article Snippet: For the experiments, the following inhibitors ( ) were used at the specified concentrations: 0.8 μM lapatinib (Sigma-Aldrich, Milan, Italy, Cat. No. CDS022971), 15 µM gefitinib (Sigma-Aldrich, SLM1657), 70 nM dasatinib (Selleckchem, Roma, Italy, Cat. No. S1021), 6 μM AZD1480 (Sigma-Aldrich, Milan, Italy, Cat. No. SML1505), and 100 μM S3I-201 (Sigma-Aldrich, Milan, Italy, Cat. No. SML0330).

Techniques: Wound Healing Assay, Incubation, Microscopy

Journal: International Journal of Molecular Sciences

Article Title: STAT3 Pathways Contribute to β-HCH Interference with Anticancer Tyrosine Kinase Inhibitors

doi: 10.3390/ijms25116181

Figure Lengend Snippet: Clonogenic assay conducted on MCF-7, H358, LNCaP, and HepG2 cell lines. β-HCH induced an increase in colony formation, and in the triple treatment (β-HCH+ TKI+ S3I-201), by inhibiting the STAT3 protein, there was a reduction in cellular colony formation. The cells were pretreated with 10 µM of β-HCH in flasks for 7 days and then seeded at a density of 500 cells/mL in 6-well plates and cotreated for 5 days with specific TKIs, as shown in . After treatments, the colonies formed were evidenced using crystal violet dye (Panel A ) and counted, and the total areas of colonies (expressed as percentages with respect to the control and SD) are shown in the histogram (Panel B ). These images are representative of three independent experiments with similar results. Statistical analysis was performed with the GraphPad Prisma software using ANOVA followed by Tukey’s post hoc test. Statistically significant differences were determined at * p < 0.05; and **** p < 0.0001, ns: not statistically significant.

Article Snippet: For the experiments, the following inhibitors ( ) were used at the specified concentrations: 0.8 μM lapatinib (Sigma-Aldrich, Milan, Italy, Cat. No. CDS022971), 15 µM gefitinib (Sigma-Aldrich, SLM1657), 70 nM dasatinib (Selleckchem, Roma, Italy, Cat. No. S1021), 6 μM AZD1480 (Sigma-Aldrich, Milan, Italy, Cat. No. SML1505), and 100 μM S3I-201 (Sigma-Aldrich, Milan, Italy, Cat. No. SML0330).

Techniques: Clonogenic Assay, Software

Journal: Journal of Cellular and Molecular Medicine

Article Title: Inhibition of STAT3 by S3I ‐201 suppress peritoneal fibroblast phenotype conversion and alleviate peritoneal fibrosis

doi: 10.1111/jcmm.18381

Figure Lengend Snippet: Increased expression of collagen‐I, α‐SMA and P‐STAT3 induced by TGF‐β1 was suppressed by S3I‐201, as assessed by western blot. * p <0.05; ** p <0.01.

Article Snippet: The STAT3‐specific inhibitor S3I‐201 (#SML0330) and CG (#C9394) were purchased from Sigma‐Aldrich (Darmstadt, Germany).

Techniques: Expressing, Western Blot

Journal: Journal of Cellular and Molecular Medicine

Article Title: Inhibition of STAT3 by S3I ‐201 suppress peritoneal fibroblast phenotype conversion and alleviate peritoneal fibrosis

doi: 10.1111/jcmm.18381

Figure Lengend Snippet: Effects of different concentrations of S3I‐201 on the expression of collagen‐I and α‐SMA in RPFBs. * p <0.05; ** p <0.01.

Article Snippet: The STAT3‐specific inhibitor S3I‐201 (#SML0330) and CG (#C9394) were purchased from Sigma‐Aldrich (Darmstadt, Germany).

Techniques: Expressing

Journal: Journal of Cellular and Molecular Medicine

Article Title: Inhibition of STAT3 by S3I ‐201 suppress peritoneal fibroblast phenotype conversion and alleviate peritoneal fibrosis

doi: 10.1111/jcmm.18381

Figure Lengend Snippet: Effects of different concentrations of S3I‐201 on the expression of collagen‐I and α‐SMA in RPFBs. * p <0.05; ** p <0.01.

Article Snippet: The STAT3‐specific inhibitor S3I‐201 (#SML0330) and CG (#C9394) were purchased from Sigma‐Aldrich (Darmstadt, Germany).

Techniques: Expressing

Journal: Journal of Cellular and Molecular Medicine

Article Title: Inhibition of STAT3 by S3I ‐201 suppress peritoneal fibroblast phenotype conversion and alleviate peritoneal fibrosis

doi: 10.1111/jcmm.18381

Figure Lengend Snippet: S3I‐201 administration significantly induced reduction of the peritoneal thickness, and collagen‐I‐positive area in mice treated with CG. (A) haematoxylin and eosin staining, (B) Masson and (C) IHC staining of mice parietal peritoneum. (D‐E) S3I‐201 markedly decreased synthesis of Collagen I and a‐SMA in fibroblasts induced by CG, as assessed by western blot. * p <0.05; ** p <0.01; *** p <0.001.

Article Snippet: The STAT3‐specific inhibitor S3I‐201 (#SML0330) and CG (#C9394) were purchased from Sigma‐Aldrich (Darmstadt, Germany).

Techniques: Staining, Immunohistochemistry, Western Blot