Journal: Stem Cell Research & Therapy

Article Title: IL-1β modulates inflammatory response of human bone marrow-derived MSCs and neutrophil recruitment in vitro via NF-kB-associated signaling

doi: 10.1186/s13287-026-05029-x

Figure Lengend Snippet: IL-1β stimulation changes the transcriptomic profile of BM-hMSCs. Schematic of experimental design A . BM-hMSCs were exposed to IL-1 β (3 replicates, 1 donor) or left unstimulated (3 replicates, 1 donor) for one hour, followed by bulk RNA sequencing. PCA plot was used to show the variance between the unstimulated control (green) and IL-1 β exposed (purple) samples B . Heatmap displaying the Z-score of the top 100 varying genes across all samples. Red color indicates higher expression of the genes and blue color indicates decreased expression C . Volcano plot of differentially expressed genes, showing their log2 fold change (X-axis) and -log10 adjusted p-values (Y-axis) D . IL-1 β Interleukin-1β, BM-hMSCs, Bone marrow derived human mesenchymal cells, PCA Principal component analysis, FC Fold change, NS not significant. Figure 1A was created using Biorender.com

Article Snippet: Following synchronization, medium was removed, and cells were stimulated with IL-1β (20 ng/ml in DPBS with 0.1% Bovine Serum Albumin, cat# 208-IL-010, R&D Systems) for 1 h (RNA-sequencing) or 24 h. Unstimulated control BM-hMSCs were exposed to serum free DMEM only.

Techniques: RNA Sequencing, Control, Expressing, Derivative Assay

Journal: Stem Cell Research & Therapy

Article Title: IL-1β modulates inflammatory response of human bone marrow-derived MSCs and neutrophil recruitment in vitro via NF-kB-associated signaling

doi: 10.1186/s13287-026-05029-x

Figure Lengend Snippet: IL-1β stimulation increases expression of neutrophil recruitment and NF-kB signaling genes by BM-hMSCs. Heatmap clustering of the Z-score of the top 20 differentially expressed genes between unstimulated control BM-hMSCs (3 replicates, 1 donor, green) and IL-1 β stimulated BM-hMSCs (3 replicates, 1 donor, purple). Red color indicates higher expression of the genes and blue color indicates decreased expression A . Protein expression of CXCL1 (10 replicates, 4 donors), CCL2 (4 replicates, 2 donors), CXCL5 (4 replicates, 2 donors), and CXCL8/IL-8 (7 replicates, 3 donors) in BM-hMSCs secretome measured by ELLA or ELISA. Data are presented as median, and statistical analysis was performed using unpaired t-test with Welch’s correction B . Bar plot of the top 20 significant Gene Ontology (GO) biological processes representing IL- 1β induced upregulated differentially expressed genes C IL-1 β, Interleukin-1β; BM-hMSCs, Bone marrow derived human mesenchymal cells; CCL2, chemokine (C–C motif) ligand 2; CXCL1, chemokine (C-X-C motif) ligand 1; CXCL2, chemokine (C-X-C motif) ligand 1; CXCL8, chemokine (C-X-C motif) ligand 8; ****, p < 0,0001

Article Snippet: Following synchronization, medium was removed, and cells were stimulated with IL-1β (20 ng/ml in DPBS with 0.1% Bovine Serum Albumin, cat# 208-IL-010, R&D Systems) for 1 h (RNA-sequencing) or 24 h. Unstimulated control BM-hMSCs were exposed to serum free DMEM only.

Techniques: Expressing, Control, Enzyme-linked Immunosorbent Assay, Derivative Assay

Journal: Stem Cell Research & Therapy

Article Title: IL-1β modulates inflammatory response of human bone marrow-derived MSCs and neutrophil recruitment in vitro via NF-kB-associated signaling

doi: 10.1186/s13287-026-05029-x

Figure Lengend Snippet: IL-1β stimulated BM-hMSCs increased neutrophil recruitment partly via the NF-kB signaling pathway. Schematic of experimental design of the neutrophil migration assay. Illustration was created with BioRender.com A . Number of neutrophils that migrated through the transwell membrane from the top well to the bottom towards control conditioned medium, conditioned medium from IL-1β stimulated BM-hMSCs, and conditioned medium from IL-1β with the NF-kB inhibitor stimulated BM-hMSCs. The experiment was performed using neutrophils from four different donors (each donor represent one data point) and the experiments were performed on three different days. B . Protein expression of CXCL1 was measured in conditioned medium from unstimulated BM-hMSCs (4 replicates, 1 donor, green), IL-1β stimulated BM-hMSCs (4 replicates, 1 donor, purple), and ILβ stimulated BM-hMSCs with 10 μM BAY 11–7082 (4 replicates, 1 donor, grey) C . Phospho-p65 levels were quantified and normalized to total p65. Data are expressed relative to control, which was set to 1 D . IL-1β Interleukin-1β BM-hMSCs Bone marrow-derived human mesenchymal cells, Ctrl control, CXCL1 chemokine (C-X-C motif) ligand 1, ns not significant; * p < 0,05; ****, p < 0,0001

Article Snippet: Following synchronization, medium was removed, and cells were stimulated with IL-1β (20 ng/ml in DPBS with 0.1% Bovine Serum Albumin, cat# 208-IL-010, R&D Systems) for 1 h (RNA-sequencing) or 24 h. Unstimulated control BM-hMSCs were exposed to serum free DMEM only.

Techniques: Migration, Membrane, Control, Expressing, Derivative Assay

Journal: bioRxiv

Article Title: The Glucose Transporter GLUT3 Controls Regulatory T Cell Function

doi: 10.64898/2026.03.26.714439

Figure Lengend Snippet: (A and B) Relative body weight changes (A) and experimental autoimmune encephalomyelitis (EAE) clinical scores (B) in WT, GLUT1-deficient ( Slc2a1 fl/fl Cd4 Cre ) and GLUT3-deficient ( Slc2a3 fl/fl Cd4 Cre ) mice following immunization with MOG 35-55 peptide emulsified in CFA; means ± SEM of 6-11 mice per cohort. (C) RT-qPCR analysis of Slc2a1 (GLUT1) and Slc2a3 (GLUT3) expression in isolated splenic CD4 + T cells from WT, GLUT1-deficient and GLUT3-deficient mice used in EAE experiments; data are shown as means ± SEM of 4-11 mice. (D and E) Representative flow cytometric analysis of Foxp3 + Treg cells in the central nervous system (CNS) of WT, GLUT1- and GLUT3-deficient mice 20 days after MOG 35-55 immunization (D) , with quantification of Treg cell frequencies and absolute cell numbers (E) ; means ± SEM of 6-11 mice. (F and G) Frequencies of GM-CSF and IL-2-producing CD4 + T cells in the CNS of WT, GLUT1-and GLUT3-deficient mice 20 days after immunization with MOG 35-55 peptide and restimulation with PMA/ionomycin for 5 h (F) , with quantification of total cell numbers of GM-CSF and IL-2 producing CD4 + T cells in the CNS (G) ; means ± SEM of 6-11 mice. Statistical analyses shown in (A, B, C, E, G) were performed using two-way ANOVA. *, p<0.05; **, p<0.01; ***, p<0.001; ns, non-significant.

Article Snippet: FACS-sorted Treg cells were activated on Delta surface 96-well plates (Nunc) with 0.25 ng/mL anti-CD3 (clone 145-2C1) and 1 ng/mL anti-CD28 (clone 37.51; both Bio X Cell), 20 ng/mL recombinant human IL2 and 10 ng/mL murine IL7 for three days at a density of 2×10 6 cells/mL.

Techniques: Quantitative RT-PCR, Expressing, Isolation

Journal: bioRxiv

Article Title: The Glucose Transporter GLUT3 Controls Regulatory T Cell Function

doi: 10.64898/2026.03.26.714439

Figure Lengend Snippet: (A and B) Relative body weight changes (A) and experimental autoimmune encephalomyelitis (EAE) clinical scores (B) in WT, GLUT1-deficient ( Slc2a1 fl/fl Cd4 Cre ) and GLUT3-deficient ( Slc2a3 fl/fl Cd4 Cre ) mice following immunization with MOG 35-55 peptide emulsified in CFA; means ± SEM of 6-11 mice per cohort. (C) RT-qPCR analysis of Slc2a1 (GLUT1) and Slc2a3 (GLUT3) expression in isolated splenic CD4 + T cells from WT, GLUT1-deficient and GLUT3-deficient mice used in EAE experiments; data are shown as means ± SEM of 4-11 mice. (D and E) Representative flow cytometric analysis of Foxp3 + Treg cells in the central nervous system (CNS) of WT, GLUT1- and GLUT3-deficient mice 20 days after MOG 35-55 immunization (D) , with quantification of Treg cell frequencies and absolute cell numbers (E) ; means ± SEM of 6-11 mice. (F and G) Frequencies of GM-CSF and IL-2-producing CD4 + T cells in the CNS of WT, GLUT1-and GLUT3-deficient mice 20 days after immunization with MOG 35-55 peptide and restimulation with PMA/ionomycin for 5 h (F) , with quantification of total cell numbers of GM-CSF and IL-2 producing CD4 + T cells in the CNS (G) ; means ± SEM of 6-11 mice. Statistical analyses shown in (A, B, C, E, G) were performed using two-way ANOVA. *, p<0.05; **, p<0.01; ***, p<0.001; ns, non-significant.

Article Snippet: For Th1 differentiation, cells were cultured with 2.5 μg/mL anti-IL-4 (clone 11B11, Bio X Cell), 10 ng/mL recombinant human IL-2 and 10 ng/mL recombinant murine IL-12 (both PeproTech).

Techniques: Quantitative RT-PCR, Expressing, Isolation

Journal: Scientific Reports

Article Title: IL-8 contributes to postoperative adhesion formation through the crosstalk of neutrophils and mesothelial cells

doi: 10.1038/s41598-026-42159-x

Figure Lengend Snippet: Evaluation of functional differences between IL-8 and CXCL1 in neutrophils. ( A ) Evaluation of IL-8 and CXCL1 activity in the U2OS-CXCR1 reporter cells ( left ) and CHO-K1-CXCR2 reporter cells ( right ). ( B ) Flow cytometric analysis of CXCR1 and CXCR2 surface expression on neutrophils. ( C ) Neutrophil chemotaxis assay toward IL-8 or CXCL1. RLU, relative luminescence units. Data in ( A ) and ( C ) are presented as the mean ± SD (n = 3).

Article Snippet: Recombinant human IL-8 (UniProt P10145 , residues 1—99) was produced in CHO cells by Chiome Bioscience Inc. Recombinant Human CXCL1/GRO alpha Protein (CXCL1, #275-GR-050) was purchased from R&D Systems, Inc. Recombinant Human TNF-alpha Protein (TNF-α, #210-TA-005 and Recombinant Human TGF-beta 1 Protein (TGF-β1, #240-B-010) were purchased from R&D Systems, Inc.

Techniques: Functional Assay, Activity Assay, Expressing, Chemotaxis Assay

Journal: Scientific Reports

Article Title: IL-8 contributes to postoperative adhesion formation through the crosstalk of neutrophils and mesothelial cells

doi: 10.1038/s41598-026-42159-x

Figure Lengend Snippet: Reciprocal amplification of IL-8 and TNF-α in MeT-5A cells. ( A , B ) Flow cytometric analysis of CXCR1 ( A ) and CXCR2 ( B ) surface expression on MeT-5A cells. Left: representative overlaid histograms. Right: quantification of MFI across biological replicates. P values were determined using Student’s t test. *** indicates P < 0.001. ( C ) Evaluation of TNF-α concentrations in culture medium. P values were determined using Tukey’s multiple comparison test. *** indicates P < 0.001. ( D ) Evaluation of IL-8 concentrations in culture medium. P values were determined using Williams’ test. * indicates P < 0.025. Quantitative data are presented as individual data points with mean ± SD. (n = 3).

Article Snippet: Recombinant human IL-8 (UniProt P10145 , residues 1—99) was produced in CHO cells by Chiome Bioscience Inc. Recombinant Human CXCL1/GRO alpha Protein (CXCL1, #275-GR-050) was purchased from R&D Systems, Inc. Recombinant Human TNF-alpha Protein (TNF-α, #210-TA-005 and Recombinant Human TGF-beta 1 Protein (TGF-β1, #240-B-010) were purchased from R&D Systems, Inc.

Techniques: Amplification, Expressing, Comparison

Journal: Scientific Reports

Article Title: IL-8 contributes to postoperative adhesion formation through the crosstalk of neutrophils and mesothelial cells

doi: 10.1038/s41598-026-42159-x

Figure Lengend Snippet: Fibrotic reactions in neutrophils and MeT-5A cells. ( A ) RNA expression change of TGFB1 in neutrophils stimulated with IL-8, IL-8 + AMY109, or TNF-α. ( B ) RNA expression change of TGFB1 , COL1A1 , FN1 , CCN2 ( CTGF ), SERPINE1 (PAI-1) and VIM in MeT-5A cells stimulated with TGF-β1 (0.4, 2, 10 ng/mL), TNF-α or IL-8. Data are presented as individual data points with mean ± SD. (n = 3) P values were determined using Dunnett’s test. * and *** indicate P < 0.05 and P < 0.001, respectively.

Article Snippet: Recombinant human IL-8 (UniProt P10145 , residues 1—99) was produced in CHO cells by Chiome Bioscience Inc. Recombinant Human CXCL1/GRO alpha Protein (CXCL1, #275-GR-050) was purchased from R&D Systems, Inc. Recombinant Human TNF-alpha Protein (TNF-α, #210-TA-005 and Recombinant Human TGF-beta 1 Protein (TGF-β1, #240-B-010) were purchased from R&D Systems, Inc.

Techniques: RNA Expression

Journal: Scientific Reports

Article Title: IL-8 contributes to postoperative adhesion formation through the crosstalk of neutrophils and mesothelial cells

doi: 10.1038/s41598-026-42159-x

Figure Lengend Snippet: Evaluation of IL-8 protein expression in injured abdominal walls from monkeys following cesarean sections (C-sections) and in postoperative adhesions (PA) model. ( A ) IL-8 concentrations in injured abdominal walls from monkeys following C-sections. Data are presented as individual data points with mean values indicated (n = 10 lesions for 0 h, 2 lesions for 6 h, Day 1, 3, 7, and 1 month). ( B ) IL-8 concentrations in injured abdominal walls from monkey PA models. Data are presented as individual data points with mean ± SD. (n = 6 lesions for 0 h, 8 lesions for 6 h, 4 lesions for Day 7) P values were determined using Steel’s test. * and ** indicate P < 0.05 and P < 0.01, respectively.

Article Snippet: Recombinant human IL-8 (UniProt P10145 , residues 1—99) was produced in CHO cells by Chiome Bioscience Inc. Recombinant Human CXCL1/GRO alpha Protein (CXCL1, #275-GR-050) was purchased from R&D Systems, Inc. Recombinant Human TNF-alpha Protein (TNF-α, #210-TA-005 and Recombinant Human TGF-beta 1 Protein (TGF-β1, #240-B-010) were purchased from R&D Systems, Inc.

Techniques: Expressing

Journal: Scientific Reports

Article Title: IL-8 contributes to postoperative adhesion formation through the crosstalk of neutrophils and mesothelial cells

doi: 10.1038/s41598-026-42159-x

Figure Lengend Snippet: Possible role of IL-8 and AMY109 in postoperative adhesion formation. IL-8 promotes neutrophil infiltration and forms a reciprocal amplification with TNF-α in mesothelial cells. Elevated TNF-α upregulates TGF-β1 in neutrophils, driving adhesion formation. Neutralization of IL-8 by AMY109 blocks neutrophil recruitment and subsequent inflammatory responses and fibrotic reactions, thereby preventing adhesion formation.

Article Snippet: Recombinant human IL-8 (UniProt P10145 , residues 1—99) was produced in CHO cells by Chiome Bioscience Inc. Recombinant Human CXCL1/GRO alpha Protein (CXCL1, #275-GR-050) was purchased from R&D Systems, Inc. Recombinant Human TNF-alpha Protein (TNF-α, #210-TA-005 and Recombinant Human TGF-beta 1 Protein (TGF-β1, #240-B-010) were purchased from R&D Systems, Inc.

Techniques: Amplification, Neutralization

Journal: Frontiers in Immunology

Article Title: A fully human IgG1 antibody targeting MICA α1 domain inhibits interaction with NKG2D and activates immune effector functions against MICA-expressing cells

doi: 10.3389/fimmu.2026.1740184

Figure Lengend Snippet: Production and biochemical characterization of the fully human anti-MICA c65 antibody. (A) Schematic representation of the antibody expression strategy in ExpiCHO cells using dual vectors encoding heavy and light chains. (B) FPLC chromatogram of Protein G-purified antibody. (C) SDS-PAGE under reducing conditions. Lane 1: protein ladder; Lane 2: anti-MICA c65 antibody; Lane 3: anti-CD20 antibody as isotype; Lane 4: PBS. (D) ELISA-based binding curve to rMICA at 3, 6, and 12 µg/mL. The binding data were used to calculate the apparent affinity constant (app K aff ) and apparent dissociation constant (app K d ), which are summarized in the table below the graph. (E) Competitive ELISA showing inhibition of NKG2D binding by anti-MICA c65 antibody. The percentage of optical density (%OD) reflects the amount of NKG2D-His bound to MICA (0, 6 and 12 µg/mL) on plates pre-coated with rMICA, following incubation with constant concentrations of NKG2D-His (9 µg/mL) and increasing concentrations of anti-MICA c65 antibody. Detection was performed using an HRP-conjugated anti-His antibody. Data represent the mean ± SD of two independent experiments.

Article Snippet: Recombinant human NKG2D-His protein was added at a fixed concentration of 281 nM, while increasing concentrations of anti-MICA c65 antibody, ranging from 0 to 323 nM, were incubated at 37°C for 2 h. Detection of NKG2D binding was performed using an HRP-conjugated anti-His antibody (Rockland, USA) with a 1 h incubation at 37°C.

Techniques: Expressing, Purification, SDS Page, Enzyme-linked Immunosorbent Assay, Binding Assay, Competitive ELISA, Inhibition, Incubation