Journal: International Journal of Molecular Medicine

Article Title: m 6 A in adipose tissue inflammation: A novel regulator of obesity and metabolic diseases (Review)

doi: 10.3892/ijmm.2026.5795

Figure Lengend Snippet: Role of m 6 A in adipogenesis. Insufficient adipogenesis in adipose tissue leads to persistent, chronic inflammation. m 6 A modification plays a crucial role in all stages of adipogenesis, from commitment to terminal differentiation. During commitment, METTL3 promotes lipogenic differentiation in BMSCs by regulating the m 6 A levels of PTH1R and JAK1, whereas silencing METTL14 reduces the expression of SMAD1, inhibiting BMSC proliferation. During terminal differentiation, m 6 A regulates MCE and the transition to mature adipocytes. FTO influences key genes such as ATG5, ATG7 and JAK2, affecting autophagy, STAT3 phosphorylation and adipogenesis. FTO knockout increases the m 6 A levels of CCND1 and CDK2, blocking MCE. m 6 A, N6-methyladenine; METTL, methyltransferase-like; PTH1R, parathyroid hormone 1 receptor; JAK, Janus kinase; BMSC, bone marrow mesenchymal stem cell; MCE, mitotic clone amplification; FTO, Fat mass and obesity-associated protein; ATG, autophagy-related; STAT3, signal transducer and activator of transcription 3; CCND1, cyclin D1; CDK2, cyclin-dependent kinase 2; IGF2BP1, insulin-like growth factor 2 mRNA-binding protein 1; YTHDF2, YTH domain family 2.

Article Snippet: In addition, for mitotic clone amplification (MCE) in the early stage of terminal differentiation, the inhibition of FTO expression in 3T3-L1 cells leads to increased m 6 A methylation levels of cyclin D1 (CCND1) and cyclin-dependent kinase 2, the protein expression of which is reduced after recognition by YTHDF2, resulting in blockade of the MCE process and in turn the inhibition of lipogenesis ( ) ( ).

Techniques: Modification, Expressing, Phospho-proteomics, Knock-Out, Blocking Assay, Amplification, Binding Assay

Journal: International Journal of Molecular Medicine

Article Title: m 6 A in adipose tissue inflammation: A novel regulator of obesity and metabolic diseases (Review)

doi: 10.3892/ijmm.2026.5795

Figure Lengend Snippet: Role of m 6 A in ATMs. ATMs are deeply involved in adipose tissue inflammation, and m 6 A plays critical roles in macrophage biology, including their development, activation, pyroptosis and metabolism of lipids. (A) m 6 A regulates macrophage development by targeting genes such as CCND1 and ATRX via YTHDF3, ALKBH5 and METTL3, affecting haematopoietic stem and progenitor cell differentiation. (B) m 6 A modification mediated by METTL3, METTL14 and IGF2BP2 controls macrophage activation and polarization by influencing key genes such as SPRED2, MYD88 and STAT1, which impact the NF-κB and PPAR-γ pathways. (C) m 6 A regulates macrophage pyroptosis by targeting CASPASE-1, IL-1β and MALAT1 and modulating pathways such as the PTBP1/USP8/TAK1 pathway. (D) Additionally, m 6 A affects macrophage lipid metabolism by regulating lipid uptake and cholesterol efflux through MSR1 and SR-B1. m 6 A, N6-methyladenine; ATMs, adipose tissue macrophages; CCND1, cyclin D1; ATRX, α-thalassemia X-linked intellectual disability syndrome; YTHDF3, YTH domain family 3; ALKBH5, alkB homologue 5; METTL, methyltransferase-like; IGF2BP2, insulin-like growth factor 2 mRNA-binding protein 2; SPRED2, sprouty-related EVH1 domain-2; MYD88, myeloid differentiation primary response 88; STAT1, signal transducer and activator of transcription 1; NF-κB, nuclear factor-κB; PPAR-γ, peroxisome proliferator-activated receptor γ; CASPASE-1, cysteinyl aspartate specific proteinase-1; IL, interleukin; MALAT1, metastasis-associated lung adenocarcinoma transcript 1; PTBP1, polypyrimidine tract-binding protein 1; USP8, ubiquitin-specific peptidase 8; TAK1, TGFβ-activated kinase 1; MSR1, macrophage scavenger receptor 1; SR-B1, scavenger receptor type B1; ROS, reactive oxygen species; TSC1, tuberous sclerosis complex 1; SOCS2, suppressor of cytokine signalling 2; GSDMD-N, gasdermin D N-terminal domain; OxLDL, oxidized low-density lipoprotein; MSR1, macrophage scavenger receptor 1; DDX5, DEAD-box helicase 5; MEHP, mono(2-ethylhexyl) phthalate.

Article Snippet: In addition, for mitotic clone amplification (MCE) in the early stage of terminal differentiation, the inhibition of FTO expression in 3T3-L1 cells leads to increased m 6 A methylation levels of cyclin D1 (CCND1) and cyclin-dependent kinase 2, the protein expression of which is reduced after recognition by YTHDF2, resulting in blockade of the MCE process and in turn the inhibition of lipogenesis ( ) ( ).

Techniques: Activation Assay, Cell Differentiation, Modification, Binding Assay, Ubiquitin Proteomics

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A CRC cell lines were treated with the indicated concentrations of TER for 72 h. Cell viability assessed using the CCK assay is shown. B Human CRC cell lines were co-cultured with hPD-1 Jurkat-T cells and treated with the indicated concentrations of TER for 72 h. C PD-L1 protein expression in CRC cells co-cultured with hPD-1 Jurkat-T cells and treated with TER for 72 h. GAPDH was used as a loading control. The results are shown as the mean ± SEM. * <0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 compared with the respective control.

Article Snippet: Next, 5 μL of 0.5 mg/mL biotinylated hPD-1 (#71109, BPS Bioscience) was added, and the plates were incubated for 2 h at room temperature.

Techniques: Cell Culture, Expressing, Control

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A The viability of hPD-1 Jurkat-T cells and hPD-L1 CHO cells following treatment with the indicated concentrations of TER for 24 h. B Luciferase activity measured using a PD-1/PD-L1 blockade bioassay. hPD-1 Jurkat-T cells (effector cells) were co-cultured with hPD-L1-expressing aAPC/CHO-K1 cells (target cells) in the presence of indicated concentrations of TER. The luminescence signal indicates the level of TCR signaling activation. αPD-L1 was used as a positive control. * <0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 compared with the respective control.

Article Snippet: Next, 5 μL of 0.5 mg/mL biotinylated hPD-1 (#71109, BPS Bioscience) was added, and the plates were incubated for 2 h at room temperature.

Techniques: Luciferase, Activity Assay, Bioassay, Cell Culture, Expressing, Activation Assay, Positive Control, Control

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A The viability of hPD-L1 MC38 cells following treatment with the indicated concentrations of TER for 72 h. B CD8 + T cells were isolated from tumors of hPD-1 knock-in mice bearing hPD-L1 MC38 tumors. These tumor-infiltrating CD8 + T cells were co-cultured with hPD-L1 MC38 cells as target cells in the presence of TER for 72 h. Cell viability measured using the CCK assay is depicted. C PD-L1 expression in hPD-L1 MC38 cells, as assessed by western blot analysis using protein lysates from co-culture conditions. GAPDH was used as a loading control. D The levels of immune-related factors, including GrB, IL-2, and IFN-γ, measured in the co-culture supernatant by ELISA. * <0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 compared with the respective control.

Article Snippet: Next, 5 μL of 0.5 mg/mL biotinylated hPD-1 (#71109, BPS Bioscience) was added, and the plates were incubated for 2 h at room temperature.

Techniques: Isolation, Knock-In, Cell Culture, Expressing, Western Blot, Co-Culture Assay, Control, Enzyme-linked Immunosorbent Assay

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A Body weight of hPD-1 knock-in mice during the treatment period. The mice were treated with vehicle or TER (10 or 30 mpk) for the indicated time. B Spleen weight of mice at the endpoint of the experiment. C Tumor volume was measured over time in hPD-1 knock-in mice bearing hPD-L1 MC38 tumors treated with vehicle or TER (10 or 30 mpk). Representative images of excised tumors from each group are shown. D Tumor weight at the endpoint of the experiment. E Flow cytometry analysis of CD8 + T-cell populations in tumors from each treatment group. F PD-L1 expression in tumors from each group, as assessed by western blot analysis. GAPDH was used as a loading control. G IHC staining of tumor sections for immune-related markers, including CD8 + T cells and GrB. Representative images from each group are shown, and the quantitation of marker-positive cells per field is presented. * <0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 compared with the respective control.

Article Snippet: Next, 5 μL of 0.5 mg/mL biotinylated hPD-1 (#71109, BPS Bioscience) was added, and the plates were incubated for 2 h at room temperature.

Techniques: Knock-In, Flow Cytometry, Expressing, Western Blot, Control, Immunohistochemistry, Quantitation Assay, Marker

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A Body weight of hPD-1 knock-in mice during the treatment period. The mice were treated with vehicle or TER (30 mpk) and received either an isotype control or a CD8 depletion antibody. B Spleen weight of mice at the endpoint of the experiment. C Tumor volume was measured in hPD-1 knock-in mice bearing hPD-L1 MC38 tumors over time following treatment with vehicle or TER (30 mpk) with or without CD8 depletion. Representative images of excised tumors from each group are shown. D Tumor weight at the endpoint of the experiment. E Flow cytometry analysis confirming CD8 + T-cell depletion in tumors from each treatment group. The proportion of CD8 + cells among total live cells was quantified. F IHC staining of tumor sections for CD8 + T cells and GrB. Representative images from each treatment group are shown, and the quantitation of marker-positive cells per field is presented. * <0.05, ** p < 0.01, and **** p < 0.0001 compared with the respective control.

Article Snippet: Next, 5 μL of 0.5 mg/mL biotinylated hPD-1 (#71109, BPS Bioscience) was added, and the plates were incubated for 2 h at room temperature.

Techniques: Knock-In, Control, Flow Cytometry, Immunohistochemistry, Quantitation Assay, Marker

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: (A) Longitudinal trajectories of serum IgG (top row) and mucosal IgA (bottom row) antibody responses against four RSV-B proteins (PreF, PostF, G, NP) over time. Individual participant trajectories are shown as thin lines with low opacity, colored by infection status: not infected (black), sero-detected infections (orange), and PCR-confirmed infections (green). (B) Mean fold-change in antibody titres between the first bleed (pre-epidemic baseline) and second bleed (post-epidemic) for serum IgG and mucosal IgA responses to RSV-B proteins. Bars represent mean fold-change (log10 scale) stratified by infection status, with error bars indicating standard error.

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Infection

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: (A) Post-infection longitudinal antibody titers for four viral RSV-B proteins (PreF, PostF, G, and NP) across different antibody types; serum IgG and mucosal IgA. Lines show the median posterior predictive fit from the fitted Bayesian model, and the points show the observational titre data, with the size correlating with the sample size for that bin. (B) Peak antibody (x axis) and persistence measured as duration above a 2-fold (left panel) and 4-fold titre rise (right panel) in days. Data points show median posterior values for measurements of four viral RSV-B proteins (PreF, PostF, G, and NP) across different antibody types: serum IgG and mucosal IgA.

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Infection

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: Serum IgG, top row; mucosal IgA, bottom row and columns are viral antigen target (PreF, PostF, G, and NP for both RSV-A and RSV-B strains). The solid green line represents the mean estimated probability of protection given exposure to infection as a function of antibody titre, with shaded ribbons indicating 95% credible intervals. Background histograms show the distribution of antibody titres at infection for infected individuals (orange) versus non-infected individuals (gray).

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Infection

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: Model performance comparison across single biomarker models and the dual biomarker model, defined by out-of-sample predictive accuracy (LOO-ELPD, x-axis) and discrimination ability (area under the ROC curve, AUC, y-axis). Circles indicate serum IgG models, squares represent mucosal IgA models, and the triangle denotes the dual biomarker model combining serum IgG and mucosal IgA to RSV-B PreF. The best-performing model within each biomarker class is highlighted with darker shading. Error bars show the standard error of LOO-ELPD (horizontal) and 95% confidence intervals for AUC (vertical). The dashed horizontal line indicates an AUC of 0.7.

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Comparison, Biomarker Discovery