Journal: Oncogene

Article Title: X-linked cancer-associated polypeptide (XCP) from lncRNA1456 modulates PHF8 histone demethylase activity to regulate the epigenome, gene expression, and cellular pathways in breast cancer

doi: 10.1038/s41388-026-03740-w

Figure Lengend Snippet: A , B Xenograft assays showing subcutaneous tumor growth of MCF-7 ( A ) or MDA-MB-231 ( B ) breast cancer cells ectopically expressing dox-inducible FLAG-GFP or XCP-FLAG ( left ). Tumor weight at end of experiment is shown ( right ). Animals injected with MCF-7 cells had E2-pellet implantations at the back of the neck to promote growth of MCF-7 cells in vivo. All animals were fed doxycycline in their chow. Each point represents the mean ± SEM. For MCF-7, GFP n = 7 and XCP n = 7; For MDA-MB-231, GFP n = 8 and XCP n = 8. Significance was calculated using unpaired t-test. C , D Expression of FLAG-GFP or XCP-FLAG in tumor tissue was validated from MCF-7 ( C ) or MDA-MB-231 ( D ) xenograft tumors by Western blot ( left ) and RT-qPCR ( right ). For Western blot, 3 representative tumors from each group are shown. β-tubulin was used as a loading control. For RT-qPCR, the average of all tumors from each group is shown. RNA levels were quantified by normalizing to housekeeping gene RPL19 mRNA. Each bar represents the mean + SEM. For MCF-7, GFP n = 7 and XCP n = 7; For MDA-MB-231, GFP n = 8 and XCP n = 8. [See also Fig. ].

Article Snippet: MCF-7 (ATCC; RRD:CVCL_0031) cells were kindly provided by Benita S. Katzenellenbogen (University of Illinois, Urbana-Champaign, Champaign, IL) and MDA-MB-231 cells were purchased from the American Type Culture Collection (ATCC; RRID:CVCL_0062).

Techniques: Expressing, Injection, In Vivo, Western Blot, Quantitative RT-PCR, Control

Journal: Oncogene

Article Title: X-linked cancer-associated polypeptide (XCP) from lncRNA1456 modulates PHF8 histone demethylase activity to regulate the epigenome, gene expression, and cellular pathways in breast cancer

doi: 10.1038/s41388-026-03740-w

Figure Lengend Snippet: A , B Heatmaps ( left ) and Gene Ontology analysis ( right ) showing XCP-mediated gene expression changes in MCF-7 ( A ) and MDA-MB-231 ( B ) xenograft tumors. C , D Box plots showing gene set analysis of XCP-induced genes and their expression levels stratified into breast cancer subtypes using PAM50 gene set analysis ( left ) and stratified by ER status ( right ) in MCF-7 ( C ) and MDA-MB-231 ( D ) xenograft tumors. Observed differences are significant as determined by an ANOVA comparison of the means ( P value < 0.00001). [See also Fig. ].

Article Snippet: MCF-7 (ATCC; RRD:CVCL_0031) cells were kindly provided by Benita S. Katzenellenbogen (University of Illinois, Urbana-Champaign, Champaign, IL) and MDA-MB-231 cells were purchased from the American Type Culture Collection (ATCC; RRID:CVCL_0062).

Techniques: Gene Expression, Expressing, Comparison

Journal: Cell Death Discovery

Article Title: Salinomycin as a death switch: how gastric cancer cells choose their demise

doi: 10.1038/s41420-026-03058-2

Figure Lengend Snippet: H2DCFA was used to evaluate ROS production after Sal treatment (48 h) by flow cytometry. Histogram reports the frequencies of ROS positive cells. Sal significantly promoted ROS production in the two cell lines (AGS and KATO-III) not undergoing apoptotic cell death. Data were obtained from three independent biological replicates. T-test was used to evaluate statistical significance (** p < 0.01, **** p < 0.0001).

Article Snippet: SNU1, NCI-N87, AGS, and KATO-III (RRID: CVCL_0099, CVCL_1603, CVCL_0139 and CVCL_0371) GC cells lines were acquired from ATCC (Manassas, VA, USA).

Techniques: Flow Cytometry

Journal: Cell Death Discovery

Article Title: Salinomycin as a death switch: how gastric cancer cells choose their demise

doi: 10.1038/s41420-026-03058-2

Figure Lengend Snippet: A Single cell suspension of Sal- and vehicle-treated cell lines were stained with anti-CD44-FITC and anti-CD133-PE and analyzed by flow cytometry. High levels of both CSC markers were measured in NCI-N87 and KATO-III cells with the latter showing the highest expression. These cell lines, after 48 h of Sal treatment, showed a marked reduction of CD44 + and CD133 + cell populations. Representative histogram overlays of Sal vs vehicle stemness markers positive cell populations. One-sample t -test was used to assess significance, using data from three independent biological replicates. B After 48 h of treatment, cells were harvested and seeded and cultured for 14 days. Morphology and size of spheroids were recorded at 3, 7, 10, and 14 days. The plots summarize radius of Sal-treated cells as compared with vehicle controls from three replicates of two independent experiments. Images were acquired at 10× and 4× for NCI-N87 and KATO-III, respectively. A marked reduction of spheroids size was observed for NCI-N87 cells, while no spheroids formation was observed for KATO-III. C Untreated cells were seeded and treated on day 7 after spheroid formation. Their morphology and size were assessed after 48 h of treatment. Plots report the ratio between spheroids radius before and after treatment from three independent experiments. Sal-treated spheroids were significantly smaller in size as compared with vehicle for both cell lines. D Cells were treated for 48 h and then harvested and seeded for colony-forming assay. Colonies were observed after 14 days of culture, few colonies formed in Sal-treated NCI-N87 cells, and no colonies were found for KATO-III cells. Three independent experiments were performed. T -test was employed to estimate significance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001).

Article Snippet: SNU1, NCI-N87, AGS, and KATO-III (RRID: CVCL_0099, CVCL_1603, CVCL_0139 and CVCL_0371) GC cells lines were acquired from ATCC (Manassas, VA, USA).

Techniques: Single Cell, Suspension, Staining, Flow Cytometry, Expressing, Cell Culture

Journal: MedComm

Article Title: Discovery of a First‐in‐Class Murine Double Minute 2‐Recruiting Positive Transcription Elongation Factor B PROTAC Degrader With Selective Antitumor Activity

doi: 10.1002/mco2.70723

Figure Lengend Snippet: MDM2‐ and p53‐dependent activities of MDM2‐recruiting P‐TEFb PROTAC degraders. (A) Effects of siRNA‐mediated MDM2 knockdown on cellular sensitivity to dCDK9‐010. Data were presented as mean ± standard deviation (SD); n = 3. (B) Effects of MDM2 knockdown on dCDK9‐010‐mediated CDK9/Cyclin T degradation. TC‐32 cells were transfected with indicated siRNAs for 48 h, followed by treatment with 2 µM dCDK9‐010 for 8 h. (C) MDM2 mRNA levels in wild type versus TP53 ‐knockout U87 cells, with or without compound treatment (2 µM, 8 h). Data were presented as mean ± SD ( n = 3); *** p < 0.001 based on one‐way analysis of variance (ANOVA); n.s., no significance. (D) Immunoblot analysis of P‐TEFb components, p53, and MDM2 in wild‐type and TP53 ‐knockout isogenic U87 cells after compound treatment (2 µM, 8 h). (E) Viability of isogenic U87 cells treated with dCDK9‐010. Data were presented as mean ± SD ( n = 3). (F) Immunoblot analysis of P‐TEFb components, p53, and MDM2 in NCI‐H226 and TC‐32 cells after siRNA‐mediated TP53 silencing and dCDK9‐010 treatment (2 µM, 8 h). (G) Effects of TP53 or MDM4 knockdown by siRNA relative to control on dCDK9‐010 sensitivity in NCI‐H226 and TC‐32 cells. Data were presented as mean ± SD ( n = 3).

Article Snippet: HEK293T (ATCC), TC‐32 (COG Repository, USA), HCT116 (ATCC), A549 (ATCC), HEPG2 (ATCC), HT1080 (ATCC), MDA‐MB‐231 (ATCC), U87 (U‐87MG, ATCC), U251 (U251MG, ATCC), and MKN45 (ATCC) cells lines were maintained in Dulbecco's modified Eagle medium (DMEM; Sigma‐Aldrich, Taufkirchen, Germany).

Techniques: Knockdown, Standard Deviation, Transfection, Knock-Out, Western Blot, Control

Journal: MedComm

Article Title: Discovery of a First‐in‐Class Murine Double Minute 2‐Recruiting Positive Transcription Elongation Factor B PROTAC Degrader With Selective Antitumor Activity

doi: 10.1002/mco2.70723

Figure Lengend Snippet: Selective activities of compounds 12 (dCDK9‐009) and 13 (dCDK9‐010) against TP53 wild‐type cancer cells. (A and B) Examination of dose‐dependent impacts of dCDK9‐009 and dCDK9‐010 in TP53 wild‐type HCT116, HT1080, NCI‐H460, and U87. Cells were treated with increasing concentrations of indicated compounds for 24 h. (C and D) Examination of impacts of dCDK9‐009 and dCDK9‐010 in non‐malignant HEK293T and mesenchymal stem cell line ASC52telo. Cells were treated with increasing concentrations of indicated compounds for 24 h. (E and F) Effect of dCDK9‐009 and dCDK9‐010 treatment on cellular viabilities of indicated cancer cell lines, as well as ASC52telo. IC 50 was presented as mean ± SD with three independent replicates. (G) Heatmap summarizing the IC 50 values of dCDK9‐009 and dCDK9‐010 across human cell lines tested in this study (related to E and F, Figures S3, S4, and S8).

Article Snippet: HEK293T (ATCC), TC‐32 (COG Repository, USA), HCT116 (ATCC), A549 (ATCC), HEPG2 (ATCC), HT1080 (ATCC), MDA‐MB‐231 (ATCC), U87 (U‐87MG, ATCC), U251 (U251MG, ATCC), and MKN45 (ATCC) cells lines were maintained in Dulbecco's modified Eagle medium (DMEM; Sigma‐Aldrich, Taufkirchen, Germany).

Techniques:

Journal: Journal of Translational Medicine

Article Title: Formyl peptide receptor 2 activation by MR-39 inhibits glioblastoma cell proliferation and invasiveness through suppression of multiple oncogenic pathways

doi: 10.1186/s12967-026-07781-3

Figure Lengend Snippet: Antiproliferative effect of MR-39 on human glioblastoma cell lines. ( A ) U87-MG, U138-MG, and U251-MG cells were exposed to 5-100 µM of MR-39 for 48 h. ( B ) Number of U87-MG, U138MG, and U251-MG cells exposed for 48 h to either the vehicle (CTRL) or 10 µM MR-39. ( C ) U87-MG, U138-MG, and U251-MG cells were exposed to either vehicle (CTRL) or 10 µM MR-39, with or without the FPR2 antagonist WRW4 (10 µM). ( D ) U87-MG cells were transfected with FPR2-targeting antisense siRNA1 or a negative control (siRNA-), followed by treatment with or without 10 µM MR-39. Cell proliferation was measured using the CCK-8 assay and is expressed as a percentage of the control. Data are expressed as means ± SEM, n = 3. Statistically significant differences are based on an unpaired t-test * p value < 0.05, ** p value < 0.005, *** p value < 0.001, **** p value < 0.0001 or one-way ANOVA followed by Tukey’s multiple comparison test

Article Snippet: EA.hy926 (CRL-2922 TM) andU87-MG (HTB-14 TM) cell lines were acquired from ATCC, while U138MG, and U251-MG were kindly provided by Prof. Generoso Luca Colucci D’Amato, University of Campania “Luigi Vanvitelli” [ ].

Techniques: Transfection, Negative Control, CCK-8 Assay, Control, Comparison

Journal: Cell Reports Medicine

Article Title: Early-stage multi-cancer detection through a plasma extracellular vesicle protein signature

doi: 10.1016/j.xcrm.2026.102694

Figure Lengend Snippet: Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, MDA231, and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .

Article Snippet: U118 MG , ATCC , HTB-15; RRID: CVCL_0633.

Techniques: Transformation Assay, Derivative Assay, Isolation, Transmission Assay, Electron Microscopy, Tunable Resistive Pulse Sensing, Western Blot, Marker, Mass Spectrometry, Enzyme-linked Immunosorbent Assay, Expressing

Journal: Central-European Journal of Immunology

Article Title: Dexmedetomidine inhibits the Wnt/β-catenin pathway, regulates ferroptosis in bladder cancer cells and the tumor immune microenvironment, and suppresses tumorigenesis in a mouse bladder cancer model

doi: 10.5114/ceji.2025.155276

Figure Lengend Snippet: Dexmedetomidine inhibited the proliferation of bladder cancer cells. A ) SV-HU-1 normal bladder cells, B ) T24 bladder cancer cells, and C ) RT4 bladder cancer cells were treated with increasing concentrations of dexmedetomidine (0, 0.125, 0.25, 0.5, 1, 2, 4 μM) for 24 hours, and cell viability was measured using the CCK8 assay. Data are presented as mean ± SD from three independent experiments. Statistical significance was determined using one-way ANOVA followed by Tukey’s posthoc test. * p < 0.05, ** p < 0.01 compared to the control group (0 μM Dex)

Article Snippet: Peripheral blood mononuclear cells (PBMCs), SV-HU-1, T24, and RT4 cells (all purchased from ATCC) were cultured under standard conditions.

Techniques: CCK-8 Assay, Control

Journal: Central-European Journal of Immunology

Article Title: Dexmedetomidine inhibits the Wnt/β-catenin pathway, regulates ferroptosis in bladder cancer cells and the tumor immune microenvironment, and suppresses tumorigenesis in a mouse bladder cancer model

doi: 10.5114/ceji.2025.155276

Figure Lengend Snippet: Dexmedetomidine induced ferroptosis and increased ROS levels in bladder cancer cells. A ) Western blot analysis of GPX4 and SLC7A11 expression in T24 and RT4 cells treated with different concentrations of Dex (0, 0.5, 1, 2 μM) for 24 hours. B ) Relative Fe2+ levels in T24 and RT4 cells treated with varying Dex concentrations. C ) Fe2+ levels in RT4 and T24 cells treated with Dex (2 μM) alone or in combination with erastin (ferroptosis inducer) or ferrostatin-1 (ferroptosis inhibitor). D ) Lipid ROS levels in T24 and RT4 cells after treatment with increasing Dex concentrations. Data are presented as mean ± SD from three independent experiments. Statistical significance was determined using one-way ANOVA followed by Tukey’s post-hoc test. * p < 0.05, ** p < 0.01 compared to the control group (0 μM Dex) E ) Immunofluorescence images showing ROS accumulation in T24 and RT4 cells treated with different Dex concentrations

Article Snippet: Peripheral blood mononuclear cells (PBMCs), SV-HU-1, T24, and RT4 cells (all purchased from ATCC) were cultured under standard conditions.

Techniques: Western Blot, Expressing, Control, Immunofluorescence

Journal: Central-European Journal of Immunology

Article Title: Dexmedetomidine inhibits the Wnt/β-catenin pathway, regulates ferroptosis in bladder cancer cells and the tumor immune microenvironment, and suppresses tumorigenesis in a mouse bladder cancer model

doi: 10.5114/ceji.2025.155276

Figure Lengend Snippet: Dexmedetomidine reduced PD-L1 expression and enhanced CD8+ T-cell activity in bladder cancer cells. A ) Western blot analysis of PD-L1 expression in T24 and RT4 cells treated with different concentrations of Dex (0, 0.5, 1, 2 μM) for 24 hours. B ) Representative flow cytometry plot showing CD3+CD8+ T-cell percentages in co-cultures of PBMCs with T24 or RT4 cells treated with 0 μM or 2 μM Dex. C ) Quantification of CD8+ T-cell percentages in PBMC co-cultures with T24 and RT4 cells. D ) IFN-γ and IL-10 levels in PBMC co-cultures with T24 and RT4 cells treated with 0 μM or 2 μM Dex, measured by ELISA. Data are presented as mean ± SD from three independent experiments. Statistical significance was determined using one-way ANOVA followed by Tukey’s post-hoc test. * p < 0.05, ** p < 0.01 compared to the control group (0 μM Dex)

Article Snippet: Peripheral blood mononuclear cells (PBMCs), SV-HU-1, T24, and RT4 cells (all purchased from ATCC) were cultured under standard conditions.

Techniques: Expressing, Activity Assay, Western Blot, Flow Cytometry, Enzyme-linked Immunosorbent Assay, Control

Journal: Central-European Journal of Immunology

Article Title: Dexmedetomidine inhibits the Wnt/β-catenin pathway, regulates ferroptosis in bladder cancer cells and the tumor immune microenvironment, and suppresses tumorigenesis in a mouse bladder cancer model

doi: 10.5114/ceji.2025.155276

Figure Lengend Snippet: Dexmedetomidine inhibited Wnt/β-catenin signaling in bladder cancer cells. A ) Western blot analysis of active β-catenin, β-catenin, c-Myc, and cyclin D1 expression in T24 and RT4 cells treated with different concentrations of Dex (0, 0.5, 1, 2 μM) for 24 hours. B ) Western blot analysis of active β-catenin, β-catenin, c-Myc, and cyclin D1 expression in RT4 cells. Data are presented as mean ± SD from three independent experiments. Statistical significance was determined using one-way ANOVA followed by Tukey’s post-hoc test. * p < 0.05, ** p < 0.01 compared to the control (0 μM Dex); # p < 0.05, ## p < 0.01 compared to the 2 μM Dex group C ) Western blot analysis and quantification of active β-catenin, β-catenin, c-Myc, and cyclin D1 in T24 cells treated with 2 μM Dex alone or in combination with 2 μM LiCl (Wnt/β-catenin activator). Data are presented as mean ± SD from three independent experiments. Statistical significance was determined using one-way ANOVA followed by Tukey’s post-hoc test. * p < 0.05, ** p < 0.01 compared to the control (0 μM Dex); # p < 0.05, ## p < 0.01 compared to the 2 μM Dex group

Article Snippet: Peripheral blood mononuclear cells (PBMCs), SV-HU-1, T24, and RT4 cells (all purchased from ATCC) were cultured under standard conditions.

Techniques: Western Blot, Expressing, Control