Journal: International Journal of Molecular Medicine

Article Title: IL-37/IL-1R8 blocks keratinocyte acantholysis via suppressing ADAM17/EGFR

doi: 10.3892/ijmm.2026.5793

Figure Lengend Snippet: IL-37/IL-1R8 protects HaCaT cells from keratinocyte dissociation and apoptosis through the ADAM17/EGFR pathway. (A) Protein expression levels of ADAM17, p-EGFR, total EGFR as well as EGFR downstream protein p-AKT, p-ERK1/2 and p-STAT3 levels were determined by western blotting. HaCaT cells were treated with EGFR activator NSC228155. (B) Cell dissociation was analyzed by cell dissociation assay. (C) Cell apoptosis was analyzed by flow cytometry. (D) Protein expression levels of Bcl-2 and Bax were analyzed by western blotting. (E) HaCaT was transfected with ADAM17 siRNA and the transfection efficiency was detected by western blotting. HaCaT cells were transfected with ADAM17 siRNA or treated with 1 μ M of EGFR inhibitor AG1478 for 30 min followed by treated with AK23. (F) Cell dissociation was analyzed by cell dissociation assay. (G) Cell apoptosis was analyzed by flow cytometry. # P<0.05 vs. Control group; & P<0.05 vs. anti-Dsg3 group; @ P<0.05 vs. anti- Dsg3 + IL-37 + si-NC group; * P<0.05; Data are presented as mean ± SD, n=3 biological indepen- dent replicates. One-way ANOVA with Bonferroni's post-hoc test was used for multiple group comparisons. IL, interleukin; ADAM17, TNF-alpha-converting enzyme; EGFR, epidermal growth factor receptor; p- phosphorylated; STAT, signal transducer and activator of transcription; si, short interfering.

Article Snippet: For EGFR inhibition assay, HaCaT cells were pre-treated with 1 μ M of EGFR inhibitor AG1478 (MedChemExpress) at 37°C for 30 min followed by treatment with AK23 for 24 h at 37°C.

Techniques: Expressing, Western Blot, Flow Cytometry, Transfection, Control

Journal: Genes & Diseases

Article Title: MFAP2 promotes metastasis and drug resistance by regulating epithelial-to-mesenchymal transition through EGFR signaling pathway in colorectal cancer cells

doi: 10.1016/j.gendis.2025.101800

Figure Lengend Snippet: MFAP2 promotes epithelial–mesenchymal transition (EMT) through the EGFR-AKT-STAT3 signaling pathway in colorectal cancer (CRC) cells. (A, B) The top 20 enrichment signaling pathways regulated by MFAP2 knockdown. (C, D) VEGFR2 signaling pathway was enriched in the MFAP2 knockdown cells, shown by Gene Set Enrichment Analysis (GSEA) and essential genes in this enrichment. (E) MFAP2 knockdown affected the EGFR-AKT-STAT3 axis.

Article Snippet: Following blocking with 5% non-fat milk in PBS with 0.02% Tween 20 detergent (PBST) at room temperature for 2 h, the membranes were incubated with primary antibodies, including MFAP2 (Solarbio, China), GAPDH (BBI Co., Ltd., China), epidermal growth factor receptor (EGFR; Proteintech, China), protein kinase B (AKT) (Proteintech), signal transducer and activator of transcription 3 (STAT3) (Proteintech), and vascular endothelial growth factor A (VEGFA) (Proteintech), p-EGFR (Cell Signaling Technology, USA), p-STAT3 (Cell Signaling Technology), and p-AKT ser473 (Cell Signaling Technology) antibodies, at 4 °C overnight.

Techniques: Protein-Protein interactions, Knockdown

Journal: RSC Advances

Article Title: Ferulic and p -coumaric acid derivatives as dual EGFR-VEGFR2 inhibitors: design, semi-synthesis, and biological investigations

doi: 10.1039/d6ra01213b

Figure Lengend Snippet: Dose–response curves of the EGFR/VEGFR2 inhibition of compound 3f. IC 50 values were calculated using the non-linear regression dose–response curves in GraphPad prism. Values are expressed as mean ± SD of three independent trials.

Article Snippet: All molecules were evaluated for their EGFR (BPS Bioscience Corporation Catalog #40321) and VEGFR-2 kinase inhibition using (BPS Bioscience Corporation catalog#40325) using ELISA kit (Enzyme-Linked Immunosorbent Assay).

Techniques: Inhibition

Journal: RSC Advances

Article Title: Ferulic and p -coumaric acid derivatives as dual EGFR-VEGFR2 inhibitors: design, semi-synthesis, and biological investigations

doi: 10.1039/d6ra01213b

Figure Lengend Snippet: Docking findings of the top-active synthesized compounds on dual kinase enzymes. Cartoon-surface 3D representation of the kinase highlighting the color-coded secondary structures; (yellow) Gly-rich loop, (red) hinge site, (magenta) activation loop, (cyan) catalytic motif, and (orange) gatekeeper residue; predicted binding modes of the 3f, 3h, and 3d compounds (blue sticks) with the redocked co-crystallized for docking protocol validation aligned co-crystallized as green sticks over the redocked blue sticked poses of EGFR's reversible inhibitor, Erlotinib (PDB ID: 4hjo) and VEGFR-2's potent reversible inhibitor, Sorafenib (PDB ID: 4asd). Only key residues of binding at a 4 Å radius around the ligand are shown as lines and polar contacts as black-dash lines.

Article Snippet: All molecules were evaluated for their EGFR (BPS Bioscience Corporation Catalog #40321) and VEGFR-2 kinase inhibition using (BPS Bioscience Corporation catalog#40325) using ELISA kit (Enzyme-Linked Immunosorbent Assay).

Techniques: Synthesized, Activation Assay, Residue, Binding Assay, Biomarker Discovery

Journal: bioRxiv

Article Title: Extracellular signalling regulates gastrin transcription through site-specific phosphorylation and nuclear redistribution of Menin

doi: 10.64898/2026.04.07.717082

Figure Lengend Snippet: (A) Hematoxylin and eosin (H&E) staining of normal duodenum containing Brunner’s glands (nDUO-BG) and duodenal neuroendocrine tumor (DNET). Dashed boxes indicate regions shown at higher magnification. (B) Immunohistochemical staining for synaptophysin (SYP) confirming neuroendocrine differentiation in DNET. (C-D) Immunohistochemical staining for TGFα and EREG in tumor-associated Brunner’s glands (tBG) and DNET. Dashed boxes indicate tumor-gland interfaces. (E-F) Quantification of TGFα and EREG expression by H-score in nDUO-BG, tBG, and DNET. Data are mean ± SEM; ns, not significant; ****P < 0.0001. (G) EGFR immunostaining in nDUO-BG and DNET showing heterogeneous expression across tissues. (H) Menin immunostaining in nDUO-BG and DNET. (I) Representative FFPE DNET specimens showing cytoplasmic or near-absent Menin expression, accompanied by strong TGFα and EREG staining within tumor cells. (J) Quantification of Menin nuclear-to-cytoplasmic (N/C) ratio in nDUO-BG and DNET. Data are mean ± SEM; ****P < 0.0001. Images were taken at 100X, 200X and 400X. Scale bars: 100 μm (low magnification) and 50 μm (high magnification).

Article Snippet: After 24 h, cells were serum-starved for 24 h, followed by treatment with either recombinant human eregulin (EREG) protein (10 nM), a potent ligand for EGFR (R&D systems, #1195-EP) or 10 μM Forskolin (FSK, ThermoFisher, #66575-29-9), activator of adenylyl cyclase and cyclic AMP or and 10nM phorbol 12-myristate 13-acetate (TPA; Sigma-Aldrich, #P8139) for 4-8 h. Cells were lysed, and luciferase activity was measured using the Dual-Luciferase Reporter Assay System (Promega, #E1980) according to the manufacturer’s instructions.

Techniques: Staining, Immunohistochemical staining, Expressing, Immunostaining

Journal: bioRxiv

Article Title: Extracellular signalling regulates gastrin transcription through site-specific phosphorylation and nuclear redistribution of Menin

doi: 10.64898/2026.04.07.717082

Figure Lengend Snippet: (A) Multiple sequence alignment of the Menin C-terminal region from the indicated vertebrate species showing strong conservation of a basic residue–rich motif encompassing Ser487. Conserved basic residues and Ser487 are highlighted. (B) Schematic of human Menin illustrating the position of Ser487 within NLS1. The expanded sequence highlights Ser487 and surrounding basic residues; constructs used in this study. (C) Immunoblot analysis of AGS cells expressing FLAG-tagged wild-type Menin or Ser487 mutants (S487A, S487D) following treatment with EREG, FSK, or TPA. Whole-cell lysates were probed with antibodies against phospho-Ser487 Menin, FLAG-Menin, and GAPDH. (D, E) Immunoblot analysis of MKN-45G and KATO III cells expressing wild-type Menin following stimulation with EREG, FSK, or TPA. Blots were probed for phospho-Ser487 Menin, FLAG-Menin, and β-tubulin. (F, H) Quantification of phospho-Ser487 Menin in AGS, KATO III and MKN-45G cells. (I) Immunoblot analysis of AGS cells examining activation of cAMP and EGFR downstream kinases under the indicated conditions. (J) Densitometric quantification of signalling outputs shown in (I), expressed as fold change relative to vector control. (K) Time-course of Ser487 phosphorylation in AGS cells stimulated with TPA in the presence of kinase inhibitors; MEK inhibitor (U0126), AKT inhibitor (MK-2206), PKC inhibitor (Gö6983), or combined MEK+AKT inhibition. (L) Quantification of Ser487 phosphorylation kinetics following TPA stimulation with the indicated inhibitors. (M) Area-under-the-curve (AUC) analysis of phosphorylation in (L). Data are presented as mean ± SEM; individual data points represent independent biological replicates (n = 3). Statistical significance was determined by one-way ANOVA with Tukey’s multiple-comparison test (*P < 0.05; **P < 0.01; ****P < 0.0001; ns, not significant).

Article Snippet: After 24 h, cells were serum-starved for 24 h, followed by treatment with either recombinant human eregulin (EREG) protein (10 nM), a potent ligand for EGFR (R&D systems, #1195-EP) or 10 μM Forskolin (FSK, ThermoFisher, #66575-29-9), activator of adenylyl cyclase and cyclic AMP or and 10nM phorbol 12-myristate 13-acetate (TPA; Sigma-Aldrich, #P8139) for 4-8 h. Cells were lysed, and luciferase activity was measured using the Dual-Luciferase Reporter Assay System (Promega, #E1980) according to the manufacturer’s instructions.

Techniques: Sequencing, Residue, Construct, Western Blot, Expressing, Activation Assay, Plasmid Preparation, Control, Phospho-proteomics, Inhibition, Comparison