Journal: Biochemical and biophysical research communications

Article Title: The regulation of soluble receptor for AGEs contributes to carbonyl stress in schizophrenia.

doi: 10.1016/j.bbrc.2016.09.074

Figure Lengend Snippet: Fig. 3. A: Serum sRAGE was significantly decreased in schizophrenia. sRAGE levels were measured in schizophrenia (N ¼ 25) and control (N ¼ 49) individuals (Schizophrenia: 650.6 ± 348.0 pg/ml, Control: 839.4 ± 304.0 pg/ml, p ¼ 0.03). B: esRAGE/sRAGE ratio was demonstrated. Serum esRAGE levels accounted for approximately 40% of the serum sRAGE levels in both groups (Schizophrenia: 39.8%, Control: 37.3%, p ¼ 0.52). Error bars indicate standard deviation (SD). *p < 0.05.

Article Snippet: Serum sRAGE levels were determined by using a human sRAGE ELISA kit (Quantikine® ELISA Human RAGE Cat#DRG00 R&D Systems).

Techniques: Control, Standard Deviation

Journal: PloS one

Article Title: HMGB1 accelerates alveolar epithelial repair via an IL-1β- and αvβ6 integrin-dependent activation of TGF-β1.

doi: 10.1371/journal.pone.0063907

Figure Lengend Snippet: Figure 1. Endogenous HMGB1 released by damaged primary rat ATII cells increases alveolar epithelial wound closure. (A) HMGB1 was elevated in cell supernatant from rat ATII monolayers that underwent scratch wounds (MS Cell Sup) compared to cell supernatant from rat ATII monolayers that did not undergo scratch wounds (condition media). (B) MS Cell Sup increases the rate of wound closure of primary rat ATII cell monolayers compared to cell supernatant from rat ATII monolayers that did not undergo scratch wounds. HMGB1 was depleted from MS Cell Sup by immunoprecipitation using 30 mg/ml of HMGB1 specific Ab (MS Cell Sup IP w/HMGB1 Ab). Controls were MS Cell Sup immunoprecipitated with a control IgG (MS Cell Sup IP w/Cont Ab). (C) HMGB1 is secreted by primary rat ATII cell monolayers after scratch wounds. Multiple scratches (MS) were performed on primary rat ATII cell monolayers. Fresh cell media were added for 6 hours to the monolayers after extensive washes. Cell supernatants were then centrifuged to remove dead cells and cell debris, then analyzed by western blot (40 ml loaded per lanes from a 1 ml MS Cell Sup sample). (D) MS Cell Sup increases the rate of wound closure of a primary rat ATII cell monolayers via RAGE- and TLR4-dependent pathways, but not via a CXCR4-dependent mechanism. MS Cell Sup, and either 30 mg/ml of blocking RAGE or TLR4 antibodies or their isotype control IgG, or 1 mM of AMD3100, a CXCR4 inhibitor, were added to the monolayers after the scratch. Rate of wound closure is expressed as percent of control 16 h after wounding. *p,0.05 from monolayers exposed to control cell media; **p,0.05 from monolayers exposed to MS Cell Sup. For western blot experiments, one representative experiment is shown, three additional experiments gave comparable results; *p,0.05 from monolayers exposed to condition media. doi:10.1371/journal.pone.0063907.g001

Article Snippet: Rat RAGE blocking antibody was obtained from R&D Systems (Minneapolis, MN).

Techniques: Immunoprecipitation, Control, Western Blot, Blocking Assay

Journal: bioRxiv

Article Title: Aerosolized ApoA1 Nanoparticles Synthesized by Microfluidics Cross the Lung Barrier and Modulate Inflammation

doi: 10.1101/2025.07.09.663869

Figure Lengend Snippet: Cellular localization of A1NPs after aerosolization. Immunofluorescence of lung sections from mice 6 hours after A1NP administration. ApoA1 appears in green and cell nuclei are stained with DAPI (blue). (A) AGER (red), specific to type I pneumocytes. (B) SFTPC (orange), marker for type II pneumocytes. (C) EMCN (red), characteristic of pulmonary endothelial cells. Representative illustration of 10 mice with A1NPs-DilC18.

Article Snippet: In parallel, specific antibodies were applied: a mouse anti-AGER rat antibody diluted 1:100 for type I pneumocytes (MAB 1179-500; R&D Systems), a mouse anti-SFTPC rabbit antibody diluted 1:200 for type II pneumocytes (10774-1AP; Proteintech), and a mouse anti-EMCN goat antibody diluted 1:100 for endothelial cells (AF4666-SP; R&D Systems).

Techniques: Immunofluorescence, Staining, Marker

Journal: Nature Communications

Article Title: Human iPSC-based Modeling of Pulmonary Fibrosis Reveals p300/CBP Inhibition Suppresses Alveolar Transitional Cell State

doi: 10.1038/s41467-026-68909-z

Figure Lengend Snippet: a Gene expression of ATCS markers in the micro-patterned culture. Each well was treated with either DMSO or p300/CBP inhibitors (10 μM) from days 11 to 14. Data are presented as mean ± SEM (n = 3 biologically independent experiments). One-way ANOVA followed by Tukey’s multiple comparisons test; ** p < 0.01, *** p < 0.001, **** p < 0.0001. b Dot plots displaying the gene expression of iATCs-specific markers in representative cell populations from the micro-patterned culture, corresponding to those shown in Fig. . c Immunostaining of CD54 (ICAM1), lineage markers for ATCS (KRT19), AT1 cells (HT1-56), AT2 cells (NaPi2b), and nuclei (Hoechst) in micro-patterned cultures. Representative images from three biologically independent experiments with similar results are shown. Scale bar: 100 μm. d, e Flow cytometry analysis assessing the CD54 + cell ratio in the micro-patterned culture. Each well was treated with either DMSO or p300/CBP inhibitors (10 μM) from days 11 to 14. Data are presented as mean ± SEM (n = 3 biologically independent experiments). One-way ANOVA followed by Tukey’s multiple comparisons test; ** p < 0.01. f Schematic outline for sorting CD54 + iATCs from day 14 of the micro-patterned culture. Created in BioRender. Tsutsui, Y. (2026) https://BioRender.com/v51i925 g Gene expression data of ATCS markers in the micro-patterned culture. Data are presented as mean ± SEM ( n = 3 biologically independent experiments). One-way ANOVA followed by Tukey’s multiple comparisons test; ** p < 0.01, *** p < 0.001, **** p < 0.0001. h Schematic outline of the co-culture experiment involving isolated CD54 + iATCs and NHLFs. Created in BioRender. Tsutsui, Y. (2026) https://BioRender.com/nbi6c0b i Gene expression analysis of ATCS markers in isolated CD54 + iATCs. Data are presented as mean ± SEM ( n = 3 biologically independent experiments). One-way ANOVA followed by Tukey’s multiple comparisons test; ** p < 0.01. ns; not significant ( p > 0.05). j Gene expression analysis of fibroblast activation markers in NHLFs cocultured with or without iATCs. Data are presented as mean ± SEM ( n = 3 biologically independent experiments). Unpaired two-tailed Student’s t test: ∗ p < 0.05.

Article Snippet: Primary antibodies used in this study included GFP (1:500, Aves Labs, GFP-1020), SFN (1:200, Abcam, ab77187), act-p300 (1:200, biorbyt, ORB6262), EpCAM (1:200, Santa Cruz Biotechnology, sc-66020), KRT19 (1:200, Merck, MABT913), KRT17 (1:100, Abcam, ab109725), COL1A1 (1:200, Abcam, ab138492), CD54 (1:200, BioLegend, 353102), CD54 (1:200, Atlas, HPA002126), HT1-56 (1:200, Terrace Biotech, TB29AHT1-56), NaPi2b (1:200, kindly provided by Dr. Gerd Ritter (MX35)), AGER (R&D systems, AF1145), H3K27ac (1:200, Cell Signaling technology, 8173), FLAG (1:500, Cell Signaling technology, 14793), alpha smooth muscle Actin (1:100, Abcam ab5694), and Fluorescin (1:1000, Vector Laboratories, FL-1171).

Techniques: Gene Expression, Immunostaining, Flow Cytometry, Co-Culture Assay, Isolation, Activation Assay, Two Tailed Test

Journal: International journal of oncology

Article Title: S100P regulates the collective invasion of pancreatic cancer cells into the lymphatic endothelial monolayer.

doi: 10.3892/ijo.2019.4812

Figure Lengend Snippet: Figure 6. S100P is involved in migration of LECs and CCID formation. (A) S100P mRNA expression in LECs following treatment with IL‑6 for 24 h. (B) LEC migration following treatment with IL‑6 (1 nM) was examined by Transwell migration assay. (C) S100P mRNA levels were significantly reduced following siRNA transfection (left panel). The IL‑6‑enhanced LEC migration was reduced following S100P knockdown (right panel). (D) CCID area fol lowing treatment with IL‑6 (1 nM). (E) LEC migration following treatment with culture supernatant from cancer cells, recombinant human S100P protein (1 nM) and RAGE antagonist peptide (1 µg/ml). (F) CCID area following treatment with recombinant human S100P protein (1nM) and RAGE antagonist peptide (1 µg/ml). (G) Comparison of S100P mRNA expression levels in cancer cells from single‑cell culture (normal plates) and from spheroid culture (low‑attachment plates) in two cell lines, BxPC3 and MIAPaCa2. *P<0.05 and ***P<0.001, with comparisons indicated by brackets. S100P, S100 calcium binding protein P; LECs, lymphatic endothelial cells; CCID, circular chemorepellent‑induced defect; IL, interleukin; si, small interfering; RAGE, receptor for advanced glycation end‑products; ctrl, control.

Article Snippet: To assess the effect of S100P on the migration of LECs, recombinant human S100P protein (Abcam), the receptor for advanced glycation end-products (RAGE) antagonist peptide (Tocris Bioscience, Bristol, UK), or recombinant human IL-6 protein (PeproTech, Inc., Rocky Hill, NJ, USA) was added to the lower chambers in 750 μl of EGM2MV medium.

Techniques: Migration, Expressing, Transwell Migration Assay, Transfection, Knockdown, Recombinant, Comparison, Binding Assay, Control