integrin α v β 3  (R&D Systems)

Journal: Cells

Article Title: MFG-E8-Derived Oligopeptide MOP3 Facilitates Anti-Inflammatory M2-like Macrophage Polarization in Gut Ischemia/Reperfusion

doi: 10.3390/cells15070606

Figure Lengend Snippet: MOP3 increases M2 activity and decreases M1 activity in an α v β 3 -dependent manner. Peritoneal macrophages from adult mice were treated with PBS or eCIRP (1 µg/mL) and MOP3 (10 µg/mL). Groups treated with eCIRP and MOP3 were pretreated with either IgG or α v β 3 antibody. Supernatant was collected at 24 h and measured for ( A ) IL-10 and ( B ) TNFα by ELISA. Data are expressed as mean ± SEM. Results were tested for normality by Shapiro–Wilk test and QQ plots. Results were evaluated by ANOVA and Tukey’s multiple-comparisons test (* p < 0.05 vs. PBS, # p < 0.05 vs. IgG).

Article Snippet: For cytokine detection experiments, separate groups of eCIRP and MOP3-treated cells were pretreated with IgG (10 μg/mL; bs-0295p; Bioss, Woburn, MA, USA) or α v β 3 polyclonal ab (10 μg/mL; cat. bs-1310r; Bioss).

Techniques: Activity Assay, Enzyme-linked Immunosorbent Assay

Journal: Cells

Article Title: MFG-E8-Derived Oligopeptide MOP3 Facilitates Anti-Inflammatory M2-like Macrophage Polarization in Gut Ischemia/Reperfusion

doi: 10.3390/cells15070606

Figure Lengend Snippet: MOP3 clearance of eCIRP promotes M2 polarization of macrophages in mesenteric ischemia/reperfusion injury. MOP3 facilitates phagocytosis of eCIRP by macrophages via α v β 3 integrin, which leads to an increase in polarization toward M2 relative to M1. This phenomenon is demonstrated in mesenteric ischemia/reperfusion, improving healing while decreasing inflammation.

Article Snippet: For cytokine detection experiments, separate groups of eCIRP and MOP3-treated cells were pretreated with IgG (10 μg/mL; bs-0295p; Bioss, Woburn, MA, USA) or α v β 3 polyclonal ab (10 μg/mL; cat. bs-1310r; Bioss).

Techniques:

Journal: Frontiers in Cell and Developmental Biology

Article Title: Persistent Wnt/β-catenin signaling disables soft palatogenesis and palatal osteogenesis by inducing mesenchymal condensation

doi: 10.3389/fcell.2026.1740081

Figure Lengend Snippet: Canonical Wnt signaling distribution, cell proliferation, adhesion, and arrangement in Osr2-cre KI ;Ctnnb1 ex3f palatal shelves. (A–F) Immunofluorescence staining of Lef1 and Ki67 in E13.5 WT palatal shelves (A–C) and E13.5 Osr2-cre KI ;Ctnnb1 ex3f mice (D–F) . (G) Ki67 positive percentages reduced from 88.64% ± 4.04% and 69.38% ± 4.51% in WT to 78.67 ± 3.59 ( p < 0.0001) and 59.26 ± 10.66 ( p < 0.05) in the Osr2-cre KI ;Ctnnb1 ex3f palatal epithelium and mesenchyme, respectively. (H–M) Immunofluorescence staining of integrin ɑv and ColII in E13.5 WT palatal shelves (H–J) and E13.5 Osr2-cre KI ;Ctnnb1 ex3f mice (K–M) . (N) The percentage of integrin ɑv-positive areas increased from 8.30% ± 6.48% in WT to 40.64% ± 22.50% ( p < 0.05) in Osr2-cre KI ;Ctnnb1 ex3f palatal shelves. (O–T) Immunofluorescence of phalloidin showed the cytoskeletal orientation in the E13.5 WT palate shelves (O–Q) and the E13.5 Osr2-cre KI ;Ctnnb1 ex3f palate shelves (R–T) . (Asterisks in (R–T) represent the centers of the convoluted mesenchymal loops; red short lines in (O–T) delineated the longitudinal axes of mesenchymal cells; *, p < 0.05; ****, p < 0.0001; scale bars: 100 μm).

Article Snippet: The primary antibodies against Lef1 (ab137827, Abcam, Cambridge, MA, United States), integrin ɑv (bs-1310R, Bioss Antibodies Inc., Beijing, China), ColII (K0921, Santa Cruz), Foxf1 (ab308633, Abcam), Dlx5 (10592-1-AP, Proteintech Group Inc., Wuhan, China), Runx2 (sc-101145, Santa Cruz Biotechnology Co., Ltd., Shanghai, China), Sox9 (ab185966, Abcam), Osterix (ab209484, Abcam), phospho-Smad1/5/8 (13820S, Cell Signaling Technology, Danvers, MA, United States), ɑ-SMA (ab7817, Abcam), ColI ( P28372 -BIF, Abmart, Shanghai, China), p-ERK1/2 (4370T, Cell Signaling Technology), Etv4 (10684-1-AP, Cloud-Clone Corp., Wuhan, China), Tbx15 (YN1399, Immunoway, Thermo Fisher Scientific, Shanghai, China), and Scx (ab307722, Abcam) were applied for immunofluorescence.

Techniques: Immunofluorescence, Staining

Journal: eBioMedicine

Article Title: Parvimonas micra exacerbates periodontitis by infiltrating host cells through TmpC and circumventing lysosomal elimination via AppA

doi: 10.1016/j.ebiom.2026.106187

Figure Lengend Snippet: P. micra interacts with PDLSCs through TmpC-integrin α v β 3 axis. ( A ) Schematic representation of His pull-down. ( B ) Co-IP assay showing the interaction between purified His-TmpC and integrin α v β 3 of PDLSCs. ( C ) Sensorgrams of integrin α v β 3 binding to immobilised TmpC and K D value. ( D ) The interaction between TmpC (blue), integrin α v (green) and integrin β 3 (red), as predicted by molecular docking. ( E–F ) Bacterial attachment assay revealing altered bacterial recovery rate in PDLSCs treated with siIntegrin α v+ β 3 ( E ) or Cyclo ( F ). ( G–H ) Flow cytometry showing the percentages of invaded PDLSCs treated with siIntegrin α v+ β 3 ( G ) or Cyclo ( H ). ( I ) Knockdown of integrin α v β 3 altered downstream pFAK and the activation of NF-κB and ERK1/2 signalling pathways triggered by P. micra . β-actin was set as control. ( J ) Western blot showing altered activation of NF-κB and ERK1/2 signalling pathways triggered by P. micra in PDLSCs pretreated with Cyclo. β-actin was set as control. ( K ) Representative image and quantification of ALP staining in Cyclo-pretreated PDLSCs infected with P. micra WT or P. micra ΔtmpC . ( L ) Representative image and quantification of ARS staining of PDLSCs with blocked TmpC-integrin α v β 3 interaction. ( M ) Western blot of Col1, ALPL, Runx2 in Cyclo-pretreated PDLSCs infected with P. micra WT or P. micra ΔtmpC . GAPDH was set as control. ( N ) Flow cytometric analysis of FDAA-labelled P. micra internalisation in Cyclo-pretreated PDLSCs. ( O ) Schematic diagram showing the experimental design and timeline of rat models infected with P. micra and/or treated with Cyclo. ( P ) Quantitative analyses of CEJ-ABC, BV/TV, BMD and Tb.Sp. of the alveolar bone. Data are represented as the mean ± SD of three independent experiments ( n = 3) in (E–N) and six independent experiments ( n = 6) in (P). P values were determined by two-tailed unpaired Student's t -test in (E–H) and one-way ANOVA test in (I–N, P). ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001; ns, not significant.

Article Snippet: Commercially available integrin α v β 3 (R&D Systems, 3050-AV-050) was diluted in sodium acetate (pH 5.0) and passed over the sensor chip in various concentrations from 0 μM to 160 μM, with the 5 μM concentration as internal control.

Techniques: Co-Immunoprecipitation Assay, Purification, Binding Assay, Flow Cytometry, Knockdown, Activation Assay, Control, Western Blot, Staining, Infection, Two Tailed Test