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R&D Systems integrin α v β 3

P. micra interacts with PDLSCs through TmpC-integrin α v <t>β</t> <t>3</t> 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.

Integrin α V β 3, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+integrin+%CE%B1+v+%CE%B2+3/Recombinant+Human+Integrin+alpha+V+beta+3+Protein%2C+CF/pmc13080454-141-2-7
Average 94 stars, based on 45 article reviews

integrin α v β 3 - by Bioz Stars, 2026-09

94/100 stars

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1) Product Images from "Parvimonas micra exacerbates periodontitis by infiltrating host cells through TmpC and circumventing lysosomal elimination via AppA"

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

Journal: eBioMedicine

doi: 10.1016/j.ebiom.2026.106187

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.

Figure Legend 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.

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

other:

Article Title: Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage
Article Snippet: hAS0326 was selected as the best MFAP4 binder in this series using Biacore T200 and the resulting light-chain and heavy-chain constructs were cloned into the mammalian expression vectors pcDNA3.1 plus.

Purification:

Article Title: Integrin binding by B orrelia burgdorferi P 66 facilitates dissemination but is not required for infectivity
Article Snippet: .. Purified recombinant mouse and human integrin α v β 3 (carrier free) were purchased from R&D Systems. ..

Recombinant:

Article Title: Pathogenic Old World Hantaviruses Infect Renal Glomerular and Tubular Cells and Induce Disassembling of Cell-to-Cell Contacts
Article Snippet: Integrin was detected with mouse anti-integrin α V β 3 (clone LM609; Millipore). .. To confirm the specificity of anti-integrin α V β 3 antibody LM609, fixed cells were incubated with anti-integrin α V β 3 antibody that was pretreated with recombinant human integrin α V β 3 (R&D Systems, Wiesbaden-Nordenstadt, Germany). ..

Incubation:

Image Search Results

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

Schematic of the parallel plate flow chamber and specific experiment. (A) The flow chamber was assembled by a lexan, a gasket (length × width × thick = 2 × 0.5 × 0.0254 cm 3 ) and 35 mm dish. There were three channels on the Lexan, including inlet, outlet, and vacuum. (B) The distance-time curve tracked by Image Plus Pro (IPP) software. Lifetime was calculated according to the upper graph from t 1 to t 2 (C) Adhesion rate of fibronectin (FN)/truncated fibronectin 1.3 (FN1.3) functionalized microspheres on phosphate-buffered saline (PBS) adn bovine serum albumin (BSA)-blocked, and integrin α v β 3 -immobiled substrates. Data represent the mean ± SD of three experiments. The significance of the difference is shown by p -value, with ns. for p > 0.05, and ** for p < 0.005. (D, E) Instantaneous velocity and cumulative distance of one tethering event. (F, G) Instantaneous velocity and cumulative distance of one rolling event.

Journal: Frontiers in Cell and Developmental Biology

Article Title: Interaction of integrin α v β 3 and fibronectin under fluid shear forces: implications for tumor cell adhesion and migration

doi: 10.3389/fcell.2025.1512672

Figure Lengend Snippet: Schematic of the parallel plate flow chamber and specific experiment. (A) The flow chamber was assembled by a lexan, a gasket (length × width × thick = 2 × 0.5 × 0.0254 cm 3 ) and 35 mm dish. There were three channels on the Lexan, including inlet, outlet, and vacuum. (B) The distance-time curve tracked by Image Plus Pro (IPP) software. Lifetime was calculated according to the upper graph from t 1 to t 2 (C) Adhesion rate of fibronectin (FN)/truncated fibronectin 1.3 (FN1.3) functionalized microspheres on phosphate-buffered saline (PBS) adn bovine serum albumin (BSA)-blocked, and integrin α v β 3 -immobiled substrates. Data represent the mean ± SD of three experiments. The significance of the difference is shown by p -value, with ns. for p > 0.05, and ** for p < 0.005. (D, E) Instantaneous velocity and cumulative distance of one tethering event. (F, G) Instantaneous velocity and cumulative distance of one rolling event.

Article Snippet: The integrin heterodimer α v β 3 , obtained from R&D Systems (Minneapolis, MN, United States; Catalog #3050-AV-050), consists of an α v extracellular subunit (110.5 kDa) and a β 3 extracellular subunit (80.8 kDa) linked by covalent bonding of disulfide bonds.

Techniques: Software, Saline

Measurement of transient tether lifetime and dissociation rate constant, k off . Lifetimes of transient tethers of fibronectin (FN) and truncated fibronectin (FN1.3)-bearing beads (A, E) on a surface with low-density integrin α v β 3 were plotted against wall shear stress. The dissociation rate constant, k off (B, F) , derived from negative slope by linear fitting the tether lifetime plot of ln (number of events with a lifetime ≥ t) vs. t for low shear stress 0.1–0.3 dyn/cm 2 (C, G) and high shear stress 0.3–0.7 dyn/cm 2 (D, H) . Data represent the mean ± SD of three experiments.

Journal: Frontiers in Cell and Developmental Biology

Article Title: Interaction of integrin α v β 3 and fibronectin under fluid shear forces: implications for tumor cell adhesion and migration

doi: 10.3389/fcell.2025.1512672

Figure Lengend Snippet: Measurement of transient tether lifetime and dissociation rate constant, k off . Lifetimes of transient tethers of fibronectin (FN) and truncated fibronectin (FN1.3)-bearing beads (A, E) on a surface with low-density integrin α v β 3 were plotted against wall shear stress. The dissociation rate constant, k off (B, F) , derived from negative slope by linear fitting the tether lifetime plot of ln (number of events with a lifetime ≥ t) vs. t for low shear stress 0.1–0.3 dyn/cm 2 (C, G) and high shear stress 0.3–0.7 dyn/cm 2 (D, H) . Data represent the mean ± SD of three experiments.

Techniques: Shear, Derivative Assay

Rolling velocity and reduced percent of rolling velocity of beads by interaction of integrin α v β 3 with fibronectin (FN) or truncated fibronectin (FN1.3). (A, B) Velocity of FN-coated beads (blue square) and FN1.3-coated beads (red square) rolling on integrin α v β 3 - immobilized bottom. (C, D) The reduced percent of rolling velocity of FN-coated beads (red diamond) and FN1.3-coated beads (blue diamond). The data were recorded at 100 frames per second, and the mean ± SD of three independent experiments was presented.

Journal: Frontiers in Cell and Developmental Biology

Article Title: Interaction of integrin α v β 3 and fibronectin under fluid shear forces: implications for tumor cell adhesion and migration

doi: 10.3389/fcell.2025.1512672

Figure Lengend Snippet: Rolling velocity and reduced percent of rolling velocity of beads by interaction of integrin α v β 3 with fibronectin (FN) or truncated fibronectin (FN1.3). (A, B) Velocity of FN-coated beads (blue square) and FN1.3-coated beads (red square) rolling on integrin α v β 3 - immobilized bottom. (C, D) The reduced percent of rolling velocity of FN-coated beads (red diamond) and FN1.3-coated beads (blue diamond). The data were recorded at 100 frames per second, and the mean ± SD of three independent experiments was presented.

Techniques:

The instantaneous rolling velocity of beads by interaction of integrin α v β 3 -fibronectin (FN)/truncated fibronectin (FN1.3). (A) Shown are instantaneous velocities of five representative free flowing microspheres under various shear stress of 0.1 (black line), 0.2 (red line), 0.3 (green line), 0.5 (dark blue line) and 0.7 dyn/cm 2 (wathet line). (B-F, H-L) Representative instantaneous velocities of FN (B–F) /FN1.3 (H–L) bearing microspheres of 3 μm radius flowing over and being arrested on a surface coated with integrin α v β 3 (200 ng/mL) at wall shear stress below, equal and above the shear optimum (0.1, 0.2, 0.3, 0.5 and 0.7 dyn/cm 2 ). The data were recorded at 100 fps. The instantaneous velocities were set as zero when their values were below 50 μm/s when the shear stress stronger than 0.2 dyn/cm 2 , while instantaneous velocities were set as zero when their values were 15 and 25 μm/s at 0.1 dyn/cm 2 and 0.2 dyn/cm 2 , respectively. (G) Free flowing beads (pentagon) were referred to the sliding beads on the same focal plane, which has not any interaction with other molecular. The R value of the fitted curve is 0.9946.

Journal: Frontiers in Cell and Developmental Biology

Article Title: Interaction of integrin α v β 3 and fibronectin under fluid shear forces: implications for tumor cell adhesion and migration

doi: 10.3389/fcell.2025.1512672

Figure Lengend Snippet: The instantaneous rolling velocity of beads by interaction of integrin α v β 3 -fibronectin (FN)/truncated fibronectin (FN1.3). (A) Shown are instantaneous velocities of five representative free flowing microspheres under various shear stress of 0.1 (black line), 0.2 (red line), 0.3 (green line), 0.5 (dark blue line) and 0.7 dyn/cm 2 (wathet line). (B-F, H-L) Representative instantaneous velocities of FN (B–F) /FN1.3 (H–L) bearing microspheres of 3 μm radius flowing over and being arrested on a surface coated with integrin α v β 3 (200 ng/mL) at wall shear stress below, equal and above the shear optimum (0.1, 0.2, 0.3, 0.5 and 0.7 dyn/cm 2 ). The data were recorded at 100 fps. The instantaneous velocities were set as zero when their values were below 50 μm/s when the shear stress stronger than 0.2 dyn/cm 2 , while instantaneous velocities were set as zero when their values were 15 and 25 μm/s at 0.1 dyn/cm 2 and 0.2 dyn/cm 2 , respectively. (G) Free flowing beads (pentagon) were referred to the sliding beads on the same focal plane, which has not any interaction with other molecular. The R value of the fitted curve is 0.9946.

Techniques: Shear

Rolling stop time and stop frequency of beads by interaction of integrin α v β 3 with fibronectin (FN) or truncated fibronectin (FN1.3). (A, B) Mean stop times and (C, D) stop frequencies for FN/FN1.3-bearing microspheres rolling on substrate coated with integrin α v β 3 (200 ng/mL) were plotted against wall shear stress. The data were recorded at 100 fps, and the mean ± SD of three independent experiments is presented.

Journal: Frontiers in Cell and Developmental Biology

Article Title: Interaction of integrin α v β 3 and fibronectin under fluid shear forces: implications for tumor cell adhesion and migration

doi: 10.3389/fcell.2025.1512672

Figure Lengend Snippet: Rolling stop time and stop frequency of beads by interaction of integrin α v β 3 with fibronectin (FN) or truncated fibronectin (FN1.3). (A, B) Mean stop times and (C, D) stop frequencies for FN/FN1.3-bearing microspheres rolling on substrate coated with integrin α v β 3 (200 ng/mL) were plotted against wall shear stress. The data were recorded at 100 fps, and the mean ± SD of three independent experiments is presented.

Techniques: Shear

MFAP4 binding and activation of RGD-dependent integrins (A) MFAP4 promotes adhesion of human pulmonary microvascular endothelial cells (HPMECs) in a dose-dependent manner. (B) MFAP4-mediated adhesion of HPMEC can be inhibited by RGD-containing peptide (GRGDS) but not control (SDGRG) peptide. Data are means (SD) of n = 3 independent experiments. Significance is calculated by two-way ANOVA. MFI, mean fluorescence intensity. Immobilized recombinant MFAP4 (2 μg/mL) was incubated with increasing concentrations of recombinant integrins. Integrin binding to recombinant MFAP4 was detected for (C) integrins α V β 3/5/6 and αIIbβ 3 but not (D) integrins α V β 1/8 and α 4/5/8 β 1 . Used detection antibodies are shown in brackets. Data are shown as means (SD) of n = 3 independent experiments. Relative band density of (E) phosphorylated FAK (pFAK)/total FAK and (F) pERK/total ERK in HPMEC after cellular adhesion to poly-D-lysine (PDL, negative control), vitronectin (VTN, positive control), or MFAP4 are shown in representative western blots and quantitated mean (SD) of n = 3 independent experiments. Quantifications of western blotting was analyzed by two-way ANOVA for MFAP4 relative to negative control and the significance is provided for treatment factor only (independent of the significant time factor).

Journal: Molecular Therapy

Article Title: Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage

doi: 10.1016/j.ymthe.2025.01.038

Figure Lengend Snippet: MFAP4 binding and activation of RGD-dependent integrins (A) MFAP4 promotes adhesion of human pulmonary microvascular endothelial cells (HPMECs) in a dose-dependent manner. (B) MFAP4-mediated adhesion of HPMEC can be inhibited by RGD-containing peptide (GRGDS) but not control (SDGRG) peptide. Data are means (SD) of n = 3 independent experiments. Significance is calculated by two-way ANOVA. MFI, mean fluorescence intensity. Immobilized recombinant MFAP4 (2 μg/mL) was incubated with increasing concentrations of recombinant integrins. Integrin binding to recombinant MFAP4 was detected for (C) integrins α V β 3/5/6 and αIIbβ 3 but not (D) integrins α V β 1/8 and α 4/5/8 β 1 . Used detection antibodies are shown in brackets. Data are shown as means (SD) of n = 3 independent experiments. Relative band density of (E) phosphorylated FAK (pFAK)/total FAK and (F) pERK/total ERK in HPMEC after cellular adhesion to poly-D-lysine (PDL, negative control), vitronectin (VTN, positive control), or MFAP4 are shown in representative western blots and quantitated mean (SD) of n = 3 independent experiments. Quantifications of western blotting was analyzed by two-way ANOVA for MFAP4 relative to negative control and the significance is provided for treatment factor only (independent of the significant time factor).

Article Snippet: 96-well MaxiSorp plates (Nunc) were coated overnight at 4°C with recombinant human integrin α v β 3 (R&D Systems) in PBS, washed with binding buffer (TBS/Tw), and incubated for 1 h with 1.5 nM recombinant human MFAP4 and co-incubated with hAS0326 Fab fragments in 2-fold dilutions from 150 nM.

Techniques: Binding Assay, Activation Assay, Control, Fluorescence, Recombinant, Incubation, Negative Control, Positive Control, Western Blot

The AS0326 antibody blocks MFAP4s interaction with endothelial integrins (A) HPMECs were subjected to MFAP4-mediated adhesion, and inhibition of adhesion was tested with integrin α V β 3 - or integrin α V β 5 -blocking antibodies. (B) mAS0326 antibody (mAS) blocks HPMEC adhesion to MFAP4. MFI is of fluorescently labeled cells. IC, isotype control. Significance is calculated relative to the MFAP4-treated positive control in (A) and (B). Flow cytometry staining of (C) integrin α V β 3 and (D) integrin α V β 5 in HPMEC compared to IC. Representative histograms of n = 3 independent experiments are shown. Human primary retinal endothelial cells (RECs) were seeded on immobilized albumin or MFAP4. RECs were stimulated with VEGF and 24-h proliferation was assessed. (E) REC proliferation was co-treated with integrin α V β 3 - or α V β 5 -blocking antibodies or hAS0326 (hAS). REC migration for 3.5 h on MFAP4-coated surface was assessed by Transwell assay using VEGF as chemoattractant. (F) MFAP4-dependent migration was treated with integrin α V β 3 - or α V β 5 -blocking antibodies or hAS0326. Data are shown as individual datapoints with mean (SD) of n = 3 independent experiments. Data are normalized to albumin control. Significance is calculated relative to the hAS0326 treatment group for (E) and (F). Significance calculations are performed using one-way ANOVA followed by Dunnett’s multiple comparison test. Representative images of REC’s (purple) migrated through the pores of the Transwell assay inserts when migration on (G) albumin-coated insert or (H) MFAP4-coated insert. Bar, 100 μm. All antibodies were provided in 10 μg/mL doses for (A), (B), (E), and (F).

Journal: Molecular Therapy

Article Title: Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage

doi: 10.1016/j.ymthe.2025.01.038

Figure Lengend Snippet: The AS0326 antibody blocks MFAP4s interaction with endothelial integrins (A) HPMECs were subjected to MFAP4-mediated adhesion, and inhibition of adhesion was tested with integrin α V β 3 - or integrin α V β 5 -blocking antibodies. (B) mAS0326 antibody (mAS) blocks HPMEC adhesion to MFAP4. MFI is of fluorescently labeled cells. IC, isotype control. Significance is calculated relative to the MFAP4-treated positive control in (A) and (B). Flow cytometry staining of (C) integrin α V β 3 and (D) integrin α V β 5 in HPMEC compared to IC. Representative histograms of n = 3 independent experiments are shown. Human primary retinal endothelial cells (RECs) were seeded on immobilized albumin or MFAP4. RECs were stimulated with VEGF and 24-h proliferation was assessed. (E) REC proliferation was co-treated with integrin α V β 3 - or α V β 5 -blocking antibodies or hAS0326 (hAS). REC migration for 3.5 h on MFAP4-coated surface was assessed by Transwell assay using VEGF as chemoattractant. (F) MFAP4-dependent migration was treated with integrin α V β 3 - or α V β 5 -blocking antibodies or hAS0326. Data are shown as individual datapoints with mean (SD) of n = 3 independent experiments. Data are normalized to albumin control. Significance is calculated relative to the hAS0326 treatment group for (E) and (F). Significance calculations are performed using one-way ANOVA followed by Dunnett’s multiple comparison test. Representative images of REC’s (purple) migrated through the pores of the Transwell assay inserts when migration on (G) albumin-coated insert or (H) MFAP4-coated insert. Bar, 100 μm. All antibodies were provided in 10 μg/mL doses for (A), (B), (E), and (F).

Techniques: Inhibition, Blocking Assay, Labeling, Control, Positive Control, Flow Cytometry, Staining, Migration, Transwell Assay, Comparison

Specificity of the AS0326 antibody (A) mAS0326 and (B) hAS0326 efficiently detect MFAP4 in WT ( Mfap4 +/+ ) mouse serum, but not in MFAP4-deficient ( Mfap4 −/− ) mouse serum. (C) Increasing concentrations of hAS0326-Fab or hAS0326Y94A L-CDR3 Fab variant were applied for inhibition of 1.5 nM MFAP4 binding to an excess of immobilized integrin α V β 3 . (D–F) Brown symbols, HG-HYB7-5; purple symbols, mAS0326; red symbols; hAS0326. (D) Both mAS0326 and hAS0326 efficiently detect immobilized recombinant human MFAP4 (rhMFAP4 coating) variant carrying RGD-AAA mutation (RGD-AAA), while HG-HYB7-5 antibody show RGD-dependent binding. Both mAS0326 and hAS0326 efficiently detect immobilized (E) recombinant mouse (rm) MFAP4, and (F) rhMFAP4, while HG-HYB7-5 is rhMFAP4 specific. Data are shown as means (SD) of n = 3 independent experiments.

Journal: Molecular Therapy

Article Title: Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage

doi: 10.1016/j.ymthe.2025.01.038

Figure Lengend Snippet: Specificity of the AS0326 antibody (A) mAS0326 and (B) hAS0326 efficiently detect MFAP4 in WT ( Mfap4 +/+ ) mouse serum, but not in MFAP4-deficient ( Mfap4 −/− ) mouse serum. (C) Increasing concentrations of hAS0326-Fab or hAS0326Y94A L-CDR3 Fab variant were applied for inhibition of 1.5 nM MFAP4 binding to an excess of immobilized integrin α V β 3 . (D–F) Brown symbols, HG-HYB7-5; purple symbols, mAS0326; red symbols; hAS0326. (D) Both mAS0326 and hAS0326 efficiently detect immobilized recombinant human MFAP4 (rhMFAP4 coating) variant carrying RGD-AAA mutation (RGD-AAA), while HG-HYB7-5 antibody show RGD-dependent binding. Both mAS0326 and hAS0326 efficiently detect immobilized (E) recombinant mouse (rm) MFAP4, and (F) rhMFAP4, while HG-HYB7-5 is rhMFAP4 specific. Data are shown as means (SD) of n = 3 independent experiments.

Techniques: Variant Assay, Inhibition, Binding Assay, Recombinant, Mutagenesis

Structural basis for the hAS0326 Fab interaction with MFAP4 The hAS0326 Fab complex and the MFAP4 octamer. (A) Cartoon representation of the octameric MFAP4-Fab complex. (B) Each Fab contacts a single MFAP4 monomer at an epitope next to the MFAP4 N terminus but far from the binding site for the Ca 2+ ion (cyan sphere). (C) The MFAP4 octamer is built from two FIBCD1-like tetramers (colored orange and red) with eight Ca 2+ ions located at the tetramer-tetramer interface. (D) Inside view showing the concave face of the tetramer. (E) Top view of the convex face of the tetramer with the four bound Fab molecules. Orange spheres mark the first MFAP4 residue that can be located. Presumably, the disordered RGD integrin-binding motif at the N terminus of MFAP4 is trapped and inaccessible inside the funnel-shaped space formed by the Fab molecules. Nt, N terminus. (F) The epitope mapped on MFAP4. Residues primarily in contact with heavy-chain and light-chain CDRs are colored blue and green, respectively. (G) Details of the intermolecular interaction centered on MFAP4 residues 24–29. Putative polar interactions are indicated by dotted lines.

Journal: Molecular Therapy

Article Title: Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage

doi: 10.1016/j.ymthe.2025.01.038

Figure Lengend Snippet: Structural basis for the hAS0326 Fab interaction with MFAP4 The hAS0326 Fab complex and the MFAP4 octamer. (A) Cartoon representation of the octameric MFAP4-Fab complex. (B) Each Fab contacts a single MFAP4 monomer at an epitope next to the MFAP4 N terminus but far from the binding site for the Ca 2+ ion (cyan sphere). (C) The MFAP4 octamer is built from two FIBCD1-like tetramers (colored orange and red) with eight Ca 2+ ions located at the tetramer-tetramer interface. (D) Inside view showing the concave face of the tetramer. (E) Top view of the convex face of the tetramer with the four bound Fab molecules. Orange spheres mark the first MFAP4 residue that can be located. Presumably, the disordered RGD integrin-binding motif at the N terminus of MFAP4 is trapped and inaccessible inside the funnel-shaped space formed by the Fab molecules. Nt, N terminus. (F) The epitope mapped on MFAP4. Residues primarily in contact with heavy-chain and light-chain CDRs are colored blue and green, respectively. (G) Details of the intermolecular interaction centered on MFAP4 residues 24–29. Putative polar interactions are indicated by dotted lines.

Techniques: Binding Assay, Residue

The macular proteome of the DL-AAA-induced model of chronic retinopathy supports integrin involvement Macular punches including choroid, RPE, and retina obtained at end-study (week 22) were analyzed by mass spectrometry and following analysis using clusterProfiler 4.0 package in R. The proteomes were generated from n = 3 eyes for non-diseased control, n = 5 eyes for DL-AAA treatment, and n = 5 eyes for hAS0326 treatment. (A) Over-representation analysis (ORA) showing the effect of DL-AAA treatment (relative to no DL-AAA treatment) and hAS0326 treatment of DL-AAA-treated eyes (relative to DL-AAA treatment), respectively. The plot was generated using compareCluster function with default settings. All ontologies with significant regulation post correction for multiple testing using the Benjamini-Hochberg procedure are shown. Dot sizes indicate the ratio (i.e., the coverage of a given term by proteins regulated for each comparison), and dot colors indicate the level of significance. (B–E) Volcano plots showing regulation of detected proteins underlying selected GO terms. For selected, significantly regulated gene ontologies, the ORA input proteins displaying significant regulation are highlighted in color. Protein IDs are shown for the top three proteins with lowest p belonging to a particular ontology. Moreover, protein IDs are shown for specific proteins of interest.

Journal: Molecular Therapy

Article Title: Pharmacological blocking of microfibrillar-associated protein 4 reduces retinal neoangiogenesis and vascular leakage

doi: 10.1016/j.ymthe.2025.01.038

Figure Lengend Snippet: The macular proteome of the DL-AAA-induced model of chronic retinopathy supports integrin involvement Macular punches including choroid, RPE, and retina obtained at end-study (week 22) were analyzed by mass spectrometry and following analysis using clusterProfiler 4.0 package in R. The proteomes were generated from n = 3 eyes for non-diseased control, n = 5 eyes for DL-AAA treatment, and n = 5 eyes for hAS0326 treatment. (A) Over-representation analysis (ORA) showing the effect of DL-AAA treatment (relative to no DL-AAA treatment) and hAS0326 treatment of DL-AAA-treated eyes (relative to DL-AAA treatment), respectively. The plot was generated using compareCluster function with default settings. All ontologies with significant regulation post correction for multiple testing using the Benjamini-Hochberg procedure are shown. Dot sizes indicate the ratio (i.e., the coverage of a given term by proteins regulated for each comparison), and dot colors indicate the level of significance. (B–E) Volcano plots showing regulation of detected proteins underlying selected GO terms. For selected, significantly regulated gene ontologies, the ORA input proteins displaying significant regulation are highlighted in color. Protein IDs are shown for the top three proteins with lowest p belonging to a particular ontology. Moreover, protein IDs are shown for specific proteins of interest.

Techniques: Mass Spectrometry, Generated, Control, Comparison

(A) Pictural description of the α V β 3 adhesion assay methodology. (B) Fold change observed in crystal violet (CV) absorbance at a wavelength of 590 for wild type (WT), non-toxic (NT) C . novyi as well as the putative RGD-modified candidates (A and B) after exposure to the α V β 3 coated surface of the adhesion assay. * denotes a p value of < 0.05 when compared to any other cohort, including WT, NT, and modification Candidate B. (C) Average CV pixel count of entire integrin coated surface for candidates A and B as well as wild-type (WT) and non-toxic (NT) C . novyi that remain on the α V β 3 coated surface. ‡ denotes a p value of 0.05 when compared to any other cohort, including WT, NT, and modification Candidate B. Error bars represent standard deviation from the cumulative mean of three experimental replications (n = 6 each) for a total n = 18.

Journal: PLOS ONE

Article Title: An intravenous pancreatic cancer therapeutic: Characterization of CRISPR/Cas9n-modified Clostridium novyi -Non Toxic

doi: 10.1371/journal.pone.0289183

Figure Lengend Snippet: (A) Pictural description of the α V β 3 adhesion assay methodology. (B) Fold change observed in crystal violet (CV) absorbance at a wavelength of 590 for wild type (WT), non-toxic (NT) C . novyi as well as the putative RGD-modified candidates (A and B) after exposure to the α V β 3 coated surface of the adhesion assay. * denotes a p value of < 0.05 when compared to any other cohort, including WT, NT, and modification Candidate B. (C) Average CV pixel count of entire integrin coated surface for candidates A and B as well as wild-type (WT) and non-toxic (NT) C . novyi that remain on the α V β 3 coated surface. ‡ denotes a p value of 0.05 when compared to any other cohort, including WT, NT, and modification Candidate B. Error bars represent standard deviation from the cumulative mean of three experimental replications (n = 6 each) for a total n = 18.

Article Snippet: Purified α V β 3 integrin (100μL of 10μg/mL carrier-free, human recombinant protein, R&D Systems Bio-Techne 3050-AV) solution was administered to the center of the corona-treated cover slips.

Techniques: Cell Adhesion Assay, Modification, Standard Deviation

Cytotoxic effect and NO assay of integrin α v β 3 treated with or without IL-1β (10 ng/mL) and treated with integrin α v β 3 (0, 0.5, 1, 2, 5, 10, 25, 50, and 100 ng/mL) on Chon-001 cells at 37 °C for 24 h. ( A ) Protein structure of integrin α v β 3 (RCSB PDB ( https://www.rcsb.org , accessed on 15 June 2023), ID 1JV2). ( B ) Integrin α v β 3 (0, 0.5, 1, 2, 5, 10, 25, 50, and 100 ng/mL) was treated by concentration without IL-1β, and further toxicity of integrin α v β 3 to cell for 24 h was measured. ( C ) Integrin α v β 3 treated with (0, 0.5, 1, 2, 5, 10, 25, 50, and 100 ng/mL) concentrations with IL-1β. ( D ) Effect of integrin α v β 3 on IL-1β-induced NO release from Chon-001 cells. Cell viability when IL-1β and integrin α v β 3 were treated together for 24 h. ### p < 0.001 vs. untreated group; * p < 0.05, ** p < 0.01, *** p < 0.001 vs IL-1β treated group.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Cytotoxic effect and NO assay of integrin α v β 3 treated with or without IL-1β (10 ng/mL) and treated with integrin α v β 3 (0, 0.5, 1, 2, 5, 10, 25, 50, and 100 ng/mL) on Chon-001 cells at 37 °C for 24 h. ( A ) Protein structure of integrin α v β 3 (RCSB PDB ( https://www.rcsb.org , accessed on 15 June 2023), ID 1JV2). ( B ) Integrin α v β 3 (0, 0.5, 1, 2, 5, 10, 25, 50, and 100 ng/mL) was treated by concentration without IL-1β, and further toxicity of integrin α v β 3 to cell for 24 h was measured. ( C ) Integrin α v β 3 treated with (0, 0.5, 1, 2, 5, 10, 25, 50, and 100 ng/mL) concentrations with IL-1β. ( D ) Effect of integrin α v β 3 on IL-1β-induced NO release from Chon-001 cells. Cell viability when IL-1β and integrin α v β 3 were treated together for 24 h. ### p < 0.001 vs. untreated group; * p < 0.05, ** p < 0.01, *** p < 0.001 vs IL-1β treated group.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Concentration Assay

The anti-inflammatory effect with or without integrin α v β 3 in IL-1β-induced Chon-001 cells. The relative density of COX-2 and iNOS expression decreased in a dose-dependent manner. ( A ) The expression of COX2 and iNOS were quantified via Western blot analysis. ( B ) Expression of COX2 with or without IL-1β (10 ng/mL). ( C ) Expression of iNOS with or without IL-1β (10 ng/mL). ( D ) Effect of integrin α v β 3 on IL-1β-induced PGE2 release from Chon-001 cells. Comparison with only IL-1β ** p < 0.01, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01, ### p < 0.001.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: The anti-inflammatory effect with or without integrin α v β 3 in IL-1β-induced Chon-001 cells. The relative density of COX-2 and iNOS expression decreased in a dose-dependent manner. ( A ) The expression of COX2 and iNOS were quantified via Western blot analysis. ( B ) Expression of COX2 with or without IL-1β (10 ng/mL). ( C ) Expression of iNOS with or without IL-1β (10 ng/mL). ( D ) Effect of integrin α v β 3 on IL-1β-induced PGE2 release from Chon-001 cells. Comparison with only IL-1β ** p < 0.01, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01, ### p < 0.001.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Effect of integrin α v β 3 with or without IL-1β-induced MAPKs protein expression in Chon-001 cells. ( A ) The expression of MAPKs was quantified via Western blot analysis. ( B ) Expression of p-ERK affected by integrin α v β 3 . ( C ) Expression of p-JNK affected by integrin α v β 3 . ( D ) Expression of p-p38 affected by integrin α v β 3 . Comparison with only IL-1β * p < 0.05, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01, ### p < 0.001.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Effect of integrin α v β 3 with or without IL-1β-induced MAPKs protein expression in Chon-001 cells. ( A ) The expression of MAPKs was quantified via Western blot analysis. ( B ) Expression of p-ERK affected by integrin α v β 3 . ( C ) Expression of p-JNK affected by integrin α v β 3 . ( D ) Expression of p-p38 affected by integrin α v β 3 . Comparison with only IL-1β * p < 0.05, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01, ### p < 0.001.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Effect of integrin α v β 3 with or without IL-1β-induced protein expression of p-p65 and p-IκBα in Chon-001 cells. Chon-001 cells were treated with integrin α v β 3 (0, 25, and 50 ng/mL) with or without IL-1β (10 ng/mL) at 37 °C 24 h. ( A ) The expression of NF-κB was quantified via Western blot analysis. ( B ) Relative density of p-IκBα for IκBα. ( C ) Relative density of p-P65 for P65. Comparison with only IL-1β ** p < 0.01, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group # p < 0.05.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Effect of integrin α v β 3 with or without IL-1β-induced protein expression of p-p65 and p-IκBα in Chon-001 cells. Chon-001 cells were treated with integrin α v β 3 (0, 25, and 50 ng/mL) with or without IL-1β (10 ng/mL) at 37 °C 24 h. ( A ) The expression of NF-κB was quantified via Western blot analysis. ( B ) Relative density of p-IκBα for IκBα. ( C ) Relative density of p-P65 for P65. Comparison with only IL-1β ** p < 0.01, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group # p < 0.05.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Effect of integrin α v β 3 with or without IL-1β-induced protein expression of p-STAT3 in Chon-001 cells. ( A ) The expression of p-STAT3 was quantified via Western blot analysis. ( B ) Relative density of p-STAT3 for β-actin. Comparison with only IL-1β *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ### p < 0.001.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Effect of integrin α v β 3 with or without IL-1β-induced protein expression of p-STAT3 in Chon-001 cells. ( A ) The expression of p-STAT3 was quantified via Western blot analysis. ( B ) Relative density of p-STAT3 for β-actin. Comparison with only IL-1β *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ### p < 0.001.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Effect of integrin α v β 3 with or without IL-1β-induced protein expression of ALP and RUNX2 in Chon-001 cells. ( A ) The expression of ALP and RUNX2 were quantified via Western blot analysis. ( B ) Relative density of ALP for β-actin. ( C ) Relative density of RUNX2 for β-actin. Comparison with only IL-1β *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ### p < 0.001.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Effect of integrin α v β 3 with or without IL-1β-induced protein expression of ALP and RUNX2 in Chon-001 cells. ( A ) The expression of ALP and RUNX2 were quantified via Western blot analysis. ( B ) Relative density of ALP for β-actin. ( C ) Relative density of RUNX2 for β-actin. Comparison with only IL-1β *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ### p < 0.001.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Effect of integrin α v β 3 with or without IL-1β-induced protein expression of BMP2 and BMP4 in Chon-001 cells. ( A ) The expression of BMP2, BMP4, SOX9, COL1A1, COL2A1, and Aggrecan were quantified via Western blot analysis. ( B ) Relative density of BMP2 for β-actin. ( C ) Relative density of BMP4 for β-actin. ( D ) Relative density of SOX9 for β-actin. ( E ) Relative density of Aggrecan for β-actin. ( F ) Relative density of COL1A1 for β-actin. ( G ) Relative density of COL2A1 for β-actin. Comparison with only IL-1β * p < 0.05, ** p < 0.01, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01, ### p < 0.001.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Effect of integrin α v β 3 with or without IL-1β-induced protein expression of BMP2 and BMP4 in Chon-001 cells. ( A ) The expression of BMP2, BMP4, SOX9, COL1A1, COL2A1, and Aggrecan were quantified via Western blot analysis. ( B ) Relative density of BMP2 for β-actin. ( C ) Relative density of BMP4 for β-actin. ( D ) Relative density of SOX9 for β-actin. ( E ) Relative density of Aggrecan for β-actin. ( F ) Relative density of COL1A1 for β-actin. ( G ) Relative density of COL2A1 for β-actin. Comparison with only IL-1β * p < 0.05, ** p < 0.01, *** p < 0.001. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01, ### p < 0.001.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Effect of integrin α v β 3 with or without IL-1β-induced protein expression of MMP2 and MMP9 in Chon-001 cells. ( A ) The expression of MMP2 and MMP9 was quantified via Western blot. ( B ) A significant decrease in MMP2 from 25 and 50 ng/mL. ( C ) In MMP9, there was a similar protein expression level. Comparison with only IL-1β * p < 0.05, ** p < 0.01. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01.

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Effect of integrin α v β 3 with or without IL-1β-induced protein expression of MMP2 and MMP9 in Chon-001 cells. ( A ) The expression of MMP2 and MMP9 was quantified via Western blot. ( B ) A significant decrease in MMP2 from 25 and 50 ng/mL. ( C ) In MMP9, there was a similar protein expression level. Comparison with only IL-1β * p < 0.05, ** p < 0.01. Comparison with integrin α v β 3 and IL-1β-treated group ## p < 0.01.

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques: Expressing, Western Blot, Comparison

Schematic representation of anti-inflammation, osteogenesis, and chondrogenesis by integrin α v β 3 .

Journal: Biomedicines

Article Title: Potential Joint Protective and Anti-Inflammatory Effects of Integrin α v β 3 in IL-1β-Treated Chondrocytes Cells

doi: 10.3390/biomedicines11102745

Figure Lengend Snippet: Schematic representation of anti-inflammation, osteogenesis, and chondrogenesis by integrin α v β 3 .

Article Snippet: Integrin α v β 3 was purchased from biotechne (Minneapolis, MN, USA)—Cat. no. 3050-AV-050.

Techniques:

Review

integrin α v β 3 (R&D Systems)

Structured Review

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1) Product Images from "Parvimonas micra exacerbates periodontitis by infiltrating host cells through TmpC and circumventing lysosomal elimination via AppA"

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