Review



rat pro il 1β  (Sino Biological)


Bioz Verified Symbol Sino Biological is a verified supplier
Bioz Manufacturer Symbol Sino Biological manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95

    Structured Review

    Sino Biological rat pro il 1β
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Rat Pro Il 1β, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pmc12909850-531-34-41?v=Sino+Biological
    Average 95 stars, based on 5 article reviews
    rat pro il 1β - by Bioz Stars, 2026-08
    95/100 stars

    Images

    1) Product Images from "Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis"

    Article Title: Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis

    Journal: Nature Communications

    doi: 10.1038/s41467-026-68366-8

    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Figure Legend Snippet: A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.

    Techniques Used: Staining, Western Blot, Control, Two Tailed Test, Mutagenesis, Incubation, Negative Control, Activation Assay, Positive Control



    Similar Products

    94
    MedChemExpress pro inflammatory cytokine il 1β
    Significant Ups genes in the acetabular cartilage of the rats with DDH, as determined by mRNA-seq analysis. (A) Neonatal rats were subjected to straight-leg swaddling for 10 days. A total of 4 weeks later, (a) morphology, (b) H&E staining and (c) SO/FG staining were assessed in the hip joints of the rats. (B) Immunohistochemical staining and (E) semi-quantitative analysis of COL2A1 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (C) Relative gene expression levels of <t>COL2A1,</t> <t>IL-1β</t> and IL-6 in the acetabular cartilage of the 4-week-old control rats and rats with DDH, as determined by reverse transcription-quantitative PCR. (D) Levels of IL-6 in the supernatants of acetabular cartilage from the 4-week-old rats with DDH, as determined by ELISA. (F) Significant Ups in the acetabular cartilage of rats with DDH were identified by mRNA-seq analysis with the screening criteria of log 2 FC >4 and P.adj<0.01. Principal component analysis results and a heatmap of these significant Ups are shown. (G) GO enrichment analysis of significant Ups in the acetabular cartilage of the rats with DDH. Data are presented as the mean ± SD. *** P<0.001. (C-E) Representative results of four independent experiments are shown. Ups, upregulated genes; BP, biological process; CC, cellular component; COL2A1, type II collagen; DDH, developmental dysplasia of the hip; FC, fold change; GO, Gene Ontology; H&E, hematoxylin and eosin; IHC, immunohistochemistry; IL, interleukin; IOD, integrated optical density; MF, molecular function; mRNA-seq, mRNA sequencing; SO/FG, Safranin O/Fast Green.
    Pro Inflammatory Cytokine Il 1β, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pmc12948554-82-15-23?v=MedChemExpress
    Average 94 stars, based on 1 article reviews
    pro inflammatory cytokine il 1β - by Bioz Stars, 2026-08
    94/100 stars
      Buy from Supplier

    95
    Sino Biological rat pro il 1β
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Rat Pro Il 1β, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pmc12909850-531-34-41?v=Sino+Biological
    Average 95 stars, based on 1 article reviews
    rat pro il 1β - by Bioz Stars, 2026-08
    95/100 stars
      Buy from Supplier

    96
    R&D Systems pro inflammatory cytokines interleukin 1β
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Pro Inflammatory Cytokines Interleukin 1β, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pmc12229159-104-1-5?v=R%26D+Systems
    Average 96 stars, based on 1 article reviews
    pro inflammatory cytokines interleukin 1β - by Bioz Stars, 2026-08
    96/100 stars
      Buy from Supplier

    96
    Cusabio rat pro il1β
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Rat Pro Il1β, supplied by Cusabio, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pm34659512-68-0-5?v=Cusabio
    Average 96 stars, based on 1 article reviews
    rat pro il1β - by Bioz Stars, 2026-08
    96/100 stars
      Buy from Supplier

    90
    Thermo Fisher apc-efluor 780 rat anti-mouse il-1β (pro-form
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Apc Efluor 780 Rat Anti Mouse Il 1β (Pro Form, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pmc08629239-56-44-51?v=Thermo+Fisher
    Average 90 stars, based on 1 article reviews
    apc-efluor 780 rat anti-mouse il-1β (pro-form - by Bioz Stars, 2026-08
    90/100 stars
      Buy from Supplier

    93
    R&D Systems mouse anti pro il 1β 12 mab5011 antibodies
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Mouse Anti Pro Il 1β 12 Mab5011 Antibodies, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pm32619679-58-4-13?v=R%26D+Systems
    Average 93 stars, based on 1 article reviews
    mouse anti pro il 1β 12 mab5011 antibodies - by Bioz Stars, 2026-08
    93/100 stars
      Buy from Supplier

    90
    Meso Scale Diagnostics LLC v-plex rat pro-inflammatory panel for tnfα and interleukin 1β (il-1β), il-6 and cxcl1
    Osmotic minipumps containing methadone or saline were implanted in pregnant rats on E16. Pups were born and serum collected on P10(A-D) and P21 (E-H). Using a translational multiplex electrochemiluminescent platform, biomarkers were assayed. On P10, those pups exposed to perinatal methadone had significantly increased IL-1β (A), TNFα (B), IL-6 (C) and <t>CXCL1</t> (D) compared to saline pups. By P21, serum levels of IL-1β (E) remained significantly increased compared to methadone pups, while other cytokines and chemokines normalized. These data reflect significant and persistent increases in pro-inflammatory proteins in the serum throughout the perinatal period, consistent with a diverse inflammatory response syndrome. *p<0.05, **p<0.01, ***p<0.001, n=3–4/group.
    V Plex Rat Pro Inflammatory Panel For Tnfα And Interleukin 1β (Il 1β), Il 6 And Cxcl1, supplied by Meso Scale Diagnostics LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rat+pro+il+1%CE%B2/pmc07010550-195-36-41?v=Meso+Scale+Diagnostics+LLC
    Average 90 stars, based on 1 article reviews
    v-plex rat pro-inflammatory panel for tnfα and interleukin 1β (il-1β), il-6 and cxcl1 - by Bioz Stars, 2026-08
    90/100 stars
      Buy from Supplier

    Image Search Results


    Significant Ups genes in the acetabular cartilage of the rats with DDH, as determined by mRNA-seq analysis. (A) Neonatal rats were subjected to straight-leg swaddling for 10 days. A total of 4 weeks later, (a) morphology, (b) H&E staining and (c) SO/FG staining were assessed in the hip joints of the rats. (B) Immunohistochemical staining and (E) semi-quantitative analysis of COL2A1 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (C) Relative gene expression levels of COL2A1, IL-1β and IL-6 in the acetabular cartilage of the 4-week-old control rats and rats with DDH, as determined by reverse transcription-quantitative PCR. (D) Levels of IL-6 in the supernatants of acetabular cartilage from the 4-week-old rats with DDH, as determined by ELISA. (F) Significant Ups in the acetabular cartilage of rats with DDH were identified by mRNA-seq analysis with the screening criteria of log 2 FC >4 and P.adj<0.01. Principal component analysis results and a heatmap of these significant Ups are shown. (G) GO enrichment analysis of significant Ups in the acetabular cartilage of the rats with DDH. Data are presented as the mean ± SD. *** P<0.001. (C-E) Representative results of four independent experiments are shown. Ups, upregulated genes; BP, biological process; CC, cellular component; COL2A1, type II collagen; DDH, developmental dysplasia of the hip; FC, fold change; GO, Gene Ontology; H&E, hematoxylin and eosin; IHC, immunohistochemistry; IL, interleukin; IOD, integrated optical density; MF, molecular function; mRNA-seq, mRNA sequencing; SO/FG, Safranin O/Fast Green.

    Journal: International Journal of Molecular Medicine

    Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

    doi: 10.3892/ijmm.2026.5776

    Figure Lengend Snippet: Significant Ups genes in the acetabular cartilage of the rats with DDH, as determined by mRNA-seq analysis. (A) Neonatal rats were subjected to straight-leg swaddling for 10 days. A total of 4 weeks later, (a) morphology, (b) H&E staining and (c) SO/FG staining were assessed in the hip joints of the rats. (B) Immunohistochemical staining and (E) semi-quantitative analysis of COL2A1 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (C) Relative gene expression levels of COL2A1, IL-1β and IL-6 in the acetabular cartilage of the 4-week-old control rats and rats with DDH, as determined by reverse transcription-quantitative PCR. (D) Levels of IL-6 in the supernatants of acetabular cartilage from the 4-week-old rats with DDH, as determined by ELISA. (F) Significant Ups in the acetabular cartilage of rats with DDH were identified by mRNA-seq analysis with the screening criteria of log 2 FC >4 and P.adj<0.01. Principal component analysis results and a heatmap of these significant Ups are shown. (G) GO enrichment analysis of significant Ups in the acetabular cartilage of the rats with DDH. Data are presented as the mean ± SD. *** P<0.001. (C-E) Representative results of four independent experiments are shown. Ups, upregulated genes; BP, biological process; CC, cellular component; COL2A1, type II collagen; DDH, developmental dysplasia of the hip; FC, fold change; GO, Gene Ontology; H&E, hematoxylin and eosin; IHC, immunohistochemistry; IL, interleukin; IOD, integrated optical density; MF, molecular function; mRNA-seq, mRNA sequencing; SO/FG, Safranin O/Fast Green.

    Article Snippet: To assess the functional integrity of chondrocytes, the P0-P1 primary chondrocytes were treated with the pro-inflammatory cytokine IL-1β (10 ng/ml; cat. no. HY-P7097; MedChemExpress) with or without the HDAC inhibitor trichostatin A (TSA; 300 nM; cat. no. T129665; Shanghai Aladdin Biochemical Technology Co., Ltd.) for 24 h at room temperature ( , ).

    Techniques: Staining, Immunohistochemical staining, Control, Gene Expression, Reverse Transcription, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Immunohistochemistry, Sequencing

    DUSP26 expression is upregulated in IL-1β-induced chondrocytes. (A) Schematic diagram showing the experimental protocol in vitro . Primary chondrocytes isolated from 5-day-old rats were subjected to treatment with 10 ng/ml IL-1β. The protein and mRNA expression levels of DUSP26 in chondrocytes were detected by RT-qPCR and western blotting. (B) Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were detected by RT-qPCR and western blotting. (C) Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were assessed by RT-qPCR and western blotting. Data are presented as the mean ± SD. ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. Ad-EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

    Journal: International Journal of Molecular Medicine

    Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

    doi: 10.3892/ijmm.2026.5776

    Figure Lengend Snippet: DUSP26 expression is upregulated in IL-1β-induced chondrocytes. (A) Schematic diagram showing the experimental protocol in vitro . Primary chondrocytes isolated from 5-day-old rats were subjected to treatment with 10 ng/ml IL-1β. The protein and mRNA expression levels of DUSP26 in chondrocytes were detected by RT-qPCR and western blotting. (B) Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were detected by RT-qPCR and western blotting. (C) Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the protein and mRNA expression levels of DUSP26 in the chondrocytes were assessed by RT-qPCR and western blotting. Data are presented as the mean ± SD. ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. Ad-EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

    Article Snippet: To assess the functional integrity of chondrocytes, the P0-P1 primary chondrocytes were treated with the pro-inflammatory cytokine IL-1β (10 ng/ml; cat. no. HY-P7097; MedChemExpress) with or without the HDAC inhibitor trichostatin A (TSA; 300 nM; cat. no. T129665; Shanghai Aladdin Biochemical Technology Co., Ltd.) for 24 h at room temperature ( , ).

    Techniques: Expressing, In Vitro, Isolation, Quantitative RT-PCR, Western Blot, Over Expression, Construct, Plasmid Preparation, Negative Control, Reverse Transcription, Real-time Polymerase Chain Reaction

    DUSP26 overexpression alleviates IL-1β-induced chondrocyte injury. Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (A) Expression levels of COL2A1 and COL1A1 in the chondrocytes were detected by RT-qPCR and western blotting. (B) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (C) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were determined by ELISA. Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (D) Expression levels of COL2A1 and COL1A1 in the chondrocytes were evaluated by RT-qPCR and western blotting. (E) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (F) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were detected by ELISA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. COL1A1, type I collagen; COL2A1, type II collagen; EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

    Journal: International Journal of Molecular Medicine

    Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

    doi: 10.3892/ijmm.2026.5776

    Figure Lengend Snippet: DUSP26 overexpression alleviates IL-1β-induced chondrocyte injury. Rat DUSP26 overexpression adenovirus was constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (A) Expression levels of COL2A1 and COL1A1 in the chondrocytes were detected by RT-qPCR and western blotting. (B) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (C) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were determined by ELISA. Two adenovirus-mediated shRNAs against rat DUSP26 were constructed and used to infect chondrocytes. After 24 h, the chondrocytes were subjected to 10 ng/ml IL-1β. (D) Expression levels of COL2A1 and COL1A1 in the chondrocytes were evaluated by RT-qPCR and western blotting. (E) Relative mRNA expression levels of TNF-α and IL-6 in the chondrocytes were determined by RT-qPCR. (F) Levels of TNF-α and IL-6 in the supernatants of the chondrocytes were detected by ELISA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. Representative results of three independent experiments are shown. COL1A1, type I collagen; COL2A1, type II collagen; EP, empty adenoviral vector; DUSP26, dual-specificity phosphatase 26; IL, interleukin; NC, negative control; RT-qPCR, reverse transcription-quantitative PCR; sh, short hairpin.

    Article Snippet: To assess the functional integrity of chondrocytes, the P0-P1 primary chondrocytes were treated with the pro-inflammatory cytokine IL-1β (10 ng/ml; cat. no. HY-P7097; MedChemExpress) with or without the HDAC inhibitor trichostatin A (TSA; 300 nM; cat. no. T129665; Shanghai Aladdin Biochemical Technology Co., Ltd.) for 24 h at room temperature ( , ).

    Techniques: Over Expression, Construct, Expressing, Quantitative RT-PCR, Western Blot, Enzyme-linked Immunosorbent Assay, Plasmid Preparation, Negative Control, Reverse Transcription, Real-time Polymerase Chain Reaction

    HDAC1, HDAC2 and HDAC8 are DUSP26-interacting proteins in chondrocytes. (A) IP/MS analysis in DUSP26-overexpressing chondrocytes under IL-1β stimulation. (B) Flow chart of target protein screening. (C) Immunohistochemical staining of HDAC1, HDAC2 and HDAC8 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (D) Protein expression levels of HDAC1, p-HDAC1, HDAC2, p-HDAC2, HDAC8 and p-HDAC8 in the chondrocytes by western blotting. (E) Co-IP experiments with DUSP26 protein from extracts of IL-1β-treated chondrocytes followed by western blotting with indicated antibodies. DEG, differentially expressed gene; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IB, immunoblot; IL, interleukin; IP, immunoprecipitation; LC-MS/MS, liquid chromatography-tandem MS; mRNA-seq, mRNA sequencing; MS, mass spectrometry; p-, phosphorylated.

    Journal: International Journal of Molecular Medicine

    Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

    doi: 10.3892/ijmm.2026.5776

    Figure Lengend Snippet: HDAC1, HDAC2 and HDAC8 are DUSP26-interacting proteins in chondrocytes. (A) IP/MS analysis in DUSP26-overexpressing chondrocytes under IL-1β stimulation. (B) Flow chart of target protein screening. (C) Immunohistochemical staining of HDAC1, HDAC2 and HDAC8 in the acetabular cartilage of the 4-week-old control rats and rats with DDH. (D) Protein expression levels of HDAC1, p-HDAC1, HDAC2, p-HDAC2, HDAC8 and p-HDAC8 in the chondrocytes by western blotting. (E) Co-IP experiments with DUSP26 protein from extracts of IL-1β-treated chondrocytes followed by western blotting with indicated antibodies. DEG, differentially expressed gene; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IB, immunoblot; IL, interleukin; IP, immunoprecipitation; LC-MS/MS, liquid chromatography-tandem MS; mRNA-seq, mRNA sequencing; MS, mass spectrometry; p-, phosphorylated.

    Article Snippet: To assess the functional integrity of chondrocytes, the P0-P1 primary chondrocytes were treated with the pro-inflammatory cytokine IL-1β (10 ng/ml; cat. no. HY-P7097; MedChemExpress) with or without the HDAC inhibitor trichostatin A (TSA; 300 nM; cat. no. T129665; Shanghai Aladdin Biochemical Technology Co., Ltd.) for 24 h at room temperature ( , ).

    Techniques: Protein-Protein interactions, Immunohistochemical staining, Staining, Control, Expressing, Western Blot, Co-Immunoprecipitation Assay, Histone Deacetylase Assay, Immunoprecipitation, Liquid Chromatography with Mass Spectroscopy, Liquid Chromatography, Sequencing, Mass Spectrometry

    Inactivation of HDAC1/2/8 inhibits DUSP26 silencing-triggered cartilage degeneration. (A) Total protein and phosphorylation levels of HDAC1, HDAC2 and HDAC8 in IL-1β-treated chondrocytes determined by western blotting. (B) Relative mRNA expression levels of HDAC1, HDAC2 and HDAC8 in chondrocytes, as determined by reverse transcription-quantitative PCR. (C) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (D) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. (E) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (F) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. (B-D) Representative results of three independent experiments are shown. COL1A1, type I collagen; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IL, interleukin; NC, negative control; ns, no significance; sh, short hairpin; TSA, trichostatin A.

    Journal: International Journal of Molecular Medicine

    Article Title: DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip-associated secondary osteoarthritis

    doi: 10.3892/ijmm.2026.5776

    Figure Lengend Snippet: Inactivation of HDAC1/2/8 inhibits DUSP26 silencing-triggered cartilage degeneration. (A) Total protein and phosphorylation levels of HDAC1, HDAC2 and HDAC8 in IL-1β-treated chondrocytes determined by western blotting. (B) Relative mRNA expression levels of HDAC1, HDAC2 and HDAC8 in chondrocytes, as determined by reverse transcription-quantitative PCR. (C) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (D) Relative mRNA expression levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. (E) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after knocking down HDAC1/2/8. (F) Protein levels of COL1A1 and TNF-α in IL-1β-treated chondrocytes after intervention with the HDAC inhibitor TSA. Data are presented as the mean ± SD. * P<0.05, ** P<0.01 and *** P<0.001. (B-D) Representative results of three independent experiments are shown. COL1A1, type I collagen; DUSP26, dual-specificity phosphatase 26; HDAC, histone deacetylase; IL, interleukin; NC, negative control; ns, no significance; sh, short hairpin; TSA, trichostatin A.

    Article Snippet: To assess the functional integrity of chondrocytes, the P0-P1 primary chondrocytes were treated with the pro-inflammatory cytokine IL-1β (10 ng/ml; cat. no. HY-P7097; MedChemExpress) with or without the HDAC inhibitor trichostatin A (TSA; 300 nM; cat. no. T129665; Shanghai Aladdin Biochemical Technology Co., Ltd.) for 24 h at room temperature ( , ).

    Techniques: Phospho-proteomics, Western Blot, Expressing, Reverse Transcription, Real-time Polymerase Chain Reaction, Histone Deacetylase Assay, Negative Control

    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis

    doi: 10.1038/s41467-026-68366-8

    Figure Lengend Snippet: A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.

    Article Snippet: E. faecalis overnight cultures of OG1RF WT and mutants were diluted 1:10 in 1 mL fresh BHI supplemented with either human pro-IL-1β (100 pg/mL), or human IL-1β (100 pg/mL, Cat. Nr. ab9617, Abcam), or rat pro-IL-1β (10 ng/mL, Cat. Nr. 80023-R07E, Sino Biological), or rat IL-1β (10 ng/mL, Cat. Nr. ab281807, Abcam) and incubated for 6 h at 37 °C, static conditions.

    Techniques: Staining, Western Blot, Control, Two Tailed Test, Mutagenesis, Incubation, Negative Control, Activation Assay, Positive Control

    Osmotic minipumps containing methadone or saline were implanted in pregnant rats on E16. Pups were born and serum collected on P10(A-D) and P21 (E-H). Using a translational multiplex electrochemiluminescent platform, biomarkers were assayed. On P10, those pups exposed to perinatal methadone had significantly increased IL-1β (A), TNFα (B), IL-6 (C) and CXCL1 (D) compared to saline pups. By P21, serum levels of IL-1β (E) remained significantly increased compared to methadone pups, while other cytokines and chemokines normalized. These data reflect significant and persistent increases in pro-inflammatory proteins in the serum throughout the perinatal period, consistent with a diverse inflammatory response syndrome. *p<0.05, **p<0.01, ***p<0.001, n=3–4/group.

    Journal: Brain, behavior, and immunity

    Article Title: Prenatal Opioid Exposure: The Next Neonatal Neuroinflammatory Disease

    doi: 10.1016/j.bbi.2019.11.007

    Figure Lengend Snippet: Osmotic minipumps containing methadone or saline were implanted in pregnant rats on E16. Pups were born and serum collected on P10(A-D) and P21 (E-H). Using a translational multiplex electrochemiluminescent platform, biomarkers were assayed. On P10, those pups exposed to perinatal methadone had significantly increased IL-1β (A), TNFα (B), IL-6 (C) and CXCL1 (D) compared to saline pups. By P21, serum levels of IL-1β (E) remained significantly increased compared to methadone pups, while other cytokines and chemokines normalized. These data reflect significant and persistent increases in pro-inflammatory proteins in the serum throughout the perinatal period, consistent with a diverse inflammatory response syndrome. *p<0.05, **p<0.01, ***p<0.001, n=3–4/group.

    Article Snippet: Cytokine and chemokine biomarker profile analysis was performed on serum (1:4 dilution), supernatants from cultured PBMCs (1:4 dilution), or brain tissue (100μg) using a V-plex rat pro-inflammatory panel for TNFα and interleukin 1β (IL-1β), IL-6 and CXCL1 consistent with prior reports (MesoScale Discovery, Gaithersburg, MD, USA).

    Techniques: Saline, Multiplex Assay

    Osmotic minipumps containing methadone or saline were implanted in pregnant rats on E16. Cerebral cortex collected on postnatal day 10 (P10) was assayed using a translational multiplex electrochemiluminescent platform to quantify cytokine and chemokine levels. Those pups exposed to methadone had significantly increased IL-1β (A), and CXCL1 (D) compared to saline control pups. Levels of TNFα (B) and IL-6 remained unchanged. These data reflect a robust and prolonged increase in pro-inflammatory proteins the brain during a critical period of neurodevelopment. *p<0.05, **p<0.01, ***p<0.001, n=6–7/group.

    Journal: Brain, behavior, and immunity

    Article Title: Prenatal Opioid Exposure: The Next Neonatal Neuroinflammatory Disease

    doi: 10.1016/j.bbi.2019.11.007

    Figure Lengend Snippet: Osmotic minipumps containing methadone or saline were implanted in pregnant rats on E16. Cerebral cortex collected on postnatal day 10 (P10) was assayed using a translational multiplex electrochemiluminescent platform to quantify cytokine and chemokine levels. Those pups exposed to methadone had significantly increased IL-1β (A), and CXCL1 (D) compared to saline control pups. Levels of TNFα (B) and IL-6 remained unchanged. These data reflect a robust and prolonged increase in pro-inflammatory proteins the brain during a critical period of neurodevelopment. *p<0.05, **p<0.01, ***p<0.001, n=6–7/group.

    Article Snippet: Cytokine and chemokine biomarker profile analysis was performed on serum (1:4 dilution), supernatants from cultured PBMCs (1:4 dilution), or brain tissue (100μg) using a V-plex rat pro-inflammatory panel for TNFα and interleukin 1β (IL-1β), IL-6 and CXCL1 consistent with prior reports (MesoScale Discovery, Gaithersburg, MD, USA).

    Techniques: Saline, Multiplex Assay, Control