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R&D Systems human tl1a recombinant protein

Two days post-confluent MEFs or 3T3-L1 cells were cultured in adipogenic induction medium supplemented with <t>TL1A</t> recombinant protein at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL). (A) Oil Red O staining was conducted after adipogenic induction for 7 days. (B) The average optical density (OD) was measured using a Universal Microplate Spectrophotometer at 490 nm. (C) Measurement of triglyceride (TG) content in MEFs 7 days after adipogenic differentiation. (D-E) Both Oil Red O staining and triglyceride assays in 3T3-L1 cells were performed on day 7 of differentiation. (F-G) qRT-PCR analysis was conducted to evaluate the expression of adipogenic markers aP2, Plin1, Plin2 and PPARγ in 3T3-L1 cells 7 days after adipogenic differentiation. (H) qRT-PCR analysis was conducted to evaluate the expression of VEGFA and several adipogenic markers C/EBPα/β/δ, PPARγ2, aP2, CD36, Plin1, Plin2, adispin, Glut4 and LPL in MEFs 7 days after adipogenic differentiation. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Human Tl1a Recombinant Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "TL1A serves as a positive regulator to promote adipocyte differentiation"

Article Title: TL1A serves as a positive regulator to promote adipocyte differentiation

Journal: PLOS One

doi: 10.1371/journal.pone.0343036

Two days post-confluent MEFs or 3T3-L1 cells were cultured in adipogenic induction medium supplemented with TL1A recombinant protein at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL). (A) Oil Red O staining was conducted after adipogenic induction for 7 days. (B) The average optical density (OD) was measured using a Universal Microplate Spectrophotometer at 490 nm. (C) Measurement of triglyceride (TG) content in MEFs 7 days after adipogenic differentiation. (D-E) Both Oil Red O staining and triglyceride assays in 3T3-L1 cells were performed on day 7 of differentiation. (F-G) qRT-PCR analysis was conducted to evaluate the expression of adipogenic markers aP2, Plin1, Plin2 and PPARγ in 3T3-L1 cells 7 days after adipogenic differentiation. (H) qRT-PCR analysis was conducted to evaluate the expression of VEGFA and several adipogenic markers C/EBPα/β/δ, PPARγ2, aP2, CD36, Plin1, Plin2, adispin, Glut4 and LPL in MEFs 7 days after adipogenic differentiation. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Figure Legend Snippet: Two days post-confluent MEFs or 3T3-L1 cells were cultured in adipogenic induction medium supplemented with TL1A recombinant protein at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL). (A) Oil Red O staining was conducted after adipogenic induction for 7 days. (B) The average optical density (OD) was measured using a Universal Microplate Spectrophotometer at 490 nm. (C) Measurement of triglyceride (TG) content in MEFs 7 days after adipogenic differentiation. (D-E) Both Oil Red O staining and triglyceride assays in 3T3-L1 cells were performed on day 7 of differentiation. (F-G) qRT-PCR analysis was conducted to evaluate the expression of adipogenic markers aP2, Plin1, Plin2 and PPARγ in 3T3-L1 cells 7 days after adipogenic differentiation. (H) qRT-PCR analysis was conducted to evaluate the expression of VEGFA and several adipogenic markers C/EBPα/β/δ, PPARγ2, aP2, CD36, Plin1, Plin2, adispin, Glut4 and LPL in MEFs 7 days after adipogenic differentiation. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Techniques Used: Cell Culture, Recombinant, Staining, Spectrophotometry, Quantitative RT-PCR, Expressing

(A-D) MEFs or 3T3-L1 cells were induced to undergo adipocyte differentiation for 3 days in the presence of the specified concentrations of TL1A. Total protein was extracted to determine C/EBPα, C/EBPβ, PPARγ2, PPARγ1 and aP2 protein expression by Western blotting with quantitation of band density. (E-H) MEFs or 3T3-L1 cells were induced to undergo adipocyte differentiation for 7 days with the indicated concentrations of TL1A. Total protein was extracted to determine PPARγ2, PPARγ1, CD36 and aP2 protein expression by Western blottingwith quantitation of band density. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Figure Legend Snippet: (A-D) MEFs or 3T3-L1 cells were induced to undergo adipocyte differentiation for 3 days in the presence of the specified concentrations of TL1A. Total protein was extracted to determine C/EBPα, C/EBPβ, PPARγ2, PPARγ1 and aP2 protein expression by Western blotting with quantitation of band density. (E-H) MEFs or 3T3-L1 cells were induced to undergo adipocyte differentiation for 7 days with the indicated concentrations of TL1A. Total protein was extracted to determine PPARγ2, PPARγ1, CD36 and aP2 protein expression by Western blottingwith quantitation of band density. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Techniques Used: Expressing, Western Blot, Quantitation Assay

After two days post-confluence, MEFs were treated with standard differentiation medium and TL1A recombinant protein (0, 10, 20, 50, 100, 200 ng/mL). At specified time points, cells were harvested for RNA isolation and subsequent qRT-PCR analysis. * P < 0.05 vs . the group of adipocytes without TL1A treatment.

Figure Legend Snippet: After two days post-confluence, MEFs were treated with standard differentiation medium and TL1A recombinant protein (0, 10, 20, 50, 100, 200 ng/mL). At specified time points, cells were harvested for RNA isolation and subsequent qRT-PCR analysis. * P < 0.05 vs . the group of adipocytes without TL1A treatment.

Techniques Used: Recombinant, Isolation, Quantitative RT-PCR

MEFs were treated with standard differentiation medium and TL1A at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL) for 7 days. (A) Total cellular proteins were extracted, and the expression levels of β-catenin, phosphorylated YAP1 S127 (p-YAP1 S127 ) and total YAP1 proteins were determined by Western blotting. (B) The relative amounts of β-catenin protein expression were calculated according to the grayscale values and were showed in the histogram. (C) The quantitation of ratio (p-YAP1 S127 /total YAP1) to reflect the inactivation of YAP1 signaling pathway. (D-E) At the end of adipogenesis induction, protein expression of phosphorylated β-catenin (p- β-catenin) and YAP1 in the cytoplasm extract from MEFs was determined by Western blotting. (F-G) Nuclear extracts were isolated from the MEFs and analyzed for protein expression by Western blotting. Nuclear proteins were isolated to evaluated the expression of β-catenin, YAP1 and PPARγ proteins through Western blotting, accompanied by a quantitative analysis of band density. GAPDH and Lamin A/C served as the internal controls for cytoplasmic and nuclear extract, respectively. All the histograms represent the relative expression levels of proteins normalized by GAPDH or Lamin A/C. * P <0.05, ** P <0.01, *** P <0.001 vs . the group of MEFs without TL1A treatment.

Figure Legend Snippet: MEFs were treated with standard differentiation medium and TL1A at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL) for 7 days. (A) Total cellular proteins were extracted, and the expression levels of β-catenin, phosphorylated YAP1 S127 (p-YAP1 S127 ) and total YAP1 proteins were determined by Western blotting. (B) The relative amounts of β-catenin protein expression were calculated according to the grayscale values and were showed in the histogram. (C) The quantitation of ratio (p-YAP1 S127 /total YAP1) to reflect the inactivation of YAP1 signaling pathway. (D-E) At the end of adipogenesis induction, protein expression of phosphorylated β-catenin (p- β-catenin) and YAP1 in the cytoplasm extract from MEFs was determined by Western blotting. (F-G) Nuclear extracts were isolated from the MEFs and analyzed for protein expression by Western blotting. Nuclear proteins were isolated to evaluated the expression of β-catenin, YAP1 and PPARγ proteins through Western blotting, accompanied by a quantitative analysis of band density. GAPDH and Lamin A/C served as the internal controls for cytoplasmic and nuclear extract, respectively. All the histograms represent the relative expression levels of proteins normalized by GAPDH or Lamin A/C. * P <0.05, ** P <0.01, *** P <0.001 vs . the group of MEFs without TL1A treatment.

Techniques Used: Expressing, Western Blot, Quantitation Assay, Isolation

Exogenous TL1A triggers the phosphorylation of YAP1 at Ser127, resulting in its cytoplasmic retention and functional inactivation. This event subsequently reduces β-catenin stability and prevents its nuclear translocation, thereby triggering the expression of essential adipogenic regulators and lipid metabolism-related proteins. Additionally, TL1A-mediated regulation of ABCA1 and ABCG1 expression facilitates cholesterol homeostasis, providing essential substrates for lipid droplet biogenesis. Collectively, these molecular mechanisms orchestrate the differentiation of MEFs and 3T3-L1 preadipocytes into terminally differentiated adipocytes.

Figure Legend Snippet: Exogenous TL1A triggers the phosphorylation of YAP1 at Ser127, resulting in its cytoplasmic retention and functional inactivation. This event subsequently reduces β-catenin stability and prevents its nuclear translocation, thereby triggering the expression of essential adipogenic regulators and lipid metabolism-related proteins. Additionally, TL1A-mediated regulation of ABCA1 and ABCG1 expression facilitates cholesterol homeostasis, providing essential substrates for lipid droplet biogenesis. Collectively, these molecular mechanisms orchestrate the differentiation of MEFs and 3T3-L1 preadipocytes into terminally differentiated adipocytes.

Techniques Used: Phospho-proteomics, Functional Assay, Translocation Assay, Expressing

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Journal: PLOS One

Article Title: TL1A serves as a positive regulator to promote adipocyte differentiation

doi: 10.1371/journal.pone.0343036

Figure Lengend Snippet: Two days post-confluent MEFs or 3T3-L1 cells were cultured in adipogenic induction medium supplemented with TL1A recombinant protein at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL). (A) Oil Red O staining was conducted after adipogenic induction for 7 days. (B) The average optical density (OD) was measured using a Universal Microplate Spectrophotometer at 490 nm. (C) Measurement of triglyceride (TG) content in MEFs 7 days after adipogenic differentiation. (D-E) Both Oil Red O staining and triglyceride assays in 3T3-L1 cells were performed on day 7 of differentiation. (F-G) qRT-PCR analysis was conducted to evaluate the expression of adipogenic markers aP2, Plin1, Plin2 and PPARγ in 3T3-L1 cells 7 days after adipogenic differentiation. (H) qRT-PCR analysis was conducted to evaluate the expression of VEGFA and several adipogenic markers C/EBPα/β/δ, PPARγ2, aP2, CD36, Plin1, Plin2, adispin, Glut4 and LPL in MEFs 7 days after adipogenic differentiation. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Article Snippet: Human TL1A recombinant protein (Cat# 1319-TL-010/CF) was purchased from R&D Systems.

Techniques: Cell Culture, Recombinant, Staining, Spectrophotometry, Quantitative RT-PCR, Expressing

Journal: PLOS One

Article Title: TL1A serves as a positive regulator to promote adipocyte differentiation

doi: 10.1371/journal.pone.0343036

Figure Lengend Snippet: (A-D) MEFs or 3T3-L1 cells were induced to undergo adipocyte differentiation for 3 days in the presence of the specified concentrations of TL1A. Total protein was extracted to determine C/EBPα, C/EBPβ, PPARγ2, PPARγ1 and aP2 protein expression by Western blotting with quantitation of band density. (E-H) MEFs or 3T3-L1 cells were induced to undergo adipocyte differentiation for 7 days with the indicated concentrations of TL1A. Total protein was extracted to determine PPARγ2, PPARγ1, CD36 and aP2 protein expression by Western blottingwith quantitation of band density. * P < 0.05, ** P < 0.01, *** P < 0.001 vs . the group of adipocytes without TL1A treatment (n = 3).

Article Snippet: Human TL1A recombinant protein (Cat# 1319-TL-010/CF) was purchased from R&D Systems.

Techniques: Expressing, Western Blot, Quantitation Assay

Journal: PLOS One

Article Title: TL1A serves as a positive regulator to promote adipocyte differentiation

doi: 10.1371/journal.pone.0343036

Figure Lengend Snippet: After two days post-confluence, MEFs were treated with standard differentiation medium and TL1A recombinant protein (0, 10, 20, 50, 100, 200 ng/mL). At specified time points, cells were harvested for RNA isolation and subsequent qRT-PCR analysis. * P < 0.05 vs . the group of adipocytes without TL1A treatment.

Article Snippet: Human TL1A recombinant protein (Cat# 1319-TL-010/CF) was purchased from R&D Systems.

Techniques: Recombinant, Isolation, Quantitative RT-PCR

Journal: PLOS One

Article Title: TL1A serves as a positive regulator to promote adipocyte differentiation

doi: 10.1371/journal.pone.0343036

Figure Lengend Snippet: MEFs were treated with standard differentiation medium and TL1A at the specified concentrations (0, 10, 20, 50, 100, 200 ng/mL) for 7 days. (A) Total cellular proteins were extracted, and the expression levels of β-catenin, phosphorylated YAP1 S127 (p-YAP1 S127 ) and total YAP1 proteins were determined by Western blotting. (B) The relative amounts of β-catenin protein expression were calculated according to the grayscale values and were showed in the histogram. (C) The quantitation of ratio (p-YAP1 S127 /total YAP1) to reflect the inactivation of YAP1 signaling pathway. (D-E) At the end of adipogenesis induction, protein expression of phosphorylated β-catenin (p- β-catenin) and YAP1 in the cytoplasm extract from MEFs was determined by Western blotting. (F-G) Nuclear extracts were isolated from the MEFs and analyzed for protein expression by Western blotting. Nuclear proteins were isolated to evaluated the expression of β-catenin, YAP1 and PPARγ proteins through Western blotting, accompanied by a quantitative analysis of band density. GAPDH and Lamin A/C served as the internal controls for cytoplasmic and nuclear extract, respectively. All the histograms represent the relative expression levels of proteins normalized by GAPDH or Lamin A/C. * P <0.05, ** P <0.01, *** P <0.001 vs . the group of MEFs without TL1A treatment.

Article Snippet: Human TL1A recombinant protein (Cat# 1319-TL-010/CF) was purchased from R&D Systems.

Techniques: Expressing, Western Blot, Quantitation Assay, Isolation

Journal: PLOS One

Article Title: TL1A serves as a positive regulator to promote adipocyte differentiation

doi: 10.1371/journal.pone.0343036

Figure Lengend Snippet: Exogenous TL1A triggers the phosphorylation of YAP1 at Ser127, resulting in its cytoplasmic retention and functional inactivation. This event subsequently reduces β-catenin stability and prevents its nuclear translocation, thereby triggering the expression of essential adipogenic regulators and lipid metabolism-related proteins. Additionally, TL1A-mediated regulation of ABCA1 and ABCG1 expression facilitates cholesterol homeostasis, providing essential substrates for lipid droplet biogenesis. Collectively, these molecular mechanisms orchestrate the differentiation of MEFs and 3T3-L1 preadipocytes into terminally differentiated adipocytes.

Article Snippet: Human TL1A recombinant protein (Cat# 1319-TL-010/CF) was purchased from R&D Systems.

Techniques: Phospho-proteomics, Functional Assay, Translocation Assay, Expressing

Figure 4 Response of DR3þ ccRCC cells to tumor necrosis factorelike 1A (TL1A). A: Light micrographs of the effect of TL1A on activation of NF-kB, mitogen-activated protein kinase (MAPK), and cell cycle entry in organ cultures of clear cell renal cell carcinoma (ccRCCoC) and adjacent normal kidney (NKoC). B: Untreated (UT) controls of ccRCC showing a rare nuclei signal for NF-kBp65-Ser276 in vascular endothelial cells (ECs), which is remarkably increased in TL1A- treated cultures with signal mainly in tumor cells (green arrows) and in ECs, and signiﬁcantly attenuated by pretreatment with Bay11-7082. C: Treated cultures of NK show a similar pattern of staining with signal mainly conﬁned to normal tubular epithelial cells (t) (red arrows) and in vascular ECs, attenuated by Bay11-7082. D: Quantiﬁcation of the percentage of positive tumor cells and in ccRCC and NK. D: TL1A also induced expression for all the three kinases in both study groups with a strong signal localized in tumor cells (white arrows), ECs, inﬁltrating mononuclear cells (MNCs), t in NK compared with UT controls. E: Quantiﬁcation of immunoﬂuorescence presented as corrected total cell ﬂuorescence (CTCF) in tumor cells and in normal t in ccRCC and NK. F: Nuclear pH3-Ser10 is rarely detected in UT controls, but expression is pronounced in tumor cells (green arrow) in TL1A-treated ccRCC cultures. Treated cultures of NK show a much-reduced level with signal seen in t (red arrow) and a rare signal detected in UT controls. G: Quantiﬁcation of the percentage of positive pH3-Ser10

Journal: The American journal of pathology

Article Title: Co-Expression and Functional Interactions of Death Receptor 3 and E-Selectin in Clear Cell Renal Cell Carcinoma.

doi: 10.1016/j.ajpath.2021.12.010

Figure Lengend Snippet: Figure 4 Response of DR3þ ccRCC cells to tumor necrosis factorelike 1A (TL1A). A: Light micrographs of the effect of TL1A on activation of NF-kB, mitogen-activated protein kinase (MAPK), and cell cycle entry in organ cultures of clear cell renal cell carcinoma (ccRCCoC) and adjacent normal kidney (NKoC). B: Untreated (UT) controls of ccRCC showing a rare nuclei signal for NF-kBp65-Ser276 in vascular endothelial cells (ECs), which is remarkably increased in TL1A- treated cultures with signal mainly in tumor cells (green arrows) and in ECs, and signiﬁcantly attenuated by pretreatment with Bay11-7082. C: Treated cultures of NK show a similar pattern of staining with signal mainly conﬁned to normal tubular epithelial cells (t) (red arrows) and in vascular ECs, attenuated by Bay11-7082. D: Quantiﬁcation of the percentage of positive tumor cells and in ccRCC and NK. D: TL1A also induced expression for all the three kinases in both study groups with a strong signal localized in tumor cells (white arrows), ECs, inﬁltrating mononuclear cells (MNCs), t in NK compared with UT controls. E: Quantiﬁcation of immunoﬂuorescence presented as corrected total cell ﬂuorescence (CTCF) in tumor cells and in normal t in ccRCC and NK. F: Nuclear pH3-Ser10 is rarely detected in UT controls, but expression is pronounced in tumor cells (green arrow) in TL1A-treated ccRCC cultures. Treated cultures of NK show a much-reduced level with signal seen in t (red arrow) and a rare signal detected in UT controls. G: Quantiﬁcation of the percentage of positive pH3-Ser10

Article Snippet: Mouse antihuman DR3/TNFRSF25 antibody (catalog number MAB943), goat anti-human TL1A/TNFSF15 antibodies (catalog number AF744), human recombinant (rh) TL1A protein, anti-goat NL493 (catalog number NL003), anti-goat NL-557 (catalog number NL001), anti-rabbit NL493 (catalog number NL006), anti-rabbit NL557 (catalog number NL004), anti-mouse NL493 (catalog number NL007), antimouse NL493 (catalog number NL009), and sheep anti- 723 human CD14 (catalog number AB383) antibodies are all from R&D Systems (Abingdon, UK).

Techniques: Activation Assay, Staining, Expressing

Figure 6 Proximity ligation assay (PLA) of organ cultures of clear cell renal cell carcinoma (ccRCCoC) grade 1 and adjacent normal kidney (NKoC) for detection of death receptor 3 (DR3) and E-selectin or cutaneous lymphocyte antigen (CLA)-1 or sialyl Lewis X (sLeX). A, C, and E: In comparison with untreated (UT) controls, tumor necrosis factorelike 1A (TL1A) treatment induced a strong interaction of DR3eE-selectin (A), DR3-CLA-1 (C), and DR3-sLeX (E), appearing as strong red ﬂuorescent spots mainly in cytoplasm of tumor cells and in normal tubular epithelial cells (t) (arrows). B, D, and F: Quantiﬁcation of the number of PLA spots per cell in tumor cells and t show a statistically signiﬁcant difference, more pronounced in ccRCCoC. Nuclei were counterstained with Hoechst 33342 (blue). n Z 5 per group with similar results. *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001. Scale bars Z 75 mM. Original magniﬁcation, 40.

Journal: The American journal of pathology

Article Title: Co-Expression and Functional Interactions of Death Receptor 3 and E-Selectin in Clear Cell Renal Cell Carcinoma.

doi: 10.1016/j.ajpath.2021.12.010

Figure Lengend Snippet: Figure 6 Proximity ligation assay (PLA) of organ cultures of clear cell renal cell carcinoma (ccRCCoC) grade 1 and adjacent normal kidney (NKoC) for detection of death receptor 3 (DR3) and E-selectin or cutaneous lymphocyte antigen (CLA)-1 or sialyl Lewis X (sLeX). A, C, and E: In comparison with untreated (UT) controls, tumor necrosis factorelike 1A (TL1A) treatment induced a strong interaction of DR3eE-selectin (A), DR3-CLA-1 (C), and DR3-sLeX (E), appearing as strong red ﬂuorescent spots mainly in cytoplasm of tumor cells and in normal tubular epithelial cells (t) (arrows). B, D, and F: Quantiﬁcation of the number of PLA spots per cell in tumor cells and t show a statistically signiﬁcant difference, more pronounced in ccRCCoC. Nuclei were counterstained with Hoechst 33342 (blue). n Z 5 per group with similar results. *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001. Scale bars Z 75 mM. Original magniﬁcation, 40.

Techniques: Proximity Ligation Assay, Comparison

Effects of the TL1A/DR3 axis on the EMT in Beas-2B cells were detected. TNF-a (50 ng/mL) stimulation for 48 h as the best cell model based on the above experimental results. The effect of sTL1A on EMT was detected by Western blotting (A, C) . The effects of TL1A siRNA on TL1A induced by TNF-a were detected by immunofluorescence (E) . Effects of TL1A siRNA on the EMT formation induced by TNF-a were measured by Western blotting analysis (G) . (E) : magnification 200 ×, scale bar 50 µm. (B, D, F, H) intensity analysis of (A, C, E, G), respectively. Data are expressed as the means ± SD for three independent experiments. # p < 0.05 versus the control group. # *p < 0.05 versus the TNF-a group.

Journal: Frontiers in Immunology

Article Title: TL1A/DR3 Axis, A Key Target of TNF-a, Augments the Epithelial–Mesenchymal Transformation of Epithelial Cells in OVA-Induced Asthma

doi: 10.3389/fimmu.2022.854995

Figure Lengend Snippet: Effects of the TL1A/DR3 axis on the EMT in Beas-2B cells were detected. TNF-a (50 ng/mL) stimulation for 48 h as the best cell model based on the above experimental results. The effect of sTL1A on EMT was detected by Western blotting (A, C) . The effects of TL1A siRNA on TL1A induced by TNF-a were detected by immunofluorescence (E) . Effects of TL1A siRNA on the EMT formation induced by TNF-a were measured by Western blotting analysis (G) . (E) : magnification 200 ×, scale bar 50 µm. (B, D, F, H) intensity analysis of (A, C, E, G), respectively. Data are expressed as the means ± SD for three independent experiments. # p < 0.05 versus the control group. # *p < 0.05 versus the TNF-a group.

Article Snippet: Recombinant human sTL1A (1319-TL) was obtained from RD Systems.

Techniques: Western Blot, Immunofluorescence, Control

sTL1A (A) and sDR3 (B) relative plasma levels (Z-score “communicome” values) in HIV-High (n=47) and HIV-Low (n=49) (Table S1). C-D) Gene expression (Table S1) of TL1A (C) and DR3 (D) in HIV-High (n=16) and HIV-Low (n=30). E-F) Unrelated validation cohorts for gene expression of TL1A (E) and DR3 (F) in dry pellet PBMC samples from seronegatives (SN, n=6) and HIV-infected individuals one year before and after initiation of treatment (untreated [n=11] and treated [n=5]) and in LTNP (n=23) (Table S1). G) Absolute DR3 quantifications in plasma (ELISA) in a confirmatory cohort including seronegatives (SN, n=8) and samples from time points one year before and after initiation of treatment (untreated [n=15] and treated [n=10]) and controllers (n=31), Table S1). The Mann-Whitney test was applied for group comparisons, and p-values < 0.05 were considered significant.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: TL1A-DR3 plasma levels are predictive of HIV-1 disease control, and DR3 co-stimulation boosts HIV-1-specific T-cell responses

doi: 10.4049/jimmunol.2000933

Figure Lengend Snippet: sTL1A (A) and sDR3 (B) relative plasma levels (Z-score “communicome” values) in HIV-High (n=47) and HIV-Low (n=49) (Table S1). C-D) Gene expression (Table S1) of TL1A (C) and DR3 (D) in HIV-High (n=16) and HIV-Low (n=30). E-F) Unrelated validation cohorts for gene expression of TL1A (E) and DR3 (F) in dry pellet PBMC samples from seronegatives (SN, n=6) and HIV-infected individuals one year before and after initiation of treatment (untreated [n=11] and treated [n=5]) and in LTNP (n=23) (Table S1). G) Absolute DR3 quantifications in plasma (ELISA) in a confirmatory cohort including seronegatives (SN, n=8) and samples from time points one year before and after initiation of treatment (untreated [n=15] and treated [n=10]) and controllers (n=31), Table S1). The Mann-Whitney test was applied for group comparisons, and p-values < 0.05 were considered significant.

Article Snippet: Then, we co-stimulated the cells with 100 ng/ml of sTL1A (Recombinant Human TL1A/TNFSF15, R&D systems), 500 ng/ml of sDR3 (Recombinant Human DR3/TNFRSF25 Fc Chimera Protein, R&D systems), and /or 100 ng/ml of mAb anti-DR3 (Purified anti-human DR3 (TRAMP) JD3, Biolegend).

Techniques: Clinical Proteomics, Gene Expression, Biomarker Discovery, Infection, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY

A) Failure of TL1A-DR3 axis during uncontrolled HIV infection. Upon HIV-specific activation, there is no upregulation of DR3 in surface membrane of CD8 T cells (A.1). The reduced levels of sTL1A do not allow the signaling through DR3 receptor (A.2) that would weaken the IFNg production (A.3). B) HIV control. Upon HIV-specific activation, DR3 protein is upregulated in cell membrane (B.1) that together with higher plasma levels of sTL1A and/or the presence of a DR3-agonist would ensure the signaling of the TL1A-DR3 axis (B.2). That co-stimulatory effect would enhance the HIV-specific IFNg responses (B.3)

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: TL1A-DR3 plasma levels are predictive of HIV-1 disease control, and DR3 co-stimulation boosts HIV-1-specific T-cell responses

doi: 10.4049/jimmunol.2000933

Figure Lengend Snippet: A) Failure of TL1A-DR3 axis during uncontrolled HIV infection. Upon HIV-specific activation, there is no upregulation of DR3 in surface membrane of CD8 T cells (A.1). The reduced levels of sTL1A do not allow the signaling through DR3 receptor (A.2) that would weaken the IFNg production (A.3). B) HIV control. Upon HIV-specific activation, DR3 protein is upregulated in cell membrane (B.1) that together with higher plasma levels of sTL1A and/or the presence of a DR3-agonist would ensure the signaling of the TL1A-DR3 axis (B.2). That co-stimulatory effect would enhance the HIV-specific IFNg responses (B.3)

Techniques: Infection, Activation Assay, Membrane, Control, Clinical Proteomics

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