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TRAF1 V203A mutation in THP-1 cells reduces secretion of caspase-1 <t>and</t> <t>IL-1β</t> by reducing K63-linked polyubiquitination of caspase-1. TRAF1 WT and TRAF1 V203A THP-1 cells were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). The culture supernatants were collected, and the proteins were precipitated using 100% TCA. (A) Supernatants were immunoblotted for immature caspase-1 (pro-caspase-1) and active caspase-1 (p20 subunit). (B) Supernatants were immunoblotted for inactive IL-1β (pro-IL-1β) and processed IL-1β (bioactive IL-1β). The blots shown in (A) and (B) are representative of five independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation. (C) TRAF1 WT cells and TRAF1 V203A THP-1 clones (C1 and C2) were primed with or without 100 ng/mL LPS for 24 hours. Cells were stimulated with 10 µM nigericin for 2, 10, and 25 minutes. Whole-cell lysates were immunoblotted for K63-linked polyubiquitin (Ub) chains. (D) The whole-cell lysates from (C) were immunoprecipitated with endogenous caspase-1 and then immunoblotted for K63-linked polyubiquitin (Ub) chains. The blots shown in (C) and (D) are representative of two independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation.

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1) Product Images from "Disrupting the TRAF1/cIAP2 interaction attenuates inflammasome activation and protects against monosodium urate crystal–induced arthritis"

Article Title: Disrupting the TRAF1/cIAP2 interaction attenuates inflammasome activation and protects against monosodium urate crystal–induced arthritis

Journal: ImmunoHorizons

doi: 10.1093/immhor/vlaf065

TRAF1 V203A mutation in THP-1 cells reduces secretion of caspase-1 and IL-1β by reducing K63-linked polyubiquitination of caspase-1. TRAF1 WT and TRAF1 V203A THP-1 cells were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). The culture supernatants were collected, and the proteins were precipitated using 100% TCA. (A) Supernatants were immunoblotted for immature caspase-1 (pro-caspase-1) and active caspase-1 (p20 subunit). (B) Supernatants were immunoblotted for inactive IL-1β (pro-IL-1β) and processed IL-1β (bioactive IL-1β). The blots shown in (A) and (B) are representative of five independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation. (C) TRAF1 WT cells and TRAF1 V203A THP-1 clones (C1 and C2) were primed with or without 100 ng/mL LPS for 24 hours. Cells were stimulated with 10 µM nigericin for 2, 10, and 25 minutes. Whole-cell lysates were immunoblotted for K63-linked polyubiquitin (Ub) chains. (D) The whole-cell lysates from (C) were immunoprecipitated with endogenous caspase-1 and then immunoblotted for K63-linked polyubiquitin (Ub) chains. The blots shown in (C) and (D) are representative of two independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation.

Figure Legend Snippet: TRAF1 V203A mutation in THP-1 cells reduces secretion of caspase-1 and IL-1β by reducing K63-linked polyubiquitination of caspase-1. TRAF1 WT and TRAF1 V203A THP-1 cells were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). The culture supernatants were collected, and the proteins were precipitated using 100% TCA. (A) Supernatants were immunoblotted for immature caspase-1 (pro-caspase-1) and active caspase-1 (p20 subunit). (B) Supernatants were immunoblotted for inactive IL-1β (pro-IL-1β) and processed IL-1β (bioactive IL-1β). The blots shown in (A) and (B) are representative of five independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation. (C) TRAF1 WT cells and TRAF1 V203A THP-1 clones (C1 and C2) were primed with or without 100 ng/mL LPS for 24 hours. Cells were stimulated with 10 µM nigericin for 2, 10, and 25 minutes. Whole-cell lysates were immunoblotted for K63-linked polyubiquitin (Ub) chains. (D) The whole-cell lysates from (C) were immunoprecipitated with endogenous caspase-1 and then immunoblotted for K63-linked polyubiquitin (Ub) chains. The blots shown in (C) and (D) are representative of two independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation.

Techniques Used: Mutagenesis, Clone Assay, Immunoprecipitation

TRAF1 V196A mice exhibit reduced inflammasome-driven IL-1β secretion in vivo and in vitro. TRAF1 WT and TRAF1 V196A BMDMs were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). IL-1β was quantified from the collected supernatant by ELISA. A total of six independent experiments were performed, three in female mice (A) and three in male mice (B). Ordinary 2-way ANOVA was performed with Tukey multiple comparisons test to determine statistical significance. (C) TRAF1 WT ( n = 4) and TRAF1 V196A ( n = 4) female littermate mice were injected intraperitoneally with a sublethal LPS dose of 10 mg/kg. Blood was collected at the 1- and 6-hour timepoints by saphenous vein and the serum was collected to perform the multiplex cytokine assay by flow cytometry. Each symbol represents one mouse. Ordinary 2-way ANOVA was performed with Sidak multiple comparisons test to determine statistical significance. The error bars represent mean ± SEM. * P < 0.05, ** P < 0.01.

Figure Legend Snippet: TRAF1 V196A mice exhibit reduced inflammasome-driven IL-1β secretion in vivo and in vitro. TRAF1 WT and TRAF1 V196A BMDMs were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). IL-1β was quantified from the collected supernatant by ELISA. A total of six independent experiments were performed, three in female mice (A) and three in male mice (B). Ordinary 2-way ANOVA was performed with Tukey multiple comparisons test to determine statistical significance. (C) TRAF1 WT ( n = 4) and TRAF1 V196A ( n = 4) female littermate mice were injected intraperitoneally with a sublethal LPS dose of 10 mg/kg. Blood was collected at the 1- and 6-hour timepoints by saphenous vein and the serum was collected to perform the multiplex cytokine assay by flow cytometry. Each symbol represents one mouse. Ordinary 2-way ANOVA was performed with Sidak multiple comparisons test to determine statistical significance. The error bars represent mean ± SEM. * P < 0.05, ** P < 0.01.

Techniques Used: In Vivo, In Vitro, Enzyme-linked Immunosorbent Assay, Injection, Multiplex Assay, Cytokine Assay, Flow Cytometry

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CTG12 inhibits NLRP3 inflammasome activation in mouse BMDMs and human THP1. A The structure of CTG12. B , C Cell viability of BMDMs ( B ) and THP1 cells ( C ) treated with CTG12. (D-H) Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), NLRP3, ASC in whole cell lysates (WCL) of LPS-primed BMDMs treated with CTG12 and then stimulated with Nigericin (25 min) ( D ), supernatants were collected for the measurement of caspase-1( E ), IL-1β ( F ), LDH ( G ) and TNF-α ( H ). (I-M) THP-1 cells primed with PMA for 12 h were treated with CTG12 for 1 h and then stimulated with nigericin for 55 min. Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), ASC in whole cell lysates (WCL) of THP-1 ( I ), supernatants were collected for the measurement of caspase-1( J ), IL-1β ( K ), LDH ( L ) and TNF-α ( M ). Coomassie blue-stained gels was used as loading control and Lamin B was used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). Compared to con, ** p < 0.01, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

Journal: Cell Communication and Signaling : CCS

Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

doi: 10.1186/s12964-026-02741-2

Figure Lengend Snippet: CTG12 inhibits NLRP3 inflammasome activation in mouse BMDMs and human THP1. A The structure of CTG12. B , C Cell viability of BMDMs ( B ) and THP1 cells ( C ) treated with CTG12. (D-H) Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), NLRP3, ASC in whole cell lysates (WCL) of LPS-primed BMDMs treated with CTG12 and then stimulated with Nigericin (25 min) ( D ), supernatants were collected for the measurement of caspase-1( E ), IL-1β ( F ), LDH ( G ) and TNF-α ( H ). (I-M) THP-1 cells primed with PMA for 12 h were treated with CTG12 for 1 h and then stimulated with nigericin for 55 min. Western blot analysis of IL-1β (p17), caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, caspase-1 (p45), ASC in whole cell lysates (WCL) of THP-1 ( I ), supernatants were collected for the measurement of caspase-1( J ), IL-1β ( K ), LDH ( L ) and TNF-α ( M ). Coomassie blue-stained gels was used as loading control and Lamin B was used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). Compared to con, ** p < 0.01, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

Article Snippet: Anti-human IL-1β (p17, 12242S), anti-Phospho-IRF3 (Ser396) (4947), caspase-1 antibody (4199S) and anti-ASC antibody (sc-22, 514-R) were obtained from Cell Signaling Technology (Germany).

Techniques: Activation Assay, Western Blot, Staining, Control, Concentration Assay

CTG12 specifically inhibits canonical and noncanonical NLRP3 inflammasome activation. A - C BMDMs were primed with LPS and then treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly (I:C), or SiO₂. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs (A), supernatants were collected for the measurement of caspase-1 ( B ) and IL-1β ( C ). D - F BMDMs primed with Pam3CSK4 treated with CTG12 (5 μM), followed by cytosolic LPS. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( D ), supernatants were collected for the measurement of caspase-1 ( E ) and IL-1β ( F ). ( G - I ) BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, Salmonella, poly (dA:dT). Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( G ), supernatants were collected for the measurement of caspase-1 ( H ) and IL-1β ( I ). Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

Journal: Cell Communication and Signaling : CCS

Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

doi: 10.1186/s12964-026-02741-2

Figure Lengend Snippet: CTG12 specifically inhibits canonical and noncanonical NLRP3 inflammasome activation. A - C BMDMs were primed with LPS and then treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly (I:C), or SiO₂. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs (A), supernatants were collected for the measurement of caspase-1 ( B ) and IL-1β ( C ). D - F BMDMs primed with Pam3CSK4 treated with CTG12 (5 μM), followed by cytosolic LPS. Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( D ), supernatants were collected for the measurement of caspase-1 ( E ) and IL-1β ( F ). ( G - I ) BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, Salmonella, poly (dA:dT). Western blot analysis of caspase-1 (p20) in culture supernatants (SN) and pro-IL-1β, pro-caspase-1 (p45), NLRP3 and ASC in whole-cell lysates (WCL); secretion of activated caspase-1 (p20) in the culture supernatant (SN) of BMDMs ( G ), supernatants were collected for the measurement of caspase-1 ( H ) and IL-1β ( I ). Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples. Data represent as mean ± SEM ( n = 3). # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

Techniques: Activation Assay, Western Blot, Staining, Control

CTG12 inhibits LPS-induced priming step of inflammasome activation and specifically inhibits canonical and noncanonical NLRP3 inflammasome activation by blocking NLRP3-dependent ASC oligomerization. A BMDMs were cultured with LPS for 4 h, then incubated with CTG12 for 1 h, or BMDMs were first treated with CTG12 for 1 h, followed by stimulation with LPS for 4 h, western blot analysis of protein levels of NLRP3, ASC, pro-IL-1β, Cas-1 p45, Lamin B. B BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. C BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly(I:C), SiO 2 , western blot analysis of in Triton X insoluble microparticle cross-linked ASC. D BMDMs were primed with Pam3CSK4 treated with CTG12 (5 μM), followed by stimulation with ultra-LPS, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. E BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, salmonella or poly (dA:dT), western blot analysis of in Triton X insoluble microparticle cross-linked ASC. Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples

Journal: Cell Communication and Signaling : CCS

Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

doi: 10.1186/s12964-026-02741-2

Figure Lengend Snippet: CTG12 inhibits LPS-induced priming step of inflammasome activation and specifically inhibits canonical and noncanonical NLRP3 inflammasome activation by blocking NLRP3-dependent ASC oligomerization. A BMDMs were cultured with LPS for 4 h, then incubated with CTG12 for 1 h, or BMDMs were first treated with CTG12 for 1 h, followed by stimulation with LPS for 4 h, western blot analysis of protein levels of NLRP3, ASC, pro-IL-1β, Cas-1 p45, Lamin B. B BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. C BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, ATP, poly(I:C), SiO 2 , western blot analysis of in Triton X insoluble microparticle cross-linked ASC. D BMDMs were primed with Pam3CSK4 treated with CTG12 (5 μM), followed by stimulation with ultra-LPS, western blot analysis of Triton X-insoluble microparticle cross-linking ASC. E BMDMs were primed with LPS treated with CTG12 (5 μM), then stimulated with Nigericin, salmonella or poly (dA:dT), western blot analysis of in Triton X insoluble microparticle cross-linked ASC. Coomassie blue-stained gels used as loading control and Lamin B used as a control for equal loading of the samples

Techniques: Activation Assay, Blocking Assay, Cell Culture, Incubation, Western Blot, Staining, Control

CTG12 alleviates LPS-induced acute systemic inflammation in mice. A - J Female mice (8 weeks) were injected intraperitoneally with CTG12 (0 mg/kg, 15 mg/kg, 30 mg/kg), MCC950 (40 mg/kg) or CTG12 (30 mg/kg) + MCC950 (40 mg/kg) for 1 h, followed by an injection of 20 mg/kg LPS for 5 h ( n = 6). The levels of IL-1β (A, B), IL-18 ( C , D ), IL-6 ( E , F ), TNF-α ( G , H ) and CXCL1/KC ( I , J ) in peritoneal lavage fluid and serum were analyzed by ELISA ( n = 6). Data represent as mean ± SD. Compared to con, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

Journal: Cell Communication and Signaling : CCS

Article Title: Investigating the impact and mechanism of Licochalcone B derivative CTG12 on NLRP3 inflammasome

doi: 10.1186/s12964-026-02741-2

Figure Lengend Snippet: CTG12 alleviates LPS-induced acute systemic inflammation in mice. A - J Female mice (8 weeks) were injected intraperitoneally with CTG12 (0 mg/kg, 15 mg/kg, 30 mg/kg), MCC950 (40 mg/kg) or CTG12 (30 mg/kg) + MCC950 (40 mg/kg) for 1 h, followed by an injection of 20 mg/kg LPS for 5 h ( n = 6). The levels of IL-1β (A, B), IL-18 ( C , D ), IL-6 ( E , F ), TNF-α ( G , H ) and CXCL1/KC ( I , J ) in peritoneal lavage fluid and serum were analyzed by ELISA ( n = 6). Data represent as mean ± SD. Compared to con, **** p < 0.0001; compared to a concentration of 0 μM, # p < 0.05, ## p < 0.01, ### p < 0.001, #### p < 0.0001 and ns: not significant (one-way ANOVA with Dunnett’s post-hoc test)

Techniques: Injection, Enzyme-linked Immunosorbent Assay, Concentration Assay

Journal: ImmunoHorizons

Article Title: Disrupting the TRAF1/cIAP2 interaction attenuates inflammasome activation and protects against monosodium urate crystal–induced arthritis

doi: 10.1093/immhor/vlaf065

Figure Lengend Snippet: TRAF1 V203A mutation in THP-1 cells reduces secretion of caspase-1 and IL-1β by reducing K63-linked polyubiquitination of caspase-1. TRAF1 WT and TRAF1 V203A THP-1 cells were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). The culture supernatants were collected, and the proteins were precipitated using 100% TCA. (A) Supernatants were immunoblotted for immature caspase-1 (pro-caspase-1) and active caspase-1 (p20 subunit). (B) Supernatants were immunoblotted for inactive IL-1β (pro-IL-1β) and processed IL-1β (bioactive IL-1β). The blots shown in (A) and (B) are representative of five independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation. (C) TRAF1 WT cells and TRAF1 V203A THP-1 clones (C1 and C2) were primed with or without 100 ng/mL LPS for 24 hours. Cells were stimulated with 10 µM nigericin for 2, 10, and 25 minutes. Whole-cell lysates were immunoblotted for K63-linked polyubiquitin (Ub) chains. (D) The whole-cell lysates from (C) were immunoprecipitated with endogenous caspase-1 and then immunoblotted for K63-linked polyubiquitin (Ub) chains. The blots shown in (C) and (D) are representative of two independent experiments with two of the identified clones containing the successful TRAF1 V203A mutation.

Article Snippet: Proteins in the culture supernatants collected from inflammasome-stimulated THP-1 cells were precipitated with 100% trichloroacetic acid (TCA) and then immunoblotted with antibodies to detect human/mouse IL-1β ELISA (R&D Systems, Minneapolis, MN, USA) and mouse caspase-1 (BioLegend).

Techniques: Mutagenesis, Clone Assay, Immunoprecipitation

Journal: ImmunoHorizons

Article Title: Disrupting the TRAF1/cIAP2 interaction attenuates inflammasome activation and protects against monosodium urate crystal–induced arthritis

doi: 10.1093/immhor/vlaf065

Figure Lengend Snippet: TRAF1 V196A mice exhibit reduced inflammasome-driven IL-1β secretion in vivo and in vitro. TRAF1 WT and TRAF1 V196A BMDMs were primed with or without 100 ng/mL LPS for 3 hours. Cells were then stimulated with either 5 mM ATP or stimulated with 10 µM nigericin for 1 hour (2 hours after priming step) and 3 hours (immediately after priming step). IL-1β was quantified from the collected supernatant by ELISA. A total of six independent experiments were performed, three in female mice (A) and three in male mice (B). Ordinary 2-way ANOVA was performed with Tukey multiple comparisons test to determine statistical significance. (C) TRAF1 WT ( n = 4) and TRAF1 V196A ( n = 4) female littermate mice were injected intraperitoneally with a sublethal LPS dose of 10 mg/kg. Blood was collected at the 1- and 6-hour timepoints by saphenous vein and the serum was collected to perform the multiplex cytokine assay by flow cytometry. Each symbol represents one mouse. Ordinary 2-way ANOVA was performed with Sidak multiple comparisons test to determine statistical significance. The error bars represent mean ± SEM. * P < 0.05, ** P < 0.01.

Techniques: In Vivo, In Vitro, Enzyme-linked Immunosorbent Assay, Injection, Multiplex Assay, Cytokine Assay, Flow Cytometry

Figure 1. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in plasma samples from patients with brain gliomas of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

Journal: International journal of molecular sciences

Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

doi: 10.3390/ijms26104802

Figure Lengend Snippet: Figure 1. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in plasma samples from patients with brain gliomas of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

Article Snippet: The following reagents were used for the construction of the biosensor and validation of the analytical method: recombinant HIF-1α protein, recombinant human ANG-2 protein, and recombinant human IL-1β protein; monoclonal mouse antibody against HIF-1α, monoclonal mouse antibody against ANG-2, and monoclonal mouse antibody against IL-1β (all from R&D Systems, Minneapolis, MN, USA); EDC (Nethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride) (SIGMA, Steinheim, Germany); 11-MUA 11-mercaptoundecanoic acid (Aldrich, Munich, Germany); NHS Nhydroxysuccinimide (Aldrich, Munich, Germany); buffered saline solution (PBS buffer) (Biomed, Lublin, Poland); absolute ethyl alcohol (POCh, Gliwice, Poland); and ethanolamine solution (SIGMA, Steinheim, Germany).

Techniques: Clinical Proteomics

Figure 2. Graphs of the changes of HIF-1α, ANG-2, and IL-1β concentrations in plasma samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann–Whitney-U test p-value results table.

Journal: International journal of molecular sciences

Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

doi: 10.3390/ijms26104802

Figure Lengend Snippet: Figure 2. Graphs of the changes of HIF-1α, ANG-2, and IL-1β concentrations in plasma samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann–Whitney-U test p-value results table.

Techniques: Clinical Proteomics, MANN-WHITNEY

Figure 3. ROC curves for (A) HIF-1α; (B) ANG-2; and (C) IL-1β.

Journal: International journal of molecular sciences

Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

doi: 10.3390/ijms26104802

Figure Lengend Snippet: Figure 3. ROC curves for (A) HIF-1α; (B) ANG-2; and (C) IL-1β.

Techniques:

Figure 4. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenate samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

Journal: International journal of molecular sciences

Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

doi: 10.3390/ijms26104802

Figure Lengend Snippet: Figure 4. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenate samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots. (D) Dunn–Bonferroni POST-HOC graphical analysis. The green boxes with statistically significant values contain the p parameter values.

Techniques:

Figure 5. Graphs of changes in HIF-1α, ANG-2, and IL-1β concentrations in tissue homogenate samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann– Whitney U test p-value results table.

Journal: International journal of molecular sciences

Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

doi: 10.3390/ijms26104802

Figure Lengend Snippet: Figure 5. Graphs of changes in HIF-1α, ANG-2, and IL-1β concentrations in tissue homogenate samples depending on (A) gender, (B) alcohol use, (C) concomitant non-cancerous diseases, and (D) family history of cancer. Information about the medians is placed above the box plots. (E) Mann– Whitney U test p-value results table.

Techniques: MANN-WHITNEY

Figure 6. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenates and plasma samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots.

Journal: International journal of molecular sciences

Article Title: A Study on the Levels of Selected Proangiogenic Proteins in Human Tissues and Plasma in Relation to Brain Glioma.

doi: 10.3390/ijms26104802

Figure Lengend Snippet: Figure 6. Graphs of changes in HIF-1α (A), ANG-2 (B), and IL-1β (C) concentrations in tissue homogenates and plasma samples from patients with brain glioma of different grades. Information about the medians is placed above the box plots.

Techniques: Clinical Proteomics

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