Journal: Scientific Reports

Article Title: Development of a multiplex and sensitive lateral flow immunoassay for the diagnosis of periprosthetic joint infection

doi: 10.1038/s41598-019-52051-6

Figure Lengend Snippet: The protein levels of alpha-defensin and CRP in 10 synovial fluid samples analyzed by ELISA.

Article Snippet: Anti-alpha-defensin antibody, Human alpha-defensin 1 DuoSet ELISA and Human C-Reactive Protein/CRP DuoSet ELISA were obtained from R&D systems (Minneapolis, MN, USA), Goat anti-mouse immunoglobulin (IgG) antibody was supplied by Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

Techniques: Enzyme-linked Immunosorbent Assay

Journal: Scientific Reports

Article Title: Development of a multiplex and sensitive lateral flow immunoassay for the diagnosis of periprosthetic joint infection

doi: 10.1038/s41598-019-52051-6

Figure Lengend Snippet: Correlation between the signal intensities of msLFIA results and ELISA measurements of CRP and alpha-defensin in synovial fluid samples. The error bars represent the standard deviation of three independent experiments.

Article Snippet: Anti-alpha-defensin antibody, Human alpha-defensin 1 DuoSet ELISA and Human C-Reactive Protein/CRP DuoSet ELISA were obtained from R&D systems (Minneapolis, MN, USA), Goat anti-mouse immunoglobulin (IgG) antibody was supplied by Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

Techniques: Enzyme-linked Immunosorbent Assay, Standard Deviation

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: Flowchart of the study. First, BEV-sensitive and BEV-resistant ovarian cancer mouse models were constructed, and RNA sequencing was performed on tumor tissue. Then, a BEV-related prognostic signature was established using machine learning, and S100B was identified as the most important molecule regulating BEV sensitivity in ovarian cancer. Its function and mechanism were analyzed in vitro. Finally, BEV efficacy when combined with an S100B inhibitor was verified in vivo. BEV: Bevacizumab; DEGs: Differentially expressed genes.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: Construct, RNA Sequencing, In Vitro, In Vivo

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: Screening S100B as the main molecule regulating the sensitivity of ovarian cancer to BEV. (A) Kaplan–Meier survival analysis of OS (left) and PFS (right) of patients with high S100B expression treated with chemotherapy with or without BEV (from the GSE140082 dataset). (B) Kaplan–Meier survival analysis of OS (left) and PFS (right) of patients with low S100B expression treated with chemotherapy with or without BEV (from the GSE140082 dataset). (C) Western blot analysis of S100B protein expression in tumor tissue from BEV-sensitive and BEV-resistant mice. (D) Western blot analysis of S100B protein levels in mouse tumor tissue. (E) Immunohistochemical staining of S100B protein in BEV-sensitive and BEV-resistant mice. (F) Statistical histochemical staining of S100B protein in mouse tumor tissue. BEV:Bevacizumab; **: P < 0.01.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: Expressing, Western Blot, Immunohistochemical staining, Staining

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: Co-culture of S100B overexpressing ovarian cancer cells promotes HUEVC angiogenesis and migration. (A) Representative Western blot images and their densitometric quantification showing comparative S100B protein expression profiles among the three ovarian cancer cell lines (A2780, HEY, and OVCAR3) (B) Western blot analysis and statistical analysis of OVCAR3 and HEY cells overexpressing S100B. RT-qPCR analysis of alternative angiogenic factor mRNA expression levels in (C) OVCAR3 and (D) HEY ovarian cancer cell lines following S100B overexpression. (E) The level of S100B in the supernatant of OVCAR3 and HEY cells overexpressing S100B significantly increased, as determined by ELISA. (F) There was no significant change in VEGFA levels in the supernatant of OVCAR3 and HEY cells overexpressing S100B. (G, H) HUVEC tube formation significantly increased after co-culture with ovarian cancer cell lines overexpressing S100B, with or without exogenous BEV. (I, J) Co-culture with ovarian cancer cells overexpressing S100B significantly promoted HUVEC sprouting with or without exogenous BEV. (K, L) Co-culture of ovarian cancer cells overexpressing S100B significantly promoted migration of HUVECs in a Transwell system with or without exogenous BEV. (M, N) Co-culture of ovarian cancer cell lines overexpressing S100B significantly promoted healing of HUVECs with or without exogenous BEV in a scratch assay. BEV: Bevacizumab; NC: negative control; OE: overexpression; *: P < 0.05; **: P < 0.01; ***: P < 0.001; ****: P < 0.0001. Scale: All panels are 50 μm.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: Co-Culture Assay, Migration, Western Blot, Expressing, Quantitative RT-PCR, Over Expression, Enzyme-linked Immunosorbent Assay, Wound Healing Assay, Negative Control

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: Exogenous recombinant S100B protein promoted vascular formation and migration of HUEVCs. Different concentrations of recombinant S100B protein, with or without BEV, promoted (A, B) angiogenesis in a tube formation assay, (C, D) sprouting in a fibrin bead sprouting assay, (E, F) migration in a Transwell assay, and (G, H) healing of endothelial cells in a wound healing assay. (I) Tip cell marker expression in HUVECs significantly increased by rt-qPCR detection after treatment with recombinant S100B protein. BEV: Bevacizumab; *: P < 0.05; **: P < 0.01; ***: P < 0.001; ****: P < 0.0001. Scale: All panels are 50 μm.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: Recombinant, Migration, Tube Formation Assay, Transwell Assay, Wound Healing Assay, Marker, Expressing, Quantitative RT-PCR

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: S100B enters endothelial cells through clathrin-dependent endocytosis to promote angiogenesis and migration. (A) Western blot detection showed that there was no significant change in RAGE receptor expression in endothelial cells after exogenous S100B treatment. (B) Western blot detection showed that protein levels of S100B in endothelial cells significantly increased after co-culture with ovarian cancer cells overexpressing S100B. (C) S100B total protein and nuclear protein in endothelial cells significantly increased after treatment with exogenous S100B, as determined by western blot analysis. (D) Western blot analysis of protein levels of S100B in endothelial cells after pretreatment with the clathrin-mediated endocytosis inhibitor Pitstop-2 or caveolae/caveolin-1-mediated endocytosis inhibitor nystatin. Changes in the (F, G) tubular phenotype, (H, I) sprouting phenotype, (J, K) migration phenotype (Transwell assay), and (L–M) wound healing phenotype (scratch migration assay) of endothelial cells after treatment with the RAGE receptor inhibitor FPS-ZM1, the clathrin-mediated endocytosis inhibitor Pitstop-2, and the caveolae/caveolin-mediated endocytosis inhibitor nystatin. BEV: Bevacizumab; *: P < 0.05; **: P < 0.01; ***: P < 0.001; ****: P < 0.0001. Scale: All panels are 50 μm.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: Migration, Western Blot, Expressing, Co-Culture Assay, Transwell Assay

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: S100B promotes tube formation and migration of endothelial cells through the FOXO1/β-catenin signaling pathway. (A) DIA proteomics thermogram of differentially expressed proteins in HUVECs with or without exogenous S100B. (B) Function and pathway enrichment analysis by Metascape database of differentially expressed proteins. (C–E) Western blot analysis showed that levels of S100B in ovarian cancer tissue of BEV-resistant mice significantly increased, while FOXO1 levels decreased. (F) Histogram of an RT-qPCR analysis of downstream transcriptional target genes of β-catenin. (G–J) Western blot analysis showed that FOXO1 total protein and nuclear protein levels in endothelial cells significantly decreased after treatment with exogenous S100B, while levels of β-catenin and MMP7 significantly increased. (K–M) Western blot analysis of FOXO1 and β-catenin levels in S100B-treated endothelial cells overexpressing FOXO1 compared with the control group. Endothelial cells transfected with a control virus or FOXO1 -overexpressing lentivirus and treated with S100B were evaluated for their (N) tubular phenotype by tube formation assay, (O) sprouting phenotype by fibrin bead sprouting assay, and (P) migration phenotype by Tranwell assay. (Q) Schematic diagram of the mechanism of exogenous S100B on endothelial cell angiogenesis. *: P < 0.05; **: P < 0.01;^: P < 0.05 vs. S100B−/oeFOXO1−; #: P < 0.05 vs. S100B−/oeFOXO1+; &: P < 0.05 vs. S100B+/oeFOXO1 − . Scale: All panels are 50 μm.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: Migration, Western Blot, Quantitative RT-PCR, Control, Transfection, Virus, Tube Formation Assay

Journal: Journal of Advanced Research

Article Title: S100B induces angiogenesis via the clathrin/FOXO1/β-catenin signaling pathway and contributes to Bevacizumab resistance in epithelial ovarian cancer

doi: 10.1016/j.jare.2025.05.060

Figure Lengend Snippet: The S100B inhibitor pentamidine in combination with BEV improves the ovarian cancer response compared to BEV alone. (A) Flowchart of the in vivo experiment. Two weeks after intraperitoneal inoculation of ovarian cancer cells, drug treatment was administered. The mice were randomly divided into a normal saline treatment control group, BEV treatment group, pentamidine treatment group, and BEV with pentamidine treatment group. (B) Line chart of the tumor fluorescence intensity of the four groups of mice. (C) Tumor fluorescence imaging of mice after tumor formation (week 2), after killing the control group and pentamidine treatment group (week 4–6), after killing the BEV treatment group (week 8–9), and after killing the BEV with pentamidine treatment group (week 13–14). (D) Kaplan–Meier survival curves of the four groups of mice. (E) CD31 immunohistochemical staining and (F) MVD statistics of tumor tissue from the four groups of mice. (E) S100B immunohistochemical staining and S100B (G) staining intensity of tumor tissue from the four groups of mice. BEV: Bevacizumab; MVD: Micro-vessel density; *: P < 0.05; **: P < 0.01;^: P < 0.05 vs. NC; #: P < 0.05 vs. pentamidine; &: P < 0.05 vs. BEV.

Article Snippet: S100B and VEGFA levels in the supernatant were measured using S100B (Elabscience, E-EL-H1297) and VEGFA (Elabscience, E-EL-H0111) ELISA kits.

Techniques: In Vivo, Saline, Control, Fluorescence, Imaging, Immunohistochemical staining, Staining

Journal: Experimental and therapeutic medicine

Article Title: Blood purification treatment initiated at the time of sepsis diagnosis effectively attenuates serum HMGB1 upregulation and improves patient prognosis.

doi: 10.3892/etm.2017.4854

Figure Lengend Snippet: Figure 1. Serum and urine HMGB1 levels upon diagnosis of sepsis. (A) Serum and (B) urine levels of HMGB1 were measured by ELISA in the different patient groups prior to the initiation of treatment. Data are presented as the mean ± standard deviation. #P<0.05 vs. Control. HMGB1, high mobility group box protein 1; CRRT, continuous renal replacement treatment; HP, hemoperfusion.

Article Snippet: Serum and urine HMGB1 levels were measured using a Human HMGB1 ELISA kit (E-EL-H1554c, Elabscience Biotechnology Co., Ltd., Wuhan, China) according to the manufacturer's protocol.

Techniques: Biomarker Discovery, Enzyme-linked Immunosorbent Assay, Standard Deviation, Control

Journal: Experimental and therapeutic medicine

Article Title: Blood purification treatment initiated at the time of sepsis diagnosis effectively attenuates serum HMGB1 upregulation and improves patient prognosis.

doi: 10.3892/etm.2017.4854

Figure Lengend Snippet: Figure 2. Changes in serum and urine HMGB1 levels over 24 h. (A) Serum and (B) urine levels of HMGB1 in the sepsis (no apheresis intervention) group at different time points. Data are presented as the mean ± standard deviation. #P<0.05 vs. 0‑h value. HMGB1, high mobility group box protein 1.

Article Snippet: Serum and urine HMGB1 levels were measured using a Human HMGB1 ELISA kit (E-EL-H1554c, Elabscience Biotechnology Co., Ltd., Wuhan, China) according to the manufacturer's protocol.

Techniques: Standard Deviation

Journal: Experimental and therapeutic medicine

Article Title: Blood purification treatment initiated at the time of sepsis diagnosis effectively attenuates serum HMGB1 upregulation and improves patient prognosis.

doi: 10.3892/etm.2017.4854

Figure Lengend Snippet: Figure 3. Association of serum HMGB1 level with urine HMGB1 level and APACHE II score. Correlations were identified between (A) urine and serum HMGB1 levels, and (B) APACHE II score and serum HMGB1 level in the sepsis (no apheresis intervention) group. HMGB1, high mobility group box protein 1; APACHE II, Acute Physiology and Chronic Health Evaluation II.

Article Snippet: Serum and urine HMGB1 levels were measured using a Human HMGB1 ELISA kit (E-EL-H1554c, Elabscience Biotechnology Co., Ltd., Wuhan, China) according to the manufacturer's protocol.

Techniques:

Journal: Experimental and therapeutic medicine

Article Title: Blood purification treatment initiated at the time of sepsis diagnosis effectively attenuates serum HMGB1 upregulation and improves patient prognosis.

doi: 10.3892/etm.2017.4854

Figure Lengend Snippet: Figure 4. Changes in serum and urine HMGB1 levels in the different patient groups over 24 h. (A) Serum and (B) urine levels of HMGB1 were measured by ELISA at different time points after the initiation of treatments. Data are presented as the mean ± standard deviation. #P<0.05 vs. 0‑h value; *P<0.05 vs. sepsis group; ^P<0.05 vs. 12‑h value. HMGB1, high mobility group box protein 1; CRRT, continuous renal replacement treatment; HP, hemoperfusion.

Article Snippet: Serum and urine HMGB1 levels were measured using a Human HMGB1 ELISA kit (E-EL-H1554c, Elabscience Biotechnology Co., Ltd., Wuhan, China) according to the manufacturer's protocol.

Techniques: Enzyme-linked Immunosorbent Assay, Standard Deviation

Journal: ImmunoTargets and Therapy

Article Title: Recombinant Antithrombin Alleviated Pulmonary Injury and Inflammation in LPS-Induced ARDS by Inhibiting IL17a/NF-κB Signaling

doi: 10.2147/ITT.S502925

Figure Lengend Snippet: rAT reduced pulmonary inflammation in LPS-induced ARDS model mice. ( A–D ) The levels of inflammatory factors, including IL-6 ( A ), TNF-α ( B ), IL-8 ( C ), and hs-CRP ( D ), were decreased in the serum of the rAT-treated group, as detected by ELISA. ( E ) Immunohistochemical staining for F4/80 revealed that rAT treatment reduced the proportion of macrophages in the lung tissue of LPS-induced ARDS model mice. ( F ) Immunohistochemical staining for MRCI, a marker of M2 macrophages, showed that rAT treatment increased the proportion of M2 macrophages in the lung tissue of LPS-induced ARDS model mice. ( G ) Immunohistochemical staining for Ly6G, a marker of neutrophils, showed that rAT treatment reduced the proportion of neutrophils in the lung tissue of LPS-induced ARDS model mice. All the data are presented as the means ± SDs of three independent experiments. One-way ANOVA, *p < 0.05, **p < 0.01, ***p < 0.001, ns, not significant; scale bar, 50 μm.

Article Snippet: A mouse CXCL15 ELISA Kit (E-EL-M0269) and a mouse hs-CRP ELISA Kit (E-EL-M0677) were purchased from Elabscience (Wuhan, China).

Techniques: Enzyme-linked Immunosorbent Assay, Immunohistochemical staining, Staining, Marker

Journal: ImmunoTargets and Therapy

Article Title: Recombinant Antithrombin Alleviated Pulmonary Injury and Inflammation in LPS-Induced ARDS by Inhibiting IL17a/NF-κB Signaling

doi: 10.2147/ITT.S502925

Figure Lengend Snippet: The efficacy of rAT in mitigating lung injury, suppressing the immune response, and inhibiting the activation of the NF-κB signaling pathway in LPS-induced ARDS mice were diminished by the administration of IL-17a. ( A ) ELISA results demonstrated that the administration of IL17a inhibited the ability of rAT to reduce inflammatory factors, including IL-6, TNF-α, and IL-8, in the serum of LPS-induced ARDS mice. ( B ) The analysis of the wet/dry weight ratio of the lung tissue revealed that the administration of IL17a counteracted the ability of rAT to alleviate pulmonary exudation in LPS-induced ARDS mice. ( C ) The administration of IL17a did not significantly affect the ability of rAT to reduce the number of cells in the BALF of LPS-induced ARDS mice. ( D ) The administration of IL17a attenuated the ability of rAT to reduce the concentrations of proteins in the BALF of LPS-induced ARDS mice. ( E ) Real-time PCR results showed that the administration of IL17a blocked the ability of rAT to downregulate the expression of target genes in the IL17a/NF-κB signaling pathway. ( F ) The protein levels of the NF-κB signaling pathway were assessed by Western blotting, and gray intensity analysis of the blots showed that the administration of IL17a in LPS-induced ARDS mice counteracted the ability of rAT to suppress the phosphorylation of IκBα, IKKα/β, and P65. The data are expressed as the means ± SDs (n=3 in each group). One-way ANOVA, *p < 0.05, **p < 0.01, ***p < 0.001, and ns not significant.

Article Snippet: A mouse CXCL15 ELISA Kit (E-EL-M0269) and a mouse hs-CRP ELISA Kit (E-EL-M0677) were purchased from Elabscience (Wuhan, China).

Techniques: Activation Assay, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Expressing, Western Blot, Phospho-proteomics