p-selectin Search Results


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  • 92
    RayBiotech mouse p selectin elisa kit
    Secretion of soluble <t>P-selectin</t> (P-sel) after granulocyte colony-stimulating factor (G-CSF) treatment was independent of erythrocytic mobilization. a The experimental outline to monitor the concentrations of soluble P-selectin after G-CSF treatment ( n = 10) is illustrated. Untreated ( n = 10) and saline-treated groups ( n = 10) served as negative controls. The concentrations of soluble P-selectin were detected by <t>ELISA</t> ( b ). The experimental outline to detect the cell counts of white blood cells (WBCs) ( d ) and red blood cells (RBCs) ( e ) in PB after G-CSF ( n = 4) and P-selectin ( n = 10) treatments is shown ( c ). Untreated groups ( n = 5) served as negative controls. Data are reported as mean ±± SD. * P
    Mouse P Selectin Elisa Kit, supplied by RayBiotech, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    R&D Systems p selectin
    Substrates for cell interactions studies were fabricated via direct, photochemical functionalization. Glass slides chemically-modified to present benzophenone moieties were immersed in a solution containing the protein of interest–here P- or <t>E-selectin.</t> Photoimmobilization is initiated by exposure to 365 nm light, which results to covalently bound protein through a radical generation mechanism. Importantly, the density of immobilized protein can be systematically defined by carefully controlling the exposure time. Substrates, prepared in batches, were then subsequently used to quantify deposition density (via fluorescence or radioimmunoassay) or utilized to study the effects of bromelain treatment on primary human neutrophil-selectin interactions.
    P Selectin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 924 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology p selectin
    Expression of vesicular nucleotide transporter (VNUT) in MEG‐01 cells. (A) The membrane from MEG‐01 cells (20 μ g) was analyzed by Western blot with anti‐hVNUT antibodies. The position of VNUT is marked by an arrow. The positions of molecular markers were also indicated. (B) Double‐labeling immunohistochemistry indicated the localization of VNUT and the marker proteins cellubrevin, MRP4, p <t>‐selectin,</t> GPllb/GPllla, and NSF in MEG‐01 cells. Bars represent 10 μ m.
    P Selectin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 261 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Elabscience p selectin
    HNA2 induces platelet aggregation and activation. (A) Platelets were incubated with ex vivo prepared HMA (1 mg/mL), HNA1 (1 mg/mL), and HNA2 (1 mg/mL), and aggregation was induced with collagen (0.2 μg/mL). Representative reading and bar graph indicate increased aggregation in HNA2‐treated platelets as compared with HNA1 and HMA. Data are expressed as percent of normalized platelet aggregation (n = 3). (B) CD40L and ROS production in healthy platelets was significantly increased when exposed to HNA2 (1 mg/mL). Pretreatment with anti‐CD36 blocking antibody (1 μg/mL) significantly reverses the effect, particularly in HNA2‐exposed platelets. (C) EGTA decreases HNA2‐induced platelet expression of CD40L and ROS production in a dose‐dependent manner. Platelets were pre‐incubated with EGTA, and activation was induced with HNA2 (1 mg/mL). (D) Histogram represents the percent expression of platelets exposed to HNA2 (1 mg/mL) showing increased expression of <t>P‐selectin,</t> PAC‐1, and intracellular calcium as compared with HNA1 (n = 5). (E) Expression of SNARE complex proteins (Syntaxin‐11, SNAP‐23, and VAMP‐8) increases in healthy platelets exposed to HNA2 (1 mg/mL) as compared with HNA1 and HMA. Interestingly, anti‐CD36 blocking antibody (1 μg/mL) reduced the effect of HNA2 over others. Results expressed as mean ± SEM (* P
    P Selectin, supplied by Elabscience, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Becton Dickinson p selectin
    (A) Release of soluble vWF from uninfected and HCMV-infected HPAEC, as measured by an ELISA. Infected cells secreted 2.5-fold more vWF than uninfected cells at 5 and 7 dpi. (B and C) Secretion of serotonin (B) and soluble <t>P-selectin</t> (C) from platelets
    P Selectin, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 1091 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Immunotec p selectin
    (A) Release of soluble vWF from uninfected and HCMV-infected HPAEC, as measured by an ELISA. Infected cells secreted 2.5-fold more vWF than uninfected cells at 5 and 7 dpi. (B and C) Secretion of serotonin (B) and soluble <t>P-selectin</t> (C) from platelets
    P Selectin, supplied by Immunotec, used in various techniques. Bioz Stars score: 92/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam p selectin
    Macrophages and adhesion molecules at rupture site. ( A – C ) Immunostaining for F4/80 (green) and DAPI (blue) of membrane 24 h after rupture by 20 G needle. Dashed lines indicate amnion ( Am , white), surface of fetal skin (yellow), chorion ( Cho , light blue), and decidua ( Dec , purple). Myo , myometrium. ( A ) Intact fetal membrane. ( B ) Macrophages within healing amnion (arrows). ( C ) Ruptured edge of chorio-decidua. Bars, 50 µm. ( D – F ) H E staining of ruptured membranes. ( D ) An amniotic fluid macrophage (arrow head) attaches to ruptured amnion at 2 h (arrow). ( E and magnified view in F ) Amniotic fluid macrophages (green) attach to amnion surface at 24 h, and mesenchymal cells migrate (arrow head). Note mesenchymal-like shape change of epithelial cells in F . Bars, 50 µm. ( G and H ) Fluorescent in situ hybridization (FISH) of Y chromosome (red) and immunostaining for F4/80 (green) at healing amnion ( G ) and intact myometrium ( H ) at 48 h. Bars, 10 µm. ( I – L ) Macrophage adhesion molecules at the ruptured site. Immunostaining for F4/80 (green), VCAM1 ( I ) or <t>P-selectin</t> ( J , red) and DAPI (blue) at ruptured amnion at 24 h after rupture by 20 G needle. Bars, 50 µm. ( K and L ) Gene expression of VCAM1 ( K ) or P-selectin ( L ) of intact or ruptured fetal membrane with 20 G needle at indicated time. Error bars represent SEM. n = 5–6 fetal membranes from 5–6 pregnant mice in each group. * P
    P Selectin, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 77 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Beckman Coulter p selectin
    Extracellular CyPA enhances platelet-activation in vitro (A) 8H7-mAb detects CyPA in monocyte as well in platelet lysate (upper line). Afterwards the same membrane was incubated with an anti-CyPA antibody (lower line) to prove the specificity of 8H7-mAb. (B) 8H7-mAb significantly reduces the CyPA-dependent platelet activation. Representative overlays of the <t>p-selectin</t> expression and bar graphs show mean±SEM of P-selectin expression on platelets. * means p ≤ 0.05 vs. CyPA+IgG. (C) Monocyte-platelet aggregate (MPA) formation was analyzed by using double staining with CD42b (as platelets marker) and CD14 (as monocyte marker) as described in material and methods. The platelets were treated as indicated and incubated with monocytes for the MPA formation. Figure shows representative flow cytometry analysis. (n ≤ 6) * means p ≤ 0.05 vs. resting. Right panel shows representative quadrat statistic for the CD14 + CD42 + double positive cells.
    P Selectin, supplied by Beckman Coulter, used in various techniques. Bioz Stars score: 92/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Luminex p selectin
    Extracellular CyPA enhances platelet-activation in vitro (A) 8H7-mAb detects CyPA in monocyte as well in platelet lysate (upper line). Afterwards the same membrane was incubated with an anti-CyPA antibody (lower line) to prove the specificity of 8H7-mAb. (B) 8H7-mAb significantly reduces the CyPA-dependent platelet activation. Representative overlays of the <t>p-selectin</t> expression and bar graphs show mean±SEM of P-selectin expression on platelets. * means p ≤ 0.05 vs. CyPA+IgG. (C) Monocyte-platelet aggregate (MPA) formation was analyzed by using double staining with CD42b (as platelets marker) and CD14 (as monocyte marker) as described in material and methods. The platelets were treated as indicated and incubated with monocytes for the MPA formation. Figure shows representative flow cytometry analysis. (n ≤ 6) * means p ≤ 0.05 vs. resting. Right panel shows representative quadrat statistic for the CD14 + CD42 + double positive cells.
    P Selectin, supplied by Luminex, used in various techniques. Bioz Stars score: 90/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bender MedSystems p selectin
    Plasma levels of biomarkers on late samples in cases and matched controls. Values indicate medians (full squares in cases and full diamonds in controls), bars indicate interquartile ranges. hsCRP = high-sensitivity C-reactive protein in mg/L; t-PA = tissue plasminogen activator in ng/mL; D-dimer in μg/100 mL; PAI-1 = plasminogen activator inhibitor-1 in μg/10 mL; IL-6 = interleukin-6 in pg/mL; <t>P-selectin</t> = platelet selectin in μg/100 mL. *p=0.002; #p=0.005 from fitting a conditional logistic regression (biomarkers in log scale) comparing cases and controls.
    P Selectin, supplied by Bender MedSystems, used in various techniques. Bioz Stars score: 92/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biospes p selectin
    Modulation of <t>P-selectin</t> correlates with change in monocyte phenotype. The table shows the P-selectin values at baseline and post-vaccination stratified among groups, with P -values calculated using rank ANCOVA. Percentage change from baseline of P-selectin in each group is shown in graph A. B and C report the correlation between change in P-selectin and change in classical CD14 high CD16 − and intermediate CD14 high CD16 + monocyte cell count, respectively. Values are reported as median and IQR. * P = 0.003; ** P = 0.011; *** P = 0.039 vs. baseline within groups using Wilcoxon matched-pairs signed-rank test.
    P Selectin, supplied by Biospes, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher p selectin
    Expression of <t>P-selectin</t> (CD62P) on activated platelets plated on different endothelialised collagen substrates (* P
    P Selectin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Wuhan EIAab Science p selectin
    Expression of <t>P-selectin</t> (CD62P) on activated platelets plated on different endothelialised collagen substrates (* P
    P Selectin, supplied by Wuhan EIAab Science, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Techne p selectin inhibitor
    Platelet EVs increase monocytic cell adhesion and cytokine release. SMC were incubated without or with platelet EV or CD40L in the presence of indicated inhibitors <t>(P-selectin</t> inhibitor, eptifibatide, F1-Fk) or blocking antibody (α-CD40L). Syto13 fluorescently labelled THP-1 were perfused at 0.15 ml/min (3 dynes/cm 2 ) and adherent cells were quantified in six different fields; n = 5–9 (a). Representative micrographs of THP-1 cells adherent to non- or platelet EV-stimulated SMC (b). SMC were incubated with indicated agonists for 24 h and IL-6 release was measured by ELISA; n = 6 (c). P-values were calculated by ANOVA with Tukey’s post-test. Scale bar: 100 µm.
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    Becton Dickinson p selectin pe
    Secretion and fibrinogen-binding defects in SLP76 KI platelets in response to CVX. (A) <t>P-selectin</t> surface expression was analyzed by flow cytometry after stimulation with 0.2 nM or 1 nM CVX, or 1 mM AYPGKF. Representative histograms are shown. (B) Platelets were treated as described in A and were stained with 100 μg/ml of Alexa Fluor 647–labeled fibrinogen. EDTA was added to control for nonspecific binding. Mean percentages ± SEM of P-selectin–positive (A) or fibrinogen-bound (B) cells after the indicated stimulations ( n = 4–6 mice per genotype) are shown. *, P
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    BioLegend p selectin
    Activation of endothelial cells with human anti-HLA I IgG1 triggers adherence of peripheral blood monocytes via FcγRI, <t>P-selectin</t> and ICAM-1.
    P Selectin, supplied by BioLegend, used in various techniques. Bioz Stars score: 92/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    R&D Systems p selectin ig
    ESL hi metastatic PCa MDA cell variants express sLe X - and <t>E-selectin-Ig-reactive</t> PSGL-1. ( A and B ) MDA cell variants were separated into ESL lo and ESL hi based on their E-selectin-binding characteristics. ( C and D ) Flow cytometric analysis of expression
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    91
    Tocris p selectin inhibitor
    <t>P-selectin</t> (SELP) is differentially expressed across various cancer types. Comparison of P-selectin expression in various cancer types from data obtained from the TCGA data portal (sorted by the median).
    P Selectin Inhibitor, supplied by Tocris, used in various techniques. Bioz Stars score: 91/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Becton Dickinson anti p selectin
    Homing of CD4 + CD25 + T reg cells to NALT is partially dependent on PSGL-1 and CD44. (A and B) CFSE-labeled CD4 + CD25 − T conv cells and CMTMR-labeled CD4 + CD25 + T reg cells were treated with or without neutralizing mAb, mixed at a ratio of 1:1, and injected into WT mice intravenously. 2 h later, lymphocytes from the NALT (A) and the PLNs (CLNs; B) were collected and analyzed by flow cytometry after gating on the CFSE- or CMTMR-positive cell fractions. The neutralizing mAbs used were <t>anti–L-selectin</t> (MEL-14), anti–PSGL-1 (4RA10), <t>anti–P-selectin</t> (RB40.34), and anti-CD44 (IM7), and rat IgG as a control. In some experiments, cells were treated with a mixture of MEL-14, 4RA10, and IM7 (mAb Mix). Each bar represents the mean ± SD. n = 4. *, P
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    R&D Systems anti p selectin
    Effect of <t>P-selectin</t> exposure on monocyte phenotype after overnight incubation Platelet-coated plates were either untreated (first column), or pretreated with an isoptype control (second column) or <t>anti-P-selectin</t> (third column). Monocytes were passed through the plates at 0.5 dyne/cm 2 then incubated overnight. The y-axis indicates the percent of monocytes which developed a phenotype consistent with DC differentiation, i.e., membrane HLA-DR + /CD83 + . Data shown are the means (+/- SD) of 3 independent experiments.
    Anti P Selectin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti p selectin
    The targeting properties of DPP‐hADSCs to balloon‐injured human femoral arteries. a) Schematic illustration of hADSCs dynamic targeting experiment. b) After dynamic culture for 1 h, 5 × 10 −6 m DPP‐modified and unmodified hADSCs binding to injured human femoral arteries were observed by BLI ( n = 4) and c) quantitatively analyzed based on Luc fluorescence intensities. d) The <t>P‐selectin</t> expression and adhesion of hADSCs on the lumen surface of injured arteries in different groups was observed by co‐staining using <t>anti‐P‐selectin</t> and anti‐CD45 antibodies ( n = 3). e) Quantitative analysis of the adhesion of hADSCs per microscopic field from the 5 × 10 −6 m DPP‐modified and unmodified hADSCs groups.
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    Abcam cd62p p selectin
    The targeting properties of DPP‐hADSCs to balloon‐injured human femoral arteries. a) Schematic illustration of hADSCs dynamic targeting experiment. b) After dynamic culture for 1 h, 5 × 10 −6 m DPP‐modified and unmodified hADSCs binding to injured human femoral arteries were observed by BLI ( n = 4) and c) quantitatively analyzed based on Luc fluorescence intensities. d) The <t>P‐selectin</t> expression and adhesion of hADSCs on the lumen surface of injured arteries in different groups was observed by co‐staining using <t>anti‐P‐selectin</t> and anti‐CD45 antibodies ( n = 3). e) Quantitative analysis of the adhesion of hADSCs per microscopic field from the 5 × 10 −6 m DPP‐modified and unmodified hADSCs groups.
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    Image Search Results


    Secretion of soluble P-selectin (P-sel) after granulocyte colony-stimulating factor (G-CSF) treatment was independent of erythrocytic mobilization. a The experimental outline to monitor the concentrations of soluble P-selectin after G-CSF treatment ( n = 10) is illustrated. Untreated ( n = 10) and saline-treated groups ( n = 10) served as negative controls. The concentrations of soluble P-selectin were detected by ELISA ( b ). The experimental outline to detect the cell counts of white blood cells (WBCs) ( d ) and red blood cells (RBCs) ( e ) in PB after G-CSF ( n = 4) and P-selectin ( n = 10) treatments is shown ( c ). Untreated groups ( n = 5) served as negative controls. Data are reported as mean ±± SD. * P

    Journal: Stem Cell Research & Therapy

    Article Title: Different effects of granulocyte colony-stimulating factor and erythropoietin on erythropoiesis

    doi: 10.1186/s13287-018-0877-2

    Figure Lengend Snippet: Secretion of soluble P-selectin (P-sel) after granulocyte colony-stimulating factor (G-CSF) treatment was independent of erythrocytic mobilization. a The experimental outline to monitor the concentrations of soluble P-selectin after G-CSF treatment ( n = 10) is illustrated. Untreated ( n = 10) and saline-treated groups ( n = 10) served as negative controls. The concentrations of soluble P-selectin were detected by ELISA ( b ). The experimental outline to detect the cell counts of white blood cells (WBCs) ( d ) and red blood cells (RBCs) ( e ) in PB after G-CSF ( n = 4) and P-selectin ( n = 10) treatments is shown ( c ). Untreated groups ( n = 5) served as negative controls. Data are reported as mean ±± SD. * P

    Article Snippet: The EPO and soluble P-selectin immunoassays were performed using an enzyme-linked immunosorbent assay (ELISA) in accordance with the manufacturers’ instructions (Quantikine® Mouse/Rat EPO immunoassay, R & D systems; Mouse P-selectin ELISA kit, RayBiotech, Inc., USA).

    Techniques: Enzyme-linked Immunosorbent Assay

    Substrates for cell interactions studies were fabricated via direct, photochemical functionalization. Glass slides chemically-modified to present benzophenone moieties were immersed in a solution containing the protein of interest–here P- or E-selectin. Photoimmobilization is initiated by exposure to 365 nm light, which results to covalently bound protein through a radical generation mechanism. Importantly, the density of immobilized protein can be systematically defined by carefully controlling the exposure time. Substrates, prepared in batches, were then subsequently used to quantify deposition density (via fluorescence or radioimmunoassay) or utilized to study the effects of bromelain treatment on primary human neutrophil-selectin interactions.

    Journal: PLoS ONE

    Article Title: Bromelain Decreases Neutrophil Interactions with P-Selectin, but Not E-Selectin, In Vitro by Proteolytic Cleavage of P-Selectin Glycoprotein Ligand-1

    doi: 10.1371/journal.pone.0078988

    Figure Lengend Snippet: Substrates for cell interactions studies were fabricated via direct, photochemical functionalization. Glass slides chemically-modified to present benzophenone moieties were immersed in a solution containing the protein of interest–here P- or E-selectin. Photoimmobilization is initiated by exposure to 365 nm light, which results to covalently bound protein through a radical generation mechanism. Importantly, the density of immobilized protein can be systematically defined by carefully controlling the exposure time. Substrates, prepared in batches, were then subsequently used to quantify deposition density (via fluorescence or radioimmunoassay) or utilized to study the effects of bromelain treatment on primary human neutrophil-selectin interactions.

    Article Snippet: HSA-blocked BP-modified substrates were used as control substrates to verify that the observed interactions were due to neutrophil interactions with immobilized P-selectin or E-selectin.

    Techniques: Modification, Fluorescence, RIA Assay

    Fluorescence images and plots of average site density from substrates presenting photoimmobilized selectins. (a) Sites densities for P-selectin substrates were determined using a previously reported radioimmunoassay [15] . (b) A similar radioimmunoassay for E-selectin (Figure S1 in File S1 ) was used to determine site densities of E-selectin substrates. Scale bar = 1 mm.

    Journal: PLoS ONE

    Article Title: Bromelain Decreases Neutrophil Interactions with P-Selectin, but Not E-Selectin, In Vitro by Proteolytic Cleavage of P-Selectin Glycoprotein Ligand-1

    doi: 10.1371/journal.pone.0078988

    Figure Lengend Snippet: Fluorescence images and plots of average site density from substrates presenting photoimmobilized selectins. (a) Sites densities for P-selectin substrates were determined using a previously reported radioimmunoassay [15] . (b) A similar radioimmunoassay for E-selectin (Figure S1 in File S1 ) was used to determine site densities of E-selectin substrates. Scale bar = 1 mm.

    Article Snippet: HSA-blocked BP-modified substrates were used as control substrates to verify that the observed interactions were due to neutrophil interactions with immobilized P-selectin or E-selectin.

    Techniques: Fluorescence, RIA Assay

    Blocking of PSGL-1 with a monoclonal anti-PSGL-1 antibody prevents subsequent proteolytic cleavage by bromelain thereby preventing further reduction in tethering on P-selectin. Data from flow assays with differentiated HL-60 promyelocytes treated with bromelain, blocking antibody, both, or untreated. For both “high” (*** p

    Journal: PLoS ONE

    Article Title: Bromelain Decreases Neutrophil Interactions with P-Selectin, but Not E-Selectin, In Vitro by Proteolytic Cleavage of P-Selectin Glycoprotein Ligand-1

    doi: 10.1371/journal.pone.0078988

    Figure Lengend Snippet: Blocking of PSGL-1 with a monoclonal anti-PSGL-1 antibody prevents subsequent proteolytic cleavage by bromelain thereby preventing further reduction in tethering on P-selectin. Data from flow assays with differentiated HL-60 promyelocytes treated with bromelain, blocking antibody, both, or untreated. For both “high” (*** p

    Article Snippet: HSA-blocked BP-modified substrates were used as control substrates to verify that the observed interactions were due to neutrophil interactions with immobilized P-selectin or E-selectin.

    Techniques: Blocking Assay, Flow Cytometry

    Flow cytometric analysis reveals bromelain cleaves PSGL-1 within its active site in a dose-dependent manner. To analyze neutrophil expression of PSGL-1, the primary ligand for P-selectin, we used two anti-PSGL-1 antibodies that recognize distinct structural motifs within the PSGL-1 active site. (a) Representative data from an analysis with clone KPL-1 reveals an 80% decrease in PSGL-1 expression following treatment with 100 µg/mL bromelain. (b) Representative data from an analysis with clone CHO131 reveals a slight increase followed by a decrease in PSGL-1 expression back to initial levels as bromelain concentrations increase from 0 to 100 µg/mL. (c) The average PSGL-1 expression levels of neutrophils from n = 3–4 donors (±SEM) plotted as a function of bromelain concentration, suggesting that bromelain cleaves PSGL-1 at a position between the two epitopes recognized by the site-specific antibodies.

    Journal: PLoS ONE

    Article Title: Bromelain Decreases Neutrophil Interactions with P-Selectin, but Not E-Selectin, In Vitro by Proteolytic Cleavage of P-Selectin Glycoprotein Ligand-1

    doi: 10.1371/journal.pone.0078988

    Figure Lengend Snippet: Flow cytometric analysis reveals bromelain cleaves PSGL-1 within its active site in a dose-dependent manner. To analyze neutrophil expression of PSGL-1, the primary ligand for P-selectin, we used two anti-PSGL-1 antibodies that recognize distinct structural motifs within the PSGL-1 active site. (a) Representative data from an analysis with clone KPL-1 reveals an 80% decrease in PSGL-1 expression following treatment with 100 µg/mL bromelain. (b) Representative data from an analysis with clone CHO131 reveals a slight increase followed by a decrease in PSGL-1 expression back to initial levels as bromelain concentrations increase from 0 to 100 µg/mL. (c) The average PSGL-1 expression levels of neutrophils from n = 3–4 donors (±SEM) plotted as a function of bromelain concentration, suggesting that bromelain cleaves PSGL-1 at a position between the two epitopes recognized by the site-specific antibodies.

    Article Snippet: HSA-blocked BP-modified substrates were used as control substrates to verify that the observed interactions were due to neutrophil interactions with immobilized P-selectin or E-selectin.

    Techniques: Flow Cytometry, Expressing, Concentration Assay

    Data from flow assays with neutrophils treated with RPMI or bromelain. Bromelain attenuates neutrophil tethering on immobilized P-selectin but has no effect on E-selectin-mediated tethering. (a) Snapshots from representative flow assay videos show neutrophils interacting with substrates presenting immobilized P-selectin. Arrows point to cells interacting with the substrate under conditions of shear stress. (b) Data from primary human neutrophil flow assays with P-selectin substrates reveal that the number of interacting cells is decreased when neutrophils are treated with 50 µg/mL bromelain in RPMI on regions of “high” and “low” immobilized P-selectin. (** p

    Journal: PLoS ONE

    Article Title: Bromelain Decreases Neutrophil Interactions with P-Selectin, but Not E-Selectin, In Vitro by Proteolytic Cleavage of P-Selectin Glycoprotein Ligand-1

    doi: 10.1371/journal.pone.0078988

    Figure Lengend Snippet: Data from flow assays with neutrophils treated with RPMI or bromelain. Bromelain attenuates neutrophil tethering on immobilized P-selectin but has no effect on E-selectin-mediated tethering. (a) Snapshots from representative flow assay videos show neutrophils interacting with substrates presenting immobilized P-selectin. Arrows point to cells interacting with the substrate under conditions of shear stress. (b) Data from primary human neutrophil flow assays with P-selectin substrates reveal that the number of interacting cells is decreased when neutrophils are treated with 50 µg/mL bromelain in RPMI on regions of “high” and “low” immobilized P-selectin. (** p

    Article Snippet: HSA-blocked BP-modified substrates were used as control substrates to verify that the observed interactions were due to neutrophil interactions with immobilized P-selectin or E-selectin.

    Techniques: Flow Cytometry

    Expression of vesicular nucleotide transporter (VNUT) in MEG‐01 cells. (A) The membrane from MEG‐01 cells (20 μ g) was analyzed by Western blot with anti‐hVNUT antibodies. The position of VNUT is marked by an arrow. The positions of molecular markers were also indicated. (B) Double‐labeling immunohistochemistry indicated the localization of VNUT and the marker proteins cellubrevin, MRP4, p ‐selectin, GPllb/GPllla, and NSF in MEG‐01 cells. Bars represent 10 μ m.

    Journal: Physiological Reports

    Article Title: Essential role of vesicular nucleotide transporter in vesicular storage and release of nucleotides in platelets

    doi: 10.14814/phy2.12034

    Figure Lengend Snippet: Expression of vesicular nucleotide transporter (VNUT) in MEG‐01 cells. (A) The membrane from MEG‐01 cells (20 μ g) was analyzed by Western blot with anti‐hVNUT antibodies. The position of VNUT is marked by an arrow. The positions of molecular markers were also indicated. (B) Double‐labeling immunohistochemistry indicated the localization of VNUT and the marker proteins cellubrevin, MRP4, p ‐selectin, GPllb/GPllla, and NSF in MEG‐01 cells. Bars represent 10 μ m.

    Article Snippet: In contrast, the fluorescence of the VNUT antibody corresponded to a lesser extent to that of p ‐selectin, a marker of α granules, GP IIb/GP IIIa, a marker of plasma membranes and cytosol, and a cytosolic protein, NSF (Fig. B).

    Techniques: Expressing, Western Blot, Labeling, Immunohistochemistry, Marker

    HNA2 induces platelet aggregation and activation. (A) Platelets were incubated with ex vivo prepared HMA (1 mg/mL), HNA1 (1 mg/mL), and HNA2 (1 mg/mL), and aggregation was induced with collagen (0.2 μg/mL). Representative reading and bar graph indicate increased aggregation in HNA2‐treated platelets as compared with HNA1 and HMA. Data are expressed as percent of normalized platelet aggregation (n = 3). (B) CD40L and ROS production in healthy platelets was significantly increased when exposed to HNA2 (1 mg/mL). Pretreatment with anti‐CD36 blocking antibody (1 μg/mL) significantly reverses the effect, particularly in HNA2‐exposed platelets. (C) EGTA decreases HNA2‐induced platelet expression of CD40L and ROS production in a dose‐dependent manner. Platelets were pre‐incubated with EGTA, and activation was induced with HNA2 (1 mg/mL). (D) Histogram represents the percent expression of platelets exposed to HNA2 (1 mg/mL) showing increased expression of P‐selectin, PAC‐1, and intracellular calcium as compared with HNA1 (n = 5). (E) Expression of SNARE complex proteins (Syntaxin‐11, SNAP‐23, and VAMP‐8) increases in healthy platelets exposed to HNA2 (1 mg/mL) as compared with HNA1 and HMA. Interestingly, anti‐CD36 blocking antibody (1 μg/mL) reduced the effect of HNA2 over others. Results expressed as mean ± SEM (* P

    Journal: Hepatology Communications

    Article Title: Hyperoxidized Albumin Modulates Platelets and Promotes Inflammation Through CD36 Receptor in Severe Alcoholic Hepatitis

    doi: 10.1002/hep4.1440

    Figure Lengend Snippet: HNA2 induces platelet aggregation and activation. (A) Platelets were incubated with ex vivo prepared HMA (1 mg/mL), HNA1 (1 mg/mL), and HNA2 (1 mg/mL), and aggregation was induced with collagen (0.2 μg/mL). Representative reading and bar graph indicate increased aggregation in HNA2‐treated platelets as compared with HNA1 and HMA. Data are expressed as percent of normalized platelet aggregation (n = 3). (B) CD40L and ROS production in healthy platelets was significantly increased when exposed to HNA2 (1 mg/mL). Pretreatment with anti‐CD36 blocking antibody (1 μg/mL) significantly reverses the effect, particularly in HNA2‐exposed platelets. (C) EGTA decreases HNA2‐induced platelet expression of CD40L and ROS production in a dose‐dependent manner. Platelets were pre‐incubated with EGTA, and activation was induced with HNA2 (1 mg/mL). (D) Histogram represents the percent expression of platelets exposed to HNA2 (1 mg/mL) showing increased expression of P‐selectin, PAC‐1, and intracellular calcium as compared with HNA1 (n = 5). (E) Expression of SNARE complex proteins (Syntaxin‐11, SNAP‐23, and VAMP‐8) increases in healthy platelets exposed to HNA2 (1 mg/mL) as compared with HNA1 and HMA. Interestingly, anti‐CD36 blocking antibody (1 μg/mL) reduced the effect of HNA2 over others. Results expressed as mean ± SEM (* P

    Article Snippet: Platelet Activation Markers and sCD40L Assay Plasma‐citrated blood samples were centrifuged for 15 minutes at 3,000g , and levels of PF‐4 (E‐EL‐H2216; Elabscience, Houston, TX), P‐selectin (E‐EL‐H0917; Elabscience), and sCD40L (E‐EL‐H0035; Elabscience) were measured.

    Techniques: Activation Assay, Incubation, Ex Vivo, Blocking Assay, Expressing

    Purified albumin induces activation and ROS production in healthy platelets. (A) SAH albumin increases the expression of P‐selectin compared with lipopolysaccharide and oxidized low‐density lipoprotein. (B) Platelets were incubated with purified albumin‐HC (Alb‐HC, 1 mg/mL), purified albumin‐AC (Alb‐AC, 1 mg/mL), and purified albumin‐SAH (Alb‐SAH, 1 mg/mL). Platelet aggregation was measured after 30 minutes according to the final protocol at 37°C. A representative recording and bar graph is shown in mean values of three independent experiments, expressed as a percentage of maximal platelet aggregation. (C,D) Histogram showing the up‐regulation of P‐selectin, PAC‐1, and intracellular Ca2+ in platelets exposed to purified Alb‐SAH (1 mg/mL) versus others (percent expression). (E) Increased CD40L and ROS production in platelets exposed to Alb‐SAH compared with others (results shown as percentage of vehicle treatment; n = 3). (F) Representative western blot expression of SNARE complex protein Syntaxin‐11, SNAP‐23, and VAMP‐8 levels in healthy platelets incubated with purified Alb‐HC, Alb‐AC, or Alb‐SAH (1 mg/mL). All values are shown as mean ± SEM (* P

    Journal: Hepatology Communications

    Article Title: Hyperoxidized Albumin Modulates Platelets and Promotes Inflammation Through CD36 Receptor in Severe Alcoholic Hepatitis

    doi: 10.1002/hep4.1440

    Figure Lengend Snippet: Purified albumin induces activation and ROS production in healthy platelets. (A) SAH albumin increases the expression of P‐selectin compared with lipopolysaccharide and oxidized low‐density lipoprotein. (B) Platelets were incubated with purified albumin‐HC (Alb‐HC, 1 mg/mL), purified albumin‐AC (Alb‐AC, 1 mg/mL), and purified albumin‐SAH (Alb‐SAH, 1 mg/mL). Platelet aggregation was measured after 30 minutes according to the final protocol at 37°C. A representative recording and bar graph is shown in mean values of three independent experiments, expressed as a percentage of maximal platelet aggregation. (C,D) Histogram showing the up‐regulation of P‐selectin, PAC‐1, and intracellular Ca2+ in platelets exposed to purified Alb‐SAH (1 mg/mL) versus others (percent expression). (E) Increased CD40L and ROS production in platelets exposed to Alb‐SAH compared with others (results shown as percentage of vehicle treatment; n = 3). (F) Representative western blot expression of SNARE complex protein Syntaxin‐11, SNAP‐23, and VAMP‐8 levels in healthy platelets incubated with purified Alb‐HC, Alb‐AC, or Alb‐SAH (1 mg/mL). All values are shown as mean ± SEM (* P

    Article Snippet: Platelet Activation Markers and sCD40L Assay Plasma‐citrated blood samples were centrifuged for 15 minutes at 3,000g , and levels of PF‐4 (E‐EL‐H2216; Elabscience, Houston, TX), P‐selectin (E‐EL‐H0917; Elabscience), and sCD40L (E‐EL‐H0035; Elabscience) were measured.

    Techniques: Purification, Activation Assay, Expressing, Incubation, Western Blot

    Validation of platelet functionality in SAH. (A) Platelet activation/aggregation in SAH histogram shows the percent expression of PAC‐1, P‐selectin (CD62p), and intracellular Ca +2 (secretion) in SAH and HC. (B) Increased expression (relative change) of various mRNA in SAH platelets linked to platelet and complement activation. Protein expression of Gp2b/3a/β‐actin ratio in platelets of patients with SAH. Results expressed as mean ± SEM (* P

    Journal: Hepatology Communications

    Article Title: Hyperoxidized Albumin Modulates Platelets and Promotes Inflammation Through CD36 Receptor in Severe Alcoholic Hepatitis

    doi: 10.1002/hep4.1440

    Figure Lengend Snippet: Validation of platelet functionality in SAH. (A) Platelet activation/aggregation in SAH histogram shows the percent expression of PAC‐1, P‐selectin (CD62p), and intracellular Ca +2 (secretion) in SAH and HC. (B) Increased expression (relative change) of various mRNA in SAH platelets linked to platelet and complement activation. Protein expression of Gp2b/3a/β‐actin ratio in platelets of patients with SAH. Results expressed as mean ± SEM (* P

    Article Snippet: Platelet Activation Markers and sCD40L Assay Plasma‐citrated blood samples were centrifuged for 15 minutes at 3,000g , and levels of PF‐4 (E‐EL‐H2216; Elabscience, Houston, TX), P‐selectin (E‐EL‐H0917; Elabscience), and sCD40L (E‐EL‐H0035; Elabscience) were measured.

    Techniques: Activation Assay, Expressing

    (A) Release of soluble vWF from uninfected and HCMV-infected HPAEC, as measured by an ELISA. Infected cells secreted 2.5-fold more vWF than uninfected cells at 5 and 7 dpi. (B and C) Secretion of serotonin (B) and soluble P-selectin (C) from platelets

    Journal:

    Article Title: Human Cytomegalovirus Infection of Endothelial Cells Triggers Platelet Adhesion and Aggregation

    doi: 10.1128/JVI.79.4.2211-2220.2005

    Figure Lengend Snippet: (A) Release of soluble vWF from uninfected and HCMV-infected HPAEC, as measured by an ELISA. Infected cells secreted 2.5-fold more vWF than uninfected cells at 5 and 7 dpi. (B and C) Secretion of serotonin (B) and soluble P-selectin (C) from platelets

    Article Snippet: The expression of P-selectin on the platelet surface was increased twofold on platelets incubated with supernatants from HCMV-infected cells compared to uninfected cells (Fig. D).

    Techniques: Infection, Enzyme-linked Immunosorbent Assay

    Macrophages and adhesion molecules at rupture site. ( A – C ) Immunostaining for F4/80 (green) and DAPI (blue) of membrane 24 h after rupture by 20 G needle. Dashed lines indicate amnion ( Am , white), surface of fetal skin (yellow), chorion ( Cho , light blue), and decidua ( Dec , purple). Myo , myometrium. ( A ) Intact fetal membrane. ( B ) Macrophages within healing amnion (arrows). ( C ) Ruptured edge of chorio-decidua. Bars, 50 µm. ( D – F ) H E staining of ruptured membranes. ( D ) An amniotic fluid macrophage (arrow head) attaches to ruptured amnion at 2 h (arrow). ( E and magnified view in F ) Amniotic fluid macrophages (green) attach to amnion surface at 24 h, and mesenchymal cells migrate (arrow head). Note mesenchymal-like shape change of epithelial cells in F . Bars, 50 µm. ( G and H ) Fluorescent in situ hybridization (FISH) of Y chromosome (red) and immunostaining for F4/80 (green) at healing amnion ( G ) and intact myometrium ( H ) at 48 h. Bars, 10 µm. ( I – L ) Macrophage adhesion molecules at the ruptured site. Immunostaining for F4/80 (green), VCAM1 ( I ) or P-selectin ( J , red) and DAPI (blue) at ruptured amnion at 24 h after rupture by 20 G needle. Bars, 50 µm. ( K and L ) Gene expression of VCAM1 ( K ) or P-selectin ( L ) of intact or ruptured fetal membrane with 20 G needle at indicated time. Error bars represent SEM. n = 5–6 fetal membranes from 5–6 pregnant mice in each group. * P

    Journal: Scientific Reports

    Article Title: Healing of Preterm Ruptured Fetal Membranes

    doi: 10.1038/s41598-017-13296-1

    Figure Lengend Snippet: Macrophages and adhesion molecules at rupture site. ( A – C ) Immunostaining for F4/80 (green) and DAPI (blue) of membrane 24 h after rupture by 20 G needle. Dashed lines indicate amnion ( Am , white), surface of fetal skin (yellow), chorion ( Cho , light blue), and decidua ( Dec , purple). Myo , myometrium. ( A ) Intact fetal membrane. ( B ) Macrophages within healing amnion (arrows). ( C ) Ruptured edge of chorio-decidua. Bars, 50 µm. ( D – F ) H E staining of ruptured membranes. ( D ) An amniotic fluid macrophage (arrow head) attaches to ruptured amnion at 2 h (arrow). ( E and magnified view in F ) Amniotic fluid macrophages (green) attach to amnion surface at 24 h, and mesenchymal cells migrate (arrow head). Note mesenchymal-like shape change of epithelial cells in F . Bars, 50 µm. ( G and H ) Fluorescent in situ hybridization (FISH) of Y chromosome (red) and immunostaining for F4/80 (green) at healing amnion ( G ) and intact myometrium ( H ) at 48 h. Bars, 10 µm. ( I – L ) Macrophage adhesion molecules at the ruptured site. Immunostaining for F4/80 (green), VCAM1 ( I ) or P-selectin ( J , red) and DAPI (blue) at ruptured amnion at 24 h after rupture by 20 G needle. Bars, 50 µm. ( K and L ) Gene expression of VCAM1 ( K ) or P-selectin ( L ) of intact or ruptured fetal membrane with 20 G needle at indicated time. Error bars represent SEM. n = 5–6 fetal membranes from 5–6 pregnant mice in each group. * P

    Article Snippet: Primary antibodies used and concentration were as follows: F4/80 (clone BM8, eBioscience, #14-4801, 1:50), Vimentin (D21H3, Cell Signaling, #5741, 1:100), E-cadherin (4A2, Cell Signaling, #14472, 1:50), VCAM1 (EPR5047, Abcam, #134047, 1:100), P-selectin (CD62P, Abcam, #202983, 1:100), NOS2 (iNOS, Abcam, #15323, 1:100), Arg1 (Arginase-1, D4E3M, Cell Signaling, #93668, 1:100), TNF (Abcam, #6671, 1:100), IL-1β (Abcam, #9722, 1:100), Ly-6G (eBioscience, #14-5931, 1:100), CD68 (KP1, Abcam, #955, 1:100), Ki67 (Abcam #15580, 1:100), HSP70 (Abcam #2787, 1:100).

    Techniques: Immunostaining, Staining, In Situ Hybridization, Fluorescence In Situ Hybridization, Expressing, Mouse Assay

    Extracellular CyPA enhances platelet-activation in vitro (A) 8H7-mAb detects CyPA in monocyte as well in platelet lysate (upper line). Afterwards the same membrane was incubated with an anti-CyPA antibody (lower line) to prove the specificity of 8H7-mAb. (B) 8H7-mAb significantly reduces the CyPA-dependent platelet activation. Representative overlays of the p-selectin expression and bar graphs show mean±SEM of P-selectin expression on platelets. * means p ≤ 0.05 vs. CyPA+IgG. (C) Monocyte-platelet aggregate (MPA) formation was analyzed by using double staining with CD42b (as platelets marker) and CD14 (as monocyte marker) as described in material and methods. The platelets were treated as indicated and incubated with monocytes for the MPA formation. Figure shows representative flow cytometry analysis. (n ≤ 6) * means p ≤ 0.05 vs. resting. Right panel shows representative quadrat statistic for the CD14 + CD42 + double positive cells.

    Journal: Thrombosis and haemostasis

    Article Title: Extracellular cyclophilin A augments platelet-dependent thrombosis and thrombo-inflammation

    doi: 10.1160/TH17-01-0067

    Figure Lengend Snippet: Extracellular CyPA enhances platelet-activation in vitro (A) 8H7-mAb detects CyPA in monocyte as well in platelet lysate (upper line). Afterwards the same membrane was incubated with an anti-CyPA antibody (lower line) to prove the specificity of 8H7-mAb. (B) 8H7-mAb significantly reduces the CyPA-dependent platelet activation. Representative overlays of the p-selectin expression and bar graphs show mean±SEM of P-selectin expression on platelets. * means p ≤ 0.05 vs. CyPA+IgG. (C) Monocyte-platelet aggregate (MPA) formation was analyzed by using double staining with CD42b (as platelets marker) and CD14 (as monocyte marker) as described in material and methods. The platelets were treated as indicated and incubated with monocytes for the MPA formation. Figure shows representative flow cytometry analysis. (n ≤ 6) * means p ≤ 0.05 vs. resting. Right panel shows representative quadrat statistic for the CD14 + CD42 + double positive cells.

    Article Snippet: Then the platelets were stained for P-selectin (CD62P, Beckman Coulter, Brea, CA, USA) for 30 minutes and analyzed by flow cytometry.

    Techniques: Activation Assay, In Vitro, Incubation, Expressing, Double Staining, Marker, Flow Cytometry, Cytometry

    Plasma levels of biomarkers on late samples in cases and matched controls. Values indicate medians (full squares in cases and full diamonds in controls), bars indicate interquartile ranges. hsCRP = high-sensitivity C-reactive protein in mg/L; t-PA = tissue plasminogen activator in ng/mL; D-dimer in μg/100 mL; PAI-1 = plasminogen activator inhibitor-1 in μg/10 mL; IL-6 = interleukin-6 in pg/mL; P-selectin = platelet selectin in μg/100 mL. *p=0.002; #p=0.005 from fitting a conditional logistic regression (biomarkers in log scale) comparing cases and controls.

    Journal: BMC Infectious Diseases

    Article Title: The association of high-sensitivity c-reactive protein and other biomarkers with cardiovascular disease in patients treated for HIV: a nested case-control study

    doi: 10.1186/1471-2334-13-414

    Figure Lengend Snippet: Plasma levels of biomarkers on late samples in cases and matched controls. Values indicate medians (full squares in cases and full diamonds in controls), bars indicate interquartile ranges. hsCRP = high-sensitivity C-reactive protein in mg/L; t-PA = tissue plasminogen activator in ng/mL; D-dimer in μg/100 mL; PAI-1 = plasminogen activator inhibitor-1 in μg/10 mL; IL-6 = interleukin-6 in pg/mL; P-selectin = platelet selectin in μg/100 mL. *p=0.002; #p=0.005 from fitting a conditional logistic regression (biomarkers in log scale) comparing cases and controls.

    Article Snippet: Increased risk of a CVD event was also evident for higher values of IL-6 and P-selectin, although the association was weaker than for hsCRP.

    Techniques:

    Modulation of P-selectin correlates with change in monocyte phenotype. The table shows the P-selectin values at baseline and post-vaccination stratified among groups, with P -values calculated using rank ANCOVA. Percentage change from baseline of P-selectin in each group is shown in graph A. B and C report the correlation between change in P-selectin and change in classical CD14 high CD16 − and intermediate CD14 high CD16 + monocyte cell count, respectively. Values are reported as median and IQR. * P = 0.003; ** P = 0.011; *** P = 0.039 vs. baseline within groups using Wilcoxon matched-pairs signed-rank test.

    Journal: Cardiovascular Research

    Article Title: Anti-platelet drugs attenuate the expansion of circulating CD14highCD16+ monocytes under pro-inflammatory conditions

    doi: 10.1093/cvr/cvw089

    Figure Lengend Snippet: Modulation of P-selectin correlates with change in monocyte phenotype. The table shows the P-selectin values at baseline and post-vaccination stratified among groups, with P -values calculated using rank ANCOVA. Percentage change from baseline of P-selectin in each group is shown in graph A. B and C report the correlation between change in P-selectin and change in classical CD14 high CD16 − and intermediate CD14 high CD16 + monocyte cell count, respectively. Values are reported as median and IQR. * P = 0.003; ** P = 0.011; *** P = 0.039 vs. baseline within groups using Wilcoxon matched-pairs signed-rank test.

    Article Snippet: We have previously shown that expression of P-selectin on activated platelets and the consequent formation of monocyte–platelet aggregates (MPA) is a key event in the acquisition of a CD16+ profile by circulating monocytes.

    Techniques: Cell Counting

    Expression of P-selectin (CD62P) on activated platelets plated on different endothelialised collagen substrates (* P

    Journal: Journal of Materials Science. Materials in Medicine

    Article Title: Surface modification of PVDF using non-mammalian sources of collagen for enhancement of endothelial cell functionality

    doi: 10.1007/s10856-015-5651-8

    Figure Lengend Snippet: Expression of P-selectin (CD62P) on activated platelets plated on different endothelialised collagen substrates (* P

    Article Snippet: SnakeSkin® dialysis tubing (10 K MWCO) and P-selectin (CD62P, Clone AK-6) were purchased from Thermo Scientific-Pierce (Rockford, IL, USA).

    Techniques: Expressing

    Platelet EVs increase monocytic cell adhesion and cytokine release. SMC were incubated without or with platelet EV or CD40L in the presence of indicated inhibitors (P-selectin inhibitor, eptifibatide, F1-Fk) or blocking antibody (α-CD40L). Syto13 fluorescently labelled THP-1 were perfused at 0.15 ml/min (3 dynes/cm 2 ) and adherent cells were quantified in six different fields; n = 5–9 (a). Representative micrographs of THP-1 cells adherent to non- or platelet EV-stimulated SMC (b). SMC were incubated with indicated agonists for 24 h and IL-6 release was measured by ELISA; n = 6 (c). P-values were calculated by ANOVA with Tukey’s post-test. Scale bar: 100 µm.

    Journal: Journal of Extracellular Vesicles

    Article Title: Platelet extracellular vesicles induce a pro-inflammatory smooth muscle cell phenotype

    doi: 10.1080/20013078.2017.1322454

    Figure Lengend Snippet: Platelet EVs increase monocytic cell adhesion and cytokine release. SMC were incubated without or with platelet EV or CD40L in the presence of indicated inhibitors (P-selectin inhibitor, eptifibatide, F1-Fk) or blocking antibody (α-CD40L). Syto13 fluorescently labelled THP-1 were perfused at 0.15 ml/min (3 dynes/cm 2 ) and adherent cells were quantified in six different fields; n = 5–9 (a). Representative micrographs of THP-1 cells adherent to non- or platelet EV-stimulated SMC (b). SMC were incubated with indicated agonists for 24 h and IL-6 release was measured by ELISA; n = 6 (c). P-values were calculated by ANOVA with Tukey’s post-test. Scale bar: 100 µm.

    Article Snippet: P-selectin inhibitor was from Bio-Techne (Minneapolis, MN).

    Techniques: Incubation, Blocking Assay, Enzyme-linked Immunosorbent Assay

    Platelet EVs interact with resting or TNFα stimulated SMC via platelet integrin α IIb β 3 or CX3CR1. CFSE-platelet EVs bound to SMC were measured by flow cytometry. Representative histograms of CFSE- platelet EVs bound to resting SMC in the presence of EDTA (filled histogram) or CaCl 2 (line histogram) (a). CFSE-labelled platelet EVs (2 × 10 8 /ml) were co-incubated with resting or TNFα-stimulated SMC in presence or absence of indicated inhibitors (eptifibatide, F1-Fk, P-selectin inhibitor) or blocking antibodies (CD40L) for 30 min at room temperature. Median fluorescence intensity of CFSE-platelet EV bound to resting (b) or TNFα-stimulated SMC (c) and platelet receptors implicated in platelet EV–SMC interaction. p -values were calculated by ANOVA with Sidak’s post-test ( n = 3–7).

    Journal: Journal of Extracellular Vesicles

    Article Title: Platelet extracellular vesicles induce a pro-inflammatory smooth muscle cell phenotype

    doi: 10.1080/20013078.2017.1322454

    Figure Lengend Snippet: Platelet EVs interact with resting or TNFα stimulated SMC via platelet integrin α IIb β 3 or CX3CR1. CFSE-platelet EVs bound to SMC were measured by flow cytometry. Representative histograms of CFSE- platelet EVs bound to resting SMC in the presence of EDTA (filled histogram) or CaCl 2 (line histogram) (a). CFSE-labelled platelet EVs (2 × 10 8 /ml) were co-incubated with resting or TNFα-stimulated SMC in presence or absence of indicated inhibitors (eptifibatide, F1-Fk, P-selectin inhibitor) or blocking antibodies (CD40L) for 30 min at room temperature. Median fluorescence intensity of CFSE-platelet EV bound to resting (b) or TNFα-stimulated SMC (c) and platelet receptors implicated in platelet EV–SMC interaction. p -values were calculated by ANOVA with Sidak’s post-test ( n = 3–7).

    Article Snippet: P-selectin inhibitor was from Bio-Techne (Minneapolis, MN).

    Techniques: Flow Cytometry, Cytometry, Incubation, Blocking Assay, Fluorescence

    Secretion and fibrinogen-binding defects in SLP76 KI platelets in response to CVX. (A) P-selectin surface expression was analyzed by flow cytometry after stimulation with 0.2 nM or 1 nM CVX, or 1 mM AYPGKF. Representative histograms are shown. (B) Platelets were treated as described in A and were stained with 100 μg/ml of Alexa Fluor 647–labeled fibrinogen. EDTA was added to control for nonspecific binding. Mean percentages ± SEM of P-selectin–positive (A) or fibrinogen-bound (B) cells after the indicated stimulations ( n = 4–6 mice per genotype) are shown. *, P

    Journal: The Journal of Experimental Medicine

    Article Title: Requirements of SLP76 tyrosines in ITAM and integrin receptor signaling and in platelet function in vivo

    doi: 10.1084/jem.20080240

    Figure Lengend Snippet: Secretion and fibrinogen-binding defects in SLP76 KI platelets in response to CVX. (A) P-selectin surface expression was analyzed by flow cytometry after stimulation with 0.2 nM or 1 nM CVX, or 1 mM AYPGKF. Representative histograms are shown. (B) Platelets were treated as described in A and were stained with 100 μg/ml of Alexa Fluor 647–labeled fibrinogen. EDTA was added to control for nonspecific binding. Mean percentages ± SEM of P-selectin–positive (A) or fibrinogen-bound (B) cells after the indicated stimulations ( n = 4–6 mice per genotype) are shown. *, P

    Article Snippet: 106 platelets, in the presence of 1 mM Ca2+ , were stimulated with 0.2–1 nM CVX, 0.5–1 mM AYPGKF, or 0.1–20 μM ADP in the presence of CD49b-FITC and P-selectin–PE (BD Biosciences) or fibrinogen-A647 (Invitrogen) for 20 min at 37°C.

    Techniques: Binding Assay, Expressing, Flow Cytometry, Cytometry, Staining, Labeling, Mouse Assay

    Activation of endothelial cells with human anti-HLA I IgG1 triggers adherence of peripheral blood monocytes via FcγRI, P-selectin and ICAM-1.

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

    Article Title: HLA class I antibodies trigger increased adherence of monocytes to endothelial cells by eliciting an increase in endothelial P-selectin and, depending on subclass, by engaging Fc?Rs

    doi: 10.4049/jimmunol.1201434

    Figure Lengend Snippet: Activation of endothelial cells with human anti-HLA I IgG1 triggers adherence of peripheral blood monocytes via FcγRI, P-selectin and ICAM-1.

    Article Snippet: Neutralizing antibodies to integrin β2 (murine IgG1 clone TS1/18, BioLegend), αL (BioLegend), αM (BioLegend), ICAM-1 (sheep IgG, R & D; murine IgG1 clone HCD54, BioLegend), PSGL-1 (murine IgG1 clone KPL-1, BioLegend), P-selectin (clone AK4, murine IgG1, BioLegend; sheep or goat IgG, R & D), FcγRI (clone 10.1, BioLegend), FcγRII (clone AT10, Abcam), FcγRIII (clone 3G8, BioLegend), and Fcα/μR (BioLegend) were used and were of isotypes shown to have low affinity for human FcγRs ( ) to minimize nonspecific blockade of FcγR.

    Techniques: Activation Assay

    HLA I crosslinking by antibodies stimulates Weibel-Palade body exocytosis and increased cell surface P-selectin on endothelial cells.

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

    Article Title: HLA class I antibodies trigger increased adherence of monocytes to endothelial cells by eliciting an increase in endothelial P-selectin and, depending on subclass, by engaging Fc?Rs

    doi: 10.4049/jimmunol.1201434

    Figure Lengend Snippet: HLA I crosslinking by antibodies stimulates Weibel-Palade body exocytosis and increased cell surface P-selectin on endothelial cells.

    Article Snippet: Neutralizing antibodies to integrin β2 (murine IgG1 clone TS1/18, BioLegend), αL (BioLegend), αM (BioLegend), ICAM-1 (sheep IgG, R & D; murine IgG1 clone HCD54, BioLegend), PSGL-1 (murine IgG1 clone KPL-1, BioLegend), P-selectin (clone AK4, murine IgG1, BioLegend; sheep or goat IgG, R & D), FcγRI (clone 10.1, BioLegend), FcγRII (clone AT10, Abcam), FcγRIII (clone 3G8, BioLegend), and Fcα/μR (BioLegend) were used and were of isotypes shown to have low affinity for human FcγRs ( ) to minimize nonspecific blockade of FcγR.

    Techniques:

    ESL hi metastatic PCa MDA cell variants express sLe X - and E-selectin-Ig-reactive PSGL-1. ( A and B ) MDA cell variants were separated into ESL lo and ESL hi based on their E-selectin-binding characteristics. ( C and D ) Flow cytometric analysis of expression

    Journal: Glycobiology

    Article Title: Analysis of glycosyltransferase expression in metastatic prostate cancer cells capable of rolling activity on microvascular endothelial (E)-selectin

    doi: 10.1093/glycob/cwn070

    Figure Lengend Snippet: ESL hi metastatic PCa MDA cell variants express sLe X - and E-selectin-Ig-reactive PSGL-1. ( A and B ) MDA cell variants were separated into ESL lo and ESL hi based on their E-selectin-binding characteristics. ( C and D ) Flow cytometric analysis of expression

    Article Snippet: Wells were coated first in triplicate with 10 μg/mL recombinant human E- or P-selectin-Ig (R & D Systems, Minneapolis, MN) or negative control human IgG for 24 h at 4°C.

    Techniques: Multiple Displacement Amplification, Binding Assay, Flow Cytometry, Expressing

    P-selectin (SELP) is differentially expressed across various cancer types. Comparison of P-selectin expression in various cancer types from data obtained from the TCGA data portal (sorted by the median).

    Journal: eLife

    Article Title: Co-targeting the tumor endothelium and P-selectin-expressing glioblastoma cells leads to a remarkable therapeutic outcome

    doi: 10.7554/eLife.25281

    Figure Lengend Snippet: P-selectin (SELP) is differentially expressed across various cancer types. Comparison of P-selectin expression in various cancer types from data obtained from the TCGA data portal (sorted by the median).

    Article Snippet: To evaluate the internalization mechanism, cells were incubated with 0.1, 1 and 10 µM P-selectin inhibitor (Tocris Bioscience, UK) for 1 hr prior to treatment with the IDCC-labeled conjugates.

    Techniques: Expressing

    Homing of CD4 + CD25 + T reg cells to NALT is partially dependent on PSGL-1 and CD44. (A and B) CFSE-labeled CD4 + CD25 − T conv cells and CMTMR-labeled CD4 + CD25 + T reg cells were treated with or without neutralizing mAb, mixed at a ratio of 1:1, and injected into WT mice intravenously. 2 h later, lymphocytes from the NALT (A) and the PLNs (CLNs; B) were collected and analyzed by flow cytometry after gating on the CFSE- or CMTMR-positive cell fractions. The neutralizing mAbs used were anti–L-selectin (MEL-14), anti–PSGL-1 (4RA10), anti–P-selectin (RB40.34), and anti-CD44 (IM7), and rat IgG as a control. In some experiments, cells were treated with a mixture of MEL-14, 4RA10, and IM7 (mAb Mix). Each bar represents the mean ± SD. n = 4. *, P

    Journal: The Journal of Experimental Medicine

    Article Title: Essential role of peripheral node addressin in lymphocyte homing to nasal-associated lymphoid tissues and allergic immune responses

    doi: 10.1084/jem.20101786

    Figure Lengend Snippet: Homing of CD4 + CD25 + T reg cells to NALT is partially dependent on PSGL-1 and CD44. (A and B) CFSE-labeled CD4 + CD25 − T conv cells and CMTMR-labeled CD4 + CD25 + T reg cells were treated with or without neutralizing mAb, mixed at a ratio of 1:1, and injected into WT mice intravenously. 2 h later, lymphocytes from the NALT (A) and the PLNs (CLNs; B) were collected and analyzed by flow cytometry after gating on the CFSE- or CMTMR-positive cell fractions. The neutralizing mAbs used were anti–L-selectin (MEL-14), anti–PSGL-1 (4RA10), anti–P-selectin (RB40.34), and anti-CD44 (IM7), and rat IgG as a control. In some experiments, cells were treated with a mixture of MEL-14, 4RA10, and IM7 (mAb Mix). Each bar represents the mean ± SD. n = 4. *, P

    Article Snippet: To determine the effects of various mAbs on Treg and Tconv cell homing, CD4+ CD25+ Treg cells and CD4+ CD25− Tconv cells were purified from PLNs, MLNs, and spleens of WT mice using a CD4+ CD25+ Treg cell isolation kit ( > 95% purity; Miltenyi Biotec), labeled with 0.75 µM CMTMR (5-(and-6)-(((4-chloromethyl)benzoyl)amino)tetramethylrhodamine; Lonza) and 0.05 µM CFSE, respectively, and treated with 33 µg/ml (10 µg/mouse) of control rat IgG or anti–PSGL-1 (4RA10; BD), anti–P-selectin (RB40.34; BD), anti-CD44 (IM7; BioLegend), or anti–L-selectin mAb (MEL-14) for 10 min.

    Techniques: Labeling, Injection, Mouse Assay, Flow Cytometry, Cytometry

    Synergistic inhibitory effects of riociguat and iloprost on platelets. (A, B) Diluted PRP was pre‐incubated with riociguat (2 μM, 10 min) and iloprost (6 pM, 2 min) followed by convulxin (5 ng·mL −1 , 2 min) stimulation. (A) PAC‐1 binding and (B) P‐selectin expression were determined as described previously. (C) Diluted PRP was pre‐incubated with riociguat (0.2 μM, 10 min) and iloprost (16 pM, 2 min) followed by ADP (2.5 μM, 2 min) stimulation. PAC‐1 binding was measured. (D) Whole blood was pre‐incubated with riociguat (500 nM, 15 min) and iloprost (500 nM, 2 min) followed by ADP (12.5 μM) stimulation. Aggregation was analysed using multiplate technology. (A–D) Data are presented as mean ± SD. Experiments were carried out at least three times and the ADP/convulxin‐induced sample was considered to be 100%. * P > 0.05, compared to the convulxin‐stimulated or ADP‐stimulated sample; # P

    Journal: British Journal of Pharmacology

    Article Title: The sGC stimulator riociguat inhibits platelet function in washed platelets but not in whole blood) The sGC stimulator riociguat inhibits platelet function in washed platelets but not in whole blood

    doi: 10.1111/bph.13286

    Figure Lengend Snippet: Synergistic inhibitory effects of riociguat and iloprost on platelets. (A, B) Diluted PRP was pre‐incubated with riociguat (2 μM, 10 min) and iloprost (6 pM, 2 min) followed by convulxin (5 ng·mL −1 , 2 min) stimulation. (A) PAC‐1 binding and (B) P‐selectin expression were determined as described previously. (C) Diluted PRP was pre‐incubated with riociguat (0.2 μM, 10 min) and iloprost (16 pM, 2 min) followed by ADP (2.5 μM, 2 min) stimulation. PAC‐1 binding was measured. (D) Whole blood was pre‐incubated with riociguat (500 nM, 15 min) and iloprost (500 nM, 2 min) followed by ADP (12.5 μM) stimulation. Aggregation was analysed using multiplate technology. (A–D) Data are presented as mean ± SD. Experiments were carried out at least three times and the ADP/convulxin‐induced sample was considered to be 100%. * P > 0.05, compared to the convulxin‐stimulated or ADP‐stimulated sample; # P

    Article Snippet: Platelets were labelled with FITC‐conjugated GPIIb/IIIa and P‐selectin antibodies (BD‐Bioscience, Heidelberg, Germany).

    Techniques: Incubation, Binding Assay, Expressing

    Riociguat inhibits platelet activation. PRP was diluted in HEPES buffer to a platelet count of 2 × 10 8 platelets·mL −1 and pre‐incubated with either the indicated concentrations of riociguat for 10 min or iloprost (2 nM, 2 min) before stimulation with convulxin (cvx; 5 ng mL −1 , 2 min) or ADP (2.5 μM, 2 min). (A, C) PAC‐1 binding and (B) P‐selectin expression were determined by flow cytometry. Data are expressed as % of mean fluorescence intensities (MFI) of PAC‐1 or P‐selectin. The convulxin/ADP‐stimulated sample was considered to be 100%. Data are presented as mean ± SD ( n = 6). * P

    Journal: British Journal of Pharmacology

    Article Title: The sGC stimulator riociguat inhibits platelet function in washed platelets but not in whole blood) The sGC stimulator riociguat inhibits platelet function in washed platelets but not in whole blood

    doi: 10.1111/bph.13286

    Figure Lengend Snippet: Riociguat inhibits platelet activation. PRP was diluted in HEPES buffer to a platelet count of 2 × 10 8 platelets·mL −1 and pre‐incubated with either the indicated concentrations of riociguat for 10 min or iloprost (2 nM, 2 min) before stimulation with convulxin (cvx; 5 ng mL −1 , 2 min) or ADP (2.5 μM, 2 min). (A, C) PAC‐1 binding and (B) P‐selectin expression were determined by flow cytometry. Data are expressed as % of mean fluorescence intensities (MFI) of PAC‐1 or P‐selectin. The convulxin/ADP‐stimulated sample was considered to be 100%. Data are presented as mean ± SD ( n = 6). * P

    Article Snippet: Platelets were labelled with FITC‐conjugated GPIIb/IIIa and P‐selectin antibodies (BD‐Bioscience, Heidelberg, Germany).

    Techniques: Activation Assay, Incubation, Binding Assay, Expressing, Flow Cytometry, Cytometry, Fluorescence

    Effect of P-selectin exposure on monocyte phenotype after overnight incubation Platelet-coated plates were either untreated (first column), or pretreated with an isoptype control (second column) or anti-P-selectin (third column). Monocytes were passed through the plates at 0.5 dyne/cm 2 then incubated overnight. The y-axis indicates the percent of monocytes which developed a phenotype consistent with DC differentiation, i.e., membrane HLA-DR + /CD83 + . Data shown are the means (+/- SD) of 3 independent experiments.

    Journal: Transfusion and apheresis science : official journal of the World Apheresis Association : official journal of the European Society for Haemapheresis

    Article Title: Induction of Monocyte-to-Dendritic Cell Maturation by Extracorporeal Photochemotherapy: Initiation via Direct Platelet Signaling

    doi: 10.1016/j.transci.2013.11.008

    Figure Lengend Snippet: Effect of P-selectin exposure on monocyte phenotype after overnight incubation Platelet-coated plates were either untreated (first column), or pretreated with an isoptype control (second column) or anti-P-selectin (third column). Monocytes were passed through the plates at 0.5 dyne/cm 2 then incubated overnight. The y-axis indicates the percent of monocytes which developed a phenotype consistent with DC differentiation, i.e., membrane HLA-DR + /CD83 + . Data shown are the means (+/- SD) of 3 independent experiments.

    Article Snippet: Monocytes were passed through parallel plates coated with high densities (108⩲36/lpf) of platelets that were either untreated (unblocked), or pretreated with either anti-P-selectin or an isotype control.

    Techniques: Incubation

    Effect of p-selectin exposure on monocyte integrins Plastic plates were coated with platelets at the relative density indicated by the x-axis. Platelets were then pretreated with anti p-selectin (dashed line) or an isotype control (gray line), or received no pretretment (black line). Monocytes were passed through the plates at 0.5 dyne/cm 2 and then immediately assessed by flowcytometry for expression of active β1 integrins. The y-axis indicates the percent of monocyte which bound an antibody directed at an epitope only exposed when the integrin is in the open confirmation. Data shown are the means (+/- SD) of 3 independent experiments.

    Journal: Transfusion and apheresis science : official journal of the World Apheresis Association : official journal of the European Society for Haemapheresis

    Article Title: Induction of Monocyte-to-Dendritic Cell Maturation by Extracorporeal Photochemotherapy: Initiation via Direct Platelet Signaling

    doi: 10.1016/j.transci.2013.11.008

    Figure Lengend Snippet: Effect of p-selectin exposure on monocyte integrins Plastic plates were coated with platelets at the relative density indicated by the x-axis. Platelets were then pretreated with anti p-selectin (dashed line) or an isotype control (gray line), or received no pretretment (black line). Monocytes were passed through the plates at 0.5 dyne/cm 2 and then immediately assessed by flowcytometry for expression of active β1 integrins. The y-axis indicates the percent of monocyte which bound an antibody directed at an epitope only exposed when the integrin is in the open confirmation. Data shown are the means (+/- SD) of 3 independent experiments.

    Article Snippet: Monocytes were passed through parallel plates coated with high densities (108⩲36/lpf) of platelets that were either untreated (unblocked), or pretreated with either anti-P-selectin or an isotype control.

    Techniques: Expressing

    The targeting properties of DPP‐hADSCs to balloon‐injured human femoral arteries. a) Schematic illustration of hADSCs dynamic targeting experiment. b) After dynamic culture for 1 h, 5 × 10 −6 m DPP‐modified and unmodified hADSCs binding to injured human femoral arteries were observed by BLI ( n = 4) and c) quantitatively analyzed based on Luc fluorescence intensities. d) The P‐selectin expression and adhesion of hADSCs on the lumen surface of injured arteries in different groups was observed by co‐staining using anti‐P‐selectin and anti‐CD45 antibodies ( n = 3). e) Quantitative analysis of the adhesion of hADSCs per microscopic field from the 5 × 10 −6 m DPP‐modified and unmodified hADSCs groups.

    Journal: Advanced Science

    Article Title: Targeted Repair of Vascular Injury by Adipose‐Derived Stem Cells Modified with P‐Selectin Binding Peptide, Targeted Repair of Vascular Injury by Adipose‐Derived Stem Cells Modified with P‐Selectin Binding Peptide

    doi: 10.1002/advs.201903516

    Figure Lengend Snippet: The targeting properties of DPP‐hADSCs to balloon‐injured human femoral arteries. a) Schematic illustration of hADSCs dynamic targeting experiment. b) After dynamic culture for 1 h, 5 × 10 −6 m DPP‐modified and unmodified hADSCs binding to injured human femoral arteries were observed by BLI ( n = 4) and c) quantitatively analyzed based on Luc fluorescence intensities. d) The P‐selectin expression and adhesion of hADSCs on the lumen surface of injured arteries in different groups was observed by co‐staining using anti‐P‐selectin and anti‐CD45 antibodies ( n = 3). e) Quantitative analysis of the adhesion of hADSCs per microscopic field from the 5 × 10 −6 m DPP‐modified and unmodified hADSCs groups.

    Article Snippet: The sections were immunofluorescent stained with FITC anti‐human CD90 (BioLegend, 328107) and anti‐P‐selectin (sc‐8419, Santa Cruz Biotechnology, USA) to assess the targeting property of DPP‐hADSCs to the injured human femoral arteries.

    Techniques: Modification, Binding Assay, Fluorescence, Expressing, Staining