35 research outputs found

    Blocking C5L2 decreased MPO concentration in the supernatant of C5a-primed neutrophils.

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    <p>MPO concentration was measured in the supernatant of C5a-primed neutrophils by ELISA. A: Human neutrophils were isolated and incubated with different concentrations of C5a for 15 min (n = 3). MPO concentration was measured in the supernatant of C5a-primed neutrophils and compared with non-stimulated cells. Bars denote means±SD of MPO concentration. B: Blocking C5L2 reduced MPO concentration in the supernatant of C5a-primed neutrophils. Bars represent mean±SD of MPO concentration, measured in the neutrophils supernatant of 6 independent experiments.</p

    Blocking C5L2 decreased C5a-primed neutrophils for ANCA-induced respiratory burst.

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    <p>Neutrophil respiratory burst induced by patient-derived MPO-ANCA (A) or PR3-ANCA (C) was measured by conversion of dihydrorhodamine-123 (DHR-123) to rhodamine-123 in C5a-primed cells in the presence and absence of blocking C5L2 mAb. Bars represent mean±SD of 4 MPO-ANCA and 2 PR3-ANCA IgG preparations, each measured on neutrophils of 10 independent experiments and donors. B and D: representative histograms showing effects of the blocking C5L2 mAb at 2.5 µg/ml, 5 µg/ml or 10 µg/ml on MPO-ANCA positive IgG or PR3-ANCA positive IgG-induced respiratory brust in C5a-primed neutrophils.</p

    No effect of CD88 expression by pre-incubation with blocking C5L2 antibody.

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    <p>No effect of CD88 expression by pre-incubation with blocking C5L2 antibody.</p

    Blocking C5L2 decreased C5a-primed neutrophils for ANCA-induced degranulation.

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    <p>ANCA-induced neutrophil degranulation was determined by measuring the lactoferrin concentrations in the supernatant. Blocking C5L2 reduced ANCA-induced lactoferrin release. Bars represent mean±SD of 4 MPO-ANCA and 2 PR3-ANCA preparations, measured on neutrophils of 10 donors.</p

    Crystal Structures and Chemical Bonding of Magnesium Carbide at High Pressure

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    Recent studies of the magnesium carbide (Mg–C) system under pressure were motivated by the successful high-pressure and high-temperature synthesis of Mg<sub>2</sub>C and Mg<sub>2</sub>C<sub>3</sub>. Here, we systematically investigate the high-pressure structures and chemical bonding of the Mg<sub>2</sub>C, Mg<sub>2</sub>C<sub>3</sub>, and MgC<sub>2</sub> system using the swarm optimization technique in combination with first-principles electronic structure methodology. The structural evolution with pressure of the Mg–C systems clearly shows a systematic trend with a progressive increase of electron donation from the Mg to C. To accommodate the electrons, the C valence sp orbitals rebybridized continually and adopted different modes of chemical bonding. We demonstrated that the evolution of the electronic and crystal structures can be explained from a Zintl–Klemen charge-transfer concept. Therefore, at sufficiently high pressure metallic MgC<sub>2</sub> and Mg<sub>2</sub>C transformed to semiconductors, while Mg<sub>2</sub>C<sub>3</sub> undergoes an insulator–metal transition. The present results established the richness of carbon bonding of different stoichiometries under high pressure

    Blocking CD88 decreased ANCA antigen translocation, ANCA-induced respiratory burst and degranulation in C5a-primed neutrophils.

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    <p>A: blocking CD88 reduced MPO concentration in the supernatant of C5a-primed neutrophils. Bars represent mean±SD of MPO concentration, measured in the neutrophils supernatant of 6 independent experiments. B: blocking CD88 decreased C5a-primed neutrophils expression of membrane-bound PR3 (mPR3). C and D: blocking CD88 decreased C5a-primed neutrophils for ANCA-induced respiratory burst. E and F: blocking CD88 decreased C5a-primed neutrophils for ANCA-induced degranulation. Bars represent mean±SD of repeated measurements on neutrophils of 6 independent experiments and donors.</p

    Effects of the p38MAPK inhibitor, ERK and PI3K inhibitor on translocation of PR3.

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    <p>A: Neutrophils were incubated with the SB202190, PD98059, LY294002 or the inhibitors mixture or vehicle for 30 min prior to incubation with C5a (100 ng/ml). Bars represent mean±SD of repeated measurements on neutrophils of 10 independent experiments and donors. T test was used for comparison. B-D: a representative histogram of effects of the above inhibitors on translocation of PR3 upon C5a priming.</p

    C5a increased membrane expression of PR3 (mPR3) on neutrophils.

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    <p>Human neutrophils were isolated and incubated with different concentrations of C5a for 15 min. mPR3 and mMPO were measured with flow cytometry and compared with non-stimulated cells. A: mPR3 expression compared with non-primed nertrophils (n = 11). B: mMPO expression compared with non-primed neutrophils (n = 11). Bars denoted means±SD of mPR3 or mMPO expression (MFI). Differences of MFI between groups were assessed using the t test.</p

    A Mild and Reliable Method to Label Enveloped Virus with Quantum Dots by Copper-Free Click Chemistry

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    Real-time tracking of the dynamic process of virus invasion is crucial to understanding the infection mechanism. For successful tracking, efficient labeling methods are indispensable. In this paper, we report a mild and reliable method for labeling viruses, especially with regard to easily disabled enveloped viruses. The copper-free click chemistry has been used to label enveloped viruses with quantum dots (QDs) by linking virions modified with azide to the QDs derived with dibenzocyclooctynes (DBCO). Both vaccinia virus (VACV) and avian influenza A virus (H9N2) can be specifically and rapidly labeled under mild conditions, with a labeling efficiency of more than 80%. The labeled virions were of intact infectivity, and their fluorescence was strong enough to realize single-virion tracking. Compared to previously reported methods, our method is less destructive, reliable, and universal, without specific requirements for the type and structure of viruses to be labeled, which has laid the foundation for long-term dynamic visualization of virus infection process
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