12 research outputs found

    Shows the receiver operating curve analysis of the LightCycler SeptiFast molecular diagnostic method for the detection of bacterial and fungal infection (Figure 1.1), bacterial infection alone (Figure 1.2), and fungal infection alone (Figure 1.3).

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    <p>Solid line, solid square, inner dashed line and outer dotted line represents hierarchical summary receiver operating characteristic (HSROC) curve, bivariate summary estimate, 95% confidence ellipse, and 95% prediction ellipse. Symbol area is proportional to study size.</p

    Summary of the subgroup analysis of the 34 included studies.

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    <p>AUROC = area under receiver operating characteristic curve. OR = odds ratio. CDI = clinically documented infection. ICU = intensive care unit.</p

    Shows forest plot of the diagnostic odds ratios of studies using the LightCycler SeptiFast diagnostic method to detect bacterial and fungal infection (Figure 2.1), bacterial infection alone (Figure 2.2), and fungal infection alone (Figure 2.3).

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    <p>Shows forest plot of the diagnostic odds ratios of studies using the LightCycler SeptiFast diagnostic method to detect bacterial and fungal infection (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062323#pone-0062323-g002" target="_blank">Figure 2</a>.1), bacterial infection alone (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062323#pone-0062323-g002" target="_blank">Figure 2</a>.2), and fungal infection alone (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062323#pone-0062323-g002" target="_blank">Figure 2</a>.3).</p

    Characteristics of the 34 included studies.

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    <p>NA =  non-available. ED = Emergency Department. ICU = Intensive Care Unit. CDI = clinically documented infection. LDI = laboratory-documented infection. BC = blood culture. Sen. = sensitivity. Spe. = specificity.</p

    Impact of thio-redox state on matriptase activation.

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    <p>184 A1N4 cells were homogenized in phosphate buffer pH(<i>A</i>) The insoluble fraction was re-suspended and incubated in phosphate buffer pH 6.0 for 20 min either on ice as a negative control (lane 1) or at room temperature as a positive control (lane 2). The insoluble fraction was also mixed with the cytosolic fraction alone (lane 3) or in the presence of various concentrations of DTNB (lanes 4, 5, and 6). Cytosolic fractions were also prepared from LNCaP and PC3 prostate cancer cells and either dialyzed or stored at 4°C for three days. The insoluble fraction prepared from 184 A1N4 cells, was incubated with the untreated, stored (S.), or dialyzed (D.) cytosolic fraction from LNCaP human prostate cells (lanes 7, 8, and 9) and PC3 prostate cancer cells (lanes 10 and 11). (<i>B</i> and <i>C</i>) The insoluble fraction of 184 A1N4 cells was incubated in phosphate buffer pH 6.0 for 20 min either on ice as a negative control (lane 1) or at room temperature as a positive control (lane 2). The insoluble fraction was also incubated with the cytosolic fraction alone (lane 3) or in the presence of increasing concentrations of oxidized glutathione GSSG (<i>B</i>, lanes 4, 5, and 6) or NEM (<i>C</i>, lanes 4, 5, and 6). Lysates were prepared from all incubation conditions and assayed by immunoblot analyses for matriptase activation.</p

    Matriptase zymogen activation can be induced by metal ions.

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    <p>(<i>A</i> and <i>D</i>) 184 A1N4 cells were incubated with increasing concentrations of CoCl<sub>2</sub> (<i>A</i>) and CdCl<sub>2</sub> (<i>D</i>), as indicated, at 37°C for 3 hrs in a CO<sub>2</sub> incubator. (<i>B</i> and <i>E</i>) 184 A1N4 cells were incubated with 200 μM CoCl<sub>2</sub> (<i>B</i>) or 40 μM CdCl<sub>2</sub> (<i>E</i>) at 37°C in a CO<sub>2</sub> incubator for indicated times. (<i>C</i> and <i>F</i>) 184 A1N4 cells were incubated with 200 μM CoCl<sub>2</sub> (C) or 40 μM CdCl<sub>2</sub> (F) in the presence of increasing concentrations of N-acetylcysteine (NAC), as indicated, at 37°C in a CO<sub>2</sub> incubator for 2 hrs. Cell lysates were prepared and assayed by immunoblot analyses for matriptase activation using mAb M24 as before.</p

    Knockdown of matriptase expression increases susceptibility to CdCl<sub>2</sub> toxicity.

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    <p>(<i>A</i>) Evaluation of matriptase and HAI-1 expression in matriptase knockdown (KD) and non-target (NT) control cells using immunoblot analyses of cell lysates to detect total matriptase (MTP) or HAI-1 (HAI-1). (<i>B</i>) Survival rates of matriptase knockdown cells (open circles) in comparison to non-target (NT) control cells (closed circles). Each cell pool was exposed to various concentrations of CdCl<sub>2</sub>, and survival ratios determined by crystal violet staining assay. The results from one representative experiment out of four replicates are shown.</p

    Time and pH-dependence of matriptase zymogen autoactivation in cell-free setting.

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    <p>The insoluble fractions of cell homogenates prepared from 184 A1N4 mammary epithelial cells were exposed to phosphate buffers at pH(A), pH 7.0 (B) or pH 6.5 (C) at room temperature for the indicated time. Lysates were prepared and assayed by immunoblot analyses for matriptase with mAb M24 (which recognizes the 70-kDa matriptase zymogen and 120-kDa activated matriptase-HAI-1 complex) or for HAI-1 with mAb M19 (which recognizes the 55-kDa HAI-1 and 120-kDa activated matriptase-HAI-1 complex). Note that both antibodies also recognize degraded forms of the activated matriptase-HAI-1 complex. (D) Kinetics for induction of matriptase activation in cell-free homogenates. Representative data showing the ratio of activated matriptase relative to total matriptase (activated plus zymogen matriptase) for each pH plotted against time using Image J.</p
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