Test characteristics of Determine HBsAg determined in comparison with a reference test in adult and antiretroviral-naïve HIV-1 positive patients in Ifakara, Tanzania.

<p>Abbreviations: CI, confidence interval; FN, false negative; FP, false positive; NPV, negative predictive value; PPV, positive predictive value; TN, true negative; TP, true positive. Agreement is measured between two independent readings of Determine HBsAg.</p

Enrollment and outcome.

<p>Study profile of the evaluation of Determine HBsAg against a reference HBsAg enzyme immuno assay.</p

Characteristics of the study population.

<p>Abbreviations: ALT, alanine aminotransferase; ARV, antiretroviral; HBe-Ag, Hepatitis B envelope antigen; HBsAg, Hepatitis B surface antigen; HCV, Hepatitis C virus; y, years.</p><p>Data are presented as median (interquartile range) for continuous variables and as count (column percentage) for categorical variables. P values hypothesis testing between HBsAg positive and HBsAg negative are derived from Mann-Whitney U test for continuous and χ2-test for categorical variables.</p

Sirt1 expression is reduced in patients suffering from atherosclerotic disease. A.

<p>HDL levels are reduced in patients suffering from CAD or ACS as compared to the healthy controls. <b>B.</b> Flow cytometry analysis demonstrates the purity of isolated monocytes. <b>C.</b> Sirt1 mRNA expression in relation to 18S rRNA in peripheral blood monocytes isolated from healthy subjects, from patients with angiographically-confirmed CAD and patients presenting with an ACS. <b>D.</b> The expression of interleukin-6 (IL-6), a negatively regulated Sirt1-dependent marker, is increased in patients with impaired Sirt1-expression.</p

Clinical characteristics of the three patient groups.

*<p>0.05* CADnts with CAD and ACS,ACS group)erosclerosis looses its cardioprotectice properties.**</p>*<p>ACS vs CAD.</p>†<p>Healthy vs CAD.</p>‡<p>Healthy vs ACS.</p

HDL regulates Sirt1 expression. A.

<p>Sirt1 protein expression in THP1 cells after incubation with HDL from healthy subjects or patients suffering from CAD and ACS, respectively. <b>B.</b> PON1 function, as measured by PON1 arylesterase activity, is significantly reduced in the CAD and ACS group.</p

Schematic presentation of the selection strategy.

<p>a) The phage library, containing billions of different phages, was amplified from the bacterial stock. ScFv are fused to minor coat protein III and as such displayed on the phage surface. b) In a subtraction step, the phage library was incubated with secretome from the healthy control tissue. Binders to common proteins were removed in this way. c) Phages that did not bind to the control secretome were incubated with the atherosclerotic secretome in this panning step. d) Unbound phages were washed off, and e) bound phages were eluted and used to infect a suitable <i>E.coli</i> strain (<i>E.coli</i> TG1). f) Bacteria infected with the selected and eluted phages were plated on large agar plates. g) To further enrich for phages that specifically bind to the atherosclerotic secretome, the selection round was repeated. h) Single colonies were induced to produce monoclonal phages. i) Monoclonal phages were analysed for their reactivity with atherosclerotic versus control secretomes in ELISA. In total, six different selections were performed. For each separate selection the control and atherosclerotic secretomes from one individual patient were used. In order not to loose diversity, only two subtractive panning rounds were performed for each selection. To analyse whether enrichment of atherosclerotic secretome-specific binders had taken place, polyclonal phage pools (as obtained in step a) after each subtractive panning round (and of the unselected library as a control) were analysed in ELISA for reactivity with atherosclerotic and control secretomes.</p

Thrombendarterectomy tissue for secretome production and immunohistochemistry.

<p>a) Tissue sample as it was received from the surgical department. b) The tissue was separated into the plaque part (I) for production of the plaque secretome, and the best preserved part (II) for production of the control secretome.</p

Detection of JUP isoforms in plasma from PAOD patients with atherosclerosis and in plasma from a swine model of myocardial infarction without atherosclerosis and plaque rupture.

<p>a) Western blot containing recombinant GST-tagged JUP (lane 1, 107 kD), ACS plasma (lane 2), control plasma (lane 3) and plasma from four PAOD patients (lanes 4 to 7) were detected with mAb 2G9 (which replaced 2C9). JUP-55 and JUP-30 are clearly detected besides JUP-81. b) Western blot containing recombinant GST-tagged JUP (lane 1, 107 kD), ACS plasma (lane 2), control plasma (lane 3) and plasma samples from swine before ligation (lanes 4 and 7), three hours after ligation (lanes 5 and 8) and three days after ligation (lanes 6 and 9) were detected with mAb 2G9. JUP-81 was not detected in the swine samples, whereas JUP-30 and a protein band with a slightly larger molecular weight were detected with similar intensities before and after ligation.</p

Schematic overview of the four different JUP isoforms.

<p>JUP-81 and JUP-63 have an identical N-terminus (the N-terminal 303 amino acids), and JUP-63 further shares its C-terminus with cytokeratin 19 (K1C19). The sequences of JUP-55 and JUP-30 are currently unknown but they contain epitopes that are shared with JUP-81 and are thought to be located in the N-terminal region of native JUP. JUP-30 lacks (at least) the N-terminal 50 amino acids of JUP-81. JUP-81, which is also referred to as gamma-catenin, is furthermore homologous to beta-catenin. Amino acids 1, 303 and 745 of JUP-81 are indicated with arrows.</p