2,263 research outputs found

    Evaluation of the first automated thyroglobulin assay

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    The aim of this study was to investigate technical and analytical performance of the first automated thyroglobulin (Tg) assay (DPC-Immulite(R); Diagnostic Products Corporation, Los Angeles, USA). In imprecision studies using several human serum pools ranging from 21 to 58 replicates, a coefficient of variation of 9.0 % was obtained at a mean Tg concentration of 0.84 ng/ml and of 6.1 % at a Tg concentration of 62.1 ng/ml. In a method comparison with a non-automated assay (BRAHMS LUMItest Tg(R), BRAHMS, Berlin, Germany) using 383 sera of 303 patients with thyroid carcinoma, regression analysis according to Passing and Bablock yielded in the following equation: Immulite Tg=1.6 x BRAHMS Tg - 0.1 ng/ml (Pearson's r=0.979). Sera obtained from 59 patients with thyroid carcinoma enabled comparative follow-up studies; in all cases qualitative agreement was found with regard to increase or decrease of serum Tg; in eight cases, however, Tg was detected with the Immulite assay but not with the BRAHMS assay. Further follow-up proved the presence of thyroid tissue in these patients. From these and further methodological data (dilution linearity, interference studies, carry-over study, high-dose hook properties, and short report time) it is concluded that the DPC-Immulite Tg assay meets the requirements of routine diagnostic use

    <i>Sfswap<sup>Tg/Tg</sup>, Jag1<sup>+/−</sup></i> mutants have enhanced phenotypes in the cochlea.

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    <p>Measurements of cochlear lengths reveal that <i>Sfswap<sup>Tg/Tg</sup>, Jag1<sup>+/−</sup></i> mutants are significantly shorter than <i>Sfswap<sup>Tg/Tg</sup></i> or <i>Jag1<sup>+/−</sup></i> mutants. Similarly, at the base and mid, <i>Sfswap<sup>Tg/Tg</sup>, Jag1<sup>+/−</sup></i> mutants have significantly fewer outer hair cells (OHC) than <i>Sfswap<sup>Tg/Tg</sup></i> or <i>Jag1<sup>+/−</sup></i> mutants alone.</p

    β-catenin protein expression in TG explants of uninfected mice.

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    TG from uninfected mice were explanted 4 or 8 hours with or without DEX, subsequently formalin fixed and paraffin embedded. TG thin sections were stained with a β-catenin antibody as described in Fig 1. Arrows denote β-catenin positive neurons and magnification of sections is 600x. Images are representative of two independent animal experiments.</p

    β-catenin expression is increased in latently infected TG.

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    TG were harvested from uninfected mice (U panel) or mice latently infected with either wt HSV-1 or dLAT2903, a LAT-null mutant (LAT-/-). TG were dissected, formalin fixed, and paraffin embedded (n = 5/group). IHC was performed as described in the methods and materials using a rabbit polyclonal CTNNB1 (β-catenin) primary antibody (LifeSpan Bio, LS-C31415, diluted 1:250). Arrows denote β-catenin positive neurons. Sections were imaged at 600x magnification. Images are representative of two independent animal experiments.</p

    Bulk viscosity in F(T, TG) gravity

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    The present paper is devoted to exploring the effect of bulk viscosity in the context of F(T, TG) gravity. We consider a time-dependent viscosity model with a particular expression of Hubble parameter. We evaluate viscous effective equation of state parameter for three well-known F(T, TG) models. The behavior of the accelerated expanding universe is explored graphically through the viscous equation of state parameter. This parameter indicates the phantom-dominated era as well as crosses the phantom divide line for all three models. We conclude that the universe shows a transition from quintessence to phantom region in the presence of bulk viscosity.The presentation of the authors' names and (or) special characters in the title of the pdf file of the accepted manuscript may differ slightly from what is displayed on the item page. The information in the pdf file of the accepted manuscript reflects the original submission by the author

    Kidney Function in SVCT2-Tg mice.

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    <p>Excreted (A) ASC and (B) albumin were measured in urine samples with the results normalized to creatinine. Data shown are mean<u>+</u>S.E.M for wild-type and SVCT2-Tg mice separately for male (white bars) and female (purple bars) mice. ** p<0.01 compared to wild-type control. N = 5−6 mice per group. (C) 2 µm sections stained with hemotoxylin and eosin (H&E) for comparison between genotypes. Glomeruli, proximal tubules and distal tubules are all clearly visible but no changes were observable in SVCT2-Tg mice (right panel) compared to wild-types (left panel). Images taken at 20X magnification.</p

    () Topology of unimolecular G-quadruplex adopted by dG(TG) and -ion-binding sites

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    <p><b>Copyright information:</b></p><p>Taken from "NMR evaluation of ammonium ion movement within a unimolecular G-quadruplex in solution"</p><p>Nucleic Acids Research 2007;35(8):2554-2563.</p><p>Published online 4 Apr 2007</p><p>PMCID:PMC1895886.</p><p>© 2007 The Author(s)</p> The three binding sites are labeled as O, I and O. The guanine bases are shown as numbered rectangles, where cyan and magenta rectangles represent nucleobases in and conformation, respectively. () Birds-eye view of a ion above an individual G-quartet

    Competition of the 13 bp substrate duplexes and the Tg-containing duplexes in the Endo III reaction

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    <p><b>Copyright information:</b></p><p>Taken from "Synthesis and characterization of oligonucleotides containing 2′-fluorinated thymidine glycol as inhibitors of the endonuclease III reaction"</p><p>Nucleic Acids Research 2006;34(5):1540-1551.</p><p>Published online 17 Mar 2006</p><p>PMCID:PMC1409675.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> The P-labeled substrates without fluorine were incubated with Endo III in the presence of the competitors containing Tg. The amounts of the nicked products (standardized to those without the competitors) were plotted against the concentrations of the competitor. Open circles, P-5-Tg + 5-Tg; filled circles, P-5-Tg + 5-Tg; open triangles, P-5-Tg + 5-Tg; filled triangles, P-5-Tg 5-Tg

    DNA fusion gene vaccination mobilizes effective anti-leukemic cytotoxic T lymphocytes from a tolerized repertoire

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    The majority of known human tumor-associated antigens derive from non-mutated self proteins. T cell tolerance, essential to prevent autoimmunity, must therefore be cautiously circumvented to generate cytotoxic T cell responses against these targets. Our strategy uses DNA fusion vaccines to activate high levels of peptide-specific CTL. Key foreign sequences from tetanus toxin activate tolerance-breaking CD4+ T cell help. Candidate MHC class Ibinding tumor peptide sequences are fused to the C terminus for optimal processing and presentation. To model performance against a leukemia-associated antigen in a tolerized setting, we constructed a fusion vaccine encoding an immunodominant CTL epitopederived from Friend murine leukemia virus gag protein (FMuLVgag) and vaccinated tolerant FMuLVgag-transgenic (gag-Tg) mice. Vaccination with the construct induced epitopespecificIFN-c-producing CD8+ T cells in normal and gag-Tg mice. The frequency and avidity of activated cells were reduced in gag-Tg mice, and no autoimmune injury resulted. However, these CD8+ T cells did exhibit gag-specific cytotoxicity in vitro and in vivo. Also, epitope-specific CTL killed FBL-3 leukemia cells expressing endogenous FMuLVgag antigen and protected against leukemia challenge in vivo. These results demonstrate a simple strategy to engage anti-microbial T cell help to activate epitope-specific polyclonal CD8+ T cell responses from a residual tolerized repertoire
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