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To evaluate the appropriateness of the screening strategy for healthcare personnel (HCP) during a hospital-associated Middle East Respiratory Syndrome (MERS) outbreak, we performed a serologic investigation in 189 rRT-PCR–negative HCP exposed and assigned to MERS patients. Although 20%–25% of HCP experienced MERS-like symptoms, none of them showed seroconversion by plaque reduction neutralization test (PRNT).
Many transgenic domestic animals have been developed to produce therapeutic proteins in the mammary gland, and this approach is one of the most important methods for agricultural and biomedical applications. However, expression and secretion of a protein varies because transgenes are integrated at random sites in the genome. In addition, distal enhancers are very important for transcriptional gene regulation and tissue-specific gene expression. Development of a vector system regulated accurately in the genome is needed to improve production of therapeutic proteins. The objective of this study was to develop a knock-in system for expression of human fibroblast growth factor 2 (FGF2) in the bovine β-casein gene locus. The F2A sequence was fused to the human FGF2 gene and inserted into exon 3 of the β-casein gene. We detected expression of human FGF2 mRNA in the HC11 mouse mammary epithelial cells by RT-PCR and human FGF2 protein in the culture media using western blot analysis when the knock-in vector was introduced. We transfected the knock-in vector into bovine ear fibroblasts and produced knock-in fibroblasts using the clustered regularly interspaced short palindromic repeats (CRISPR)/Cas9 system. Moreover, the CRISPR/Cas9 system was more efficient than conventional methods. In addition, we produced knock-in blastocysts by somatic cell nuclear transfer using the knock-in fibroblasts. Our knock-in fibroblasts may help to create cloned embryos for development of transgenic dairy cattle expressing human FGF2 protein in the mammary gland via the expression system of the bovine β-casein gene.
The activation of PPARγ by ligands, including conjugated linoleic acid (CLA) isomers, plays an important role in the immune response. Among CLA isomers, trans-10, cis-12 (t10c12)-CLA is known to participate in the modulation of pro-inflammatory cytokine secretion. The aim of the present study was to assess the effect of t10c12-CLA on PPARγ activation, NF-κB activation and TNF-α expression in lipopolysaccharide (LPS)-naive and LPS-stimulated porcine peripheral blood mononuclear cells (PBMC). In addition, the effect of PPARγ inhibition on NF-κB activation and TNF-α expression in porcine PBMC was examined. t10c12-CLA was found to increase TNF-α expression and NF-κB activity in LPS-naive porcine PBMC. In contrast, t10c12-CLA decreased TNF-α expression and NF-κB activity in LPS-stimulated porcine PBMC. t10c12-CLA up-regulated PPARγ activity and mRNA expression in both LPS-naive and LPS-stimulated porcine PBMC. GW9662, a PPARγ antagonist, completely negated the modulating effects of t10c12-CLA on TNF-α expression and NF-κB activity in both LPS-naive and LPS-stimulated porcine PBMC. These results suggest that t10c12-CLA can modulate TNF-α production and NF-κB activation by a PPARγ-dependent pathway in porcine PBMC.
We introduce a simple preparation method for ultrathin carbon support
films that is especially useful for high-resolution electron microscopy
(HREM) of nanoparticles. Oxidized iron nanoparticles were used as a test
sample in a demonstration of this method. The film qualities are discussed
on the basis of electron-energy-loss spectroscopy (EELS) and image
analysis techniques such as thickness maps and histograms. We carried out
a comparison between the homemade and commercial film qualities. The
relative thickness of the homemade support films was 0.6 times less than
that of the commercial films, which was calculated from the EELS analysis,
whereas the thicknesses of both carbon support films varied within about
3%. The percentage of the observable area was about 67 ± 7.6% of
the support film. This was about twice as large as the commercial film (32
± 9.3%). The HREM image of the sample prepared with our support
film improved 9% in brightness and 15% in contrast compared with images
obtained with the commercial support.
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