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ABSTRACT Poly(ionic liquid)s have been demonstrated as high efficient CO2 absorbents. In the current study, a kind of poly(ionic liquid)s, Poly[2-(methacryloyloxy)-ethyl] trimethylammonium tetrafluoroborate (P[MATMA][BF4]) was used to functionalize graphene oxide (GO). The hybrid in which P[MATMA][BF4] was covalently bonded on GO platelets was prepared by a simple method, that is, traditional radical polymerization. The characterizations based on transmission electron microscopy, scanning electron microscope, Fourier transform infrared spectroscopy, Raman spectroscopy, X-ray diffraction, and X-ray photoelectron spectroscopy demonstrated the graft of P[MATMA][BF4] on GO. N2 adsorption measurements indicated that P[MATMA][BF4] also greatly increased the specific surface area of GO. Due to the higher specific surface area and the CO2 affinity of P[MATMA][BF4], the GO-P[MATMA][BF4] hybrid exhibited a much higher CO2 adsorption capacity compared with GO, GO-NH2, and P[MATMA][BF4]. Their study showed that the combinations of poly(ionic liquid)s and GO could be promising CO2 absorbents. © 2016 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 44592. [ABSTRACT FROM AUTHOR]

B7H4 is a member of the B7 family, which is expressed on antigen-presenting cells (APCs) and which negatively regulates the immune response of T cells through the inhibition of their proliferation, cytokine production, and cell cycle progression. Acyl-CoA thioesterase 4 (ACOT4) is an isoform of the ACOTs family that catalyzes the hydrolysis of fatty acyl-CoA to CoA-SH and free fatty acids. An abnormal metabolism of lipids and fatty acids is observed during tumor progression. In our study, a tissue microarray was constructed from 288 cases of gastric adenocarcinoma (GC). ACOT4 expression in cancer-associated fibroblasts (CAFs) and B7H4 expression in cancer tissues were analyzed by immunohistochemistry. The correlations among B7H4 in GC cells, ACOT4 in CAFs, and survival were analyzed. The results showed that the expression rate of B7H4 in tumor cells and ACOT4 in CAFs in 288 tissues was 71.9% (207/288) and 26.4% (76/288), respectively, and a Kaplan-Meier survival analysis showed that a low expression of ACOT4 in fibroblasts was positively correlated with poor survival. However, in a subgroup showing a high ACOT4 expression, the overall survival rate was associated with a high expression of B7H4 and correlated with poor prognosis in GC. In conclusion, ACOT4 expression in CAFs could be an independent prognostic factor for GC patients, and the co-expression with B7H4 in cancer tissues was significantly correlated with GC patients' prognosis. This evidence can represent a comprehensive prediction and a targeted therapy for gastric cancer patients. Tumor immunotherapy targeting might be affected by tumor microenvironment metabolism., Competing Interests: None., (IJCEP Copyright © 2019.)

The aim of this study was to study the expression level of interferon-γ (IFN-γ) and monocyte chemoattractant protein-1 (MCP-1) in peripheral blood and its auxiliary diagnostic value in active tuberculosis. A chemiluminescence enzyme immunoassay method was used to detect the levels of IFN-γ and MCP-1 in peripheral blood. Then the receiver operating characteristic curve were drawn to determine the threshold of IFN-γ and MCP-1 for diagnosis of active tuberculosis and to evaluate their diagnostic performance. The specific IFN-γ and MCP-1 levels in the active tuberculosis group were significantly higher than those in the non-tuberculous pulmonary disease group (P < 0.01) and those in the healthy control group (P < 0.01). The IFN-γ levels in the healthy control group and the non-tuberculous respiratory disease group showed no statistically significant difference (P > 0.05), but the MCP-1 levels in the non-tuberculous respiratory disease group were significantly higher than those of the healthy control group (P < 0.05). The specific IFN-γ and MCP-1 level cut off values were 256 pg/ml and 389 pg/ml as an active tuberculosis diagnostic standard. The sensitivities of IFN-γ and MCP-1 were 57.3% and 92.8%, respectively; specificities were 80% and 80.7%, respectively; the positive predictive values were 76.9% and 84.9%, respectively; negative predictive values were 61.7% and 78.7%, respectively; and accuracy rates were 76.9% and 84.9%, respectively. Compared with the detection of IFN-γ, we observed a better diagnostic performance of MCP-1 in peripheral blood in active tuberculosis. MCP-1 may become one of the active tuberculosis auxiliary diagnostic targets.

In order to increase the expression of the fusion (F) protein and lay a foundation for the construction of a genetically engineered vaccine and rapid clinical detection, the F protein of the human respiratory syncytial virus (HRSV) was expressed and purified, and a sandwich enzyme-linked immunosorbent assay (ELISA) method was established. The F1 fragment of the HRSV F protein was amplified following reverse transcription, and was then combined with the vector and transformed into eukaryotic cells. The recombinant protein was induced and purified. The purified protein was used to immunize mice to produce antiserum and establish indirect ELISA. The established method was tested and verified by analyzing 100 samples using gold immunochromatography (GICA). The F1 fragment of the F gene was successfully amplified, the DNA (+) recombinant was selected, and a protein of molecular weight approximately 45,000 was obtained after the induction. The optimal reaction conditions and working concentration of ELISA were determined. The optimal concentration of mice anti-F1 IgG is 3.2 µg/ml, the best reaction time of the samples is 70 min at 37 ˚C, and the working concentration of the rabbit anti‑mouse IgG is 1:6,000. Compared with the GICA method, the sample's positive co-efficient of variation was 3.2-8.6%, and the negative co-efficient of variation was 5.1-8.3%. These were <10%, indicating that the ELISA method was reproducible. The F1 protein can be greatly expressed in transfected eukaryotic cells, and the purified F1 protein has good immunogenicity. The antiserum produced by the purified recombinant protein can be precisely detected using the ELISA detection method described in this study.