246 research outputs found

    Parasite-Derived Proteins Inhibit Allergic Specific Th2 Response

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    Free-Living Amoeba Acanthamoeba Triggers Allergic Inflammation of Airways

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    Ionized gas outflows in infrared-bright dust-obscured galaxies selected with WISE and SDSS

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    We present the ionized gas properties of infrared (IR)-bright dust-obscured galaxies (DOGs) that show an extreme optical/IR color, (i[22])AB>7.0(i - [22])_{\rm AB} > 7.0, selected with the Sloan Digital Sky Survey (SDSS) and Wide-field Infrared Survey Explorer (WISE). For 36 IR-bright DOGs that show [OIII]λ\lambda5007 emission in the SDSS spectra, we performed a detailed spectral analysis to investigate their ionized gas properties. In particular, we measured the velocity offset (the velocity with respect to the systemic velocity measured from the stellar absorption lines) and the velocity dispersion of the [OIII] line. We found that the derived velocity offset and dispersion of most IR-bright DOGs are larger than those of Seyfert 2 galaxies (Sy2s) at z<0.3z < 0.3, meaning that the IR-bright DOGs show relatively strong outflows compared to Sy2s. This can be explained by the difference of IR luminosity contributed from active galactic nucleus, LIRL_{\rm IR} (AGN), because we found that (i) LIRL_{\rm IR} (AGN) correlates with the velocity offset and dispersion of [OIII] and (ii) our IR-bright DOGs sample has larger LIRL_{\rm IR} (AGN) than Sy2s. Nevertheless, the fact that about 75% IR-bright DOGs have a large (>> 300 km s1^{-1}) velocity dispersion, which is a larger fraction compared to other AGN populations, suggests that IR-bright DOGs are good laboratories to investigate AGN feedback. The velocity offset and dispersion of [OIII] and [NeIII]λ\lambda3869 are larger than those of [OII]λ\lambda3727, which indicates that the highly ionized gas tends to show more stronger outflows.Comment: 19 pages, 16 figures, and 2 tables, accepted for publication in Ap

    Salinomycin enhances doxorubicin-induced cytotoxicity in multidrug resistant MCF-7/MDR human breast cancer cells via decreased efflux of doxorubicin

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    Salinomycin is a monocarboxylic polyether antibiotic, which is widely used as an anticoccidial agent. The anticancer property of salinomycin has been recognized and is based on its ability to induce apoptosis in human multidrug resistance (MDR). The present study investigated whether salinomycin reverses MDR towards chemotherapeutic agents in doxorubicin-resistant MCF-7/MDR human breast cancer cells. The results demonstrated that doxorubicin-mediated cytotoxicity was significantly enhanced by salinomycin in the MCF-7/MDR cells, and this occurred in a dose-dependent manner. This finding was consistent with subsequent observations made under a confocal microscope, in which the doxorubicin fluorescence signals of the salinomycin-treated cells were higher compared with the cells treated with doxorubicin alone. In addition, flow cytometric analysis revealed that salinomycin significantly increased the net cellular uptake and decreased the efflux of doxorubicin. The expression levels of MDR-1 and MRP-1 were not altered at either the mRNA or protein levels in the cells treated with salinomycin. These results indicated that salinomycin was mediated by its ability to increase the uptake and decrease the efflux of doxorubicin in MCF-7/MDR cells. Salinomycin reversed the resistance of doxorubicin, suggesting that chemotherapy in combination with salinomycin may benefit MDR cancer therapyopen

    Culture supernatant of adipose stem cells can ameliorate allergic airway inflammation via recruitment of CD4+CD25+Foxp3 T cells

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    SDS-PAGE of supernatant after ASC cultivation. Comparison of protein composition of con sup (concentrated medium for ASCs cultivation) and ASC sup (concentrated culture supernatant after ASC cultivation for 3 days) using SDS-PAGE. Thirty micrograms of each sample was loaded into an SDS-PAGE gel. After electrophoresis, the gel was stained by Coomassie Blue (M molecular marker, arrow indicated extra proteins compared to control). (PPT 370 kb

    Expression and Characterization of α-Methylacyl CoA Racemase from Anisakis simplex Larvae

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    Larval excretory-secretory products of Anisakis simplex are known to cause allergic reactions in humans. A cDNA library of A. simplex 3rd-stage larvae (L3) was immunoscreened with polyclonal rabbit serum raised against A. simplex L3 excretory-secretory products to identify an antigen that elicits the immune response. One cDNA clone, designated as α-methylacyl CoA racemase (Amacr) contained a 1,412 bp cDNA transcript with a single open reading frame that encoded 418 amino acids. A. simplex Amacr showed a high degree of homology compared to Amacr orthologs from other species. Amacr mRNA was highly and constitutively expressed regardless of temperature (10-40℃) and time (24-48 hr). Immunohistochemical analysis revealed that Amacr was expressed mainly in the ventriculus of A. simplex larvae. The Amacr protein produced in large quantities from the ventriculus is probably responsible for many functions in the development and growth of A. simplex larvae

    Protease Allergens Induce the Expression of IL-25 via Erk and p38 MAPK Pathway

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    Allergic diseases, including asthma, are characterized by T helper type 2 (Th2) cell-mediated inflammations, coupled with tissue infiltration by eosinophils. In this study, we demonstrate that multiple protease allergens, including papain and DerP1, efficiently induce interleukin (IL)-25 and thymic stromal lymphopoietin (TSLP) gene expression, and this phenomenon is dependent on the protease activities of these allergens. The IL-25 cytokine level in bronchial alveolar lavage (BAL) was also profoundly and significantly increased after treatment with papain. Additionally, the levels of Th2 cytokines were significantly increased, as compared to those in the OVA-only treatment group. The various protease allergens triggered the expression of IL-25 and TSLP mRNA in mouse lung epithelial cells (MLE12) and primary mouse lung epithelial cells; these effects were inhibited by the deactivation of the protease activity of papain. The allergen papain activates the ErK and p38 MAP pathways; the inhibition of these pathways, but not the NFκB or PI-3 kinase pathways, impairs the induction of IL-25 and TSLP expression by proteases. In this study, we demonstrate that the protease allergens induce IL-25 and TSLP via the MAP kinase signal pathways, and their protease activities are essential to this pathway
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