Activity

In contrast, prolonged treatment with 30 μM AHL promoted osteoblast differentiation concomitantly with cell apoptosis. The elevation of [Ca2+]i levels in osteoblasts treated with 50 μM AHL was spatially autocorrelated, while no such phenomenon was observed in 30 μM AHL-treated osteoblasts. The blocking of cell-to-cell spatial autocorrelation in the osteoblasts provoked by 50 μM AHL significantly inhibited apoptosis and partially restored differentiation. Our observations suggest that AHL affects the fate of osteoblasts (apoptosis and differentiation) by affecting the spatial correlation of [Ca2+]i changes. Thus, AHL acts as a double-edged sword for osteoblast function.The evolutionarily-conserved 14-3-3 proteins regulate many cellular processes through binding to various phosphorylated targets in eukaryotes. It first appears in Dictyostelium, however its role in this organism is poorly understood. Here we show that down-regulation of the 14-3-3 impairs chemotaxis and causes multiple-tip formation in Dictyostelium. Mechanistically, the 14-3-3 is a critical component of cyclic AMP (cAMP) signaling and binds to nearly a hundred of proteins in Dictyostelium, including a number of evolutionarily-conserved proteins. 14-3-3 – interaction with its targets is up-regulated in response to developmental cues/regulators including starvation, osmotic stress and cAMP. selleck kinase inhibitor cAMP stimulates 14-3-3 – binding to phospho-Ser431 on a guanine nucleotide exchange factor Gef-Q. Interestingly, overexpression of Gef-QSer431Ala mutant but not wild-type Gef-Q protein causes a multiple-tip phenotype in Dictyostelium, which partially resembles phenotypes of the 14-3-3 – deficient mutant. Collectively, these data demonstrate that the 14-3-3 plays an important role in Dictyostelium and may help to deepen our understanding of the evolution of 14-3-3 – interactomes in eukaryotes.

Our study aimed to study the role of lncRNA TP73-AS1/miR-539/MMP-8 axis in modulating M2 macrophage polarization in hepatocellular carcinoma (HCC).

The gene expression levels of TP73-AS1, miR-539 and MMP-8 were modified by transfection with the overexpression or knockdown vectors. The patient survival rate was analyzed using Kaplan-Meier method. The levels of TP73-AS1, miR-539, MMP-8 and M1/2 macrophage polarization markers were analyzed by qRT-PCR, western blot, and flow cytometry. The release of TGF-β1 in the supernatant was determined by ELISA assay. The interaction between TP73-AS1, miR-539 and MMP-8 was analyzed by bioinformatics analysis and dual-luciferase reporter assays. Mouse xenograft model was further established to examine the therapeutic effects of the TP73-AS1 knockdown and miR-539 overexpression in vivo.

We found TP73-AS1 and MMP-8 upregulation, and miR-539 downregulation in HCC tissues and cell lines. Lower TP73-AS1 and MMP-8 expressions and higher miR-539 expression were associated with higher survival rate of patients. M2-macrophage markers CD206, Arg-1 and CD163 were significantly upregulated in the tumor tissues. TP73-AS1 negatively and directly regulated miR-539 and knockdown of TP73-AS1 inhibited MMP-8 expression and M2 macrophage polarization. Also, overexpression of miR-539 suppressed M2 macrophage polarization by negatively regulating MMP-8. Furthermore, knockdown of MMP-8 also restrained M2 macrophage polarization via inhibiting TGF-β1 signaling. We also found knockdown of TP73-AS1 or overexpression of miR-539 inhibited HCC tumor growth and M2 macrophage infiltration in vivo.

Our study demonstrated lncRNA TP73-AS1 negatively regulated miR-539 to promote MMP-8 expression, which activated TGF-β1 signaling to induce M2 macrophage polarization in HCC.

Our study demonstrated lncRNA TP73-AS1 negatively regulated miR-539 to promote MMP-8 expression, which activated TGF-β1 signaling to induce M2 macrophage polarization in HCC.Soil contamination with cadmium (Cd) has become a serious problem, adversely affecting food safety and human health. Effective methods are urgently needed to alleviate toxicity of Cd in plants. In this study, a nine-week continuous pot experiments was conducted to explore the effectiveness of the different nano iron oxide (α-Fe2O3, γ-Fe2O3, Fe3O4) alone and combined with biochar in muskmelon grown on a Cd-contaminated soil. The antioxidant system, chlorophyll, soluble protein, other physiological indexes of muskmelon leaves and the distribution of Cd in matrix soil, leaves and fruit were detected. The results showed that Cd was readily absorbed by plants and caused oxidative stress on plants, while biochar, α-Fe2O3 nanoparticles (NPs) and their mixture group (BFe1 group) could significantly improve it. Specifically, the three treatments reduced the Cd content of the fruit by 19.51-78.86%, reduced the Cd content of leaves by 15.44-36.23% and 22.36-31.77% in weeks 3 and 5, respectively. For the activity of enzymes, three treatments decreased superoxide dismutase (SOD) activity and catalase (CAT) activity by 3.41-38.57% and 24.27-30.33% in week 7, respectively. So BFe1 group application immobilized Cd in soil and reduced Cd partitioning in the aboveground tissues. Overall the combination of biochar and α-Fe2O3 NPs can alleviate Cd toxicity in muskmelon and can protect human beings from Cd exposure.

The aim of this study was to characterise a multidrug-resistant (MDR) Citrobacter freundii strain carrying a bla

-harbouring conjugative IncA/C2-type plasmid in China.

The whole genome of C. freundii strain L75 was sequenced both on HiSeq® (Novogene Corp., China) and GridION X5 (GrandOmics Biosciences Co., Ltd.) platforms. De novo genome assembly, genome annotation, multilocus sequence typing (MLST) and plasmid replicon typing were performed.

Citrobacter freundii L75 was assigned to ST396 and contains a 5.1-Mb chromosome and two plasmids (∼146 kb and ∼73 kb) designated pCf75 and pCf76, respectively. The antibiotic resistance determinants bla

, sul1, sul2, arr-3, mph(A), aadA16, aph(3″)-Ib, aac(3)-IId, aph(6)-Id, aac(6′)-Ib-cr and dfrA27 were located on plasmid pCf75, whilst bla

was chromosomally encoded. A 22.1-kb MDR-encoding region (MDRR) in a complex class 1 integron contained all of the resistance genes of plasmid pCf75.

We detected and characterised a plasmid carrying a novel MDRR in which a complex class 1 integron plays an essential role.