Colorimetric detection of Hg2+ based on the enhanced oxidase-mimic activity of CuO/Au@Cu3(BTC)2 triggered by Hg2.

It is imperative to develop a rapid detection method for Hg2+ due to its harm to human health and the ecological environment. In this research, CuO/Au@Cu3(BTC)2 was synthesized through reducing HAuCl4 by CuxO@Cu3(BTC)2, which was obtained by reducing Cu3(BTC)2 with hydrazine hydrate. The oxidase-mimic activity of CuO/Au@Cu3(BTC)2 can be enhanced by Hg2+ through forming a Au-Hg alloy. Therefore, a colorimetric method was designed for Hg2+ detection with a linear relationship in the 0.05-25 µM range and a limit of detection of 9.7 nM. This strategy exhibited a strong selectivity to Hg2+ and was applied in a real water sample with reliable recoveries. This work provides a possibility for the rapid detection of Hg2+.

Hesperetin derivative-16 attenuates CCl4-induced inflammation and liver fibrosis by activating AMPK/SIRT3 pathway.

Liver fibrosis, a chronic inflammatory healing reaction, progresses to hepatocirrhosis without effective intervention. Hesperetin derivative (HD-16), a monomer compound derived from hesperitin, exerts anti-inflammatory and hepatoprotective effects against a spectrum of liver diseases. However, the anti-fibrotic potential of HD-16 in liver fibrosis and its underlying mechanism have not yet been elucidated. In this study, we investigated the anti-fibrotic effect of HD-16 on mouse liver fibrosis induced by CCl4 and on LX-2 cells (human immortalized HSCs) stimulated by TGF-ß1, in vivo and in vitro. HD-16 exerted an anti-fibrotic effect via regulation of the AMPK/SIRT3 pathway. Pharmacodynamic results showed that HD-16 alleviated the degree of injury and inflammation in CCl4-induced mouse liver fibrosis. Consistently, HD-16 also effectively inhibited the expression of α-SMA, Col1α1, Col3α1, and TIMP-1 in TGF-ß1-activated LX-2 cells. Mechanistically, HD-16 promoted SIRT3 expression and activity in fibrotic liver and activated LX-2 cells. Furthermore, SIRT3 depletion attenuated the anti-fibrotic effects of HD-16. Intriguingly, HD-16 increased AMPK phosphorylation, whereas inhibition of SIRT3 expression did not affect AMPK phosphorylation. In contrast, AMPK silencing suppressed SIRT3 expression, suggesting that SIRT3 is a downstream target of AMPK in liver fibrosis. Overall, HD-16 attenuated CCl4-induced liver inflammation and fibrosis by activating the AMPK/SIRT3 pathway, and HD-16 may be a potential anti-fibrotic compound in the treatment of liver fibrosis.

Synthesis, Electronic Structure, and Electrochemical Properties of the Cubic Mg2MnO4 Spinel with Porous-Spongy Structure.

Mg2MnO4 nanoparticles with cubic spinel structure were synthesized by the sol-gel method using polyvinyl alcohol (PVA) as a chelating agent. X-ray powder diffraction, infrared spectrum (IR), scanning electron microscope (SEM), and transmission electron microscope (TEM) were used to characterize the crystalline phase and particle size of as-synthesized nanoparticles. The electronic structure of Mg2MnO4 spinel was studied by X-ray photoelectron spectroscopy (XPS). The results showed that pure cubic Mg2MnO4 spinel nanoparticles were obtained when the annealing temperature was 500-700 °C. The samples had a porous-spongy structure assembled by nanoparticles. XPS studies indicated that Mg2MnO4 nanoparticles were mixed spinel structures and the degree of cation inversion decreased with increasing annealing temperature. Furthermore, the performance of Mg2MnO4 as lithium anode material was studied. The results showed that Mg2MnO4 samples had good cycle stability except for the slight decay in the capacity at 50 cycles. The coulombic efficiency (ratio of discharge and charge capacity) in most cycles was near 100%. The sample annealed at 600 °C exhibited good electrochemical properties, the first discharge capacity was 771.5 mAh/g, and the capacity remained 340 mAh/g after 100 cycles. The effect of calcination temperature on the charge-discharge performance of the samples was studied and discussed.

Putative PmrA and PmcA are important for normal growth, morphogenesis and cell wall integrity, but not for viability in Aspergillus nidulans.

P-type Ca(2+)-transporting ATPases are Ca(2+) pumps, extruding cytosolic Ca(2+) to the extracellular environment or the intracellular Ca(2+) store lumens. In budding yeast, Pmr1 (plasma membrane ATPase related), and Pmc1 (plasma membrane calcium-ATPase) cannot be deleted simultaneously for it to survive in standard medium. Here, we deleted two putative Ca(2+) pumps, designated AnPmrA and AnPmcA, from Aspergillus nidulans, and obtained the mutants ΔanpmrA and ΔanpmcA, respectively. Then, using ΔanpmrA as the starting strain, the promoter of its anpmcA was replaced with the alcA promoter to secure the mutant ΔanpmrAalcApmcA or its anpmcA was deleted completely to produce the mutant ΔanpmrAΔpmcA. Different from the case in Saccharomyces cerevisiae, double deletion of anpmrA and anpmcA was not lethal in A. nidulans. In addition, deletion of anpmrA and/or anpmcA had produced growth defects, although overexpression of AnPmc1 in ΔanpmrAalcApmcA could not restore the growth defects that resulted from the loss of AnPmrA. Moreover, we found AnPmrA was indispensable for maintenance of normal morphogenesis, especially in low-Ca(2+)/Mn(2+) environments. Thus, our findings suggest AnPmrA and AnPmcA might play important roles in growth, morphogenesis and cell wall integrity in A. nidulans in a different way from that in yeasts.

Deletion of the putative stretch-activated ion channel Mid1 is hypervirulent in Aspergillus fumigatus.

Calcium ion is a universal and physiologically important molecule affecting almost every cellular function, while Mid1 (mating induced death) is a stretch-activated ion channel localized in the plasma membrane, which can replenish the fungus with extracellular calcium. Aspergillus fumigatus is one of the most important fungal pathogens but little is known about its calcium channels in the plasma membrane. In this study, a homolog of Saccharomyces cerevisiae Mid1 was identified in A. fumigatus and its encoding gene afmid1 was deleted by replacing it with pyr4 selectable marker, designated as Δafmid1. Analysis of the phenotypes demonstrated that Δafmid1 had growth defects under solid and liquid cultural conditions. The mutant Δafmid1 had delayed germination in minimal medium and abnormal morphogenesis in the medium containing ethylene glycol tetraacetic acid (EGTA), an agent with major affinity for Ca(2+) and minor affinity for Mn(2+). The sensitivity against cell wall disturbing agents, osmotic stress, alkaline environments, high temperatures or starvation in Δafmid1 resembled wild type. However, the mutant Δafmid1 demonstrated more sensitivity to oxidative agents (H2O2 and Menadione) than wild type. Most surprisingly, deletion of afmid1 from A. fumigatus led to hypervirulence in the immunosuppressed mice model.

Porous copper zinc tin sulfide thin film as photocathode for double junction photoelectrochemical solar cells.

Porous copper zinc tin sulfide (CZTS) thin film was prepared via a solvothermal approach. Compared with conventional dye-sensitized solar cells (DSSCs), double junction photoelectrochemical cells using dye-sensitized n-type TiO(2) (DS-TiO(2)) as the photoanode and porous p-type CZTS film as the photocathode shows an increased short circuit current, external quantum efficiency and power conversion efficiency.

Osmotic stabilizer-coupled suppression of NDR defects is dependent on the calcium-calcineurin signaling cascade in Aspergillus nidulans.

Establishment and maintenance of cell polarity are coordinated by signaling pathways such as NDR (nuclear Dbf2-related) protein-kinase signaling and calcium signaling pathway. The NDR family of kinase is structurally related to the human myotonic dystrophy kinase, which, when impaired, confers a disease that involves changes in cytoarchitecture and ion homeostasis. CotA kinase, a member of the NDR protein kinase family, forms a complex with MobB to regulate cell polarized growth in Aspergillus nidulans. Our previous study demonstrated that mobB/cotA defects could be suppressed by the osmotic stress in the presence of external calcium. In this study, via the genetic and molecular approach, we further demonstrated that Ca(2+)-permeable stretch-activated nonselective cation channel-MidA, calcium/calmodulin-dependent protein phosphatase catalatic subunit-CnaA and external calcium, but not voltage-gated calcium channel homolog-CchA, were required for the osmotic stabilizer-coupled suppression. The up-regulation of calcium/calcineurin signaling pathway induced by osmotic stress might be the reason for bypassing the requirements of NDR kinase complex, which is otherwise necessary for polar morphogenesis. Our results suggest that calcium-calcineurin signaling pathway coordinates with MobB/CotA kinase complex in regulating polarity growth via maintaining cellular calcium homeostasis. However, CchA may act differently as other components in calcium signaling pathway in Aspergillus nidulans. These findings provide an excellent opportunity to identify the potential pathway linking NDR protein-kinase network to calcium signaling pathway.

GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability of Aspergillus fumigatus.

GDP-mannose pyrophosphorylase (GMPP) catalyses the synthesis of GDP-mannose, which is the precursor for the mannose residues in glycoconjugates, using mannose 1-phosphate and GTP as substrates. Repression of GMPP in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation. Although several GMPPs have been isolated and characterized in filamentous fungi, the physiological consequences of their actions are not clear. In this study, Afsrb1, which is a homologue of yeast SRB1/PSA1/VIG9, was identified in the Aspergillus fumigatus genome. The Afsrb1 gene was expressed in Escherichia coli, and recombinant AfSrb1 was functionally confirmed as a GMPP. By the replacement of the native Afsrb1 promoter with an inducible Aspergillus nidulans alcA promoter, the conditional inactivation mutant strain YJ-gmpp was constructed. The presence of 3 % glucose completely blocked transcription of P(alcA)-Afsrb1, and was lethal to strain YJ-gmpp. Repression of Afsrb1 expression in strain YJ-gmpp led to phenotypes including hyphal lysis, defective cell wall, impaired polarity maintenance, and branching site selection. Also, rapid germination and reduced conidiation were documented. However, in contrast to yeast, strain YJ-gmpp retained the ability to direct polarity establishment and septation. Our results showed that the Afsrb1 gene is essential for cell wall integrity, morphogenesis and viability of Aspergillus fumigatus.