Amorphous MoS2 Decorated Ni3 S2 with a Core-shell Structure of Urchin-Like on Nickel-Foam Efficient Hydrogen Evolution in Acidic and Alkaline Media.

The large-scale commercialization of the hydrogen evolution reaction (HER) necessitates the development of cost-effective and highly efficient electrocatalysts. Although transition metal sulfides, such as MoS2 and Ni3 S2 , hold great potential in the field of HER, their catalytic performance has been unsatisfactory due to incomplete exposure of active sites and poor electrical conductivity. In this work, via a simple hydrothermal strategy, amorphous MoS2 nanoshells in the form of urchin-like MoS2 -Ni3 S2 core-shell heterogeneous structure is realized and in situ loaded on nickel foam (A-MoS2 -Ni3 S2 -NF). In particular, XPS analysis results show that the coupling of amorphous MoS2 and Ni3 S2 makes the electrode surface exhibit electron-abundant property, which will have a positive impact on HER catalytic activity. In addition, the fully exposed active site of amorphous MoS2 is another crucial factor contributing to its high catalytic performance of A-MoS2 -Ni3 S2 -NF electrode. In particular, at a current density of 10 mA cm⁻2 , the overpotential of electrode is 95 mV (1.0 m KOH) and 145 mV (0.5 m H2 SO4 ). This work highlights the importance of amorphous MoS2 and MoS2 -Ni3 S2 of sea-urchin core-shell structure in optimizing HER performance, which provides an important reference for HER research.

The GR-gp78 Pathway is involved in Hepatic Lipid Accumulation Induced by Overexpression of 11ß-HSD1.

Glucocorticoids are essential participants in the regulation of lipid metabolism. On a tissue-specific level, glucocorticoid signal is controlled by 11ß-Hydroxysteroid dehydrogenase 1 (11ß-HSD1). Up-regulation of 11ß-HSD1 expression during non-alcoholic fatty liver disease (NAFLD) has been previously shown, while 11ß-HSD1 inhibition has been shown to reduce hepatic lipids in NAFLD, but the underlying mechanisms remain unclear. Here, in this study, we created in vitro cell culture and in vivo transgenic hepatocyte-specific 11ß-HSD1 mouse models of NAFLD to determine the regulatory mechanisms of 11ß-HSD1 during lipid metabolism dysfunction. We found that 11ß-HSD1 overexpression activated glucocorticoid receptors and promoted their nuclear translocation, and then stimulating gp78. The induction of gp78 sharply reduced expression of Insig2, but not Insig1, which led to up-regulation of lipogenesis regulatory proteins including SREBP1, FAS, SCD1, and ACC1. Our results suggested that overexpression of 11ß-HSD1 induced lipid accumulation, at least partially through the GR/gp78/Insig2/SREBP1 pathway, which may serve as a potential diagnostic and therapeutic target for treatment of NAFLD.