Motivated by the observation of a gapless spin liquid state in κ-(BEDT-TTF)2Cu2(CN)3, we analyze the anisotropic triangular lattice S = 1/2 Heisenberg model with the resonating valence bond mean-field approximation. Paying attention to the small quasi-one-dimensional anisotropy of the material, we take an approach from one-dimensional (1D) chains coupled with frustrating zig-zag bonds. By calculating one-particle excitation spectra changing anisotropy parameter J ′ /J from the decoupled 1D chains to the isotropic triangular lattice, we find almost gapless excitations in the wide range from the 1D limit. This one-dimensionalization by frustration is considered to be a candidate for the mechanism of the gapless spin liquid state.
Quercetin is a flavonoid with a wide variety of cytoprotective and modulatory functions. Heme oxygenase-1 (HO-1) is an inducible enzyme. Its reaction product, carbon monoxide (CO), confers cellular protection in a number of conditions and diseases associated with oxidative or inflammatory lung injury. Furthermore, quercetin was reported to be a potent inducer of HO-1 in several cell types. We hypothesized that quercetin suppresses the production of collagen in fibroblasts via the induction of HO-1. Here, we showed that quercetin suppresses transforming growth factor-β (TGF-β)-induced collagen production in NIH3T3 cells and in normal human lung fibroblasts. This suppressive effect of quercetin was mediated by quercetin-induced HO-1. The suppression of collagen production was conferred by the reaction product of HO-1, CO, but not by bilirubin. Furthermore, the translocation of the nuclear factor E2-related factor-2 (Nrf2), an important transcription factor that regulates the expression of HO-1 from the cytoplasm to the nuclei, was demonstrated in NIH3T3 cells by exposure to quercetin. Assessment of the signal transduction pathway involved in TGF-β signaling showed that quercetin stimulated the Smad and mitogen-activated protein kinase pathway to varying degrees. Our results demonstrate that quercetin exerts suppressive effects on the expression of collagen by the induction of HO-1. Idiopathic pulmonary fibrosis is the most lethal diffuse fibrosing lung disease, and is characterized by the deposition of extracellular matrix. Given that HO-1 is one of the important molecules emerging as a central player in diseases, quercetin or its derivatives, which effectively induced HO-1, will lead to new therapeutic strategies for promoting antifibrotic therapy in respiratory diseases.
The optimal activity of Bacillus sp. TB-90 urate oxidase (BTUO) is 45 °C, but this enzyme is one of the most thermostable urate oxidases. A marked increase (>10 °C) in its thermal stability is induced by high concentrations (0.8–1.2 M) of sodium sulfate. Calorimetric measurements and size exclusion chromatographic analyses suggested that sulfate-induced thermal stabilization is related to the binding of a sulfate anion that repressed the dissociation of BTUO tetramers into dimers. To determine the sulfate binding site, the crystal structure was determined at 1.75 Å resolution. The bound sulfate anion was found at the subunit interface of the symmetrical related subunits and formed a salt bridge with two Arg298 residues in the flexible loop that is involved in subunit assembly. Site-directed mutagenesis of Arg298 to Glu was used to extensively characterize the sulfate binding site at the subunit interface. The network of charged hydrogen bonds via the bound sulfate is suggested to contribute significantly to the thermal stabilization of both subunit dimers and the tetrameric assembly of BTUO. Knowledge of the mechanism of salt-induced stabilization will help to develop new strategies for enhancing protein thermal stabilization.
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