Abstract Lentinula edodes (L. edodes), which imparts various health benefits to humans, is considered a novel source of soluble dietary fiber (SDF). In this study, ultrasonic-assisted hot-water method was used to extract SDF (U-SDF) from L. edodes, and physicochemical, antioxidant and hypoglycemic properties of the U-SDF were investigated. Physicochemical properties of U-SDF showed that water solubility, water holding capacity, swelling capacity, and oil holding capacity were higher than that the SDF extracted using hot water method without ultrasonication. The DPPH, •OH, and •O2- radical clearance rates indicated that U-SDF exhibited better antioxidant activities. U-SDF also exhibited notable α-amylase and α-glucosidase inhibition activities. Treatment with U-SDF alleviated glucose and peroxidation metabolism disorders in vivo. Histological analysis indicated that U-SDF improved the oxidative tissue damage in diabetic mice. These results provided a theoretical basis for the development and utilization of SDF derived from L. edodes.

A highly efficient and reusable catalyst QA-HPMV was successfully prepared by the reaction of quinoline-2-formic acid (QA) with molybdovanadophosphoric heteropolyacid (H4PMo11VO40, HPMV) for the nitration of benzene. The physical and chemical properties of the sample was characterized by X-ray diffraction analysis (XRD), Fourier transform infrared spectroscopy (FTIR), UV-Vis and thermogravimetric analysis (TG). The characterization results showed that the formed QA-HPMV retained the Keggin structure of HPMV. As a catalyst for benzene nitration, QA-HPMV showed good catalytic performance and the yield of nitrobenzene was 82.5% under the optimized reaction conditions. As a heterogeneous catalyst, QA-HPMV can be easily recycled from the reaction medium by filtering and remained highly catalytic performance even after five runs of recycling.

Abstract: Background: Myeloid leukemia cutis is the terminology used for cutaneous manifestations of myeloid leukemia. Objective: The purpose of this study was to study the clinical, histopathological and immunohistochemical features of myeloid leukemia cutis. Methods: This was a retrospective study of clinical and pathological features of 10 patients with myeloid leukemia cutis. Results: One patient developed skin lesions before the onset of leukemia, seven patients developed skin infiltration within 4-72 months after the onset of leukemia, and two patients developed skin lesions and systemic leukemia simultaneously. Of these patients, five presented with generalized papules or nodules, and five with localized masses. The biopsy of skin lesions showed a large number of tumor cells within the dermis and subcutaneous fat layer. Immunohistochemical analysis showed strong reactivity to myeloperoxidase (MPO), CD15, CD43 and CD45 (LCA) in most cases. NPM1 (nucleophosmin I) and FLT3-ITD (Fms-like tyrosine kinase 3-internal tandem duplication) mutations were identified in one case. Five patients with acute myelogenous leukemia and one patient with chronic myelomonocytic leukemia died within two months to one year after the onset of skin lesions. Study limitations: This was a retrospective and small sample study. Conclusions: In patients with myelogenous leukemia, skin infiltration usually occurs after, but occasionally before, the appearance of hemogram and myelogram abnormalities, and the presence of skin infiltration is often associated with a poor prognosis and short survival time. myeloid leukemia cutis often presents as generalized or localized nodules or masses with characteristic pathological and histochemical findings.

Abstract Background This study determined the regulatory effects of inducible T-cell co-stimulators (ICOS) in human hepatocellular carcinoma HepG2 cells using a RNA interference (RNAi) technique. Methods A RNAi technique was used to knockdown the expression of ICOS. ICOS expression after knockdown was detected as mRNA and protein levels by RT-PCR and Western blot, respectively. A MTT colorimetric assay was used to detect cell proliferation, and the Transwell assay was used to detect cell invasion. Western blot was carried out to detect the level of Bcl-2, AKT, and PI3K protein expression in different groups. Results The proliferation of HepG2 cells were significantly decreased after ICOS siRNA transfection (EG group). Similarly, the results of the Transwell experiment showed that invasion of HepG2 cells in the EG group was clearly reduced compared to the negative control (NC) and blank control groups (CON). Western blot analysis showed that knockdown of ICOS expression reduced the levels of Bcl-2 and AKT, and also significantly up-regulated the level of PI3K phosphorylation (P < 0.01). Conclusion Down-regulating ICOS expression in HepG2 cells suppressed cell proliferation and invasion. The underlying mechanism may be related to the expression of the downstream factor, PI3K/AKT.

Abstract Background: Deubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38's functions on the LSD1 protein and on cell physiology were investigated. Materials and methods: Western blotting, real-time quantitative PCR, immunoprecipitation, denaturing immunoprecipitation and luciferase reporter assays were used to analyze the protein stability, protein interactions and changes in the ubiquitin chain. Cell proliferation assays, colony formation assays, drug treatments and western blotting were used to explore the functions of USP38 in cells. Results: The deubiquitinase USP38 stabilizes protein LSD1 in cells by binding LSD1 and cleaving its ubiquitin chain to prevent the degradation of LSD1 by the intracellular proteasome. USP38 enhances the ability of LSD1 to activate signaling pathways and hence promotes cellular abilities of proliferation and colony formation through interacting with LSD1. Furthermore, USP38 enhances the drug tolerance of human colon cancer cells. Conclusions: USP38 is an LSD1-specific deubiquitinase that affects cellular physiology through interacting with LSD1.