58 research outputs found

    Degradation of Cationic Red GTL by Catalytic Wet Air Oxidation over Mo–Zn–Al–O Catalyst under Room Temperature and Atmospheric pressure

    No full text
    To overcome the drawback of catalytic wet air oxidation (CWAO) with high temperature and high pressure, the catalytic activity of Mo–Zn–Al–O catalyst for degradation of cationic red GTL under room temperature and atmospheric pressure was investigated. Mo–Zn–Al–O catalyst was prepared by coprecipitation and impregnation. XRD, TG-DTG, and XPS were used to characterize the resulting sample. Central composition design using response surface methodology was employed to optimize correlation of factors on the decolorization of cationic red GTL. The results show that the optimal conditions of pH value, initial concentration of dye and catalyst dosage were found to be 4.0, 85 mg/L and 2.72 g/L, respectively, for maximum decolorization of 80.1% and TOC removal of 50.9%. Furthermore, the reaction on the Mo–Zn–Al–O catalyst and degradation mechanism of cationic red GTL was studied by Electron spin resonance (ESR) and GC-MS technique. The possible reaction mechanism was that the Mo–Zn–Al–O catalyst can efficiently react with adsorbed oxygen/H<sub>2</sub>O to produce ·OH and <sup>1</sup>O<sub>2</sub> and finally induce the degradation of cationic red GTL. GC-MS analysis of the degradation products indicates that cationic red GTL was initiated by the cleavage of NN and the intermediates were further oxidized by ·OH or <sup>1</sup>O<sub>2</sub>

    TIMP-1 Promotes Accumulation of Cancer Associated Fibroblasts and Cancer Progression

    Get PDF
    <div><p>Treatment options for late stage prostate and colon cancer are limited and there is an urgent need to develop more effective and targeted novel therapies, which starts with identification and validation of novel therapeutic targets. Recent clinical studies have demonstrated that tissue inhibitor matrix metalloproteinase-1 (TIMP-1) levels are elevated in cancer patient plasma and elevated TIMP-1 levels are associated with worse clinical outcomes. However, it is unknown whether TIMP-1 serves merely as a biomarker of cancer progression or has a functional role in promoting cancer progression and can serve as a cancer therapeutic target, which is the main objective of this study. Here, we show that stroma of human prostate and colon cancer express higher levels of TIMP-1 compared to their normal counterparts and increased expression of TIMP-1 promotes <i>in vivo</i> growth of both cancer types. We demonstrate for the first time that increased TIMP-1 expression stimulates accumulation of cancer associated fibroblasts (CAFs) within prostate and colon cancer tissues and that TIMP-1 enhances prostate CAF proliferation and migration <i>in vitro</i> and promotes ERK1/2 kinase activation in these CAF cells. Our results establish the novel promotive effects of TIMP-1 on cancer progression and on accumulation of CAFs that in turn provides a pro-tumor microenvironment. Together, these results establish the potential of TIMP-1 as a novel target for cancer therapy and the mechanism underlying the pro-tumor activity of TIMP-1.</p> </div

    Synthesis and Material Properties of Bi<sub>2</sub>Se<sub>3</sub> Nanostructures Deposited by SILAR

    No full text
    Bi<sub>2</sub>Se<sub>3</sub> was synthesized by a room-temperature deposition technique and successive ionic layer adsorption and reaction (SILAR) method with the aim to understand the formation, crystallinity, optical properties, and energy band structure of this material. The Bi<sub>2</sub>Se<sub>3</sub> morphology was found to change from nanoparticles to that of a nanocluster network by increasing the SILAR deposition cycles. The crystalline structure of as-prepared Bi<sub>2</sub>Se<sub>3</sub> determined from the grazing-incidence X-ray diffraction (GI-XRD) pattern was found to have a mixed of metastable orthorhombic and rhombohedral phases which was further confirmed from our analysis of the Raman spectra. The optical bandgap of Bi<sub>2</sub>Se<sub>3</sub> varied from 1.58 to 1.05 eV for 15–90 cycles of deposition, in contrast to the semimetallic 0.3 eV bandgap exhibited by the pure rhombohedral phase. A schematic band diagram of Bi<sub>2</sub>Se<sub>3</sub> prepared by 45 SILAR cycles was constructed for the mixed-phase Bi<sub>2</sub>Se<sub>3</sub>. The flat-band potential was determined to be at 0.46 V vs. RHE from Mott–Schottky analysis. Low-temperature annealing at 100 °C for 1 h resulted in the improvement of the rhombohedral phase fraction which was confirmed from analysis of GI-XRD pattern and pronounced E<sup>2</sup><sub>g</sub> and A<sup>2</sup><sub>1g</sub> bulk vibrational modes in the Raman spectrum. The absorption cutoff after annealing was found to be red-shifted combined with a sub-bandgap absorption above 0.78 eV. The post-annealing results indicated the onset of an early stage transition from semiconductor to semi-metallic properties for Bi<sub>2</sub>Se<sub>3</sub>

    TIMP-1 enhances expression of Snail, MMP-2, and MMP-9 in prostate cancers.

    No full text
    <p>Expression levels of several EMT markers, such as Snail (A, E, I, M), Slug (B, F, J, N), MMP-2 (C, G, K, O), and MMP-9 (D, H, L, P) were assessed on the tumor sections derived from PC3/LAPC-4 control cells (A-D and I-L, respectively) and PC3/LAPC-4-TIMP-1 cells (E-H and M-P, respectively). The results show that TIMP-1 enhances expression of Snail, MMP-2, and MMP-9 but not Slug in the prostate cancer tissues. Bar, 50 µm in A, B, E, F, I, J, M, N and 100 µm in C, D, G, H, K, L, O, P. </p

    <i>A model</i> of action of TIMP-1 during tumor progression

    No full text
    <p>: Increased expression of TIMP-1 by tumor cells and CAFs leads to increased CAF proliferation and migration through binding of TIMP-1 to the TIMP-1 receptor, CD63 expressed on CAFs, which leads to accumulation of CAFs within cancer tissues. These CAFs in turn provide a pro-tumor microenvironment to facilitate the cancer progression by secreting pro-tumor growth factors/cytokines, modulating tumor angiogenesis, and regulating infiltration and expansion of inflammatory cells. </p

    TIMP-1 promotes the prostate CAF proliferation and migration through transwells.

    No full text
    <p><b>A</b>-<b>C</b>. Prostate CAFs or prostate cancer cells were seeded at 2 x 10<sup>3</sup> cells/well into 96-well plates in triplicate. Prostate cancer cell and prostate CAF proliferation assays were performed every day using a set of 96-well plates using Premix WST1 kit (TaKaRa) following the manufacturer’s instruction. <sup>*</sup><i>p</i><0.05. <b>D</b>. Prostate CAFs were assessed for their motility across transwell barrier over the course of 30 hours in the presence or absence of 250ng/ml of TIMP-1. 0.5 x 10<sup>6</sup> cells/ml prostate CAFs were placed in the upper chambers of Transwell inserts (Costar) in triplicates. Representative images of prostate CAF cells migrated through the transwell inserts are shown. The prostate CAFs migrated through transwell inserts in 20 random selected 200 x microscopic fields were counted. <sup>*</sup><i>p</i><0.05. A-D, the results show representative means +/-SDs of triplicates of one of two independent experiments. </p
    • …
    corecore