How do hospital characteristics affect veteran patients’ satisfaction in South Korea?

This study examined the impact of the characteristics of commissioned hospitals on the satisfaction of veterans by using the satisfaction survey data of Korean veterans. As a result of a regression analysis using departments, beds, and specialists as independent variables and satisfaction scores as dependent variables, it was found that there was a positive correlation between the number of specialists and satisfaction in general hospitals. However, in clinics and tertiary hospitals, the number of beds was found to have a negative effect on satisfaction. Additionally, the presence or absence of a Veterans Affairs hospital did not have a significant effect on satisfaction with the referral hospital. Despite limitations, such as using only one year of survey data, this study may provide selection criteria for the ministry of Patriots and Veterans Affairs in designating commissioned hospitals

Mitochondrial ROS-derived PTEN oxidation activates PI3K pathway for mTOR-induced myogenic autophagy.

Muscle differentiation is a crucial process controlling muscle development and homeostasis. Mitochondrial reactive oxygen species (mtROS) rapidly increase and function as critical cell signaling intermediates during the muscle differentiation. However, it has not yet been elucidated how they control myogenic signaling. Autophagy, a lysosome-mediated degradation pathway, is importantly recognized as intracellular remodeling mechanism of cellular organelles during muscle differentiation. Here, we demonstrated that the mtROS stimulated phosphatidylinositol 3 kinase/AKT/mammalian target of rapamycin (mTOR) cascade, and the activated mTORC1 subsequently induced autophagic signaling via phosphorylation of uncoordinated-51-like kinase 1 (ULK1) at serine 317 and upregulation of Atg proteins to prompt muscle differentiation. Treatment with MitoQ or rapamycin impaired both phosphorylation of ULK1 and expression of Atg proteins. Therefore, we propose a novel regulatory paradigm in which mtROS are required to initiate autophagic reconstruction of cellular organization through mTOR activation in muscle differentiation.This study was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (NRF-2016R1D1A1B03933763 to TGC, and NRF-2011-0030072, NRF-2017R1A2B2007870, and NRF-2018R1A6A1A03025124 to SSK)

Effect of thiacremonone on apoptotic cell death and the expression of apoptosis regulatory proteins.

<p>(A) The lung cancer cells were treated in the absence (<i>left panels</i>) and presence of thiacremonone (50 μg/ml, <i>right pannels</i>) for 72 hrs, and then labeled with DAPI and TUNEL solution. Total number of cells in a given area was determined by using DAPI nuclear staining (fluorescent microscope). The green color in the fixed cells marks TUNEL-labeled cells. For quantification, three randomly selected areas were assessed. The apoptotic index (%) was determined as the (TUNEL-positive cell number/total DAPI stained cell number) x 100 (magnification, 200×). Values are mean ±S.D. * P<0.05 compared with significantly different from untreated control cells. (B) The lung cancer cells were treated with different concentrations of thiacremonone (10, 20, and 50 μg/ml) for 72 hrs. Expression of apoptosis regulatory proteins was determined using Western blot analysis. Each image and band is representative of three independent experiments.</p

Anti-Cancer Effect of Thiacremonone through Down Regulation of Peroxiredoxin 6

<div><p>Thiacremonone (2, 4-dihydroxy-2, 5-dimethyl-thiophene-3-one) is an antioxidant substance as a novel sulfur compound generated from High-Temperature-High-Pressure-treated garlic. Peroxiredoxin 6 (PRDX6) is a member of peroxidases, and has glutathione peroxidase and calcium-independent phospholipase A2 (iPLA2) activities. Several studies have demonstrated that PRDX6 stimulates lung cancer cell growth via an increase of glutathione peroxidase activity. A docking model study and pull down assay showed that thiacremonone completely fits on the active site (cys-47) of glutathione peroxidase of PRDX6 and interacts with PRDX6. Thus, we investigated whether thiacremonone inhibits cell growth by blocking glutathione peroxidase of PRDX6 in the human lung cancer cells, A549 and NCI-H460. Thiacremonone (0–50 μg/ml) inhibited lung cancer cell growth in a concentration dependent manner through induction of apoptotic cell death accompanied by induction of cleaved caspase-3, -8, -9, Bax, p21 and p53, but decrease of xIAP, cIAP and Bcl2 expression. Thiacremonone further inhibited glutathione peroxidase activity in lung cancer cells. However, the cell growth inhibitory effect of thiacremonone was not observed in the lung cancer cells transfected with mutant PRDX6 (C47S) and in the presence of dithiothreitol and glutathione. In an allograft in vivo model, thiacremonone (30 mg/kg) also inhibited tumor growth accompanied with the reduction of PRDX6 expression and glutathione peroxidase activity, but increased expression of cleaved caspase-3, -8, -9, Bax, p21 and p53. These data indicate that thiacremonone inhibits tumor growth via inhibition of glutathione peroxidase activity of PRDX6 through interaction. These data suggest that thiacremonone may have potentially beneficial effects in lung cancer.</p></div

Effect of thiacremonone on tumor growth in allograft model.

<p>(A) Tumor volumes, weights, and images of normal mice. (B) Tumor volumes, weights, and images of PRDX6 overexpressed mice. Values (A and B) are mean ±S.D. * P<0.05 significantly different from untreated mice. (C) Tumor sections of normal mice were analyzed by H&E stain and expression of proteins by immunohistochemistry. The resultant tissues were developed with DAB, and counterstained with hematoxylin. (D) Tumor sections of PRDX6 overexpressed mice were analyzed by H&E stain and expression of proteins by immunohistochemistry. The resultant tissues were developed with DAB, and counterstained with hematoxylin. For quantification, 200 cells at three randomly selected areas were assessed, and the specific protein positively stained cells were counted. Scale bar indicates 50 μm.</p

Reverse of inhibitory effect of thiacremonone by DTT and glutathione GSH.

<p>(A) Lung cancer cells were co-treated with indicated concentrations of DTT (10 and 100 nM) or GSH (100 and 200 μM) with thiacremonone (50 μg/ml) for 72 hrs. The cells were harvested by trypsinization and stained with 0.2% trypan blue. (B) Cell extracts were analyzed by western blotting. Each image and band is representative of three independent experiments. (C) The levels of glutathione peroxidase activity in lung cancer cells were measured using assay kits, as described in Materials and methods. Values (A and C) are mean ±S.D. #, p<0.05 compared with significantly different from untreated cells with thiacremonone. *, p<0.05, significantly different from untreated cells with DTT or GSH.. ^&, p<0.05, significantly different between treated cell with thiacremonone and co-treated cells with DTT or GSH and thiacremonone.</p

Reverse of inhibitory effect of thiacremonone by transfection of mutant prdx6 (C47S).

<p>(A) Lung cancer cells were transfected with pcDNA-prdx6 or pcDNA-prdx6 C47S, and then, thiacremonone was treated (50 μg/ml) for another 72 hrs. The cells were harvested by trypsinization and stained with 0.2% trypan blue. (B) Cell extracts were analyzed by western blotting. Each image and band is representative of three independent experiments. (C) The levels of glutathione peroxidase activity in lung cancer cells were measured using assay kits, as described in Materials and methods. Values are mean ±S.D. #, p<0.05 significantly different from untreated control cells. *, p<0.05, significantly different from untreated control cells transfected with pcDNA-prdx6 C47S. ^&, p<0.05, significantly different between pcDNA-prdx6 and pcDNA-prdx6 C47S treated with thiacremonone.</p