vans

[Marlon Jonathan]

Cell nuclei (blue) vans were counterstained by DAPI. ( d ) The apoptotic index was calculated by counting a minimum of 20 randomly selected fields following TUNEL staining. The index was obtained by dividing the TUNEL-positive cells by the total number of cells. The values are expressed as the means±S.D. ( n =3 in each group). * P versus SO mice, # P versus PUMA -WT miceAbove these results have demonstrated that PUMA is an important mediator in PHT-induced gastric mucosal injury and apoptosis. PUMA is one of the most potent mediators that transduce death signals primarily to mitochondrion.

To investigate mechanism of PUMA mediated ER stress-induced apoptosis, two gastric cell lines GES-1 and SGC7901 were used in this study. GES-1 cells and SGC7901 cells were treated with tunicamycin, which blocks ER protein glycosylation to induce ER stress. Following the treatment of tunicamycin, GRP78 expression was observably upregulated after tunicamycin treatment for 4 h in GES-1 cells vans simpsons and SGC7901 cells, and reached maximal levels at 24 and 16 h, respectively. Furthermore, nearly the same trend was observed in ER-localized caspase and cleaved caspase-4, PUMA and cleaved caspase-3 were also induced in both of the two types of cells ( Figure 8a ).

( b ) TUNEL (green) staining showed that vans shoe tunicamycin remarkably induced apoptosis in GES-1 and SGC7901 cell lines. Cell nuclei (blue) were counterstained by DAPI ( × 200). ( c ) The apoptotic index was calculated by counting a minimum of 20 randomly selected fields following TUNEL staining. The index was obtained by dividing the TUNEL-positive cells by the total number of cells. ( d ) Western blotting showed that PUMA -siRNA significantly knocked down PUMA expression in GES-1 and SGC7901 cell lines. ( e ) PUMA -siRNA did not affect GRP78 expression and caspase-4 activation after tunicamycin treatment, however, PUMA knocked down evidently inhibited ER stress-induced caspase-9 and caspase-3 activation vans the simpson by tunicamycin.

In this study, the gastric mucosa from PHG patients showed a destruction of architecture, edema with erosion, vasodilatation with lymphocyte infiltration and significant apoptosis induction compared with the uninvolved normal mucosa. Furthermore, PUMA expression was significantly increased, and a number of apoptotic cells were observed in the gastric mucosa of PHG patients. The results indicated that PUMA has an essential role in PHG. Several studies have revealed PHG improvement after transjugular intrajugular intrahepatic portosystemic shunt (TIPS) and shunt surgery, suggesting an association between PHG and the severity of PHT; however, others have failed to show this linear correlation with the severity of PHT.

23 , 24 On the basis of these findings, we used two types of PHG mouse models to explore the effect of PUMA on PHG, which were PVL- and CCl 4 -induced PHG in mice. Our previous study demonstrated that PVL induced evident PHG after PVL for 2 weeks, 7 and another report showed that CCl 4 induced prominent PHG. 25 In the study, the results showed that two mouse models led to significant PHT and PHG, upregulated gastric mucosal PUMA expression and induced mucosal epithelial apoptosis. The animal model data were consistent with human PHG.

29 In this study, our data indicated that PUMA-mediated gastric mucosal simpsons vans epithelial apoptosis in PHG via its regulation of Bax/Bak, cytochrome c release and caspase activation. The mitochondrial pathway of apoptosis requires the release of cytochrome c from the mitochondrion to the cytosol. Once released, cytochrome c cooperates with the adaptor protein, pro-caspase-9, to promote the activation of caspase-3, which is the apoptotic executor leading to cell death. PUMA acts through the proapoptotic multi-domain Bcl-2 effector proteins, Bax and Bak, which oligomerize into proteolipid pores and permeate the outer membrane of the mitochondrion to allow the efflux of cytochrome c and [img]https://www.cbye.ca/images/c/simpsons vans-019krt.jpg[/img] other intermembrane space proteins to the cytosol to induce apoptosis.