Fig 1: GPR43 is involved in the activation of NLRP3 inflammasome in sepsis model by PPAR?. Survival rate (A) in GRP43-/- mice with CLP and PPAR? a for 72 h; W/D rate (B), lung injury score (C), lung tissue using HE staining (D), serum IL-1ß levels (E), PPAR?/NOX-1/EBP50/ p47phox/NLRP3/caspase-1/ IL-1ß protein expressions (F) in GRP43-/- mice with CLP and PPAR? a for 24 h; PPAR?, NOX-1, EBP50, p47phox, NLRP3, Caspase-1 and IL-1ß protein expressions in cells and IL-1ß protein expression in supernatant (G, I), IL-1ß levels (H), ROS production level (J), and SOD activity levels (K) in macrophage by down-regulation of GPR43 and LPS+ATP+GPR43 agonist for 24 h. GPR43-/-, GPR43-/- mice with CLP; GPR43-/-+ PPAR? a, GPR43-/- mice of CLP with PPAR? a; Negative, negative control; Si-GPR43, down-regulation of GPR43; PPAR? a, Pioglitazone; LPS+ATP+4-CMTB, macrophage by treated with LPS+ATP+4-CMTB. ##p<0.01 compared with GPR43-/- mice with CLP or GPR43-/- mice with CLP; **p<0.01 compared with down-regulation of GPR43.
Fig 2: Effect of transfection of p22phox siRNA on the expression of p47phox in HUVECs. (A) Total expression of p47phox was examined using western blotting assays in HUVECs treated with or without UA. There was no significant difference between the total protein expression of p47phox in HUVECs treated with or without UA. (B) HUVECs were transfected with p22phox siRNA and treated with UA. The levels of membrane bound p47phox were detected using western blotting assays. Data are presented as the mean ± SEM. n=3. &P<0.05 vs. control; *P<0.05 vs. the UA group. HUVEC, human umbilical vein endothelial cell; siRNA, small interfering RNA; UA, uric acid.
Fig 3: Effect of transfection of p47phox siRNA on the UA-induced generation of ROS and activation of NADPH oxidase in HUVECs. (A) ROS were detected following treatment with UA in HUVECs transfected with p47phox siRNA. (B) NADPH oxidase activity was detected following treatment with UA in HUVECs transfected with p47phox siRNA. Data are presented as the mean ± SD. n=3. &P<0.05 vs. control; *P<0.05 vs. UA-treated group. HUVEC, human umbilical vein endothelial cell; ROS, reactive oxidative species; siRNA, small interfering RNA; UA, uric acid; DCF, dichlorofluorescein.
Fig 4: Diagram illustrating the process of UA-induced NADPH oxidase activation on the generation of ROS in HUVECs and the impact of LXA4 on the extent of oxidative stress. UA enters the HUVECs and stimulates cytoplasmic subunits. The cytoplasmic subunits migrate to the membrane and bind with the membrane subunits under the guidance of p47phox, which results in the activation of NADPH oxidase. NADPH oxidase then interacts with O2 to produce ROS. LXA4 blocks the transfer of p47phox to the membrane, thus inhibiting the activation of NADPH oxidase and finally reducing the production of ROS. UA, uric acid; LXA4, lipoxin A4; ROS, reactive oxygen species; HUVEC, human umbilical vein endothelial cell.
Fig 5: Protein expression of p47phox in the laryngeal tissues of rats. Four groups of rats were exposed to room air (RA) or intermittent hypoxia (IH) for 14 days with or without daily treatment with YC-1 (YC-1 + IH14) or its vehicle (Vehicle + IH14). The protein expression levels of p47phox in the membrane and cytosolic fractions of laryngeal tissues were measured by Western blot analysis to evaluate the activation of NADPH oxidase. Data in each group are means ± SE of five rats. *p < 0.05 compared with the level of the same fraction in the RA rats; #p < 0.05 compared with the level of the same fraction in the Vehicle + IH14 rats.
Supplier Page from Abcam for Anti-NCF1/p47-phox antibody