Fig 1: TXNIP inhibitor (Resveratrol) alleviates pancreatic necrosis, systemic inflammation and oxidative stress in L-arginine-induced acute pancreatitis without changes in GSDMD. (a) The experimental schedule. (b–d) The levels of amylase (b), lipase (c) and LDH (d) in serum were detected (n = 3). (e) The levels of IL-1ß in pancreas tissues were detected (n = 3). (f) The general morphology of the pancreas was observed. (gi–giv) Representative H&E images and histopathological scores of the pancreas in L-arginine-acute pancreatitis (n = 5). Scale bars, 100 µm. (hi,hii) Representative immunofluorescence staining of GSDMD (red), CALNEXIN (green) and DAPI (dark blue) in formalin-fixed paraffin-embedded of pancreas tissues and pearson’s correlation coefficient of GSDMD and CALNEXIN (n = 5). Scale bars, 100 µm. (ii,iii,ji,jii) Representative immunofluorescence staining of TXNIP, HIF-1a (red) and DAPI (dark blue) in formalin-fixed paraffin-embedded of pancreas tissues (n = 5). Scale bars, 100 µm. All values were shown as the mean ± SEM. # p < 0.05 compared with control group, * p < 0.05, ** p < 0.01 compared with mice acute pancreatitis model groups. Unpaired Student’s t-tests were used in (b–e,gii–giv,hii,iii,jii). Resveratrol represents RES.
Fig 2: Acidosis drives MondoA transcriptional activity.(A) TXNIP mRNA levels in murine embryonic fibroblasts (MEFs) following treatment with HBSS for the indicated times. (B) Glucose uptake was determined by quantifying the rate of 3H-2-deoxyglucose uptake in MEFs following a 4 hr treatment with HBSS. (C) TXNIP mRNA levels from MEFs treated for 4 hr with DMEM, HBSS and HBSS supplemented with sodium bicarbonate to the amount in DMEM (3.7 g/L). (D) CRISPR/Cas9 was used to disrupt expression of MondoA in HeLa cells. Amounts of the indicated proteins in HeLa and HeLa:MondoA-KO cells were determined using immunoblotting. Consistent with our previous findings TXNIP expression was highly dependent on MondoA. TXNIP mRNA levels from HeLa and HeLa:MondoA-KO cells following a 4 hr treatment with DMEMAcidic. (E) TXNIP mRNA levels in HEK-293T, HeLa and HepG2 cells following 4 hr treatments with DMEMAcidic. In A, C, D and E, TXNIP mRNA levels were determined by reverse transcriptase-quantitative PCR (RT-qPCR). ***p<0.001; ****p<0.0001; ns – not significant.
Fig 3: LUT inhibits the TXNIP/NLRP3 pathway in CYP-induced cystitis. (a) The expression of TXNIP, TRX, NLRP3, ASC, and caspase-1 in each test group was detected by western blot. LUT inhibited the upregulation of TXNIP, NLRP3, ASC, and caspase-1 in CYP-induced cystitis and increased the expression of TRX. The expression analysis of TXNIP (b), TRX (c), NLRP3 (d), ASC (e), and caspase-1 (f) protein in the bladder of each group (n = 6). *P < 0.05, **P < 0.01, and ***P < 0.001; NS: not significant.
Fig 4: Expression levels of TXNIP and NLRP3 inflammasome-associated proteins in renal tissue of DN rats. (A) Western blot images and (B) quantified protein levels of TXNIP, NLRP3, cleaved-caspase-1, caspase-1, IL-1 and IL-18 in the control and DN groups. (C) Streptavidin-peroxidase staining was used to detect the TXNIP and NLRP3 proteins expression in kidneys tissues (magnification, ×100), and (D) the quantified staining intensity is shown. *P<0.05 and **P<0.01, vs. control group. DN, diabetic nephropathy; TXNIP, thioredoxin interacting protein; NLRP3, NOD-like receptor protein 3; IL, interleukin.
Fig 5: The TXN or TXNIP protein expression level in the APP/PS1 mice. Representative images of Western blotting for TXN, TXNIP, and ß-actin in (a) the brain and (b) liver. Densitometric analysis of TXN or TXNIP and calculation of the ratio of TXN/TXNIP in the cerebral cortex of the brain (c–e) and the liver (f–h). Data are presented as mean ± SEM (n = 6). Significance: ** p < 0.01, * p < 0.05. Full-length blots are presented in Supplementary Figures S1 and S2.
Supplier Page from Abcam for Anti-TXNIP antibody [EPR14774]