Fig 1: JunD was activated in islets of T2DM mice and PA-stimulated INS-1 cells. Blood glucose (A) and body weights (B) of T2DM mice compared with control mice before or after STZ injection. Intraperitoneal glucose tolerance test (IPGTT) (C) and intraperitoneal insulin tolerance test (IPITT) (D) were performed 1 week after the establishment of the T2DM mice model, and the area under curve (AUC) was also calculated. (E) The representative dual-energy X-ray absorptiometry image showed the body fat of the mice and the comparison of body fat percent (BFP%). (F) The representative immunofluorescence images of pancreases stained with insulin and glucagon, and the percentage immune-positive area of the islet insulin and glucagon, scale bar=20 µm. (G) The protein expression of JunD in islets was detected by Western blot. (H) The protein mRNA levels of JunD in PA-stimulated INS-1 cells. Data are expressed as the mean ± SEM. *p < 0.05; **p <0.01; ***p < 0.001 (compared with control group).
Fig 2: The inhibition efficiency of JunD. (A) Western blot analyses and real-time PCR (B) for inhibition efficiency of JunD in INS-1 cells. (C) The protein and (D) mRNA levels of JunD. Data are expressed as the mean± SEM. **p < 0.01; ***p < 0.001 (compared with control group), ###p < 0.001 (compared with PA group).
Fig 3: Schematic diagram of the hypothesis indicating that platelets participate in the pathology of ischemic stroke. Ischemic stroke leads to astrogliosis in the cerebral cortex, while AP-1 transcriptionally upregulates TNF-a, and TNF-a released by activated astrocytes induces high platelet reactivity through the RIP1/RIP3/AKT pathway. These platelets eventually invade and accumulate in the ischemic area, which aggravates the pathological progression of ischemic stroke
Fig 4: JunD/PPAR? signaling pathway involved in PA-induced INS-1 cells dysfunction. INS-1 cells were transfected with JunD siRNA 470 followed by treatment with 0.4 mmol/L PA for 24 hours. (A, B) Expressions of PPAR? in protein and mRNA levels. (C) Apoptosis was assessed by TUNEL assay, scale bar=50 µm. (D) The protein expressions of cleaved-caspase3 and Bax were detected by Western blot. (E) GSIS was performed to show the dysfunction of insulin secretion after PA stimulation. (F) The mRNA expressions of insulin secretion-related genes, including Pdx1, Nkx6.1, Irs-2, Glut2, and Ucp2. (G) Oil Red O staining was performed to detect the intracellular lipid accumulation, scale bar=20 µm. (H) The protein expression of SREBP1c was detected by Western blot. (I) The mRNA levels of TG synthesis, uptake, hydrolysis, and storage-related genes, including Fas, Scd1, Cd36, Fabp4, Lpl, and Plin5. Data are expressed as the mean± SEM. *p < 0.05; **p < 0.01; ***p < 0.001 (compared with control group), #p < 0.05, ##p < 0.01, ###p < 0.001 (compared with PA group).
Fig 5: AP-1 regulates the expression of TNF-a. A Transcription factors that target TNF-a were predicted using the PROMO ALGGEN database within a dissimilarity margin less than or equal to 5%. B–D Luciferase activity levels of HEK293T cells co-transfected with the TNF-a promoter-Luc reporter and B GV230-Jun, C GV230-Fos, or D GV230-JunD or empty vector. E Luciferase activity levels of HEK293T cells co-transfected with the TNF-a promoter-Luc reporter and GV230-vector containing Jun, Fos, and JunD or an empty vector as the control. Data are presented as the mean ± SD of two independent experiments. n = 9 mice/group. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001
Supplier Page from Abcam for Anti-JunD antibody [EPR17365]