GLUT3 Antibody - #AF5463

Figure 5 RH reduced brain GLUT3-mediated glucose uptake in STZ-induced APP/PS1-DM mice. (A) Representative PET/CT images showing in vivo brain 18F-FDG uptake (coronal, sagittal, and transaxial sections, n = 6 mice for each group). Cor, Cortex; Hip, hippocampus; Mid, midbrain; HPOA, hypothalamus; BS, brain stem; Cer, cerebellum; OB, Olfactory Bulb; BF, basal forebrain; Tha, thalamus; SC, superior colliculi; CG, central gray; Str, striatum. (B) Quantification for SUV of 18F-FDG in brain region (n = 6 for mice for each group). (C) Western blot and quantitation for GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, SGLT1, and SGLT2 in hippocampal homogenates (n = 3 mice for each group). The data are expressed as the mean ± SEM. Statistical significance was assessed using unpaired Student’s t test. *P < 0.05 and **P < 0.01, APP/PS1-DM versus APP/PS1; #P < 0.05 and ##P < 0.01, APP/PS1-DM-RH versus APP/PS1-DM; WT versus APP/PS1; NS, no significant difference.

Figure 6 Effects of ICA on glucose transporters in the cerebral cortex of 3×Tg-AD mice. The protein expression of GLUT1 (A) and GLUT3 (B) in the cerebral cortex. The expression levels were normalized to those in the WT + vehicle group. The data are presented as the means ± SEM (n = 4–5). *P < 0.05, vs. WT + vehicle group; #P < 0.05, vs. 3×Tg-AD + vehicle group (one-way analysis of variance followed by the least significant difference test). 3×Tg-AD: A triple-transgenic mouse model of Alzheimer’s disease; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GLUT: glucose transporter; ICA: icariin; WT: wild-type.

Fig. 6. GLUT1 and GLUT3 expression. Representative immunoblots of GLUT1 (A, B) and GLUT3 (C, D) in the cortex and hippocampus in each group. Protein immunoreactivity was normalized to -actin. Individual data are presented as the mean ± S.E.M. from 5 individual mice in each group.

Fig. 3. IL13 secreted by YAP1-overexpressed GC cells stimulates resistance to 5-FU via inducing M2 subtype macrophage glycolysis reprogramming. A-C. RT-PCR was used to detect the mRNA expression of glycolysis enzymes, fatty acid and amino acid metabolism enzymes in THP1 after co-cultured with MKN-YAP1 or MKN45-Vetor. D. Protein level change of glycolysis enzymes in THP1 after co-cultured with MKN-YAP1, MKN45-Vetor, SGC7901-siYAP1 or SGC7901-NC. E. RT-PCR revealed the mRNA expression of glycolysis enzymes and M2 TAMs markers in THP1 after co-cultured with SGC7901-siYAP1 or SGC7901-NC. F-G. Relative lactate release from cells was determined by colorimetric analysis. Relative glucose uptake cells by Flow cytometry detection. All data presented are the mean ± SD (*p < 0.05, **p < 0.01) of triplicate determination from three independent experiments.

Figure 2 Zinc promoted glucose transport in PC12 neurons. (a–c) The expression levels of GLUT3 and GLUT4 proteins were assessed by WB (n = 6). (d, e) Glucose uptake assay was performed by using 2-NBDG (n = 6, scale bar = 10 μm). (f, g) Immunofluorescence was used to detect the level of GLUT3 (cytoskeleton was labeled with β-tubulin) (n = 6, scale bar = 50 μm). (h, i) The expression of GLUT4 was detected by immunofluorescence (cytoskeleton was labeled with phalloidin) (n = 6, scale bar = 50 μm). Data are represented as the means ± SD. ∗p < 0.05, ∗∗p < 0.01, and ∗∗∗p < 0.001.