GLUT1 Antibody - #AF0173

Fig. 4. | Bruceine A induces cell growth inhibition and apoptosis via PFKFB4-mediated glycolysis in MIA PaCa-2 cells. (C) MIA PaCa-2 cells were treated with various concentrations of bruceine A for 24 h. Protein levels of GLUT1, HK2, PFKFB4, PFKM, PKM2, LDHA, and β-actin were detected. β-actin was served was as control. Results were expressed as means ± SD of three independent experiments. *p < 0.05, **p < 0.01, ***p < 0.001 versus control cultured with 0.1% DMSO by one-way ANOVA and post hoc tests.

FIGURE 1 | Angiopoietin like-8 (ANGPTL8) was increased in serum and placenta tissues of gestational diabetes mellitus (GDM) mice. (K) The expression levels of glucose transporter 1 (GLUT1) and GLUT4 in placenta tissues.

FIGURE 2 | Silencing of ANGPTL8 inhibited IR in trophoblast cells.(F, G) Immunofluorescent staining was used to detect the expression and distribution of GLUT1 and GLUT4 in HTR-8/SVneo cells. (the scale bar represents 50 mm; *p < 0.05, ***p < 0.001,ns, no significance).

Figure 1 Angiopoietin like-8 (ANGPTL8) was increased in serum and placenta tissues of gestational diabetes mellitus (GDM) mice. (A) The mice were treated as described in the chart. (B) The body weight of mice in normal fat diet (NFD) and high fat diet (HFD) groups. (C) Oral glucose tolerance test (OGTT) was performed at gestational day (GD)0.5, 11.5 and 16.5. (D, E) Fasting blood glucose and insulin levels were measured at GD18.5. (F) Homeostasis model assessment insulin resistance (HOMA-IR) was calculated as follow: HOMA-IR= blood glucose (mM)×blood insulin (mU/l)/22.5. (G) The contents of triglyceride (TG), total cholesterol (TC), high density lipoprotein (HDL-C) and low density lipoprotein (LDL-C) in serum were detected. (H) HE staining was performed to detect the pathological changes in labyrinth zone of placenta tissues. (I) Periodic acid Schiff (PAS) staining was carried out to detect the glycogen accumulation in labyrinth zone of placenta tissues. (J) Western blot was used to determine the levels of insulin signaling related molecules, p-IRβ(Tyr1361), IRβ, p-IRS-1(Ser307), p-IRS-1(Tyr896), IRS-1, p-Akt and Akt in placenta tissues. (K) The expression levels of glucose transporter 1 (GLUT1) and GLUT4 in placenta tissues. (L) The serum level of ANGPTL8 in mice. (M, N) The mRNA and protein levels of ANGPTL8 in placenta tissues. (the scale bar represents 100 μm; **p < 0.01, ***p < 0.001 vs. NFD).

Figure 1 Identification and charactorization of circATP2B1 in gastric cancer tissues and cells. (A). Relative expression of circATP2B1 in normal gastric tissues (GT), highly differentiated adenocarcinoma cancer (HDAC) and poorly differentiated gastric adenocarcinoma cancer (PDAC) specimens. (B). Relative expression of circATP2B1 in gastric cancer cell lines MKN45 and SGC7901 as well as GES-1. (C). Relative expression of ATP2B1 mRNA in GT, HDAC and PDAC specimens. (D). Schematic illustration showing the genomic loci of ATP2B1 gene and circATP2B1 derided from exons 2 and 3 of ATP2B1. (E). Fluorescence hybridization in situ (FISH) assay showed the localization of circATP2B1 in cell. The circATP2B1 probe was labeled with FITC (green). Nucleus was stained with DAPI (blue). The image was taken at 1,000× magnification. The scale bar represented 10 μm. (F). Actinomycin assay was performed to evaluate the stability of circATP2B1 and ATP2B1 mRNA in MKN45 cell. (G). Expressions of glycolysis-related proteins GLUT1, GLUT3, LDHA, PKM2 in GT, HDAC and PDAC. (H). EdU incorporation assay and (I) CCK8 Cell proliferation assay in circATP2B1(+) and circATP2B1(−) cells. (J). The glucose uptake assay (K) lactate accumulation and (L) ATP/ADP ratio (M) NAD+/NADH ratio of MKN45 and SGC7901 cell lines stably overexpressing or knockdown of circATP2B1. (Data represented means ± SD, n=3, *P < 0.05, **P<0.01, # P < 0.05, ## P < 0.01 compared with circATP2B1(-)NC group).

Figure 7. TXNIP expression correlated inversely with GLUT1 expression in prostate cancer and TXNIP overexpression attenuated glucose uptake in the PC-3 cells. (A) GLUT1 protein expression level in 50 prostate cancer tissues were detected by IHC. (B) Negative correlation between TXNIP and GLUT1 mRNA expression patterns in prostate cancer tissues from TCGA cBioportal database. (C) The mRNA expression level of GLUT1 in normal prostatic epithelial cell line and prostate cancer cell lines was examined by qRT-PCR assay. (D and E) The protein expression level of GLUT1 in normal prostatic epithelial cell line and prostate cancer cell lines was examined by Western blot assay. (F) After overexpression of TXNIP in PC-3 cells, the mRNA expression level of GLUT1 was examined by qRT-PCR assay. (G and H) After overexpression of TXNIP in PC-3 cells, the protein expression level of GLUT1 was examined by Western blot assay. (I) The 2-NBDG glucose uptake demonstrated that TXNIP overexpression suppressed glucose uptake in PC-3 cells. The β-actin gene and protein were used as internal controls. Data represented the mean ± standard deviation of 3 independent experiments (*P < 0.05, **P < 0.01, ***P < 0.001).