Journal: Oncology letters

Article Title: Synergistic cytotoxicity of cisplatin and Taxol in overcoming Taxol resistance through the inhibition of LDHA in oral squamous cell carcinoma.

doi: 10.3892/ol.2015.2931

Figure Lengend Snippet: Figure 1. Cisplatin (CDDP) treatments decrease lactate dehydrogenase‑A (LDHA) expression. (A) CDDP treatments at 5, 10 and 50 µM in OECM‑1 and H‑1 cells decreased the level of LDHA expression. β‑actin served as a loading control. (B) Generation of the CDDP‑resistant cell line. OECM‑1 CDDP‑sensitive (Cis S) and CDDP‑resistant (Cis R) cells were treated at 10, 50 and 100 µM CDDP, followed by the measurement of cell viability. (C) Cis R clone number 1 (C1), and Cis R clone number 2 (C2) and the Cis R pool were cultured, and western blotting was performed to examine the LDHA expression levels. β‑actin served as a loading control. The data in the columns represents the mean of three independent experiments and the bars represent the standard error. *P<0.05 and **P<0.01 vs. control.

Article Snippet: A vector containing wild-type LDHA was purchased from Origene (RC209378; Rockville, MD, USA).

Techniques: Expressing, Control, Cell Culture, Western Blot

Journal: Oncology letters

Article Title: Synergistic cytotoxicity of cisplatin and Taxol in overcoming Taxol resistance through the inhibition of LDHA in oral squamous cell carcinoma.

doi: 10.3892/ol.2015.2931

Figure Lengend Snippet: Figure 2. Taxol‑resistant cells shows increased lactate dehydrogenase‑A (LDHA) expression. (A) Taxol treatments of 0.1, 1 and 10 µM in the OECM‑1 cells induced LDHA expression. β‑actin served as a loading control. (B) Generation of the Taxol‑resistant cell line. OECM‑1 Taxol‑sensitive (Tax S) and Taxol‑resistant (Tax R) cells were treated with 0.1, 1 and 20 µM Taxol, followed by the measurement of cell viability. (C) Tax R clone number 1 (C1), Tax R clone number 2 (C2) and the Tax R pool were cultured, and western blotting was performed to examine the LDHA expression levels. β‑actin served as a loading control. The data in the columns represent the mean of three independent experiments, and the bars represent the standard error. *P<0.05 vs. control.

Article Snippet: A vector containing wild-type LDHA was purchased from Origene (RC209378; Rockville, MD, USA).

Techniques: Expressing, Control, Cell Culture, Western Blot

Journal: Oncology letters

Article Title: Synergistic cytotoxicity of cisplatin and Taxol in overcoming Taxol resistance through the inhibition of LDHA in oral squamous cell carcinoma.

doi: 10.3892/ol.2015.2931

Figure Lengend Snippet: Figure 3. Lactate dehydrogenase‑A (LDHA) plays reverse roles in response to Taxol and cisplatin (CDDP) treatments. (A) Knockdown of LHDA sensitized the OECM‑1 cells to Taxol treatment, but desensitized the OECM‑1 cells to the CDDP treatment. The OECM‑1 cells were transfected with small interfering (si)RNA for 48 h, then treated with CDDP at 10, 50 and 100 µM or Taxol at 0.1, 0.5 and 1 µM, followed by the measurement of cell viability. (B) Overexpression of LDHA sensitized the OECM‑1 cells to CDDP treatment, but desensitized the OECM‑1 cells to Taxol treatment. The OECM‑1 cells were transfected with overexpression vector containing wild‑type LDHA (V) for 48 h, then treated with CDDP at 5, 10 and 50 µM or Taxol at 0.1, 5 and 20 µM, followed by the measurement of cell viability. The columns represent the mean of three independent experiments, and the bars represent the standard error. *P<0.05 and **P<0.01 vs. control.

Article Snippet: A vector containing wild-type LDHA was purchased from Origene (RC209378; Rockville, MD, USA).

Techniques: Knockdown, Transfection, Over Expression, Plasmid Preparation, Control

Journal: Oncology letters

Article Title: Synergistic cytotoxicity of cisplatin and Taxol in overcoming Taxol resistance through the inhibition of LDHA in oral squamous cell carcinoma.

doi: 10.3892/ol.2015.2931

Figure Lengend Snippet: Figure 4. Combination of Taxol and cisplatin (CDDP) shows synergistic effects on the Taxol‑resistant (Tax R) cells through the inhibition of lactate dehydro genase‑A (LDHA). (A) Tax R cells were treated with Taxol alone at 0.1, 1 and 20 µM, CDDP alone at 10 µM, 5‑FU alone at 500µM, Taxol plus CDDP or Taxol plus 5‑fluorouracil (FU), followed by the measurement of cell viability. (B) LDHA was downregulated in response to the treatment with the combination of Taxol and CDDP, but exhibited no change following treatment with the combination of Taxol and 5‑FU. (C) The overexpression of LDHA in the Taxol‑resistant (Tax R) cells resulted in acquired resistance to treatment with the combination of Taxol and CDDP. The cells were transfected with a vector containing wild‑type LDHA (V) for 48 h, followed by depletion of the medium and treatment with the drugs for 24 h. A cell viability assay was performed. Columns represent the mean of three independent experiments, and bars represent the standard error. *P<0.05 vs. control.

Article Snippet: A vector containing wild-type LDHA was purchased from Origene (RC209378; Rockville, MD, USA).

Techniques: Inhibition, Over Expression, Transfection, Plasmid Preparation, Viability Assay, Control

Journal: bioRxiv

Article Title: Mitochondrial Dysfunction and Senescence Accompany Glioblastoma Cell Death Triggered by a Putative Metabolic Inhibitor

doi: 10.1101/2025.09.08.674975

Figure Lengend Snippet: (A) Immunoblot showing overexpression of LDHA at 5 and 10 mg concentration of the LDHA plasmid in U87 cells, represented with LDHA and Myc tag LDHA. Quantification of the percentage of overexpression observed. (B) Cell viability of control, empty vector, and LDHA plasmid overexpression. Cell viability graphs of STP, TMZ, and GSK without overexpression of LDHA and with overexpression of LDHA. (C) Immunoblot representing LDHA knockdown by siLDHA. Quantification of the percentage decrease in LDHA expression. (D) Cell viability analysis of STP, TMZ, and GSK upon knockdown of LDHA. (E) Kinetic evaluation of LDHA enzyme activity assay with STP, and sodium oxamate. (F) Cell viability of SKNSH cells upon treatment with STP and Diazepam. n=3, *p<0.033, **p<0.002, ***p<0.001, one-way ANOVA Tukey test.

Article Snippet: U87 cell line was purchased from ATCC (USA), fetal bovine serum (FBS) (Atlanta Bio, USA), Dulbecco’s modified Eagle medium (DMEM), PSA, and Trypsin (Corning, USA), stiripentol and temozolomide (Fisher, USA), GSK2837807 sodium oxamate (Sigma, USA), siLDHA and Lipofectamine RNAimax (Life technologies, USA), LDHA plasmid (Origene, USA), Transit LT-1 (Mirrus, USA), Opti-MEM (Gibco, USA), BCA (Thermoscientific, USA), Direct-Zol RNA extraction kit (Zymo research, USA), CMH 2 DCFDA and CMXROS (Invitrogen, USA), primary antibodies β-actin, ALDHA13, AOX1, CPA4, TXNIP, KYNU, (Proteintech, USA), LC3 (Sigma) secondary antibodies anti-mouse, anti-rabbit, and senescence kit (Cell signaling, USA).

Techniques: Western Blot, Over Expression, Concentration Assay, Plasmid Preparation, Control, Knockdown, Expressing, Enzyme Activity Assay

Journal: Cell Death & Disease

Article Title: Targeting LINC01711 in FAP + cancer-associated fibroblasts overcomes lactate-mediated immunosuppression and enhances anti-PD-1 efficacy in lung adenocarcinoma

doi: 10.1038/s41419-025-07974-6

Figure Lengend Snippet: A The results of ECAR assays performed in FAP + CAFs transfected with si-LINC01711 or si-NC ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. B – D The results of glucose uptake, intracellular lactate production and extracellular lactate production measurement performed in FAP + CAFs transfected with si-LINC01711 or si-NC ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. E Flow chart of [U13 C] Glucose stable isotope tracer analysis. F [U13 C] Glucose stable isotope tracer analysis was performed in FAP + CAFs transfected with si-LINC01711 or si-NC. The lactate was shown ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. G Silver SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) image revealing proteins immunoprecipitated by LINC01711 and its antisense RNA in FAP + CAFs. H Western blotting validated the interaction between LINC01711 and LDHA. I RNA-pulldown assay was performed using biotin-LINC01711 and recombinant LDHA, followed by western blotting validation. J RIP (RNA immunoprecipitation) assay followed by RT-qPCR analysis confirmed that LINC01711 bound to LDHA, rather than LDHB ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. K Dual RNA-FISH (fluorescence in situ hybridization) and immunofluorescence assay showing the colocalization of LINC01711 and LDHA in FAP + CAFs. Scale bars: 10 μm. L RT-qPCR detection of LINC01711 expression in the cytoplasmic and nuclear fractions of FAP + CAFs. M Immunoblot detection of LDHA protein in FAP + CAFs by searching for biotinylated RNA or its antisense sequence of LINC01711 isoform transcribed in vitro. N Molecular docking predicted 3D structure of the LDHA-LINC01711-Δ1 complex. O RIP (RNA immunoprecipitation) assay followed by RT-qPCR analysis confirmed the interaction between LDHA-mutant and LINC01711 ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. P Western blotting validated the interaction between the interaction between LDHA-mutant and LINC01711. Q Western blotting confirmed that altering LINC01711 expression would not affect LDHA expression. R RT-qPCR confirmed that altering LINC01711 expression would not affect LDHA expression ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. All the results were shown as mean ± S.E.M. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001.

Article Snippet: Recombinant human LDHA variants ( P01711 , Solarbio) were mixed with active recombinant His tagged-FGFR1 ( P09665 , Solarbio) in kinase reaction buffers (HER2: 20 mM Tris (pH 7.5), 5 mM MnCl2, 0.5 mM Na3VO4, 1 mM EGTA, 2 mM DTT, 5 mM β-glycerophosphate, 0.01% CHAPS) at 30 ° C for 30 min. Terminate the reaction by soaking in a boiling water bath for 5 min. Quickly freeze the protein in liquid nitrogen and perform Western blot analysis of LDHA-Y10 phosphorylation.

Techniques: Transfection, Two Tailed Test, SDS Page, Polyacrylamide Gel Electrophoresis, Immunoprecipitation, Western Blot, Recombinant, Biomarker Discovery, RNA Immunoprecipitation, Quantitative RT-PCR, Fluorescence, In Situ Hybridization, Immunofluorescence, Expressing, Sequencing, In Vitro, Mutagenesis

Journal: Cell Death & Disease

Article Title: Targeting LINC01711 in FAP + cancer-associated fibroblasts overcomes lactate-mediated immunosuppression and enhances anti-PD-1 efficacy in lung adenocarcinoma

doi: 10.1038/s41419-025-07974-6

Figure Lengend Snippet: A LDHA activity detection revealed that LINC01711 knockdown inhibited LDHA activity ( n = 5 biological repeats). The P -value was calculated by two-tailed unpaired t- test. B Western blot revealed that phosphorylation level of LDHA significantly decreased when LINC01711 was knockdown. C The results of western blot indicated the level of phosphorylation at the Y10 site of LDHA when FGFR1, Her2 or JAK was knocked down. D Western blot detected the level of phosphorylation at the Y10 site of LDHA in FAP + CAFs treated with PD166866 , oe-LINC01711, and both. E , F RNA-pulldown assay was performed using biotin-LINC01711 and endogenous FGFR1, or biotin-LINC01711 and recombinant LDHA, followed by western blotting validation. G RIP (RNA immunoprecipitation) assay followed by RT-qPCR analysis confirmed that LINC01711 bound to FGFR1 ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. H BiFC (Bimolecular fluorescence complementation) experiment revealed LINC01711 could modulates the phosphorylation by FGFR1. I , J Immunoprecipitation experiment revealed that LINC01711 could promotes the interaction between FGFR1 and LDHA. K The in vitro kinase assay was conducted using recombinant His-tagged LDHA and His-tagged FGFR1. The result showed that LINC01711 could significantly promote FGFR1 mediated phosphorylation of LDHA. L Western blot, indicated that overexpression of LINC01711 could upregulated LDHA phosphorylation and the process depends on FGFR1. M Crosslinking followed by western blot revealed that LINC01711 could promote the tetramer formation of LDHA, which was dependent on the participant of FGFR1. N The result of size exclusion chromatography followed by western blot was consistent with crosslinking results. All the results were shown as mean ± S.E.M. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001.

Article Snippet: Recombinant human LDHA variants ( P01711 , Solarbio) were mixed with active recombinant His tagged-FGFR1 ( P09665 , Solarbio) in kinase reaction buffers (HER2: 20 mM Tris (pH 7.5), 5 mM MnCl2, 0.5 mM Na3VO4, 1 mM EGTA, 2 mM DTT, 5 mM β-glycerophosphate, 0.01% CHAPS) at 30 ° C for 30 min. Terminate the reaction by soaking in a boiling water bath for 5 min. Quickly freeze the protein in liquid nitrogen and perform Western blot analysis of LDHA-Y10 phosphorylation.

Techniques: Activity Assay, Knockdown, Two Tailed Test, Western Blot, Phospho-proteomics, Recombinant, Biomarker Discovery, RNA Immunoprecipitation, Quantitative RT-PCR, Fluorescence, Immunoprecipitation, In Vitro, Kinase Assay, Over Expression, Size-exclusion Chromatography

Journal: Cell Death & Disease

Article Title: Targeting LINC01711 in FAP + cancer-associated fibroblasts overcomes lactate-mediated immunosuppression and enhances anti-PD-1 efficacy in lung adenocarcinoma

doi: 10.1038/s41419-025-07974-6

Figure Lengend Snippet: A – E ECAR assay, glucose uptake assay, lactate production assay and LDHA activity assay were performed in FAP+ CAFs transfected with si-LINC01711 or si-NC, treated with LDH inhibitor or not ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. F – J . ECAR assay, glucose uptake assay, lactate production assay and LDHA activity assay were performed in FAP + CAFs transfected with si-LINC01711 or si-NC, co-transfected with LDHA WT or LDHA mutant ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. K – O ECAR assay, glucose uptake assay, lactate production assay and LDHA activity assay were performed in FAP + CAFs transfected with si-LINC01711 or si-NC, co-transfected with si-FGFR1 or si-NC ( n = 3 biological repeats). The P -value was calculated by two-tailed unpaired t -test. P Flow chart of in vitro co-culture model. Q Flow cytometry analysis on CD8-positive T cells infiltration, GZMB + CD8-positive T cells infiltration and CD69 + CD8-positive T cells infiltration in in vitro co-culture model. R Flow chart of in vivo model. S Representative image of subcutaneous tumors. n = 5 biological repeats. T Tumor volume of subcutaneous tumors ( n = 5 biological repeats, the P -value was determined by two-way ANOVA with Tukey’s multiple comparison test). U Tumor weight of subcutaneous tumors ( n = 5 biological repeats, the P -value was calculated by two-tailed unpaired t -test). All the results were shown as mean ± S.E.M. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001.

Article Snippet: Recombinant human LDHA variants ( P01711 , Solarbio) were mixed with active recombinant His tagged-FGFR1 ( P09665 , Solarbio) in kinase reaction buffers (HER2: 20 mM Tris (pH 7.5), 5 mM MnCl2, 0.5 mM Na3VO4, 1 mM EGTA, 2 mM DTT, 5 mM β-glycerophosphate, 0.01% CHAPS) at 30 ° C for 30 min. Terminate the reaction by soaking in a boiling water bath for 5 min. Quickly freeze the protein in liquid nitrogen and perform Western blot analysis of LDHA-Y10 phosphorylation.

Techniques: ECAR Assay, Activity Assay, Transfection, Two Tailed Test, Mutagenesis, In Vitro, Co-Culture Assay, Flow Cytometry, In Vivo, Comparison

Journal: International Journal of Molecular Sciences

Article Title: Effect of LDHA Inhibition on TNF-α-Induced Cell Migration in Esophageal Cancers

doi: 10.3390/ijms232416062

Figure Lengend Snippet: Expression levels of LDHA and LDHB in esophageal cancer cells. ( A ) RT-qPCR analysis of LDHA and LDHB expression changes in response to TNF-α (30 ng/mL) stimulation for 24 h in ESCC and EAC cells (KYSE150 and EC7, respectively). Statistically significant increase in TNF-α-dependent expression for both LDHA (FC = 1.98 ± 0.08 vs. untreated control) and LDHB (FC = 1.88 ± 0.2 vs. untreated control) was found in KYSE150 cells. In the presence of TNF-α in EC7 cells, only LDHA levels significantly increased (FC = 2.28 ± 0.26 vs. untreated control). ( B ) LDHA and LDHB mRNA expression in two esophageal cancer cell lines, KYSE150 and EC7, by regular RT-PCR. ACTB (β-actin) was used as an internal control. * p < 0.05, ** p < 0.001.

Article Snippet: Primers for the LDHA and LDHB genes were products of OriGene (HP208683 and HP208217).

Techniques: Expressing, Quantitative RT-PCR, Control, Reverse Transcription Polymerase Chain Reaction

Journal: International Journal of Molecular Sciences

Article Title: Effect of LDHA Inhibition on TNF-α-Induced Cell Migration in Esophageal Cancers

doi: 10.3390/ijms232416062

Figure Lengend Snippet: The effect of TNF-α on the composition of LDH isoforms and on the protein levels of LDHA and MMP9 in esophageal cancer cells. ( A ) Electrophoretic patterns in KYSE150 cells stimulated with TNF-α at different concentrations (upper panel) and the corresponding isoform profiles (lower panel) showing no change in the percentage of LDH isoforms. ( B ) Dose-dependent changes in electrophoretic patterns in EC7 cells under TNF-α stimulation; FC—fold change vs. untreated control calculated from differential densitometry of signals from the gel. ( C ) Changes in MMP9 activity by gelatin zymography and protein levels of LDHA, LDHB, HIF-1α, phospho-LDHA(Tyr10), LDHA by Western blotting in EC7 (upper panel) and KYSE150 (lower panel), respectively, in relation to TNF-α concentration and time. ( D ) Electrophoretic pattern in TNF-α (30 ng/mL) stimulated KYSE150 for 24 h in the presence of SO (25 and 50 mM) showing no change in the relative percentage of isoenzymes. Ctrl—control, LD1-LD5—LDH isoenzymes, ACTB—β-actin/loading control.

Article Snippet: Primers for the LDHA and LDHB genes were products of OriGene (HP208683 and HP208217).

Techniques: Control, Activity Assay, Zymography, Western Blot, Concentration Assay

Journal: Disease markers

Article Title: lncRNA-DANCR Promotes Taxol Resistance of Prostate Cancer Cells through Modulating the miR-33b-5p-LDHA Axis.

doi: 10.1155/2022/9516774

Figure Lengend Snippet: Figure 8: Restoration of LDHA rescues the miR-33b-5p-promoted Taxol sensitization. (a) PC3-TXR cells without or with LDHA knockdown were treated with Taxol. Cell survival was evaluated by clonogenic assay and (b) MTT assay. (c) PC3-TXR cells were transfected with control miRNA, miR-33b-5p alone, or plus LDHA overexpression plasmid. Protein expression of LDHA was determined. (d) Glucose uptake and (e) lactate product from the above transfected cells were examined. (f) The above transfected PC3- TXR cells were treated with Taxol at the indicated concentrations. Cell viability was determined by MTT assay. ∗p < 0:05 and ∗∗p < 0:01.

Article Snippet: LDHA overexpression plasmid was purchased from http://Origene.com. miRNA-33b-5p and control miRNA were synthesized by GenePharma (Shanghai, China). siRNA and miRNA were transfected at 25nM for 48 hours.

Techniques: Knockdown, Clonogenic Assay, MTT Assay, Transfection, Control, Over Expression, Plasmid Preparation, Expressing

Journal: Disease markers

Article Title: lncRNA-DANCR Promotes Taxol Resistance of Prostate Cancer Cells through Modulating the miR-33b-5p-LDHA Axis.

doi: 10.1155/2022/9516774

Figure Lengend Snippet: Figure 9: The roles of DANCR-miR-33b-5p-LDHA in Taxol resistance of PCa cells. (a) Control vector, DANCR alone, or plus miR-33b-5p was transfected into PC3-TXR cells. Expressions of miR-33b-5p, (b) LDHA, (c) glucose uptake, and (d) lactate product were detected. (e) The above transfected cells were treated with Taxol at the indicated concentrations. Cell survival was evaluated by MTT assay and (f) Annexin V apoptosis assay. ∗p < 0:05 and ∗∗p < 0:01.

Article Snippet: LDHA overexpression plasmid was purchased from http://Origene.com. miRNA-33b-5p and control miRNA were synthesized by GenePharma (Shanghai, China). siRNA and miRNA were transfected at 25nM for 48 hours.

Techniques: Control, Plasmid Preparation, Transfection, MTT Assay, Apoptosis Assay

Journal: Aging (Albany NY)

Article Title: Metformin suppresses Nrf2-mediated chemoresistance in hepatocellular carcinoma cells by increasing glycolysis

doi: 10.18632/aging.103777

Figure Lengend Snippet: Metformin increased glucose uptake and glycolysis in HepG2/DDP cells. ( A ) Metformin increased glucose uptake. Indicated cells were treated with or without metformin (1mM) for 24 hours and glucose uptake assay were conducted with Glucose Uptake-Glo. Cell Titer-Glo was also carried out to measure the relative viability, which was used to normalize the data in glucose uptake assay. Data from 3 independent biological samples of 3 replicates were statistically analyzed by student’s t-test (*** P<0.0001). ( B ) Metformin increased the expression of glucose transporter Glut1 and Glut4. HepG2/DDP cells were treated with or without metformin (1mM) for 24 hours and total cell lysates were separated by SDS-PAGE. Glut1 and Glut4 protein levels were detected by Western blot using specific antibodies to Glut1 and Glut4. Tubulin was used as internal control. Representative images of were shown. Quantification of N= 2 biological repeats were shown in bar graph. ( C ) Metformin increased intracellular glucose concentration in HepG2/DDP cells. HepG2/DDP cells were treated with or without metformin (1mM) for 24 hours, washed extensively and intracellular glucose concentration was measured by using Glucose-Glo kit. Data from 2 independent biological samples of 3 replicates were plotted and statistically analyzed by student’s t-test (** P<0.001). ( D ) Metformin increased the protein levels of glycolytic enzymes HK2 and LDHA. Experiment was conducted as in (B) except HK2 and LDHA antibodies were used. Representative images of were shown. Quantification of N= 3 biological repeats were shown in bar graph. ( E ) Metformin increased intracellular lactate production. Indicated cells were treated with or without metformin (1mM) for 24 hours, washed extensively then intracellular lactate concentration was measured by using lactate-Glo kit. Data from 2 independent biological samples of 3 replicates were plotted and statistically analyzed by student’s t-test (** P<0.001, *** P<0.0001). ( F ) Metformin increased intracellular NAD/NADH production. HepG2/DDP cells were treated with or without metformin (1mM) for 24 hours and lactate concentration was measured by using NAD/NADH -Glo kit. Data from 2 independent biological samples of 3 replicates plotted and statistically analyzed by student’s t-test (* P<0.05, **P<0.001). ( G ) Metformin increased intracellular NADP/NADPH production. HepG2/DDP cells were treated with or without metformin (1mM) for 24 hours and lactate concentration was measured by using NADP/NADPH -Glo kit. Data from 2 independent biological samples of 3 replicates were plotted and statistically analyzed by student’s t-test (*** P<0.0001).

Article Snippet: Membranes were blocked in 5% non-fat milk and probed with primary antibodies in 5% non-fat milk at the following concentration: Nrf2 (Promab Biotechnologies, #30597) at 2000X, Tubulin (Promab Biotechnologies, #20374) 0.2 ug/ml, Glut1 (R&D Systems, MAB14181) 2 ug/ml, Glut4 (Abcam, ab654) at 2500X dilution, HK2 (R&D Systems, MAB8179) at 0.2 ug/ml, LDHA (R&D Systems, AF7304).

Techniques: Expressing, SDS Page, Western Blot, Control, Concentration Assay