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Image Search Results

Journal: Nature Communications
Article Title: Nuclear lactate dehydrogenase A senses ROS to produce α-hydroxybutyrate for HPV-induced cervical tumor growth
doi: 10.1038/s41467-018-06841-7
Figure Lengend Snippet: HPV16/18 E7 induces LDHA nuclear translocation by ROS accumulation. a LDHA is significantly translocated into nucleus in HPV16 positive cervical cancer tissues. Representative IHC images for LDHA localization in HPV16-negative and positive cervical tumor samples. Scale bar, 100 μm. b Nuclear LDHA is dramatically increased in HPV16-positive cervical cancer tissues. Semi-quantitative cytoplasmic LDHA and nuclear LDHA scoring was performed in HPV16 negative ( n = 27) and positive ( n = 39) cervical tumor samples. c , d HPV16/18 E7 promotes LDHA nuclear translocation in a ROS-dependent manner. Primary human cervix keratinocytes (PHKs) stably expressing vector or Flag-tagged HPV16/18 E7 were treated with or without 1 mM NAC for 6 h, followed by staining with anti-LDHA (green), anti-Flag (red) antibodies, and DAPI (blue). Scale bars, 10 μm ( c ). The percentage of cells with nucleus-localized LDHA compared to total cell number was quantified ( d ). e HPV16/18 E7 enhances ROS production. Cellular ROS were measured in PHKs stably expressing vector or HPV16/18 E7 coupled with or without 1 mM NAC treatment for 6 h, followed by using the ROS-sensitive fluorescent dye (CM-H 2 DCFDA) with flow cytometry according to the manufacturer’s protocol. f , g LDHA nuclear translocation is profoundly increased in an H 2 O 2 -dose-dependent manner. Immunofluorescent images of LDHA (green) in HaCaT cells upon different dose of H 2 O 2 treatment as indicated. DAPI, blue. Scale bars, 10 μm ( f ). The percentage of cells with nucleus-localized LDHA compared with total cell number was quantified ( g ). h ROS promote LDHA nuclear translocation. HT-3 cells were treated with or without 10 μM H 2 O 2 for 6 h, and supplemented with or without 1 mM NAC for extended 6 h as indicated for nuclear isolating, followed by blotting with LDHA, Tubulin, and Lamin B1. Results are representative of three independent experiments. All data are shown as mean ± SEM. The p values were determined by two-tailed t -test. The values of p
Article Snippet: Hydrogen peroxide solution (H2 O2 ) (Sigma, 323381),
Techniques: Translocation Assay, Immunohistochemistry, Stable Transfection, Expressing, Plasmid Preparation, Staining, Flow Cytometry, Cytometry, Two Tailed Test

Journal: International Journal of Oncology
Article Title: Long non-coding RNA HOXD-AS1 promotes tumor progression and predicts poor prognosis in colorectal cancer
doi: 10.3892/ijo.2018.4400
Figure Lengend Snippet: Long non-coding RNA HOXD-AS1 regulates epithelial-mesenchymal transition and stem cell formation in colorectal cancer cells. (A) Knockdown of HOXD-AS1 increased E-cadherin expression and reduced Vimentin expression in HCT116 cell. Magnification, ×200. (B) RT-qPCR analysis demonstrated that knockdown of HOXD-AS1 decreased the expression levels of Vimentin, N-cadherin, Slug and Snail, and increased the expression of E-cadherin, α-catenin and β-catenin in HCT116 cells ( * P
Article Snippet: The following antibodies were used in the present study: E-cadherin (#3199S) and
Techniques: Expressing, Quantitative RT-PCR

Journal: Oncology Letters
Article Title: Role of epithelial-mesenchymal transition markers E-cadherin, N-cadherin, β-catenin and ZEB2 in laryngeal squamous cell carcinoma
doi: 10.3892/ol.2018.7751
Figure Lengend Snippet: Association of four epithelial-mesenchymal transition-a ssociated markers with overall survival. Kaplan-Meier overall survival curves stratified by the expression of (A) E-cadherin, (B) N-cadherin, (C) β-catenin and (D) ZEB2. P-values were calculated using the log-rank test. ZEB2, zinc finger E-box binding homeobox 2.
Article Snippet: Sections were subsequently incubated with primary antibodies against E-cadherin (mouse monoclonal; cat. no., ab1416),
Techniques: Expressing, Binding Assay

Journal: International Journal of Molecular Sciences
Article Title: Mesenchymal Stem Cell Protection of Neurons against Glutamate Excitotoxicity Involves Reduction of NMDA-Triggered Calcium Responses and Surface GluR1, and Is Partly Mediated by TNF
doi: 10.3390/ijms19030651
Figure Lengend Snippet: TNF is produced by MSC and contributes to MSC CM-mediated neuroprotection against glutamate excitotoxicity. ( A ) DIV 9 neurons (N) were pre-treated with high glucose DMEM medium alone (hgDMEM) or MSC CM without or with etanercept (100 ng/ml) (24 h), then left untreated or challenged with NMDA (50 μM) supplemented with glycine (10 μM) (24 h), and death was measured at DIV 11 by Hoechst staining. Etanercept treatment consistently resulted in a small but significant increase in NMDA-induced excitotoxicity, as measured by fold changes in proportions of cells with pyknotic nuclei compared to those in cells treated with MSC CM alone ( Ai and ii , arrows show pyknotic nuclei). Neuron death is represented as fold differences compared to measurements in untreated cultures ( Ai ). Representative fields from each culture are shown in the photographs ( Aii ). ( B ) TNF-induced cytotoxicity of L929 fibroblasts was measured in the presence of 1 μg/ml emetine, using increasing amounts of recombinant human TNF (rhTNF) (1, 10, 100 and 1000 pg/ml) added to non-conditioned hgDMEM or MSC CM without or with etanercept (200 ng/ml). MSC CM consistently induced more cytotoxicity than non-conditioned hgDMEM at each concentration of added rhTNF used, demonstrating that MSC CM contains TNF bioactivity (estimated between 0.15–0.24 U/ml). Etanercept inhibited cytotoxicity in all preparations showing that cytotoxicity was specifically induced by TNF. Scale bars 50 μM. Results shown are means ± SEM of triplicate samples from one representative of three independent experiments. * p
Article Snippet: Excitotoxic death was induced in DIV 10 neurons by exposure to 50 μM
Techniques: Produced, Staining, Recombinant, Concentration Assay

Journal: Viruses
Article Title: N-glycosylation in the Pre-Membrane Protein Is Essential for the Zika Virus Life Cycle
doi: 10.3390/v12090925
Figure Lengend Snippet: The N -glycan on ZIKV prM is important for the virus life cycle. ( a ) Schematic diagram of experiments. ( b ) Representative picture of ZsGreen expression from four variants of ZIKV RNA transfected into Vero B4 cells. The monitoring was performed as scheduled in Figure 3 a . Scale bar = 20 µm. ( c ) Virus egress kinetics by qRT-PCR, depicted as copy number of ZIKV NS5 RNA in 100 µL of harvested supernatant, as scheduled in Figure 3 a . Mean values and standard deviations are shown from three independent experiments. ( d ) Representative picture of the plaque-forming ability of harvested viruses. The ZIKV strains MR766 and BeH819015 (approximately, 100 plaque-forming units) were used as positive controls. Respectively, virus titer was measured using plaque assay and the average of virus titer and standard deviations are shown from two independent experiments. ( e ) Confirmation of presence/absence of the N -glycan sites in the prM and E proteins. Vero B4 cells were infected with supernatant from day 6 ( Figure 3 a ). Three days after infection, the cell lysate was harvested and used for prM and E protein detection by Western blotting, with either absence or presence of peptide N-glycosidase F (PNGase F) treatment. The ZIKV strains MR766 (absence of N -glycan in E) and BeH819015 (presence of N -glycan in E) were used as controls.
Article Snippet: Glycosidase Treatment In order to confirm the absence or presence of an N-glycan in the prM and E proteins,
Techniques: Expressing, Transfection, Quantitative RT-PCR, Plaque Assay, Infection, Western Blot

Journal: Viruses
Article Title: N-glycosylation in the Pre-Membrane Protein Is Essential for the Zika Virus Life Cycle
doi: 10.3390/v12090925
Figure Lengend Snippet: The lack of N -glycan on the pre-membrane (prM) or/and E protein caused impairment in the E protein expression and secretion. ( a ) Confirmation of absence/presence of N -glycosylation in the prM- and E proteins expressed from constructed plasmids. For the Western blotting, proteins were stained with anti-ZIKV E -, anti-ZIKV prM- or anti-β actin protein antibody ( b ) Representative Western blot picture of E- and β-actin protein expression in harvested cell lysate and cell culture supernatant from three independent experiments. ( c ) Quantification of E protein expression with Image J. To normalize the E protein expression in the cell lysate, the expression level of E protein was divided by the expression level of β-actin. To normalize the E protein expression in the supernatant, the expression level of E protein from the supernatant was divided by the expression level of E protein from the cell lysate. The experiment was repeated three times, average and SD are shown. Statistical significance was determined by two-tailed t-test. p = p value. GFP = pcDNA3.1-GFP vector; WT clone = pcDNA3.1-prME vectors with wild-type ZIKV prM-E genes; N69Q = pcDNA3.1-prME vector with a mutated N -glycosylation site in prM; N154Q = pcDNA3.1-prME vector with a mutated N -glycosylation site in E; N69Q/N154Q = pcDNA3.1-prME vector with mutated N -glycosylation sites in prM and E; PNGase F = Peptide:N-glycosidase F.
Article Snippet: Glycosidase Treatment In order to confirm the absence or presence of an N-glycan in the prM and E proteins,
Techniques: Expressing, Construct, Western Blot, Staining, Cell Culture, Two Tailed Test, Plasmid Preparation