ht1080 6tg cell cultures Search Results


ht 1080 6tg cells  (ATCC)
98
ATCC ht 1080 6tg cells
Figure 3. eIF2α phosphorylation in Ras-transformed cells. (A) eIF2α phosphorylation during adenovirus infection. H125 and H1299 cells were infected with 309p, dVAI, dVAII or dVAs at an M. O. I. of 1, in the absence or presence of interferon α. 24 hours post infection, cells were harvested and lysates were subjected to immunoblot analysis with specific antibodies against the indicated proteins. (B) PKR activation and induction of apoptosis by polyIC. H125 and H1299 cells were transfected with polyIC, and cells were harvested at different time points post transfection, followed by immunoblot analysis. (C) eIF2α phosphorylation in response to dVAI infection in different cell species. The indicated cells (derivatives of HT-1080: <t>6TG</t> and DSMZ) were infected with dVAI at an M. O. I. of 1. Twenty-four hours post infection, cells were harvested, and phosphorylated and total eIF2α were simultaneously visualized by immunoblot analysis using specific primary antibodies and differentially fluorescence-labelled secondary antibodies. Signal intensities for every sample were assessed with an infrared imager, and the ratio between phosphorylated and unphosphorylated eIF2α was calculated. The value in BJ-ET cells was arbitrarily set to one, and the other values were normalized accordingly. Graphs show the average values and standard deviations of three independent experiments in each case.
Ht 1080 6tg Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cancer cell lines  (ATCC)
99
ATCC cancer cell lines
Figure 3. eIF2α phosphorylation in Ras-transformed cells. (A) eIF2α phosphorylation during adenovirus infection. H125 and H1299 cells were infected with 309p, dVAI, dVAII or dVAs at an M. O. I. of 1, in the absence or presence of interferon α. 24 hours post infection, cells were harvested and lysates were subjected to immunoblot analysis with specific antibodies against the indicated proteins. (B) PKR activation and induction of apoptosis by polyIC. H125 and H1299 cells were transfected with polyIC, and cells were harvested at different time points post transfection, followed by immunoblot analysis. (C) eIF2α phosphorylation in response to dVAI infection in different cell species. The indicated cells (derivatives of HT-1080: <t>6TG</t> and DSMZ) were infected with dVAI at an M. O. I. of 1. Twenty-four hours post infection, cells were harvested, and phosphorylated and total eIF2α were simultaneously visualized by immunoblot analysis using specific primary antibodies and differentially fluorescence-labelled secondary antibodies. Signal intensities for every sample were assessed with an infrared imager, and the ratio between phosphorylated and unphosphorylated eIF2α was calculated. The value in BJ-ET cells was arbitrarily set to one, and the other values were normalized accordingly. Graphs show the average values and standard deviations of three independent experiments in each case.
Cancer Cell Lines, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 3. eIF2α phosphorylation in Ras-transformed cells. (A) eIF2α phosphorylation during adenovirus infection. H125 and H1299 cells were infected with 309p, dVAI, dVAII or dVAs at an M. O. I. of 1, in the absence or presence of interferon α. 24 hours post infection, cells were harvested and lysates were subjected to immunoblot analysis with specific antibodies against the indicated proteins. (B) PKR activation and induction of apoptosis by polyIC. H125 and H1299 cells were transfected with polyIC, and cells were harvested at different time points post transfection, followed by immunoblot analysis. (C) eIF2α phosphorylation in response to dVAI infection in different cell species. The indicated cells (derivatives of HT-1080: 6TG and DSMZ) were infected with dVAI at an M. O. I. of 1. Twenty-four hours post infection, cells were harvested, and phosphorylated and total eIF2α were simultaneously visualized by immunoblot analysis using specific primary antibodies and differentially fluorescence-labelled secondary antibodies. Signal intensities for every sample were assessed with an infrared imager, and the ratio between phosphorylated and unphosphorylated eIF2α was calculated. The value in BJ-ET cells was arbitrarily set to one, and the other values were normalized accordingly. Graphs show the average values and standard deviations of three independent experiments in each case.

Journal: Cell cycle (Georgetown, Tex.)

Article Title: Activating Ras mutations fail to ensure efficient replication of adenovirus mutants lacking VA-RNA.

doi: 10.4161/cc.5.3.2411

Figure Lengend Snippet: Figure 3. eIF2α phosphorylation in Ras-transformed cells. (A) eIF2α phosphorylation during adenovirus infection. H125 and H1299 cells were infected with 309p, dVAI, dVAII or dVAs at an M. O. I. of 1, in the absence or presence of interferon α. 24 hours post infection, cells were harvested and lysates were subjected to immunoblot analysis with specific antibodies against the indicated proteins. (B) PKR activation and induction of apoptosis by polyIC. H125 and H1299 cells were transfected with polyIC, and cells were harvested at different time points post transfection, followed by immunoblot analysis. (C) eIF2α phosphorylation in response to dVAI infection in different cell species. The indicated cells (derivatives of HT-1080: 6TG and DSMZ) were infected with dVAI at an M. O. I. of 1. Twenty-four hours post infection, cells were harvested, and phosphorylated and total eIF2α were simultaneously visualized by immunoblot analysis using specific primary antibodies and differentially fluorescence-labelled secondary antibodies. Signal intensities for every sample were assessed with an infrared imager, and the ratio between phosphorylated and unphosphorylated eIF2α was calculated. The value in BJ-ET cells was arbitrarily set to one, and the other values were normalized accordingly. Graphs show the average values and standard deviations of three independent experiments in each case.

Article Snippet: HT-1080 6TG cells, hypoxanthine phosphoribosyltransferase-deficient variants of the HT-1080 cell line, and MCH603c8 cells contain either a heterozygous N-Ras Q61K mutation or two wild-type N-Ras alleles and have been described.15 NCI-H125, NCI-H322, NCI-H1373, and NCI-H2347 cells (ATCC) were maintained in RPMI 1640 containing 10% FBS.

Techniques: Phospho-proteomics, Transformation Assay, Infection, Western Blot, Activation Assay, Transfection, Fluorescence

Figure 4. dVA replication and eIF2α phosphorylation in cells with a deletion of mutant Ras. (A) Virus replication. Cells of the isogenic lines MCH603c8 (Ras wild type) and HT-1080 6TG (Ras mutant) were infected with 309p, dVAI, dVAII and dVAs at an M.O.I. of 0.5, in the presence or absence of interferon α. Seventy-two hours post infection, cells were harvested and virus yields were determined through immunofluo- rescence-based titration in H1299 cells. Note that both cell lines were less permissive to VA-less viruses than the parental line HT1080 that we obtained from the German Collection of Microorganisms (DSMZ), perhaps as a result of the transduction and selection process that both sublines had undergone.15,23 (B) PKR activation during virus infection. MCH603c8 and HT-1080 6TG cells were infected with 309p, dVAI, dVAs with an M. O. I. of 1 or mock infected, in the presence of interferon α, and harvested 24 hours post infection. Lysates were subjected to immunoblot analysis with antibodies against the indicated proteins. (C) PKR activation by polyIC. MCH603c8 and HT-1080 6TG cells were transfected with polyIC and harvested at the indicated time points post infection, followed by immunoblot analysis.

Journal: Cell cycle (Georgetown, Tex.)

Article Title: Activating Ras mutations fail to ensure efficient replication of adenovirus mutants lacking VA-RNA.

doi: 10.4161/cc.5.3.2411

Figure Lengend Snippet: Figure 4. dVA replication and eIF2α phosphorylation in cells with a deletion of mutant Ras. (A) Virus replication. Cells of the isogenic lines MCH603c8 (Ras wild type) and HT-1080 6TG (Ras mutant) were infected with 309p, dVAI, dVAII and dVAs at an M.O.I. of 0.5, in the presence or absence of interferon α. Seventy-two hours post infection, cells were harvested and virus yields were determined through immunofluo- rescence-based titration in H1299 cells. Note that both cell lines were less permissive to VA-less viruses than the parental line HT1080 that we obtained from the German Collection of Microorganisms (DSMZ), perhaps as a result of the transduction and selection process that both sublines had undergone.15,23 (B) PKR activation during virus infection. MCH603c8 and HT-1080 6TG cells were infected with 309p, dVAI, dVAs with an M. O. I. of 1 or mock infected, in the presence of interferon α, and harvested 24 hours post infection. Lysates were subjected to immunoblot analysis with antibodies against the indicated proteins. (C) PKR activation by polyIC. MCH603c8 and HT-1080 6TG cells were transfected with polyIC and harvested at the indicated time points post infection, followed by immunoblot analysis.

Article Snippet: HT-1080 6TG cells, hypoxanthine phosphoribosyltransferase-deficient variants of the HT-1080 cell line, and MCH603c8 cells contain either a heterozygous N-Ras Q61K mutation or two wild-type N-Ras alleles and have been described.15 NCI-H125, NCI-H322, NCI-H1373, and NCI-H2347 cells (ATCC) were maintained in RPMI 1640 containing 10% FBS.

Techniques: Phospho-proteomics, Mutagenesis, Virus, Infection, Titration, Transduction, Selection, Activation Assay, Western Blot, Transfection