bxpc 3  (ATCC)


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    Name:
    BxPC 3
    Description:
    Applications This cell line is a suitable transfection host Host Homo sapiens human
    Catalog Number:
    CRL-1687
    Price:
    None
    Applications:
    This cell line is a suitable transfection host.
    Host:
    Homo sapiens, human
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    Structured Review

    ATCC bxpc 3
    Characterization of select inhibitors in 2D and 3D formats (A–B) Validation and specificity of select hits towards KRAS mutant cells in 3D ( A ) or 2D ( B ) formats. The top seven compounds from the Spectrum library screen were analyzed at ~ 12.4 μM in triplicate on <t>BxPC-3-KRAS</t> G12V and BxPC-3-KRAS WT cells in 3D and 2D formats. (C–D) Evaluation of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cell growth rates in 3D ( C ) and 2D ( D ) formats. Cells were plated at 2500 cells/well in 3D and 2D formats and the growth rate was evaluated at 24, 48, and 72 hour time points using CTG3D or CTG, respectively. Statistical significance was determined by unpaired t -test. NS = Non significant, * = p
    Applications This cell line is a suitable transfection host Host Homo sapiens human
    https://www.bioz.com/result/bxpc 3/product/ATCC
    Average 99 stars, based on 1 article reviews
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    bxpc 3 - by Bioz Stars, 2021-04
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    Images

    1) Product Images from "A Novel 3-dimensional High Throughput Screening Approach Identifies Inducers of a Mutant KRAS Selective Lethal Phenotype"

    Article Title: A Novel 3-dimensional High Throughput Screening Approach Identifies Inducers of a Mutant KRAS Selective Lethal Phenotype

    Journal: Oncogene

    doi: 10.1038/s41388-018-0257-5

    Characterization of select inhibitors in 2D and 3D formats (A–B) Validation and specificity of select hits towards KRAS mutant cells in 3D ( A ) or 2D ( B ) formats. The top seven compounds from the Spectrum library screen were analyzed at ~ 12.4 μM in triplicate on BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D and 2D formats. (C–D) Evaluation of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cell growth rates in 3D ( C ) and 2D ( D ) formats. Cells were plated at 2500 cells/well in 3D and 2D formats and the growth rate was evaluated at 24, 48, and 72 hour time points using CTG3D or CTG, respectively. Statistical significance was determined by unpaired t -test. NS = Non significant, * = p
    Figure Legend Snippet: Characterization of select inhibitors in 2D and 3D formats (A–B) Validation and specificity of select hits towards KRAS mutant cells in 3D ( A ) or 2D ( B ) formats. The top seven compounds from the Spectrum library screen were analyzed at ~ 12.4 μM in triplicate on BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D and 2D formats. (C–D) Evaluation of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cell growth rates in 3D ( C ) and 2D ( D ) formats. Cells were plated at 2500 cells/well in 3D and 2D formats and the growth rate was evaluated at 24, 48, and 72 hour time points using CTG3D or CTG, respectively. Statistical significance was determined by unpaired t -test. NS = Non significant, * = p

    Techniques Used: Mutagenesis, CTG Assay

    Spectrum Library Screen of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D and 2D formats ( A–B ) 2400 compounds from the Spectrum Library were screened in duplicate on 3D against BxPC-3-KRAS G12V to validate the 3D assay. ( A ) The activity of the compounds was plotted (duplicate data but showing single point percent response), with high control, low control and hit cutoff (dashed line) shown. ( B ) Correlation plot for the two replicate screening datasets. (C–F) Activity of 2,400 compounds on BxPC-3-KRAS WT and BxPC-3-KRAS G12V cells in 3D and 2D formats (singlicate showing single point percent response along with high control, low control and hit cutoff shown): ( C ) 3D format BxPC-3-KRAS G12V , ( D ) 3D format BxPC-3-KRAS WT , ( E ) 2D format BxPC-3-KRAS G12V , ( F ) 2D BxPC-3 KRAS WT .
    Figure Legend Snippet: Spectrum Library Screen of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D and 2D formats ( A–B ) 2400 compounds from the Spectrum Library were screened in duplicate on 3D against BxPC-3-KRAS G12V to validate the 3D assay. ( A ) The activity of the compounds was plotted (duplicate data but showing single point percent response), with high control, low control and hit cutoff (dashed line) shown. ( B ) Correlation plot for the two replicate screening datasets. (C–F) Activity of 2,400 compounds on BxPC-3-KRAS WT and BxPC-3-KRAS G12V cells in 3D and 2D formats (singlicate showing single point percent response along with high control, low control and hit cutoff shown): ( C ) 3D format BxPC-3-KRAS G12V , ( D ) 3D format BxPC-3-KRAS WT , ( E ) 2D format BxPC-3-KRAS G12V , ( F ) 2D BxPC-3 KRAS WT .

    Techniques Used: Activity Assay

    Comparison of performance of compounds in BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D and 2D formats Primary screening results of Spectrum library against BxPC-3-KRAS WT and BxPC-3-KRAS G12V in 3D and 2D formats. (A) Four-way Venn diagram of active compounds identified from the four screens. A hit was identified as any compound with % inhibition > the corresponding screen hit cutoff. The numbers in parentheses are the numbers of hits specific for that cell line. The numbers in the boxes represent the number of compounds found to active in those overlapping assays. (B–E) Correlation plots of the % inhibition values of compounds in each of the screens: ( B ) BxPC-3-KRAS WT , 2D vs. 3D. ( C ) BxPC-3-KRAS G12V , 2D vs. 3D. ( D ) BxPC-3-KRAS G12V vs. BxPC-3-KRAS WT , 2D. ( E ) BxPC-3-KRAS G12V vs. BxPC-3-KRAS WT , 3D.
    Figure Legend Snippet: Comparison of performance of compounds in BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D and 2D formats Primary screening results of Spectrum library against BxPC-3-KRAS WT and BxPC-3-KRAS G12V in 3D and 2D formats. (A) Four-way Venn diagram of active compounds identified from the four screens. A hit was identified as any compound with % inhibition > the corresponding screen hit cutoff. The numbers in parentheses are the numbers of hits specific for that cell line. The numbers in the boxes represent the number of compounds found to active in those overlapping assays. (B–E) Correlation plots of the % inhibition values of compounds in each of the screens: ( B ) BxPC-3-KRAS WT , 2D vs. 3D. ( C ) BxPC-3-KRAS G12V , 2D vs. 3D. ( D ) BxPC-3-KRAS G12V vs. BxPC-3-KRAS WT , 2D. ( E ) BxPC-3-KRAS G12V vs. BxPC-3-KRAS WT , 3D.

    Techniques Used: Inhibition

    Validation of specificity of select inhibitors toward KRAS mutant cells (A) Top 15 compounds from the Spectrum library screen were analyzed at 12.4 μM in triplicate against BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D format. Statistical significance was determined by unpaired t -test. NS = Non significant, * = p
    Figure Legend Snippet: Validation of specificity of select inhibitors toward KRAS mutant cells (A) Top 15 compounds from the Spectrum library screen were analyzed at 12.4 μM in triplicate against BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells in 3D format. Statistical significance was determined by unpaired t -test. NS = Non significant, * = p

    Techniques Used: Mutagenesis

    Assessing the Na + /K + -ATPase as the potential target of Proscillaridin A ( A–D ) BxPC-3-KRAS G12V and BxPC-3-KRAS WT were transfected with siRNA targeting ATP1A1 or control siRNA and knockdown of the ATP1A1 subunit was confirmed by western blotting in cells grown in ( A ) 3D format or ( B ) 2D format. Viability of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells transfected with siRNA targeting ATP1A1 or control siRNA grown in grown in ( C ) 3D format or ( D ) 2D format was determined at 48 hours post-transfection using CTG3D or CTG, respectively. Statistical significance was determined by unpaired t -test. NS = Non significant, ** = p
    Figure Legend Snippet: Assessing the Na + /K + -ATPase as the potential target of Proscillaridin A ( A–D ) BxPC-3-KRAS G12V and BxPC-3-KRAS WT were transfected with siRNA targeting ATP1A1 or control siRNA and knockdown of the ATP1A1 subunit was confirmed by western blotting in cells grown in ( A ) 3D format or ( B ) 2D format. Viability of BxPC-3-KRAS G12V and BxPC-3-KRAS WT cells transfected with siRNA targeting ATP1A1 or control siRNA grown in grown in ( C ) 3D format or ( D ) 2D format was determined at 48 hours post-transfection using CTG3D or CTG, respectively. Statistical significance was determined by unpaired t -test. NS = Non significant, ** = p

    Techniques Used: Transfection, Western Blot, CTG Assay

    Characterization of the BxPC-3 isogenic cell pair (A) Analysis of KRAS expression levels in BxPC-3-KRAS G12V and BxPC-3-KRAS WT stable cell lines. Individual clones were isolated and evaluated for the expression of KRAS by western blotting analysis using anti-KRAS or anti-Vinculin (loading control) antibodies. ( B ) Analysis of KRAS expression levels in selected BxPC-3-KRAS G12V and BxPC-3-KRAS WT stable cell lines and BxPC-3-parental cell line. Confirmation of spheroidicity of (C) BxPC-3-KRAS WT or (D) BxPC-3-KRAS G12V cells by confocal imaging. Z-stack images were taken at 10 μm increments from the equator of Hoechst-stained spheroids of BxPC-3-KRAS G12V and BxPC-3-KRAS WT on a GE IN Cell 6000 Analyzer (10× objective, f =1.18AU). Maximum intensity projection along the z-axis of the 12 individual planes aligned in Image J to generate an intensity projection biased by color scale are shown in the left panel. (E–F) Determination of cell viability assay conditions using CellTiter-Glo 3D (CTG3D). BxPC-3 cells were seeded at increasing numbers in a 384-well spheroid plate, grown for 24 hours and treated with CTG3D to assess viability. Relative luminescence of cells was determined at 48 hours post-seeding, using a ViewLux microplate imager (PerkinElmer). Error Bars = S.D. The data shown represent the mean of 3 independent replicates with triplicate data points.
    Figure Legend Snippet: Characterization of the BxPC-3 isogenic cell pair (A) Analysis of KRAS expression levels in BxPC-3-KRAS G12V and BxPC-3-KRAS WT stable cell lines. Individual clones were isolated and evaluated for the expression of KRAS by western blotting analysis using anti-KRAS or anti-Vinculin (loading control) antibodies. ( B ) Analysis of KRAS expression levels in selected BxPC-3-KRAS G12V and BxPC-3-KRAS WT stable cell lines and BxPC-3-parental cell line. Confirmation of spheroidicity of (C) BxPC-3-KRAS WT or (D) BxPC-3-KRAS G12V cells by confocal imaging. Z-stack images were taken at 10 μm increments from the equator of Hoechst-stained spheroids of BxPC-3-KRAS G12V and BxPC-3-KRAS WT on a GE IN Cell 6000 Analyzer (10× objective, f =1.18AU). Maximum intensity projection along the z-axis of the 12 individual planes aligned in Image J to generate an intensity projection biased by color scale are shown in the left panel. (E–F) Determination of cell viability assay conditions using CellTiter-Glo 3D (CTG3D). BxPC-3 cells were seeded at increasing numbers in a 384-well spheroid plate, grown for 24 hours and treated with CTG3D to assess viability. Relative luminescence of cells was determined at 48 hours post-seeding, using a ViewLux microplate imager (PerkinElmer). Error Bars = S.D. The data shown represent the mean of 3 independent replicates with triplicate data points.

    Techniques Used: Expressing, Stable Transfection, Clone Assay, Isolation, Western Blot, Imaging, Staining, Viability Assay

    2) Product Images from "?-Mangostin suppresses lipopolysaccharide-induced invasion by inhibiting matrix metalloproteinase-2/9 and increasing E-cadherin expression through extracellular signal-regulated kinase signaling in pancreatic cancer cells"

    Article Title: ?-Mangostin suppresses lipopolysaccharide-induced invasion by inhibiting matrix metalloproteinase-2/9 and increasing E-cadherin expression through extracellular signal-regulated kinase signaling in pancreatic cancer cells

    Journal: Oncology Letters

    doi: 10.3892/ol.2013.1290

    Effect of α-mangostin on the viability of BxPC-3 and MIAPaCa-2 cells. (A) Garcinia mangostana Linn (GML). (B) Chemical structure of α-mangostin. (C) The BxPC-3 and (D) MIAPaCa-2 cells were treated with various concentrations (0, 5, 7.5, 10 or 15 μ M) of α-mangostin for 6, 12, 18, 24 and 48 h. The number of surviving cells was directly proportional to the formazan level, which was measured spectrophotometrically at 563 nm. Values represent the mean ± SD of three independent experiments. * P
    Figure Legend Snippet: Effect of α-mangostin on the viability of BxPC-3 and MIAPaCa-2 cells. (A) Garcinia mangostana Linn (GML). (B) Chemical structure of α-mangostin. (C) The BxPC-3 and (D) MIAPaCa-2 cells were treated with various concentrations (0, 5, 7.5, 10 or 15 μ M) of α-mangostin for 6, 12, 18, 24 and 48 h. The number of surviving cells was directly proportional to the formazan level, which was measured spectrophotometrically at 563 nm. Values represent the mean ± SD of three independent experiments. * P

    Techniques Used:

    Effects of α-mangostin on the migration of BxPC-3 and MIAPaCa-2 pancreatic cancer cells. The cells were treated with LPS (5 μ g/ml) and/or α-mangostin (5 μ M) for 24 h, and were subjected to analyses for cell migration. (A) Images of migratory BxPC-3 and MIAPaCa-2 cells were captured under a microscope at ×40 magnification. Data are represented as the mean ± SD of three independent experiments. * P
    Figure Legend Snippet: Effects of α-mangostin on the migration of BxPC-3 and MIAPaCa-2 pancreatic cancer cells. The cells were treated with LPS (5 μ g/ml) and/or α-mangostin (5 μ M) for 24 h, and were subjected to analyses for cell migration. (A) Images of migratory BxPC-3 and MIAPaCa-2 cells were captured under a microscope at ×40 magnification. Data are represented as the mean ± SD of three independent experiments. * P

    Techniques Used: Migration, Microscopy

    α-mangostin prevented the LPS-induced decrease in the expression of E-cadherin mRNA and the increase in the expression of MMP-9 and MMP-2 mRNA. (A) The mRNA expression levels of E-cadherin, MMP-9 and MMP-2 in BxPC-3 and MIAPaCa-2 cells were determined by RT-PCR. (B) Quantification of the mRNA levels. Data from at least three independent experiments with duplicate determinations are expressed as the mean ± SEM. * P
    Figure Legend Snippet: α-mangostin prevented the LPS-induced decrease in the expression of E-cadherin mRNA and the increase in the expression of MMP-9 and MMP-2 mRNA. (A) The mRNA expression levels of E-cadherin, MMP-9 and MMP-2 in BxPC-3 and MIAPaCa-2 cells were determined by RT-PCR. (B) Quantification of the mRNA levels. Data from at least three independent experiments with duplicate determinations are expressed as the mean ± SEM. * P

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    α-mangostin prevented the LPS-induced decrease in the expression of E-cadherin protein and LPS-induced increase in the expression of MMP-9 and MMP-2 protein. (A) Protein expression levels of E-cadherin, MMP-9, and MMP-2 in BxPC-3 and MIAPaCa-2 cells were determined via western blotting. (B) Quantification of the protein levels. Data from at least three independent experiments with duplicate determinations are expressed as the mean ± SEM. * P
    Figure Legend Snippet: α-mangostin prevented the LPS-induced decrease in the expression of E-cadherin protein and LPS-induced increase in the expression of MMP-9 and MMP-2 protein. (A) Protein expression levels of E-cadherin, MMP-9, and MMP-2 in BxPC-3 and MIAPaCa-2 cells were determined via western blotting. (B) Quantification of the protein levels. Data from at least three independent experiments with duplicate determinations are expressed as the mean ± SEM. * P

    Techniques Used: Expressing, Western Blot

    Effects of α-mangostin on the invasion of BxPC-3 and MIAPaCa-2 pancreatic cancer cells. The cells were treated with LPS (5 g/ml) and/or α-mangostin (5 M) for 24 h, then subjected to analyses for cell invasion. LPS significantly (P
    Figure Legend Snippet: Effects of α-mangostin on the invasion of BxPC-3 and MIAPaCa-2 pancreatic cancer cells. The cells were treated with LPS (5 g/ml) and/or α-mangostin (5 M) for 24 h, then subjected to analyses for cell invasion. LPS significantly (P

    Techniques Used:

    ERK signaling is key to the effect of α-mangostin on the expression of MMP-2, MMP-9 and E-cadherin. (A) α-mangostin reversed LPS-induced ERK1/2 activation. (B) Quantification of protein levels. (C) The efficacy of ERK siRNA for knocking down ERK protein was demonstrated by western blotting. (D) Cells were treated with LPS (5 μ g/ml), α-mangostin (5 μ M) and/or ERK siRNA for 24 h, then subjected to analyses for cell invasion. (E) BxPC-3 cells were treated with LPS (5 μ g/ml) and/or α-mangostin (5 μ M), with or without ERK siRNA. After 24 h, the E-cadherin, MMP-9 and MMP-2 protein expression levels were detected using western blotting. (F) Quantification of protein levels. Data from at least three independent experiments with duplicate determinations are expressed as the mean ± SEM. * P
    Figure Legend Snippet: ERK signaling is key to the effect of α-mangostin on the expression of MMP-2, MMP-9 and E-cadherin. (A) α-mangostin reversed LPS-induced ERK1/2 activation. (B) Quantification of protein levels. (C) The efficacy of ERK siRNA for knocking down ERK protein was demonstrated by western blotting. (D) Cells were treated with LPS (5 μ g/ml), α-mangostin (5 μ M) and/or ERK siRNA for 24 h, then subjected to analyses for cell invasion. (E) BxPC-3 cells were treated with LPS (5 μ g/ml) and/or α-mangostin (5 μ M), with or without ERK siRNA. After 24 h, the E-cadherin, MMP-9 and MMP-2 protein expression levels were detected using western blotting. (F) Quantification of protein levels. Data from at least three independent experiments with duplicate determinations are expressed as the mean ± SEM. * P

    Techniques Used: Expressing, Activation Assay, Western Blot

    3) Product Images from "Antiproliferative Effects and Mechanisms of Liver X Receptor Ligands in Pancreatic Ductal Adenocarcinoma Cells"

    Article Title: Antiproliferative Effects and Mechanisms of Liver X Receptor Ligands in Pancreatic Ductal Adenocarcinoma Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0106289

    GW 3965 downregulates oncogenes involved in cancer progression. A, GW3965 treatment downregulates SKP2 and EGFR protein levels in BxPC-3 and MIA-PaCa-2 cells. Downregulation of EGFR was concomitant with a downregulation of its own phosphorylation in BxPC-3 and MIA-PaCa-2 at 5 uM GW 3965. ERK1/2 and its phosphorylation were not statistically different in any of the cell lines B, C, D Densitometric quantification of SKP2, EGFR, Phospho-EGFR, ERK1/2, and Phospho-ERK1/2 upon treatment with GW3965. Samples were normalized to actin controls. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: GW 3965 downregulates oncogenes involved in cancer progression. A, GW3965 treatment downregulates SKP2 and EGFR protein levels in BxPC-3 and MIA-PaCa-2 cells. Downregulation of EGFR was concomitant with a downregulation of its own phosphorylation in BxPC-3 and MIA-PaCa-2 at 5 uM GW 3965. ERK1/2 and its phosphorylation were not statistically different in any of the cell lines B, C, D Densitometric quantification of SKP2, EGFR, Phospho-EGFR, ERK1/2, and Phospho-ERK1/2 upon treatment with GW3965. Samples were normalized to actin controls. Asterisks indicated statistically significant changes.

    Techniques Used:

    LXR agonists block pancreatic cancer cell progression through the cell cycle. A, GW3965 treatment arrests a significant proportion of the cells in the G1/G0 stage of the cell cycle as measured by propidium iodide staining and flow cytometry. B, Fewer cells are found in S, G2, or M phases following ligand treatment. C, BrdU-pulse analysis demonstrates that GW3965 treatments reduce transit through the S-phase of the cell cycle. D, E, F Representative cell cycle analysis diagram of BxPC-3, MIA-PaCa-2, and PANC-1 cells respectively. G, H, I Density plot depicting the number of cells staining for BrdU as a measure of S-phase transit in BxPC-3, MIA-PaCa-2, and PANC-1 cells. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: LXR agonists block pancreatic cancer cell progression through the cell cycle. A, GW3965 treatment arrests a significant proportion of the cells in the G1/G0 stage of the cell cycle as measured by propidium iodide staining and flow cytometry. B, Fewer cells are found in S, G2, or M phases following ligand treatment. C, BrdU-pulse analysis demonstrates that GW3965 treatments reduce transit through the S-phase of the cell cycle. D, E, F Representative cell cycle analysis diagram of BxPC-3, MIA-PaCa-2, and PANC-1 cells respectively. G, H, I Density plot depicting the number of cells staining for BrdU as a measure of S-phase transit in BxPC-3, MIA-PaCa-2, and PANC-1 cells. Asterisks indicated statistically significant changes.

    Techniques Used: Blocking Assay, Staining, Flow Cytometry, Cytometry, Cell Cycle Assay

    Microarray analysis of pancreatic cancer cell lines treated with LXR ligands defines common and cell line-specific effects on gene networks. A, B, Venn diagrams of up-regulated and down-regulated genes (1.1 fold change cutoff) after treatment with GW 3965 for 72 hours. These cell lines show common and cell-line specific transcriptomic responses to ligand treatment. C, Microarray analysis of up-regulated genes show that all cell lines share up-regulation of lipid metabolic, glucose metabolic, and cell proliferation responses. All cell lines down-regulate pathways that regulate response to viral infection, transmembrane support, as well as viral mRNA transcription. Treatments of BxPC-3 and PANC-1 cells down-regulate the expression of genes involved in cell cycle and DNA replication machinery.
    Figure Legend Snippet: Microarray analysis of pancreatic cancer cell lines treated with LXR ligands defines common and cell line-specific effects on gene networks. A, B, Venn diagrams of up-regulated and down-regulated genes (1.1 fold change cutoff) after treatment with GW 3965 for 72 hours. These cell lines show common and cell-line specific transcriptomic responses to ligand treatment. C, Microarray analysis of up-regulated genes show that all cell lines share up-regulation of lipid metabolic, glucose metabolic, and cell proliferation responses. All cell lines down-regulate pathways that regulate response to viral infection, transmembrane support, as well as viral mRNA transcription. Treatments of BxPC-3 and PANC-1 cells down-regulate the expression of genes involved in cell cycle and DNA replication machinery.

    Techniques Used: Microarray, Infection, Expressing

    LXR agonists block cell proliferation and colony-formation in pancreatic cancer cells. A, B, C, PDAC cells (BxPC-3, Mia-PaCa-2, and PANC-1 cell lines, respectively) show dose-dependent decreases in cell proliferation upon treatment with increasing GW3965 concentrations. EC50 calculations indicate that BxPC-3 and Mia-PaCa-2 cells are more sensitive to ligand treatment than PANC-1 cells. D, Results from MTS assays, a separate measure of overall cell metabolic rate and indirect measurement of cell proliferation, demonstrate a dose-dependent drop in overall metabolism in cells treated with increasing concentrations of GW3965. E, Colony-formation ability in all three cell lines was blocked by GW3965 treatment. F, Colony formation of GW3965 treated cells was quantified relative to vehicle-treated controls. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: LXR agonists block cell proliferation and colony-formation in pancreatic cancer cells. A, B, C, PDAC cells (BxPC-3, Mia-PaCa-2, and PANC-1 cell lines, respectively) show dose-dependent decreases in cell proliferation upon treatment with increasing GW3965 concentrations. EC50 calculations indicate that BxPC-3 and Mia-PaCa-2 cells are more sensitive to ligand treatment than PANC-1 cells. D, Results from MTS assays, a separate measure of overall cell metabolic rate and indirect measurement of cell proliferation, demonstrate a dose-dependent drop in overall metabolism in cells treated with increasing concentrations of GW3965. E, Colony-formation ability in all three cell lines was blocked by GW3965 treatment. F, Colony formation of GW3965 treated cells was quantified relative to vehicle-treated controls. Asterisks indicated statistically significant changes.

    Techniques Used: Blocking Assay

    Co-treatment of pancreatic cancer cells with LXR ligands and gemcitibine reveals additive antiproliferative effects. A, Cell proliferation is blocked in BxPC-3, MIA-PaCa-2, and PANC-1 cell lines upon treatment with 10 µM GW 3965. B, LXR agonist T0901317 blocks proliferation in BxPC-3 and MIA-PaCa-2 cells, but is unable to block cell proliferation in PANC-1 cells. C, GW3965 and gemcitibine block proliferation in all three pancreatic cancer cell lines and are additive in their inhibition of proliferation when administered concomitantly. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: Co-treatment of pancreatic cancer cells with LXR ligands and gemcitibine reveals additive antiproliferative effects. A, Cell proliferation is blocked in BxPC-3, MIA-PaCa-2, and PANC-1 cell lines upon treatment with 10 µM GW 3965. B, LXR agonist T0901317 blocks proliferation in BxPC-3 and MIA-PaCa-2 cells, but is unable to block cell proliferation in PANC-1 cells. C, GW3965 and gemcitibine block proliferation in all three pancreatic cancer cell lines and are additive in their inhibition of proliferation when administered concomitantly. Asterisks indicated statistically significant changes.

    Techniques Used: Blocking Assay, Inhibition

    LXRβ is the main LXR isoform expressed in pancreatic cancer samples and in three pancreatic adenocarcinoma cell lines. A, LXRβ was detected in the nuclei of normal pancreatic ductal epithelial cells (female, age 59). B, C, LXRβ positive immunoreactivity was evident in both the cytosol and the nuclei of neoplastic cells of patients with pancreatic adenocarcinoma (male, age 59 and female, age 65 respectively. D, LXRβ expression was undetectable in the pancreatic adenoma sample (female, age 59). E, F LXRα immunoreactivity is not detectable in normal ductal epithelial cells (female, age 59) and in pancreatic adenocarcinoma (male age 65). G, LXRβ is expressed in BxPC-3, Mia-PaCa-2, and PANC-1 cells. H, LXRα is not expressed in PDAC cell lines. Scale bar = 50 µM.
    Figure Legend Snippet: LXRβ is the main LXR isoform expressed in pancreatic cancer samples and in three pancreatic adenocarcinoma cell lines. A, LXRβ was detected in the nuclei of normal pancreatic ductal epithelial cells (female, age 59). B, C, LXRβ positive immunoreactivity was evident in both the cytosol and the nuclei of neoplastic cells of patients with pancreatic adenocarcinoma (male, age 59 and female, age 65 respectively. D, LXRβ expression was undetectable in the pancreatic adenoma sample (female, age 59). E, F LXRα immunoreactivity is not detectable in normal ductal epithelial cells (female, age 59) and in pancreatic adenocarcinoma (male age 65). G, LXRβ is expressed in BxPC-3, Mia-PaCa-2, and PANC-1 cells. H, LXRα is not expressed in PDAC cell lines. Scale bar = 50 µM.

    Techniques Used: Expressing

    4) Product Images from "Role of fatty acid synthase in gemcitabine and radiation resistance of pancreatic cancers"

    Article Title: Role of fatty acid synthase in gemcitabine and radiation resistance of pancreatic cancers

    Journal: International Journal of Biochemistry and Molecular Biology

    doi:

    Correlation between FASN expression and gemcitabine resistance. A. FASN expression level in Panc-1, MiaPaCa-2, and BxPc-3 cells. Lysates from Panc-1, MiaPaCa-2, and BxPc-3 cells were prepared for Western blot analyses of FASN and actin loading control.
    Figure Legend Snippet: Correlation between FASN expression and gemcitabine resistance. A. FASN expression level in Panc-1, MiaPaCa-2, and BxPc-3 cells. Lysates from Panc-1, MiaPaCa-2, and BxPc-3 cells were prepared for Western blot analyses of FASN and actin loading control.

    Techniques Used: Expressing, Western Blot

    5) Product Images from "A Novel Indole Ethyl Isothiocyanate (7Me-IEITC) with Anti-proliferative and Pro-apoptotic Effects on Platinum-resistant Human Ovarian Cancer Cells 1"

    Article Title: A Novel Indole Ethyl Isothiocyanate (7Me-IEITC) with Anti-proliferative and Pro-apoptotic Effects on Platinum-resistant Human Ovarian Cancer Cells 1

    Journal: Gynecologic oncology

    doi: 10.1016/j.ygyno.2008.01.042

    Comparative analysis of the cytotoxic effect of 7Me-IEITC in various human cancer and control cell lines SKOV-3, OVCAR-3 (ovarian epithelial adenocarcinomas), PC-3 (prostate adenocarcinoma), BxPC-3 (pancreatic adenocarcinoma), A-431 (epidermoid skin carcinoma), TCL-1 (trophoblasts) and HTR-8 (first trimester cytotrophoblasts) human cell lines were treated with various concentrations (2.5 to 20μM) of 7Me-IEITC for 48 hrs. The MTS viability assay was carried out as described (Materials and Methods). Experiments were performed in triplicates; data are expressed as the mean of the triplicate determinations (X±SD) of a representative experiment in % cell viability of samples with untreated cells [100%].
    Figure Legend Snippet: Comparative analysis of the cytotoxic effect of 7Me-IEITC in various human cancer and control cell lines SKOV-3, OVCAR-3 (ovarian epithelial adenocarcinomas), PC-3 (prostate adenocarcinoma), BxPC-3 (pancreatic adenocarcinoma), A-431 (epidermoid skin carcinoma), TCL-1 (trophoblasts) and HTR-8 (first trimester cytotrophoblasts) human cell lines were treated with various concentrations (2.5 to 20μM) of 7Me-IEITC for 48 hrs. The MTS viability assay was carried out as described (Materials and Methods). Experiments were performed in triplicates; data are expressed as the mean of the triplicate determinations (X±SD) of a representative experiment in % cell viability of samples with untreated cells [100%].

    Techniques Used: Viability Assay

    6) Product Images from "The NAD+-dependent Histone Deacetylase SIRT6 Promotes Cytokine Production and Migration in Pancreatic Cancer Cells by Regulating Ca2+ Responses *"

    Article Title: The NAD+-dependent Histone Deacetylase SIRT6 Promotes Cytokine Production and Migration in Pancreatic Cancer Cells by Regulating Ca2+ Responses *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M112.405837

    SIRT6 regulates cytokine expression in pancreatic cancer cells. BxPC-3 cells were engineered by retroviral transduction to express SIRT6 WT ( A ) or sh2 SIRT6 ( B ) or the respective empty vector pBP or pRS, and protein extracts were analyzed by immunoblotting
    Figure Legend Snippet: SIRT6 regulates cytokine expression in pancreatic cancer cells. BxPC-3 cells were engineered by retroviral transduction to express SIRT6 WT ( A ) or sh2 SIRT6 ( B ) or the respective empty vector pBP or pRS, and protein extracts were analyzed by immunoblotting

    Techniques Used: Expressing, Transduction, Plasmid Preparation

    The calcineurin-NFAT pathway promotes TNF and IL8 induction downstream of SIRT6. A , pBP, SIRT6 WT, pRS, and sh2 SIRT6 BxPC-3 cells were incubated with 25 ng/ml PMA for 45 min. Nuclear extracts were analyzed with a cAMP/Ca 2+ protein/DNA array. A semiquantitative
    Figure Legend Snippet: The calcineurin-NFAT pathway promotes TNF and IL8 induction downstream of SIRT6. A , pBP, SIRT6 WT, pRS, and sh2 SIRT6 BxPC-3 cells were incubated with 25 ng/ml PMA for 45 min. Nuclear extracts were analyzed with a cAMP/Ca 2+ protein/DNA array. A semiquantitative

    Techniques Used: Incubation, DNA Array

    SIRT1 reduces TNF expression in PDAC cells. A and B , BxPC-3 cells were engineered by retroviral transduction to express SIRT1 WT, SIRT1 H363Y, or pBP. Cells were stimulated with or without 25 ng/ml PMA for 48 h and subsequently used for RNA extraction.
    Figure Legend Snippet: SIRT1 reduces TNF expression in PDAC cells. A and B , BxPC-3 cells were engineered by retroviral transduction to express SIRT1 WT, SIRT1 H363Y, or pBP. Cells were stimulated with or without 25 ng/ml PMA for 48 h and subsequently used for RNA extraction.

    Techniques Used: Expressing, Transduction, RNA Extraction

    SIRT6 overexpression leads to increased cytokine expression in pancreatic cancer cells. BxPC-3 cells were engineered by retroviral transduction to express SIRT6 WT, SIRT6 H133Y, or pBP. A , thereafter, nuclear protein extracts were analyzed by immunoblotting
    Figure Legend Snippet: SIRT6 overexpression leads to increased cytokine expression in pancreatic cancer cells. BxPC-3 cells were engineered by retroviral transduction to express SIRT6 WT, SIRT6 H133Y, or pBP. A , thereafter, nuclear protein extracts were analyzed by immunoblotting

    Techniques Used: Over Expression, Expressing, Transduction

    SIRT6 regulates Ca 2+ responses and cell migration in PDAC cells. A , serum-starved BxPC-3 cells were preincubated for 30 min with 50 μ m EGTA-AM, and then cells were washed twice with PBS and treated for 1 h with 25 ng/ml PMA in HBSS; alternatively,
    Figure Legend Snippet: SIRT6 regulates Ca 2+ responses and cell migration in PDAC cells. A , serum-starved BxPC-3 cells were preincubated for 30 min with 50 μ m EGTA-AM, and then cells were washed twice with PBS and treated for 1 h with 25 ng/ml PMA in HBSS; alternatively,

    Techniques Used: Migration

    SIRT6 does not affect NF-κB transcriptional activity in BxPC-3 cells. A , NF-κB-dependent transcription was measured with an NF-κB reporter gene system in BxPC-3 cells stimulated or not with 25 ng/ml PMA for 15 h. Before PMA addition,
    Figure Legend Snippet: SIRT6 does not affect NF-κB transcriptional activity in BxPC-3 cells. A , NF-κB-dependent transcription was measured with an NF-κB reporter gene system in BxPC-3 cells stimulated or not with 25 ng/ml PMA for 15 h. Before PMA addition,

    Techniques Used: Activity Assay

    SIRT6 regulates intracellular levels of ADPr, an activator of TRPM2. A and B , pBP, SIRT6 WT, SIRT6 H133Y, pRS, and sh2 SIRT6 BxPC-3 cell extracts were supplemented with [ 14 C]ADPr and then injected into a first HPLC analysis. Fractions were collected,
    Figure Legend Snippet: SIRT6 regulates intracellular levels of ADPr, an activator of TRPM2. A and B , pBP, SIRT6 WT, SIRT6 H133Y, pRS, and sh2 SIRT6 BxPC-3 cell extracts were supplemented with [ 14 C]ADPr and then injected into a first HPLC analysis. Fractions were collected,

    Techniques Used: Injection, High Performance Liquid Chromatography

    NAD + depletion and sirtuin inhibition reduce cytokine expression in PDAC cells. A , BxPC-3 cells were treated for 48 h with or without 100 n m FK866 in the presence or absence of 1 m m nicotinic acid ( Na ). Cells were harvested and lysed in 0.6 m perchloric
    Figure Legend Snippet: NAD + depletion and sirtuin inhibition reduce cytokine expression in PDAC cells. A , BxPC-3 cells were treated for 48 h with or without 100 n m FK866 in the presence or absence of 1 m m nicotinic acid ( Na ). Cells were harvested and lysed in 0.6 m perchloric

    Techniques Used: Inhibition, Expressing

    SIRT6 silencing reduces cytokine expression in PDAC cells. BxPC-3 cells were engineered by retroviral transduction to express SIRT6 shRNA sh2 or the empty vector pRS. A , nuclear protein extracts were analyzed by immunoblotting for SIRT6, acetyl-H3K9,
    Figure Legend Snippet: SIRT6 silencing reduces cytokine expression in PDAC cells. BxPC-3 cells were engineered by retroviral transduction to express SIRT6 shRNA sh2 or the empty vector pRS. A , nuclear protein extracts were analyzed by immunoblotting for SIRT6, acetyl-H3K9,

    Techniques Used: Expressing, Transduction, shRNA, Plasmid Preparation

    7) Product Images from "Antiproliferative Effects and Mechanisms of Liver X Receptor Ligands in Pancreatic Ductal Adenocarcinoma Cells"

    Article Title: Antiproliferative Effects and Mechanisms of Liver X Receptor Ligands in Pancreatic Ductal Adenocarcinoma Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0106289

    GW 3965 downregulates oncogenes involved in cancer progression. A, GW3965 treatment downregulates SKP2 and EGFR protein levels in BxPC-3 and MIA-PaCa-2 cells. Downregulation of EGFR was concomitant with a downregulation of its own phosphorylation in BxPC-3 and MIA-PaCa-2 at 5 uM GW 3965. ERK1/2 and its phosphorylation were not statistically different in any of the cell lines B, C, D Densitometric quantification of SKP2, EGFR, Phospho-EGFR, ERK1/2, and Phospho-ERK1/2 upon treatment with GW3965. Samples were normalized to actin controls. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: GW 3965 downregulates oncogenes involved in cancer progression. A, GW3965 treatment downregulates SKP2 and EGFR protein levels in BxPC-3 and MIA-PaCa-2 cells. Downregulation of EGFR was concomitant with a downregulation of its own phosphorylation in BxPC-3 and MIA-PaCa-2 at 5 uM GW 3965. ERK1/2 and its phosphorylation were not statistically different in any of the cell lines B, C, D Densitometric quantification of SKP2, EGFR, Phospho-EGFR, ERK1/2, and Phospho-ERK1/2 upon treatment with GW3965. Samples were normalized to actin controls. Asterisks indicated statistically significant changes.

    Techniques Used:

    LXR agonists block pancreatic cancer cell progression through the cell cycle. A, GW3965 treatment arrests a significant proportion of the cells in the G1/G0 stage of the cell cycle as measured by propidium iodide staining and flow cytometry. B, Fewer cells are found in S, G2, or M phases following ligand treatment. C, BrdU-pulse analysis demonstrates that GW3965 treatments reduce transit through the S-phase of the cell cycle. D, E, F Representative cell cycle analysis diagram of BxPC-3, MIA-PaCa-2, and PANC-1 cells respectively. G, H, I Density plot depicting the number of cells staining for BrdU as a measure of S-phase transit in BxPC-3, MIA-PaCa-2, and PANC-1 cells. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: LXR agonists block pancreatic cancer cell progression through the cell cycle. A, GW3965 treatment arrests a significant proportion of the cells in the G1/G0 stage of the cell cycle as measured by propidium iodide staining and flow cytometry. B, Fewer cells are found in S, G2, or M phases following ligand treatment. C, BrdU-pulse analysis demonstrates that GW3965 treatments reduce transit through the S-phase of the cell cycle. D, E, F Representative cell cycle analysis diagram of BxPC-3, MIA-PaCa-2, and PANC-1 cells respectively. G, H, I Density plot depicting the number of cells staining for BrdU as a measure of S-phase transit in BxPC-3, MIA-PaCa-2, and PANC-1 cells. Asterisks indicated statistically significant changes.

    Techniques Used: Blocking Assay, Staining, Flow Cytometry, Cytometry, Cell Cycle Assay

    Microarray analysis of pancreatic cancer cell lines treated with LXR ligands defines common and cell line-specific effects on gene networks. A, B, Venn diagrams of up-regulated and down-regulated genes (1.1 fold change cutoff) after treatment with GW 3965 for 72 hours. These cell lines show common and cell-line specific transcriptomic responses to ligand treatment. C, Microarray analysis of up-regulated genes show that all cell lines share up-regulation of lipid metabolic, glucose metabolic, and cell proliferation responses. All cell lines down-regulate pathways that regulate response to viral infection, transmembrane support, as well as viral mRNA transcription. Treatments of BxPC-3 and PANC-1 cells down-regulate the expression of genes involved in cell cycle and DNA replication machinery.
    Figure Legend Snippet: Microarray analysis of pancreatic cancer cell lines treated with LXR ligands defines common and cell line-specific effects on gene networks. A, B, Venn diagrams of up-regulated and down-regulated genes (1.1 fold change cutoff) after treatment with GW 3965 for 72 hours. These cell lines show common and cell-line specific transcriptomic responses to ligand treatment. C, Microarray analysis of up-regulated genes show that all cell lines share up-regulation of lipid metabolic, glucose metabolic, and cell proliferation responses. All cell lines down-regulate pathways that regulate response to viral infection, transmembrane support, as well as viral mRNA transcription. Treatments of BxPC-3 and PANC-1 cells down-regulate the expression of genes involved in cell cycle and DNA replication machinery.

    Techniques Used: Microarray, Infection, Expressing

    LXR agonists block cell proliferation and colony-formation in pancreatic cancer cells. A, B, C, PDAC cells (BxPC-3, Mia-PaCa-2, and PANC-1 cell lines, respectively) show dose-dependent decreases in cell proliferation upon treatment with increasing GW3965 concentrations. EC50 calculations indicate that BxPC-3 and Mia-PaCa-2 cells are more sensitive to ligand treatment than PANC-1 cells. D, Results from MTS assays, a separate measure of overall cell metabolic rate and indirect measurement of cell proliferation, demonstrate a dose-dependent drop in overall metabolism in cells treated with increasing concentrations of GW3965. E, Colony-formation ability in all three cell lines was blocked by GW3965 treatment. F, Colony formation of GW3965 treated cells was quantified relative to vehicle-treated controls. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: LXR agonists block cell proliferation and colony-formation in pancreatic cancer cells. A, B, C, PDAC cells (BxPC-3, Mia-PaCa-2, and PANC-1 cell lines, respectively) show dose-dependent decreases in cell proliferation upon treatment with increasing GW3965 concentrations. EC50 calculations indicate that BxPC-3 and Mia-PaCa-2 cells are more sensitive to ligand treatment than PANC-1 cells. D, Results from MTS assays, a separate measure of overall cell metabolic rate and indirect measurement of cell proliferation, demonstrate a dose-dependent drop in overall metabolism in cells treated with increasing concentrations of GW3965. E, Colony-formation ability in all three cell lines was blocked by GW3965 treatment. F, Colony formation of GW3965 treated cells was quantified relative to vehicle-treated controls. Asterisks indicated statistically significant changes.

    Techniques Used: Blocking Assay

    Co-treatment of pancreatic cancer cells with LXR ligands and gemcitibine reveals additive antiproliferative effects. A, Cell proliferation is blocked in BxPC-3, MIA-PaCa-2, and PANC-1 cell lines upon treatment with 10 µM GW 3965. B, LXR agonist T0901317 blocks proliferation in BxPC-3 and MIA-PaCa-2 cells, but is unable to block cell proliferation in PANC-1 cells. C, GW3965 and gemcitibine block proliferation in all three pancreatic cancer cell lines and are additive in their inhibition of proliferation when administered concomitantly. Asterisks indicated statistically significant changes.
    Figure Legend Snippet: Co-treatment of pancreatic cancer cells with LXR ligands and gemcitibine reveals additive antiproliferative effects. A, Cell proliferation is blocked in BxPC-3, MIA-PaCa-2, and PANC-1 cell lines upon treatment with 10 µM GW 3965. B, LXR agonist T0901317 blocks proliferation in BxPC-3 and MIA-PaCa-2 cells, but is unable to block cell proliferation in PANC-1 cells. C, GW3965 and gemcitibine block proliferation in all three pancreatic cancer cell lines and are additive in their inhibition of proliferation when administered concomitantly. Asterisks indicated statistically significant changes.

    Techniques Used: Blocking Assay, Inhibition

    LXRβ is the main LXR isoform expressed in pancreatic cancer samples and in three pancreatic adenocarcinoma cell lines. A, LXRβ was detected in the nuclei of normal pancreatic ductal epithelial cells (female, age 59). B, C, LXRβ positive immunoreactivity was evident in both the cytosol and the nuclei of neoplastic cells of patients with pancreatic adenocarcinoma (male, age 59 and female, age 65 respectively. D, LXRβ expression was undetectable in the pancreatic adenoma sample (female, age 59). E, F LXRα immunoreactivity is not detectable in normal ductal epithelial cells (female, age 59) and in pancreatic adenocarcinoma (male age 65). G, LXRβ is expressed in BxPC-3, Mia-PaCa-2, and PANC-1 cells. H, LXRα is not expressed in PDAC cell lines. Scale bar = 50 µM.
    Figure Legend Snippet: LXRβ is the main LXR isoform expressed in pancreatic cancer samples and in three pancreatic adenocarcinoma cell lines. A, LXRβ was detected in the nuclei of normal pancreatic ductal epithelial cells (female, age 59). B, C, LXRβ positive immunoreactivity was evident in both the cytosol and the nuclei of neoplastic cells of patients with pancreatic adenocarcinoma (male, age 59 and female, age 65 respectively. D, LXRβ expression was undetectable in the pancreatic adenoma sample (female, age 59). E, F LXRα immunoreactivity is not detectable in normal ductal epithelial cells (female, age 59) and in pancreatic adenocarcinoma (male age 65). G, LXRβ is expressed in BxPC-3, Mia-PaCa-2, and PANC-1 cells. H, LXRα is not expressed in PDAC cell lines. Scale bar = 50 µM.

    Techniques Used: Expressing

    8) Product Images from "Silencing of FTX suppresses pancreatic cancer cell proliferation and invasion by upregulating miR-513b-5p"

    Article Title: Silencing of FTX suppresses pancreatic cancer cell proliferation and invasion by upregulating miR-513b-5p

    Journal: BMC Cancer

    doi: 10.1186/s12885-021-07975-6

    Expression of FTX and miR-513b-5p in PC cell lines. Detection of the FTX ( a ) and miR-513b-5p ( b ) expression in PC cell lines (HPDE6-C7, AsPC-1, BxPC-3, PANC-1, SW1990 and HS-766 T) by qRT-PCR. * P
    Figure Legend Snippet: Expression of FTX and miR-513b-5p in PC cell lines. Detection of the FTX ( a ) and miR-513b-5p ( b ) expression in PC cell lines (HPDE6-C7, AsPC-1, BxPC-3, PANC-1, SW1990 and HS-766 T) by qRT-PCR. * P

    Techniques Used: Expressing, Quantitative RT-PCR

    9) Product Images from "A Novel PET Imaging Using 64Cu-Labeled Monoclonal Antibody against Mesothelin Commonly Expressed on Cancer Cells"

    Article Title: A Novel PET Imaging Using 64Cu-Labeled Monoclonal Antibody against Mesothelin Commonly Expressed on Cancer Cells

    Journal: Journal of Immunology Research

    doi: 10.1155/2015/268172

    Immunohistochemical analysis of MSLN expression. (a) Expression of MSLN protein in cultured cancer cells detected by immunocytochemistry. BxPC-3, CFPAC-1, and PANC-1 cells were plated in 8-well chamber slides, cultured for 3 days, and incubated with 11-25 mAb followed by treatment with FITC-labeled anti-mouse IgG, Alexa Fluor 594-labeled wheat germ agglutinin (WGA), and DAPI. (b) Expression of MSLN in xenografts. Frozen sections of tumors derived from BxPC-3, CFPAC-1, and PANC-1 were treated with Alexa Fluor 488-labeled 11-25 mAb, Alexa Fluor 594-WGA, and DAPI. Bar: 20 μ m.
    Figure Legend Snippet: Immunohistochemical analysis of MSLN expression. (a) Expression of MSLN protein in cultured cancer cells detected by immunocytochemistry. BxPC-3, CFPAC-1, and PANC-1 cells were plated in 8-well chamber slides, cultured for 3 days, and incubated with 11-25 mAb followed by treatment with FITC-labeled anti-mouse IgG, Alexa Fluor 594-labeled wheat germ agglutinin (WGA), and DAPI. (b) Expression of MSLN in xenografts. Frozen sections of tumors derived from BxPC-3, CFPAC-1, and PANC-1 were treated with Alexa Fluor 488-labeled 11-25 mAb, Alexa Fluor 594-WGA, and DAPI. Bar: 20 μ m.

    Techniques Used: Immunohistochemistry, Expressing, Cell Culture, Immunocytochemistry, Incubation, Labeling, Whole Genome Amplification, Derivative Assay

    Representative PET images of mice bearing CFPAC-1, BxPC-3, and PANC-1. (a) A 3D volume rendering CT image of a mouse and a scheme showing the direction of PET images. The positions of xenografts and cross sections are shown on the CT image. CFPAC-1, BxPC-3, and PANC-1 xenografts were at the right shoulder, the left femur, and the right femur, respectively. (b) Serial PET/CT images of the nude mice at 0, 24, and 48 hours after administration of 64 Cu-DOTA-11-25 mAb and (c) 64 Cu-DOTA-anti-KLH mAb. Upper panels showed maximum intensity projections (MIP) of whole bodies. Lower panels are transverse PET/CT images at the position of tumors. Upper images (U) showed center of CFPAC-1 (CF), and lower images (L) showed BxPC-3 (Bx) and PANC-1 (P).
    Figure Legend Snippet: Representative PET images of mice bearing CFPAC-1, BxPC-3, and PANC-1. (a) A 3D volume rendering CT image of a mouse and a scheme showing the direction of PET images. The positions of xenografts and cross sections are shown on the CT image. CFPAC-1, BxPC-3, and PANC-1 xenografts were at the right shoulder, the left femur, and the right femur, respectively. (b) Serial PET/CT images of the nude mice at 0, 24, and 48 hours after administration of 64 Cu-DOTA-11-25 mAb and (c) 64 Cu-DOTA-anti-KLH mAb. Upper panels showed maximum intensity projections (MIP) of whole bodies. Lower panels are transverse PET/CT images at the position of tumors. Upper images (U) showed center of CFPAC-1 (CF), and lower images (L) showed BxPC-3 (Bx) and PANC-1 (P).

    Techniques Used: Positron Emission Tomography, Mouse Assay

    Biodistribution of 64 Cu-DOTA-mAbs in mice bearing BxPC-3, CFPAC-1, and PANC-1 tumors at 24 hours (a) and 48 hours (b) after intravenous injection. The mice were sacrificed at 24 hours and 48 hours after intravenous injection of 11 MBq of 64 Cu-DOTA-11-25 mAb (black bars) or 64 Cu-DOTA-anti-KLH mAb (white bars). The organs were collected and weighed and radioactivity was measured by γ -counter. ∗ P
    Figure Legend Snippet: Biodistribution of 64 Cu-DOTA-mAbs in mice bearing BxPC-3, CFPAC-1, and PANC-1 tumors at 24 hours (a) and 48 hours (b) after intravenous injection. The mice were sacrificed at 24 hours and 48 hours after intravenous injection of 11 MBq of 64 Cu-DOTA-11-25 mAb (black bars) or 64 Cu-DOTA-anti-KLH mAb (white bars). The organs were collected and weighed and radioactivity was measured by γ -counter. ∗ P

    Techniques Used: Mouse Assay, Injection, Radioactivity

    In vivo and ex vivo NIR optical imaging by Alexa Fluor 750-labeled 11-25 mAb. (a) Alexa Fluor 750-labeled 11-25 mAb (90 μ g/mouse) was administered to mice bearing BxPC-3 and PANC-1 intravenously. Alexa Fluor 750 fluorescence was then monitored by IVIS-200 imaging system 24, 48, and 72 hours after the injection. The minimum and maximum values of the photon gage are shown under each photograph. (b) 24 hours after administration of Alexa Fluor 750-labeled 11-25 mAb, tumors were dissected from mice and ex vivo fluorescence images were taken.
    Figure Legend Snippet: In vivo and ex vivo NIR optical imaging by Alexa Fluor 750-labeled 11-25 mAb. (a) Alexa Fluor 750-labeled 11-25 mAb (90 μ g/mouse) was administered to mice bearing BxPC-3 and PANC-1 intravenously. Alexa Fluor 750 fluorescence was then monitored by IVIS-200 imaging system 24, 48, and 72 hours after the injection. The minimum and maximum values of the photon gage are shown under each photograph. (b) 24 hours after administration of Alexa Fluor 750-labeled 11-25 mAb, tumors were dissected from mice and ex vivo fluorescence images were taken.

    Techniques Used: In Vivo, Ex Vivo, Optical Imaging, Labeling, Mouse Assay, Fluorescence, Imaging, Injection

    Analysis of MSLN protein expression in cancer cell lines by Western blot (a and b) and by flow cytometry using 11-25 mAb (b). β -actin served as a loading control. Expression of MSLN mRNA in cultured BxPC-3 (open circles), CFPAC-1 (closed triangles), PANC-1 (open squares), and A-431 (x-marks) cells (d and e).
    Figure Legend Snippet: Analysis of MSLN protein expression in cancer cell lines by Western blot (a and b) and by flow cytometry using 11-25 mAb (b). β -actin served as a loading control. Expression of MSLN mRNA in cultured BxPC-3 (open circles), CFPAC-1 (closed triangles), PANC-1 (open squares), and A-431 (x-marks) cells (d and e).

    Techniques Used: Expressing, Western Blot, Flow Cytometry, Cytometry, Cell Culture

    Cell binding assay with 64 Cu-DOTA-11-25 mAb. BxPC-3 cells were transferred to 24-well plates at 5 × 10 4 cells/well/mL and cultured for 4 days. Various concentrations of 64 Cu-DOTA-11-25 mAb were incubated with the cell monolayers for 2 hours on ice in complete growth media (RPMI-1640 medium containing 10% fetal bovine serum). The cells were washed and lysed and their radioactivity was counted in a γ -counter. Inner graph showed the Scatchard plot of the specific binding versus the concentration of 64 Cu-DOTA-11-25 mAb.
    Figure Legend Snippet: Cell binding assay with 64 Cu-DOTA-11-25 mAb. BxPC-3 cells were transferred to 24-well plates at 5 × 10 4 cells/well/mL and cultured for 4 days. Various concentrations of 64 Cu-DOTA-11-25 mAb were incubated with the cell monolayers for 2 hours on ice in complete growth media (RPMI-1640 medium containing 10% fetal bovine serum). The cells were washed and lysed and their radioactivity was counted in a γ -counter. Inner graph showed the Scatchard plot of the specific binding versus the concentration of 64 Cu-DOTA-11-25 mAb.

    Techniques Used: Cell Binding Assay, Cell Culture, Incubation, Radioactivity, Binding Assay, Concentration Assay

    10) Product Images from "PEG-b-poly (carbonate)-derived Nanocarrier Platform with pH-responsive properties for Pancreatic Cancer Combination Therapy"

    Article Title: PEG-b-poly (carbonate)-derived Nanocarrier Platform with pH-responsive properties for Pancreatic Cancer Combination Therapy

    Journal: Colloids and surfaces. B, Biointerfaces

    doi: 10.1016/j.colsurfb.2018.10.069

    ( a ) Both PEG-DB and PEG-PY block copolymers in their unassembled form are non-toxic to MIAPaCa-2 cells (N = 3) (b) Cell viability for GEM (0.8 μM) encapsulated in PEG-DB and GDC 0449 (1.5 μM) in PEG-PY NPs in BxPC-3 cells. (c) Cellular viability studies of Mia PaCa-2 cells when treated with increasing concentration of GEM in either free or PEG-DB encapsulated form in the presence of 10 nM GDC (free or PEG-PY encapsulated form, N = 3) (d) Immobilization of iRGD peptide on PEG-DB nanoparticles enhances uptake of the nanoparticles in Mia PaCa-2 cells at 37 °C.
    Figure Legend Snippet: ( a ) Both PEG-DB and PEG-PY block copolymers in their unassembled form are non-toxic to MIAPaCa-2 cells (N = 3) (b) Cell viability for GEM (0.8 μM) encapsulated in PEG-DB and GDC 0449 (1.5 μM) in PEG-PY NPs in BxPC-3 cells. (c) Cellular viability studies of Mia PaCa-2 cells when treated with increasing concentration of GEM in either free or PEG-DB encapsulated form in the presence of 10 nM GDC (free or PEG-PY encapsulated form, N = 3) (d) Immobilization of iRGD peptide on PEG-DB nanoparticles enhances uptake of the nanoparticles in Mia PaCa-2 cells at 37 °C.

    Techniques Used: Blocking Assay, Concentration Assay

    11) Product Images from "ImmunoPET imaging of tissue factor expression in pancreatic cancer with 89Zr-Df-ALT-836"

    Article Title: ImmunoPET imaging of tissue factor expression in pancreatic cancer with 89Zr-Df-ALT-836

    Journal: Journal of controlled release : official journal of the Controlled Release Society

    doi: 10.1016/j.jconrel.2017.08.029

    TF/CD31 immunofluorescence co-staining of pancreatic tumors, spleen, kidney, and liver tissues. TF staining (green channel) was pronounced in BXPC-3 tumors whereas green fluorescence signal was at background levels in PANC-1 tumors, spleen, kidney, and liver. No significant overlap between CD31 (vasculature) and TF staining was observed. Scale bar = 50 μm.
    Figure Legend Snippet: TF/CD31 immunofluorescence co-staining of pancreatic tumors, spleen, kidney, and liver tissues. TF staining (green channel) was pronounced in BXPC-3 tumors whereas green fluorescence signal was at background levels in PANC-1 tumors, spleen, kidney, and liver. No significant overlap between CD31 (vasculature) and TF staining was observed. Scale bar = 50 μm.

    Techniques Used: Immunofluorescence, Staining, Fluorescence

    Representative maximum-intensity projection (MIP) of longitudinal in vivo PET images of pancreatic cancer-bearing mice administered 89 Zr-Df-ALT-836 (7.4–11.1 MBq). Prominent tumor uptake of 89 Zr-Df-ALT-836 was observed in mice bearing BXPC-3 xenografts (top row), while PANC-1 tumors (middle row) exhibited negligible radioactivity accumulation. Mice pre-injected with a TF-blocking dose of ALT-836 (50 mg/kg) displayed significantly lower accrual of the tracer in BXPC-3 tumors (bottom row).
    Figure Legend Snippet: Representative maximum-intensity projection (MIP) of longitudinal in vivo PET images of pancreatic cancer-bearing mice administered 89 Zr-Df-ALT-836 (7.4–11.1 MBq). Prominent tumor uptake of 89 Zr-Df-ALT-836 was observed in mice bearing BXPC-3 xenografts (top row), while PANC-1 tumors (middle row) exhibited negligible radioactivity accumulation. Mice pre-injected with a TF-blocking dose of ALT-836 (50 mg/kg) displayed significantly lower accrual of the tracer in BXPC-3 tumors (bottom row).

    Techniques Used: In Vivo, Positron Emission Tomography, Mouse Assay, Radioactivity, Injection, Blocking Assay

    Quantitative analysis of longitudinal PET images. (A) Representative 3D rendering of PET/CT images acquired in mice administered 89 Zr-Df-ALT-836 at 48 h post-injection. (B) Time-activity curves (TACs) describing 89 Zr-Df-ALT-836 uptake in mice bearing BXPC-3, PANC-1, and TF-blocked BXPC-3 xenografts. Uptake of the tracer was significantly higher in BXPC-3 tumors at all timepoints. (C) TACs describing the clearance of the tracer from heart/blood, liver, and muscle. Quantitative data was generated from a region-of-interest analysis of the PET images and reported as %ID/g (mean ± SD).
    Figure Legend Snippet: Quantitative analysis of longitudinal PET images. (A) Representative 3D rendering of PET/CT images acquired in mice administered 89 Zr-Df-ALT-836 at 48 h post-injection. (B) Time-activity curves (TACs) describing 89 Zr-Df-ALT-836 uptake in mice bearing BXPC-3, PANC-1, and TF-blocked BXPC-3 xenografts. Uptake of the tracer was significantly higher in BXPC-3 tumors at all timepoints. (C) TACs describing the clearance of the tracer from heart/blood, liver, and muscle. Quantitative data was generated from a region-of-interest analysis of the PET images and reported as %ID/g (mean ± SD).

    Techniques Used: Positron Emission Tomography, Mouse Assay, Injection, Activity Assay, Generated

    Ex vivo biodistribution of 89 Zr-Df-ALT-836 in mice bearing BXPC-3 or PANC-1 tumor xenografts. Mice were euthanized 120 h after injection of 89 Zr-Df-ALT-836 and tracer biodistribution in the tumor and normal tissues was determined via gamma counting. Results were expressed as %ID/g (mean ± SD).
    Figure Legend Snippet: Ex vivo biodistribution of 89 Zr-Df-ALT-836 in mice bearing BXPC-3 or PANC-1 tumor xenografts. Mice were euthanized 120 h after injection of 89 Zr-Df-ALT-836 and tracer biodistribution in the tumor and normal tissues was determined via gamma counting. Results were expressed as %ID/g (mean ± SD).

    Techniques Used: Ex Vivo, Mouse Assay, Injection

    In vitro characterization of 89 Zr-Df-ALT-836. (A) Flow cytometry analysis of TF-binding of ALT-836 and Df-ALT-836 in BXPC-3 (TF-high) and PANC-1 (TF-low) human pancreatic cancer cells. (B) Concentration-depended displacement of bound 89 Zr-Df-ALT-836 by Df-ALT-836 in BXPC-3 cells (IC 50 : 1.38 ± 0.34 nM). (C) TF saturation binding assay curve in BXPC-3 cells. The TF-affinity constant of 89 Zr-Df-ALT-836 (K d : 1.49 ± 0.66 nM) and the number of TF per cell (6.36×10 5 ) were determined. (D) Cell internalization assay displaying the kinetics of 89 Zr-Df-ALT-836 (E) and efflux in BXPC-3 cancer cells.
    Figure Legend Snippet: In vitro characterization of 89 Zr-Df-ALT-836. (A) Flow cytometry analysis of TF-binding of ALT-836 and Df-ALT-836 in BXPC-3 (TF-high) and PANC-1 (TF-low) human pancreatic cancer cells. (B) Concentration-depended displacement of bound 89 Zr-Df-ALT-836 by Df-ALT-836 in BXPC-3 cells (IC 50 : 1.38 ± 0.34 nM). (C) TF saturation binding assay curve in BXPC-3 cells. The TF-affinity constant of 89 Zr-Df-ALT-836 (K d : 1.49 ± 0.66 nM) and the number of TF per cell (6.36×10 5 ) were determined. (D) Cell internalization assay displaying the kinetics of 89 Zr-Df-ALT-836 (E) and efflux in BXPC-3 cancer cells.

    Techniques Used: In Vitro, Flow Cytometry, Cytometry, Binding Assay, Concentration Assay, Saturation Assay

    12) Product Images from "Rapid transport of deformation-tuned nanoparticles across biological hydrogels and cellular barriers"

    Article Title: Rapid transport of deformation-tuned nanoparticles across biological hydrogels and cellular barriers

    Journal: Nature Communications

    doi: 10.1038/s41467-018-05061-3

    NP entry into tissues covered with hydrogels in vivo. a Distribution of NPs in rat intestines. Intestinal ligated loops were incubated with DiI-labeled NPs for 1 h. Fluorescence micrographs were obtained from transverse cryo-sections of the intestines. “L” indicates the lumen of the intestine. Blue: nuclei of the intestinal villi. Red: NPs. b In vivo imaging of BxPC-3 and HPSC tumor-bearing mice taken at the indicated time points before and after peritumoral injection of IR783-labeled soft, semi-elastic, or hard NPs. c Distribution of DiI-labeled softer, semi-elastic, and harder NPs in tumor slices of BxPC-3 and HPSC tumor xenografts 6 h after peritumoral injection. The cell nuclei were counterstained with DAPI. The tumor vessels were labeled with anti-CD31 antibody. Scale bars: 50 μm. Softer: Lip-F127 5% NPs; Semi: PLGA 70 -Lip-F127 5% NPs; Harder: PLGA 160 -Lip-F127 5% NPs. ( n = 3)
    Figure Legend Snippet: NP entry into tissues covered with hydrogels in vivo. a Distribution of NPs in rat intestines. Intestinal ligated loops were incubated with DiI-labeled NPs for 1 h. Fluorescence micrographs were obtained from transverse cryo-sections of the intestines. “L” indicates the lumen of the intestine. Blue: nuclei of the intestinal villi. Red: NPs. b In vivo imaging of BxPC-3 and HPSC tumor-bearing mice taken at the indicated time points before and after peritumoral injection of IR783-labeled soft, semi-elastic, or hard NPs. c Distribution of DiI-labeled softer, semi-elastic, and harder NPs in tumor slices of BxPC-3 and HPSC tumor xenografts 6 h after peritumoral injection. The cell nuclei were counterstained with DAPI. The tumor vessels were labeled with anti-CD31 antibody. Scale bars: 50 μm. Softer: Lip-F127 5% NPs; Semi: PLGA 70 -Lip-F127 5% NPs; Harder: PLGA 160 -Lip-F127 5% NPs. ( n = 3)

    Techniques Used: In Vivo, Incubation, Labeling, Fluorescence, In Vivo Imaging, Mouse Assay, Injection

    Cellular penetration and uptake in vitro. a The internalization of NPs by E12 cells with or without pretreatment to remove mucus. Soft: Lip-F127 5% NPs; Semi-elastic: PLGA 70 -Lip-F127 5% NPs; Hard: PLGA 160 -Lip-F127 5% NPs. b Caco-2 cell-associated fluorescence after different incubation times. c 3D images of the mucus penetration and cellular internalization of NPs in the E12 cell monolayer. Green: mucus stained with Alexa Fluor 488-wheat germ agglutinin. Blue: nuclei stained with Hoechst stain. Red: DiI-labeled NPs. Scale bar: 20 μm. d Fluorescent confocal images of E12 cells (stained with 4’,6-diamidino-2-phenylindole [DAPI]) incubated with NPs for 2 h. Colocalization of the PLGA core entrapping DiO (green) and the lipid layer labeled by DiI (red) is indicated in yellow. Scale bar: 20 μm. e NP penetration into the BxPC-3 and HPSC multicellular spheroids. Z-stack images were obtained starting from the top and into the core of the spheroid at intervals of 20 µm. Scale bar: 50 μm. Data are shown as the means ± standard deviations (SDs). ( n = 3) (ns, P > 0.05; * P
    Figure Legend Snippet: Cellular penetration and uptake in vitro. a The internalization of NPs by E12 cells with or without pretreatment to remove mucus. Soft: Lip-F127 5% NPs; Semi-elastic: PLGA 70 -Lip-F127 5% NPs; Hard: PLGA 160 -Lip-F127 5% NPs. b Caco-2 cell-associated fluorescence after different incubation times. c 3D images of the mucus penetration and cellular internalization of NPs in the E12 cell monolayer. Green: mucus stained with Alexa Fluor 488-wheat germ agglutinin. Blue: nuclei stained with Hoechst stain. Red: DiI-labeled NPs. Scale bar: 20 μm. d Fluorescent confocal images of E12 cells (stained with 4’,6-diamidino-2-phenylindole [DAPI]) incubated with NPs for 2 h. Colocalization of the PLGA core entrapping DiO (green) and the lipid layer labeled by DiI (red) is indicated in yellow. Scale bar: 20 μm. e NP penetration into the BxPC-3 and HPSC multicellular spheroids. Z-stack images were obtained starting from the top and into the core of the spheroid at intervals of 20 µm. Scale bar: 50 μm. Data are shown as the means ± standard deviations (SDs). ( n = 3) (ns, P > 0.05; * P

    Techniques Used: In Vitro, Fluorescence, Incubation, Staining, Labeling

    13) Product Images from "TGF-β induces miR-100 and miR-125b but blocks let-7a through LIN28B controlling PDAC progression"

    Article Title: TGF-β induces miR-100 and miR-125b but blocks let-7a through LIN28B controlling PDAC progression

    Journal: Nature Communications

    doi: 10.1038/s41467-018-03962-x

    Effects of miR-100 and miR-125b on EMT and stemness. a Phase-contrast images of BxPC-3, PANC-1, and CHX45 cells treated with control mimic (pre-nc) or mature miRNA mimics (pre-miRs) for 12 days (5 nM). Scale bar: 100 µm. b Immunofluorescence (IF) staining for CDH1 (red) and F-actin (green) in BxPC-3 treated as in a . Nuclei are visualized with TO-PRO-3 stain (blue); scale bar: 20 µm. In a , b representative images from three independent experiments are shown. c Morphology of S2-007 stable knockdown clones for miR-100 (Z100), miR-125 (Z125b), and control (Zc) generated with Zip technology. Representative pictures from two different clones per treatment are shown. Phase-contrast images are shown at the top and corresponding GFP images at the bottom. Scale bar: 400 µm. d – f Sphere-forming assays in BxPC-3 cells transiently transfected with precursor miRNA mimics ( d ), in PANC-1 cells treated with anti-miRNA inhibitors ( e ), and in four independent PANC-1 Zip stable knockdown clones ( n = 4) ( f ). Representative spheres are shown in lower panels in phase-contrast images and corresponding GFP images. Values represent the mean ± s.e.m. Data are from three independent experiments each performed in triplicate. g Mice were subcutaneously injected with the indicated number of S2-007 Zip control cells (Zc-11) on the right flank and S2-007 Zip stable miR-100 knockdown (Z100-3) or miR-125b knockdown (Z125b-5) on the left flank ( n ). h Images of resected tumors are shown. ** P -value
    Figure Legend Snippet: Effects of miR-100 and miR-125b on EMT and stemness. a Phase-contrast images of BxPC-3, PANC-1, and CHX45 cells treated with control mimic (pre-nc) or mature miRNA mimics (pre-miRs) for 12 days (5 nM). Scale bar: 100 µm. b Immunofluorescence (IF) staining for CDH1 (red) and F-actin (green) in BxPC-3 treated as in a . Nuclei are visualized with TO-PRO-3 stain (blue); scale bar: 20 µm. In a , b representative images from three independent experiments are shown. c Morphology of S2-007 stable knockdown clones for miR-100 (Z100), miR-125 (Z125b), and control (Zc) generated with Zip technology. Representative pictures from two different clones per treatment are shown. Phase-contrast images are shown at the top and corresponding GFP images at the bottom. Scale bar: 400 µm. d – f Sphere-forming assays in BxPC-3 cells transiently transfected with precursor miRNA mimics ( d ), in PANC-1 cells treated with anti-miRNA inhibitors ( e ), and in four independent PANC-1 Zip stable knockdown clones ( n = 4) ( f ). Representative spheres are shown in lower panels in phase-contrast images and corresponding GFP images. Values represent the mean ± s.e.m. Data are from three independent experiments each performed in triplicate. g Mice were subcutaneously injected with the indicated number of S2-007 Zip control cells (Zc-11) on the right flank and S2-007 Zip stable miR-100 knockdown (Z100-3) or miR-125b knockdown (Z125b-5) on the left flank ( n ). h Images of resected tumors are shown. ** P -value

    Techniques Used: Immunofluorescence, Staining, Clone Assay, Generated, Transfection, Mouse Assay, Injection

    14) Product Images from "Long non-coding RNA MVIH promotes cell proliferation, migration, invasion through regulating multiple cancer-related pathways, and correlates with worse prognosis in pancreatic ductal adenocarcinomas"

    Article Title: Long non-coding RNA MVIH promotes cell proliferation, migration, invasion through regulating multiple cancer-related pathways, and correlates with worse prognosis in pancreatic ductal adenocarcinomas

    Journal: American Journal of Translational Research

    doi:

    Lnc-MVIH reduced cell chemosensitivity. In BxPC-3 cells, lnc-MVIH overexpression reduced Gemcitabine chemosensitivity (A) and 5-FU chemosensitivity (B). In PANC-1 cells, lnc-MVIH knockdown increased Gemcitabine chemosensitivity (C) and 5-FU chemosensitivity (D). Lnc-MVIH: long non-coding RNAs associated with microvascular invasion in hepatocellular carcinoma; 5-FU: 5-Fluorouracil.
    Figure Legend Snippet: Lnc-MVIH reduced cell chemosensitivity. In BxPC-3 cells, lnc-MVIH overexpression reduced Gemcitabine chemosensitivity (A) and 5-FU chemosensitivity (B). In PANC-1 cells, lnc-MVIH knockdown increased Gemcitabine chemosensitivity (C) and 5-FU chemosensitivity (D). Lnc-MVIH: long non-coding RNAs associated with microvascular invasion in hepatocellular carcinoma; 5-FU: 5-Fluorouracil.

    Techniques Used: Over Expression

    Lnc-MVIH promoted cell migration and increased cell invasion. In BxPC-3 cells, cell migration was increased in OE-MVIH group compared to OE-NC group (A, B); cell invasion was enhanced in OE-MVIH group compared to OE-NC group (C, D). In PANC-1 cells, cell migration was reduced in KD-MVIH group compared to KD-NC group (E, F); cell invasion was decreased in KD-MVIH group compared to KD-NC group as well (G, H). Lnc-MVIH: long non-coding RNAs associated with microvascular invasion in hepatocellular carcinoma.
    Figure Legend Snippet: Lnc-MVIH promoted cell migration and increased cell invasion. In BxPC-3 cells, cell migration was increased in OE-MVIH group compared to OE-NC group (A, B); cell invasion was enhanced in OE-MVIH group compared to OE-NC group (C, D). In PANC-1 cells, cell migration was reduced in KD-MVIH group compared to KD-NC group (E, F); cell invasion was decreased in KD-MVIH group compared to KD-NC group as well (G, H). Lnc-MVIH: long non-coding RNAs associated with microvascular invasion in hepatocellular carcinoma.

    Techniques Used: Migration

    Lnc-MVIH promoted cell proliferation but inhibited apoptosis. In BxPC-3 cells, transfection was successful (A); cell proliferation was increased in OE-MVIH group compared to OE-NC group at 48 h and 72 h (B); cell apoptosis was decreased in OE-MVIH group compared to OE-NC group at 48 h (C, D). In PANC-1 cells, transfection was successful (E); Cell proliferation was reduced in KD-MVIH group compared to KD-NC group at 48 h and 72 h (F). Cell apoptosis was enhanced in KD-MVIH group compared to KD-NC group at 48 h (G, H). Lnc-MVIH: long non-coding RNAs associated with microvascular invasion in hepatocellular carcinoma. OD: optical density.
    Figure Legend Snippet: Lnc-MVIH promoted cell proliferation but inhibited apoptosis. In BxPC-3 cells, transfection was successful (A); cell proliferation was increased in OE-MVIH group compared to OE-NC group at 48 h and 72 h (B); cell apoptosis was decreased in OE-MVIH group compared to OE-NC group at 48 h (C, D). In PANC-1 cells, transfection was successful (E); Cell proliferation was reduced in KD-MVIH group compared to KD-NC group at 48 h and 72 h (F). Cell apoptosis was enhanced in KD-MVIH group compared to KD-NC group at 48 h (G, H). Lnc-MVIH: long non-coding RNAs associated with microvascular invasion in hepatocellular carcinoma. OD: optical density.

    Techniques Used: Transfection

    15) Product Images from "Extract of the Medicinal Plant Pao Pereira Inhibits Pancreatic Cancer Stem-Like Cell In Vitro and In Vivo"

    Article Title: Extract of the Medicinal Plant Pao Pereira Inhibits Pancreatic Cancer Stem-Like Cell In Vitro and In Vivo

    Journal: Integrative Cancer Therapies

    doi: 10.1177/1534735418786027

    Inhibition of the proliferation of pancreatic cancer cells by Pao. (A) Dose-response curves. Human pancreatic cancer cells PANC-1, AsPC-1, HPAF-II, BxPC-3, and MIA PaCa-2 were exposed to serial concentrations of Pao for 48 hours. Cell viability was detected by MTT assay. An immortalized noncancerous epithelial cell line, MCR-5, was subjected to the same treatment. (B) IC 50 values of Pao in pancreatic cancer cells and MRC-5 cells. *** P
    Figure Legend Snippet: Inhibition of the proliferation of pancreatic cancer cells by Pao. (A) Dose-response curves. Human pancreatic cancer cells PANC-1, AsPC-1, HPAF-II, BxPC-3, and MIA PaCa-2 were exposed to serial concentrations of Pao for 48 hours. Cell viability was detected by MTT assay. An immortalized noncancerous epithelial cell line, MCR-5, was subjected to the same treatment. (B) IC 50 values of Pao in pancreatic cancer cells and MRC-5 cells. *** P

    Techniques Used: Inhibition, MTT Assay

    16) Product Images from "Targeting STAT3 by a small molecule suppresses pancreatic cancer progression"

    Article Title: Targeting STAT3 by a small molecule suppresses pancreatic cancer progression

    Journal: Oncogene

    doi: 10.1038/s41388-020-01626-z

    N4 inhibits STAT3 activation in pancreatic cancer cells. A PANC-1, CAPAN-2, and BXPC-3 cells were treated with the indicated concentrations of N4 for 24 h. Then, p-STAT3 (Y705), p-STAT3 (S727), and STAT3 were detected by western blot assays with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) used as the loading control. B Pancreatic cancer cells were starved in a medium lacking fetal bovine serum (FBS; basic medium) for 24 h, and then pretreated with N4 in basic medium for 24 h. Then, stimulated with IL-6 (20 ng/mL) for 30 min and lysed for western blot analysis using the indicated antibodies. C Expression levels of STAT3 downstream genes were detected by western blot following treatment of PANC-1 and CAPAN-2 cells with N4. D PANC-1 cells were seeded and allowed to attach, and then pretreated with 2 μM of N4 in FBS-free medium for 24 h. The cells were stimulated for 30 min using IL-6 (20 ng/mL). The STAT3 antibody (green) and 4, 6-diamidino-2-phenylindole (DAPI) (blue) was used for staining and STAT3 and the nucleus, respectively. The samples were photographed and analyzed. The scale bar represents 20 μm. E After 24 h treatment with 2 μM N4, PANC-1 cells were stimulated with IL-6 (20 ng/mL) for 30 min, and the cytoplasmic and nuclear extractions were analyzed by western blot. p-STAT3 (Y705) was used to detect STAT3, and GAPDH and H3 were used as the cytoplasm and nucleus internal control, respectively.
    Figure Legend Snippet: N4 inhibits STAT3 activation in pancreatic cancer cells. A PANC-1, CAPAN-2, and BXPC-3 cells were treated with the indicated concentrations of N4 for 24 h. Then, p-STAT3 (Y705), p-STAT3 (S727), and STAT3 were detected by western blot assays with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) used as the loading control. B Pancreatic cancer cells were starved in a medium lacking fetal bovine serum (FBS; basic medium) for 24 h, and then pretreated with N4 in basic medium for 24 h. Then, stimulated with IL-6 (20 ng/mL) for 30 min and lysed for western blot analysis using the indicated antibodies. C Expression levels of STAT3 downstream genes were detected by western blot following treatment of PANC-1 and CAPAN-2 cells with N4. D PANC-1 cells were seeded and allowed to attach, and then pretreated with 2 μM of N4 in FBS-free medium for 24 h. The cells were stimulated for 30 min using IL-6 (20 ng/mL). The STAT3 antibody (green) and 4, 6-diamidino-2-phenylindole (DAPI) (blue) was used for staining and STAT3 and the nucleus, respectively. The samples were photographed and analyzed. The scale bar represents 20 μm. E After 24 h treatment with 2 μM N4, PANC-1 cells were stimulated with IL-6 (20 ng/mL) for 30 min, and the cytoplasmic and nuclear extractions were analyzed by western blot. p-STAT3 (Y705) was used to detect STAT3, and GAPDH and H3 were used as the cytoplasm and nucleus internal control, respectively.

    Techniques Used: Activation Assay, Western Blot, Expressing, Staining

    N4 suppresses pancreatic cancer cell proliferation and migration and induces apoptosis. A Pancreatic cancer cells (CAPAN-2, PANC-1, MIAPACA-2, BXPC-3, HPAC, and CFPAC-1) and normal cells (HPNE, HAF) were incubated with the indicated concentration of N4 for 48 h. MTS assays were performed to detect the N4-mediated inhibition of cell proliferation. Data are shown as mean ± SD, * P
    Figure Legend Snippet: N4 suppresses pancreatic cancer cell proliferation and migration and induces apoptosis. A Pancreatic cancer cells (CAPAN-2, PANC-1, MIAPACA-2, BXPC-3, HPAC, and CFPAC-1) and normal cells (HPNE, HAF) were incubated with the indicated concentration of N4 for 48 h. MTS assays were performed to detect the N4-mediated inhibition of cell proliferation. Data are shown as mean ± SD, * P

    Techniques Used: Migration, Incubation, Concentration Assay, Inhibition

    17) Product Images from "Exosomes Facilitate Therapeutic Targeting of Oncogenic Kras in Pancreatic Cancer"

    Article Title: Exosomes Facilitate Therapeutic Targeting of Oncogenic Kras in Pancreatic Cancer

    Journal: Nature

    doi: 10.1038/nature22341

    CD47 and macropinocytosis enhance iExosomes uptake and therapeutic efficacy ( A ) Panc-1 orthotopic tumor growth, n=3 mice per group. ( B ) KPC689 orthotopic tumor growth, n=8 mice per group. ( C ) Kaplan-Meier curve, KPC689 orthotopic tumor bearing mice, Log-rank Mantel-Cox test, n=8 mice per group. ( D ) Confocal micrographs (scale bar: 100μm) of increased (preferential) entry of labeled exosomes into tumor tissue. ( E ) Macropinocytic uptake in Panc-1 or BxPC-3 cells, unpaired two-tailed t test. ( F–G ) Macropinocytic and exosomes uptake in BxPC-3 (unpaired two-tailed t test, F ) or Panc-1 (one-way ANOVA comparing treated groups to non-treated group (0 μM EIPA, G ) cells treated with vehicle (DMSO) or EIPA at the indicated concentrations ( H ) Macropinocytic and liposomes uptake, unpaired two-tailed t test. E, G, H: 5 distinct wells, F: 3 distinct wells. In E–H, scale bar: 50μm. The data is presented as the mean ± SEM. * p
    Figure Legend Snippet: CD47 and macropinocytosis enhance iExosomes uptake and therapeutic efficacy ( A ) Panc-1 orthotopic tumor growth, n=3 mice per group. ( B ) KPC689 orthotopic tumor growth, n=8 mice per group. ( C ) Kaplan-Meier curve, KPC689 orthotopic tumor bearing mice, Log-rank Mantel-Cox test, n=8 mice per group. ( D ) Confocal micrographs (scale bar: 100μm) of increased (preferential) entry of labeled exosomes into tumor tissue. ( E ) Macropinocytic uptake in Panc-1 or BxPC-3 cells, unpaired two-tailed t test. ( F–G ) Macropinocytic and exosomes uptake in BxPC-3 (unpaired two-tailed t test, F ) or Panc-1 (one-way ANOVA comparing treated groups to non-treated group (0 μM EIPA, G ) cells treated with vehicle (DMSO) or EIPA at the indicated concentrations ( H ) Macropinocytic and liposomes uptake, unpaired two-tailed t test. E, G, H: 5 distinct wells, F: 3 distinct wells. In E–H, scale bar: 50μm. The data is presented as the mean ± SEM. * p

    Techniques Used: Mouse Assay, Labeling, Two Tailed Test

    Kras G12D RNAi containing exosomes suppress Panc-1 orthotopic tumor growth but not BxPC-3 orthotopic tumor growth ( A ) Experimental scheme. ( B ) Representative micrographs (scale bar: 100μm,) depicting accumulation of internalized AF647-tagged siRNA from exosomes. ( C ) Panc-1 orthotopic tumor growth. PBS: n=6 mice, Control exos: n=6 mice, siKras G12D iLipo: n=3 mice, shKras G12D iLipo: n=3 mice, siKras G12D iExo: n=7 mice, shKras G12D iExo: n=7 mice, siScrbl iExo: n=5 mice, shScramble iExo: n=5 mice. Statistical test compares treatment groups to PBS control group at day 42-post cancer cell injection, or day 28 for siKras G12D exos group. Unpaired two-tailed t test. This graph is an inset from the graph shown in Fig. 2C . ( D ) Tumor bioluminescence at day 77 (total flux), PBS: n=4 mice, Control Exo: n=3 mice, shKras G12D iExo: n=6 mice, shKras G12D iLipo: n=3 mice, shScramble iExo: n=3 mice, siScramble iExo: n=4 mice. (E) Luciferase activity at day 7, 35, 77 and moribund stage or day 200 (shKras G12D iExo)-post cancer cell injection. Some of these panels are also shown in Fig. 2a . ( F ) Bioluminescence from Panc-1 orthotopic tumors over time (total flux). PBS: n=7 mice, Control Exo: n=6 mice, shKras G12D iExo: n=7 mice, shKras G12D iLipo: n=4 mice, shScramble iExo: n=5 mice, siScramble iExo: n=5 mice ( G ) Representative H E of the Panc-1 orthotopic pancreas (scale bar: 100μm). ( H ) Representative micrographs (scale bar: 100μm) of tumors immunolabeled for phosphorylated AKT (p-AKT) and quantification. Control Exo, n=4 mice; shKras G12D iExo, n=6 mice. Unpaired two-tailed t test. ( I–J ) BxPC-3 orthotopic tumor growth, n=3 mice per group. ( K ) Luciferase activity at day 14 and day 77-post cancer cell (BxPC-3) injection. ( L ) Representative H E of the BxPC-3 orthotopic pancreas at the indicated experimental endpoints (scale bar: 100μm). ( M ) Kaplan-Meier curve of BxPC-3 tumor bearing mice, Log-rank Mantel-Cox, n=3 mice per group. The data is presented as the mean ± SEM. Unless otherwise stated, one-way ANOVA was used to determine statistical significance. * p
    Figure Legend Snippet: Kras G12D RNAi containing exosomes suppress Panc-1 orthotopic tumor growth but not BxPC-3 orthotopic tumor growth ( A ) Experimental scheme. ( B ) Representative micrographs (scale bar: 100μm,) depicting accumulation of internalized AF647-tagged siRNA from exosomes. ( C ) Panc-1 orthotopic tumor growth. PBS: n=6 mice, Control exos: n=6 mice, siKras G12D iLipo: n=3 mice, shKras G12D iLipo: n=3 mice, siKras G12D iExo: n=7 mice, shKras G12D iExo: n=7 mice, siScrbl iExo: n=5 mice, shScramble iExo: n=5 mice. Statistical test compares treatment groups to PBS control group at day 42-post cancer cell injection, or day 28 for siKras G12D exos group. Unpaired two-tailed t test. This graph is an inset from the graph shown in Fig. 2C . ( D ) Tumor bioluminescence at day 77 (total flux), PBS: n=4 mice, Control Exo: n=3 mice, shKras G12D iExo: n=6 mice, shKras G12D iLipo: n=3 mice, shScramble iExo: n=3 mice, siScramble iExo: n=4 mice. (E) Luciferase activity at day 7, 35, 77 and moribund stage or day 200 (shKras G12D iExo)-post cancer cell injection. Some of these panels are also shown in Fig. 2a . ( F ) Bioluminescence from Panc-1 orthotopic tumors over time (total flux). PBS: n=7 mice, Control Exo: n=6 mice, shKras G12D iExo: n=7 mice, shKras G12D iLipo: n=4 mice, shScramble iExo: n=5 mice, siScramble iExo: n=5 mice ( G ) Representative H E of the Panc-1 orthotopic pancreas (scale bar: 100μm). ( H ) Representative micrographs (scale bar: 100μm) of tumors immunolabeled for phosphorylated AKT (p-AKT) and quantification. Control Exo, n=4 mice; shKras G12D iExo, n=6 mice. Unpaired two-tailed t test. ( I–J ) BxPC-3 orthotopic tumor growth, n=3 mice per group. ( K ) Luciferase activity at day 14 and day 77-post cancer cell (BxPC-3) injection. ( L ) Representative H E of the BxPC-3 orthotopic pancreas at the indicated experimental endpoints (scale bar: 100μm). ( M ) Kaplan-Meier curve of BxPC-3 tumor bearing mice, Log-rank Mantel-Cox, n=3 mice per group. The data is presented as the mean ± SEM. Unless otherwise stated, one-way ANOVA was used to determine statistical significance. * p

    Techniques Used: Mouse Assay, Injection, Two Tailed Test, Luciferase, Activity Assay, Immunolabeling

    iExosomes specifically target Kras G12D expression ( A ) KRAS G12D transcript levels in Panc-1 cells (n=3 independent experiments). ( B–C ) 1/Ct values from RT-PCR analysis under the listed conditions, to determine the loading efficiency of siRNA. Standards (siKras G12D , 1:2 and 1:4 dilution): n=1, experimental groups: n=3 independent experiments. ( D ) KRAS G12D transcript levels in Panc-1 cells, n=3 independent experiments. The experiments with 400 exos per cell is the same data that is also presented in panel A. ( E–G ) KRAS G12D transcript levels in Panc-1 cells under the listed conditions. In all groups, n=3 independent experiments. ( H ) Western blotting (Panc-1 cells) for phosphorylated ERK (p-ERK) and Vinculin. si and sh Kras G12D iExo: One way ANOVA, iLipo: two-tailed t-test, n=2 independent experiments. ( I ) RAS pull-down assay. ( J–K ) Panc-1 cells MTT assay (n=5 partitions of indicated treatments with 3 or 6 wells for each partition of treatment) (J) and separate independent experiment (K). ( L–M) TUNEL assay (n=3 distinct wells of Panc-1 cells) (L) and separate independent experiment (M). ( N ) FC analysis of apoptosis in Panc-1 cells. Three different treatments were used to treat n=3 distinct wells of cells. ( O ) Wild-type KRAS transcript levels in BxPC-3 cells (n=3 independent experiments). ( P ) KRAS G12V transcript levels in Capan-1 cells (n=3 independent experiments) ( Q ) KRAS G12C transcript levels in MIA PaCa-2 cells (n=3 independent experiments). ( R–U ) MTT assay: n=5 partitions of treatment given to 3 wells each, BxPC-3 cells ( R ) and separate independent experiment ( S ), n=3 partitions of treatment given to 10 wells each, Capan1 cells ( T ), n=3 partitions of treatment given to 10 wells each, MIA PaCa-2 cells, ( U ). The data is presented as the mean ± SEM. Unless otherwise stated, one-way ANOVA was used to determine statistical significance. * p
    Figure Legend Snippet: iExosomes specifically target Kras G12D expression ( A ) KRAS G12D transcript levels in Panc-1 cells (n=3 independent experiments). ( B–C ) 1/Ct values from RT-PCR analysis under the listed conditions, to determine the loading efficiency of siRNA. Standards (siKras G12D , 1:2 and 1:4 dilution): n=1, experimental groups: n=3 independent experiments. ( D ) KRAS G12D transcript levels in Panc-1 cells, n=3 independent experiments. The experiments with 400 exos per cell is the same data that is also presented in panel A. ( E–G ) KRAS G12D transcript levels in Panc-1 cells under the listed conditions. In all groups, n=3 independent experiments. ( H ) Western blotting (Panc-1 cells) for phosphorylated ERK (p-ERK) and Vinculin. si and sh Kras G12D iExo: One way ANOVA, iLipo: two-tailed t-test, n=2 independent experiments. ( I ) RAS pull-down assay. ( J–K ) Panc-1 cells MTT assay (n=5 partitions of indicated treatments with 3 or 6 wells for each partition of treatment) (J) and separate independent experiment (K). ( L–M) TUNEL assay (n=3 distinct wells of Panc-1 cells) (L) and separate independent experiment (M). ( N ) FC analysis of apoptosis in Panc-1 cells. Three different treatments were used to treat n=3 distinct wells of cells. ( O ) Wild-type KRAS transcript levels in BxPC-3 cells (n=3 independent experiments). ( P ) KRAS G12V transcript levels in Capan-1 cells (n=3 independent experiments) ( Q ) KRAS G12C transcript levels in MIA PaCa-2 cells (n=3 independent experiments). ( R–U ) MTT assay: n=5 partitions of treatment given to 3 wells each, BxPC-3 cells ( R ) and separate independent experiment ( S ), n=3 partitions of treatment given to 10 wells each, Capan1 cells ( T ), n=3 partitions of treatment given to 10 wells each, MIA PaCa-2 cells, ( U ). The data is presented as the mean ± SEM. Unless otherwise stated, one-way ANOVA was used to determine statistical significance. * p

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot, Two Tailed Test, Pull Down Assay, MTT Assay, TUNEL Assay

    Pancreas localization and macropinocytosis promotes iExosomes uptake into tumor cells ( A ) Quantification and representative pictures (scale bar: 100μm) of pancreas structure in KTC mice injected with exosomes with AF647 tagged siRNA, n=3 mice. ( B ) Quantification and representative images (scale bar: 100μm) of pancreas of mice injected with the indicated conditions, n=3 mice, unpaired two-tailed t test. ( C ) Representative images (scale bar: 50μm) for data presented in Fig. 3E–H . ( D ) Quantification of macropinocytic and exosomes uptake (independent experiment, identical statistical analyses). ( E ) AF647 RNAi-tagged exosomes/liposomes uptake in Panc-1 cells (scale bar: 100μm). n=3 independent experiments. ( F ) CM-DiI tagged CD47 k/o vs . WT exosomes uptake in Panc-1 cells (scale bar: 100μm). n=3 independent experiments. ( G ) CM-DiI tagged CD47 k/o vs . WT exosomes uptake in BxPC-3 cells (scale bar: 100μm). n=3 independent experiments. The data is presented as the mean ± SEM. Unless otherwise stated, one-way ANOVA was used to determine statistical significance. ns: not significant. * p
    Figure Legend Snippet: Pancreas localization and macropinocytosis promotes iExosomes uptake into tumor cells ( A ) Quantification and representative pictures (scale bar: 100μm) of pancreas structure in KTC mice injected with exosomes with AF647 tagged siRNA, n=3 mice. ( B ) Quantification and representative images (scale bar: 100μm) of pancreas of mice injected with the indicated conditions, n=3 mice, unpaired two-tailed t test. ( C ) Representative images (scale bar: 50μm) for data presented in Fig. 3E–H . ( D ) Quantification of macropinocytic and exosomes uptake (independent experiment, identical statistical analyses). ( E ) AF647 RNAi-tagged exosomes/liposomes uptake in Panc-1 cells (scale bar: 100μm). n=3 independent experiments. ( F ) CM-DiI tagged CD47 k/o vs . WT exosomes uptake in Panc-1 cells (scale bar: 100μm). n=3 independent experiments. ( G ) CM-DiI tagged CD47 k/o vs . WT exosomes uptake in BxPC-3 cells (scale bar: 100μm). n=3 independent experiments. The data is presented as the mean ± SEM. Unless otherwise stated, one-way ANOVA was used to determine statistical significance. ns: not significant. * p

    Techniques Used: Mouse Assay, Injection, Two Tailed Test

    18) Product Images from "BAICALEIN, A COMPONENT OF SCUTELLARIA BAICALENSIS, INDUCES APOPTOSIS BY MCL-1 DOWN-REGULATION IN HUMAN PANCREATIC CANCER CELLS"

    Article Title: BAICALEIN, A COMPONENT OF SCUTELLARIA BAICALENSIS, INDUCES APOPTOSIS BY MCL-1 DOWN-REGULATION IN HUMAN PANCREATIC CANCER CELLS

    Journal: Biochimica et biophysica acta

    doi: 10.1016/j.bbamcr.2011.05.003

    Baicalein modulated expression of a subset of anti-apoptotic Bcl-2 family proteins and induced cytochrome c release from mitochondria. A, endogenous expression of anti-apoptotic Bcl-2 family proteins in BxPC-3 (B), HPAF-II (H), MIA PaCa-2 (M), Panc-1
    Figure Legend Snippet: Baicalein modulated expression of a subset of anti-apoptotic Bcl-2 family proteins and induced cytochrome c release from mitochondria. A, endogenous expression of anti-apoptotic Bcl-2 family proteins in BxPC-3 (B), HPAF-II (H), MIA PaCa-2 (M), Panc-1

    Techniques Used: Expressing

    Changes in expression of pro-apoptotic Bcl-2 family proteins by baicalein. A, endogenous expression of pro-apoptotic multi-domain and BH3-only proteins in BxPC-3 (B), HPAF-II (H), MIA PaCa-2 (M), Panc-1 (P), Capan-2 (C), and AsPc-1 (A) cells. B, endogenous
    Figure Legend Snippet: Changes in expression of pro-apoptotic Bcl-2 family proteins by baicalein. A, endogenous expression of pro-apoptotic multi-domain and BH3-only proteins in BxPC-3 (B), HPAF-II (H), MIA PaCa-2 (M), Panc-1 (P), Capan-2 (C), and AsPc-1 (A) cells. B, endogenous

    Techniques Used: Expressing

    19) Product Images from "Establishment of highly invasive pancreatic cancer cell lines and the expression of IL-32"

    Article Title: Establishment of highly invasive pancreatic cancer cell lines and the expression of IL-32

    Journal: Oncology Letters

    doi: 10.3892/ol.2020.11825

    Immunocytochemistry of IL-32 in BxPC-3. (A) P of BxPC-3 cells. IL-32 expression is hardly observed. (B) S of BxPC-3 cells. IL-32-positive cells may be seen. IL, interleukin; S, selected; P, parent
    Figure Legend Snippet: Immunocytochemistry of IL-32 in BxPC-3. (A) P of BxPC-3 cells. IL-32 expression is hardly observed. (B) S of BxPC-3 cells. IL-32-positive cells may be seen. IL, interleukin; S, selected; P, parent

    Techniques Used: Immunocytochemistry, Expressing

    Establishment of highly invasive cell lines (A-D) and low invasive cell lines (E and F). Four cell lines (highly invasive group) had a greater invasion capacity in S than P but two cell lines (low invasive group) showed almost no change between P and S. (A) PANC-1, (B) KP3, (C) BxPC-3, (D) TCC-PAN2, (E) AsPC-1 and (F) MIA PaCa-2. S, selected; P, parent.
    Figure Legend Snippet: Establishment of highly invasive cell lines (A-D) and low invasive cell lines (E and F). Four cell lines (highly invasive group) had a greater invasion capacity in S than P but two cell lines (low invasive group) showed almost no change between P and S. (A) PANC-1, (B) KP3, (C) BxPC-3, (D) TCC-PAN2, (E) AsPC-1 and (F) MIA PaCa-2. S, selected; P, parent.

    Techniques Used:

    20) Product Images from "Suppression of Tumor Growth and Muscle Wasting in a Transgenic Mouse Model of Pancreatic Cancer by the Novel Histone Deacetylase Inhibitor AR-42"

    Article Title: Suppression of Tumor Growth and Muscle Wasting in a Transgenic Mouse Model of Pancreatic Cancer by the Novel Histone Deacetylase Inhibitor AR-42

    Journal: Neoplasia (New York, N.Y.)

    doi: 10.1016/j.neo.2016.10.003

    Effects of AR-42 on various biomarkers of apoptosis, HDAC inhibition, and proliferation. Human PDAC cells (AsPC-1, SW1990, BxPC-3, COLO-357, and PANC-1) were treated with AR-42 for 48 hours at the concentrations indicated, and cell lysates were made for Western blotting. Immunoblots of markers of HDAC inhibition (A), apoptosis (B), and proliferation and G2 cell cycle arrest (C). β-Actin was used as a loading control.
    Figure Legend Snippet: Effects of AR-42 on various biomarkers of apoptosis, HDAC inhibition, and proliferation. Human PDAC cells (AsPC-1, SW1990, BxPC-3, COLO-357, and PANC-1) were treated with AR-42 for 48 hours at the concentrations indicated, and cell lysates were made for Western blotting. Immunoblots of markers of HDAC inhibition (A), apoptosis (B), and proliferation and G2 cell cycle arrest (C). β-Actin was used as a loading control.

    Techniques Used: Inhibition, Western Blot

    Effects of AR-42 on cell cycle. Pancreatic cancer cells were treated with vehicle control and 0.5 μM AR-42 (AsPC-1, BxPC-3, COLO-357, SW1990, and MiaPaCa-2) or 2 μM AR-42 (PANC-1) for 48 hours. Cells were harvested, stained with propodium iodide, and analyzed through fluorescence-activated cell sorting. The percent of cells in Sub-G1, G0/G1, S, and G2/M cell cycle phase is shown.
    Figure Legend Snippet: Effects of AR-42 on cell cycle. Pancreatic cancer cells were treated with vehicle control and 0.5 μM AR-42 (AsPC-1, BxPC-3, COLO-357, SW1990, and MiaPaCa-2) or 2 μM AR-42 (PANC-1) for 48 hours. Cells were harvested, stained with propodium iodide, and analyzed through fluorescence-activated cell sorting. The percent of cells in Sub-G1, G0/G1, S, and G2/M cell cycle phase is shown.

    Techniques Used: Staining, Fluorescence, FACS

    Antiproliferative effects of AR-42 in six different pancreatic cancer cell lines. Human PDAC cell lines (A) AsPC-1, (B) SW1990, (C) BxPC-3, (D) COLO-357, (E) MiaPaCa-2, and (F) PANC-1 were treated for 72 hours with AR-42 (Arno Therapeutics, Inc., Flemington, NJ). Cell viability was measured via MTT assay. The data are shown as mean ± SD of n = 6 replicates.
    Figure Legend Snippet: Antiproliferative effects of AR-42 in six different pancreatic cancer cell lines. Human PDAC cell lines (A) AsPC-1, (B) SW1990, (C) BxPC-3, (D) COLO-357, (E) MiaPaCa-2, and (F) PANC-1 were treated for 72 hours with AR-42 (Arno Therapeutics, Inc., Flemington, NJ). Cell viability was measured via MTT assay. The data are shown as mean ± SD of n = 6 replicates.

    Techniques Used: MTT Assay

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    Article Snippet: .. Cell Culture MCF-7, BxPC-3 and MG-63 cells were purchased from American Type Culture Collection (ATCC, Manassas, VA, USA). .. MCF-7 and MG-63 cells were cultured in DMEM medium, while BxPC-3 in RPMI medium, at 37 °C in a 5% CO2 humidified atmosphere.

    Article Title: Leptin-Notch signaling axis is involved in pancreatic cancer progression
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    ATCC bxpc3 human pancreatic cancer cells
    (A) Time course of Lef1 and Axin2 levels in NS (○) or GSK3β shRNA (●) <t>BxPC3</t> and Panc1 cells subjected to 2-Gy radiation. Mean of three experiments with SDs, * P ≤ 0.05. (B) BxPC3 or Panc1 xenografts were treated with 2-Gy
    Bxpc3 Human Pancreatic Cancer Cells, 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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    (A) Time course of Lef1 and Axin2 levels in NS (○) or GSK3β shRNA (●) BxPC3 and Panc1 cells subjected to 2-Gy radiation. Mean of three experiments with SDs, * P ≤ 0.05. (B) BxPC3 or Panc1 xenografts were treated with 2-Gy

    Journal: Neoplasia (New York, N.Y.)

    Article Title: GSK3? and ?-Catenin Modulate Radiation Cytotoxicity in Pancreatic Cancer 1

    doi:

    Figure Lengend Snippet: (A) Time course of Lef1 and Axin2 levels in NS (○) or GSK3β shRNA (●) BxPC3 and Panc1 cells subjected to 2-Gy radiation. Mean of three experiments with SDs, * P ≤ 0.05. (B) BxPC3 or Panc1 xenografts were treated with 2-Gy

    Article Snippet: Panc-1 and BxPc3 human pancreatic cancer cells were obtained from the American Type Culture Collection (Manassas, VA) and were maintained according to standard tissue culture conditions.

    Techniques: shRNA

    (A) BxPC3 and Panc1 cells expressing NS or GSK3β shRNA were treated with 2 Gy, and Western blot analysis for total and phosphorylated GSK3β was performed. The blots were confirmed in at least three independent experiments. (B) Clonogenic

    Journal: Neoplasia (New York, N.Y.)

    Article Title: GSK3? and ?-Catenin Modulate Radiation Cytotoxicity in Pancreatic Cancer 1

    doi:

    Figure Lengend Snippet: (A) BxPC3 and Panc1 cells expressing NS or GSK3β shRNA were treated with 2 Gy, and Western blot analysis for total and phosphorylated GSK3β was performed. The blots were confirmed in at least three independent experiments. (B) Clonogenic

    Article Snippet: Panc-1 and BxPc3 human pancreatic cancer cells were obtained from the American Type Culture Collection (Manassas, VA) and were maintained according to standard tissue culture conditions.

    Techniques: Expressing, shRNA, Western Blot

    (A) Xenografts from BxPC3 and Panc1 cells expressing NS or GSK3β shRNA were analyzed for expression of GSK3β. The blots were confirmed in at least three independent experiments. BxPC3 NS shRNA and GSK3β knockdown xenografts were

    Journal: Neoplasia (New York, N.Y.)

    Article Title: GSK3? and ?-Catenin Modulate Radiation Cytotoxicity in Pancreatic Cancer 1

    doi:

    Figure Lengend Snippet: (A) Xenografts from BxPC3 and Panc1 cells expressing NS or GSK3β shRNA were analyzed for expression of GSK3β. The blots were confirmed in at least three independent experiments. BxPC3 NS shRNA and GSK3β knockdown xenografts were

    Article Snippet: Panc-1 and BxPc3 human pancreatic cancer cells were obtained from the American Type Culture Collection (Manassas, VA) and were maintained according to standard tissue culture conditions.

    Techniques: Expressing, shRNA

    Xenografts from BxPC3 and Panc1 cells expressing NS or GSK3β shRNA were analyzed by H E (A). Black arrows indicate glandular structures present in the NS shRNA xenografts, which are absent in GSK3β shRNA xenografts. Panc1 xenografts

    Journal: Neoplasia (New York, N.Y.)

    Article Title: GSK3? and ?-Catenin Modulate Radiation Cytotoxicity in Pancreatic Cancer 1

    doi:

    Figure Lengend Snippet: Xenografts from BxPC3 and Panc1 cells expressing NS or GSK3β shRNA were analyzed by H E (A). Black arrows indicate glandular structures present in the NS shRNA xenografts, which are absent in GSK3β shRNA xenografts. Panc1 xenografts

    Article Snippet: Panc-1 and BxPc3 human pancreatic cancer cells were obtained from the American Type Culture Collection (Manassas, VA) and were maintained according to standard tissue culture conditions.

    Techniques: Expressing, shRNA

    Clonogenic survival of NS, (○) or β-catenin shRNA, (●) BxPC3, (A) and Panc1, (B) cells. Clonogenic survival of empty vector control, (○) or β-catenin S33YFLAG (●) Panc1 cells, (C). Error bars are SD of three

    Journal: Neoplasia (New York, N.Y.)

    Article Title: GSK3? and ?-Catenin Modulate Radiation Cytotoxicity in Pancreatic Cancer 1

    doi:

    Figure Lengend Snippet: Clonogenic survival of NS, (○) or β-catenin shRNA, (●) BxPC3, (A) and Panc1, (B) cells. Clonogenic survival of empty vector control, (○) or β-catenin S33YFLAG (●) Panc1 cells, (C). Error bars are SD of three

    Article Snippet: Panc-1 and BxPc3 human pancreatic cancer cells were obtained from the American Type Culture Collection (Manassas, VA) and were maintained according to standard tissue culture conditions.

    Techniques: shRNA, Plasmid Preparation

    (A) BxPC3 and Panc1 cells were treated with LiCl for 6 hours, and Western blot analysis for total and phosphorylated GSK3β was performed. (B) Clonogenic survival of control (○) or LiCl-pretreated (●) BxPC3 and Panc1 cells. * P ≤

    Journal: Neoplasia (New York, N.Y.)

    Article Title: GSK3? and ?-Catenin Modulate Radiation Cytotoxicity in Pancreatic Cancer 1

    doi:

    Figure Lengend Snippet: (A) BxPC3 and Panc1 cells were treated with LiCl for 6 hours, and Western blot analysis for total and phosphorylated GSK3β was performed. (B) Clonogenic survival of control (○) or LiCl-pretreated (●) BxPC3 and Panc1 cells. * P ≤

    Article Snippet: Panc-1 and BxPc3 human pancreatic cancer cells were obtained from the American Type Culture Collection (Manassas, VA) and were maintained according to standard tissue culture conditions.

    Techniques: Western Blot

    Leptin-induced Notch is linked to proliferation of PC cells ( A ) Representative western blot results of leptin induction of Notch receptors, ligands and targeted molecules in PC cells. ( B ) Quantitative analysis of leptin-induced effects on Notch, ligands and targets. ( C ) Effects of DAPT (a gamma secretase inhibitor) and IONP-LPrA2 (a leptin signaling inhibitor) on leptin-induced proliferation of PC cells. BxPC-3 and MiaPaCa-2 cells were treated with leptin and IONP-LPrA2 for 24 hours. Whole cell lysates were analyzed by western blot. GAPDH was used as protein loading control. Proliferation was determined by MTT assay. PC cells were treated with leptin, IONP-LPrA2 and DAPT for 24 h. Basal (untreated) condition was used as control (100%). Data are expressed as % of control and represent at least three independent experiments. B = basal; L = leptin (1.2 nM); I = IONP-LPrA2 (0.0036 pM); L+I = leptin (1.2 nM) + IONP-LPrA2 (0.0036 pM); L+DAPT = leptin(1.2 nM) + DAPT (20 μM); a: p ≤ 0.05 compared to basal condition.

    Journal: Oncotarget

    Article Title: Leptin-Notch signaling axis is involved in pancreatic cancer progression

    doi: 10.18632/oncotarget.13946

    Figure Lengend Snippet: Leptin-induced Notch is linked to proliferation of PC cells ( A ) Representative western blot results of leptin induction of Notch receptors, ligands and targeted molecules in PC cells. ( B ) Quantitative analysis of leptin-induced effects on Notch, ligands and targets. ( C ) Effects of DAPT (a gamma secretase inhibitor) and IONP-LPrA2 (a leptin signaling inhibitor) on leptin-induced proliferation of PC cells. BxPC-3 and MiaPaCa-2 cells were treated with leptin and IONP-LPrA2 for 24 hours. Whole cell lysates were analyzed by western blot. GAPDH was used as protein loading control. Proliferation was determined by MTT assay. PC cells were treated with leptin, IONP-LPrA2 and DAPT for 24 h. Basal (untreated) condition was used as control (100%). Data are expressed as % of control and represent at least three independent experiments. B = basal; L = leptin (1.2 nM); I = IONP-LPrA2 (0.0036 pM); L+I = leptin (1.2 nM) + IONP-LPrA2 (0.0036 pM); L+DAPT = leptin(1.2 nM) + DAPT (20 μM); a: p ≤ 0.05 compared to basal condition.

    Article Snippet: Cell culture Pancreatic cancer cell lines BxPC-3, MiaPaCa-2, Panc-1 (from primary tumor) and AsPC-1 (from metastasis to peritoneum) were obtained from ATCC and cultured in DMEM supplemented with 10% FBS and 1% Penicillin (100U/ml) /Streptomycin (100μg/ml) (P/S).

    Techniques: Western Blot, MTT Assay

    Effects of leptin and Notch on number and size of primary tumorspheres and PC stem cells (PCSC) ( A ) Representative images of tumorspheres (scale bar = 60 μm) ( B ) Number of PC tumorspheres ( C ) Number of PC tumorspheres by size ( D ) Relative expression of PCSC markers in cells from PC tumorspheres. BxPC-3, Panc-1 and MiaPaCa-2 cells (20,000 cells/well in low attachment plates) were cultured in Mammocult medium containing leptin, IONP-LPrA2 and DAPT (γ-secretase inhibitor-GSI) for 1 week. Tumorsphere number and size were determined under microscope and PCSC markers were assessed by flow cytometry analysis. Basal condition (untreated) was used as control (100%). Effects of treatment on tumorspheres and PCSC markers was expressed as % of control. All experiments were performed in triplicate. a: p ≤ 0.05 when compared to control; b: p ≤ 0.05 when compared to leptin. B = basal; L = leptin (1.2 nM); L+I = leptin (1.2 nM) + IONP-LPrA2 (0.0036 pM); L+D = leptin (1.2 nM) + DAPT (20 μM); S = small tumorsphere; M = medium tumorsphere; Lg = large tumorsphere.

    Journal: Oncotarget

    Article Title: Leptin-Notch signaling axis is involved in pancreatic cancer progression

    doi: 10.18632/oncotarget.13946

    Figure Lengend Snippet: Effects of leptin and Notch on number and size of primary tumorspheres and PC stem cells (PCSC) ( A ) Representative images of tumorspheres (scale bar = 60 μm) ( B ) Number of PC tumorspheres ( C ) Number of PC tumorspheres by size ( D ) Relative expression of PCSC markers in cells from PC tumorspheres. BxPC-3, Panc-1 and MiaPaCa-2 cells (20,000 cells/well in low attachment plates) were cultured in Mammocult medium containing leptin, IONP-LPrA2 and DAPT (γ-secretase inhibitor-GSI) for 1 week. Tumorsphere number and size were determined under microscope and PCSC markers were assessed by flow cytometry analysis. Basal condition (untreated) was used as control (100%). Effects of treatment on tumorspheres and PCSC markers was expressed as % of control. All experiments were performed in triplicate. a: p ≤ 0.05 when compared to control; b: p ≤ 0.05 when compared to leptin. B = basal; L = leptin (1.2 nM); L+I = leptin (1.2 nM) + IONP-LPrA2 (0.0036 pM); L+D = leptin (1.2 nM) + DAPT (20 μM); S = small tumorsphere; M = medium tumorsphere; Lg = large tumorsphere.

    Article Snippet: Cell culture Pancreatic cancer cell lines BxPC-3, MiaPaCa-2, Panc-1 (from primary tumor) and AsPC-1 (from metastasis to peritoneum) were obtained from ATCC and cultured in DMEM supplemented with 10% FBS and 1% Penicillin (100U/ml) /Streptomycin (100μg/ml) (P/S).

    Techniques: Expressing, Cell Culture, Microscopy, Flow Cytometry, Cytometry

    Induction of autophagy with penfluridol treatment. ( A–D ) BxPC-3, AsPC-1 and Panc-1 cells were plated in six well plates and treated with different concentration of penfluridol for 24 h. Cells were stained with 0.4 μg/ml acridine orange and evaluated by Accuri C6 flow cytometer. Values were plotted as means ± SD. Experiment was repeated three times. *Statistically significant when compared with control at p ≤ 0.05. ( E ) BxPC-3, AsPC-1 and Panc-1 cells were treated with different concentration of penfluridol for 24 h. Representative blots showing concentration-dependent effect of penfluridol on p62 and LC3B expression. Actin was used as loading control. Figure shown is the representative blots of at least three independent experiments.

    Journal: Scientific Reports

    Article Title: Penfluridol suppresses pancreatic tumor growth by autophagy-mediated apoptosis

    doi: 10.1038/srep26165

    Figure Lengend Snippet: Induction of autophagy with penfluridol treatment. ( A–D ) BxPC-3, AsPC-1 and Panc-1 cells were plated in six well plates and treated with different concentration of penfluridol for 24 h. Cells were stained with 0.4 μg/ml acridine orange and evaluated by Accuri C6 flow cytometer. Values were plotted as means ± SD. Experiment was repeated three times. *Statistically significant when compared with control at p ≤ 0.05. ( E ) BxPC-3, AsPC-1 and Panc-1 cells were treated with different concentration of penfluridol for 24 h. Representative blots showing concentration-dependent effect of penfluridol on p62 and LC3B expression. Actin was used as loading control. Figure shown is the representative blots of at least three independent experiments.

    Article Snippet: Cell culture BxPC-3 and AsPC-1 human pancreatic cancer cell lines were procured from ATCC, Manassas, VA. Panc-1 cells were kind gift from Dr. Thomas L. Brown (Wright State University, Dayton, OH).

    Techniques: Concentration Assay, Staining, Flow Cytometry, Cytometry, Expressing

    Penfluridol suppresses the growth of subcutaneously implanted BxPC-3 pancreatic tumors by autophagy-mediated apoptosis. ( A ) About 1 × 10 6 BxPC-3 pancreatic cancer cells were injected subcutaneously in flanks of 4–6 week old athymic nude mice. Once tumor volume reached around 70 mm 3 , mice were randomly divided into 4 groups. Group I received vehicle only and served as control. Group II received 10 mg/kg penfluridol by oral gavage every day. Group III received 50 mg/kg chloroquine (i.p) every day whereas Group IV received 10 mg/kg penfluridol as well as 50 mg/kg chloroquine every day till day 27. Tumors volume was measured twice a week using vernier caliper. Values were plotted as mean ± SEM. Statistically different at p ≤ 0.05 ( B ) Subcutaneously implanted tumors were removed aseptically after terminating the experiments. Tumors were homogenized, lysed and analyzed for Cl Caspase 3. Actin was used as loading control. Each lane of blot represents tumor from individual mice. ( C ) Blots were quantitated, normalized with actin and represented as bars. Values were plotted as means ± SEM and considered statistically significant at p ≤ 0.05 ( D ) Tumors were sectioned and immunostained for Cl Caspase 3 and TUNEL as described in method section.

    Journal: Scientific Reports

    Article Title: Penfluridol suppresses pancreatic tumor growth by autophagy-mediated apoptosis

    doi: 10.1038/srep26165

    Figure Lengend Snippet: Penfluridol suppresses the growth of subcutaneously implanted BxPC-3 pancreatic tumors by autophagy-mediated apoptosis. ( A ) About 1 × 10 6 BxPC-3 pancreatic cancer cells were injected subcutaneously in flanks of 4–6 week old athymic nude mice. Once tumor volume reached around 70 mm 3 , mice were randomly divided into 4 groups. Group I received vehicle only and served as control. Group II received 10 mg/kg penfluridol by oral gavage every day. Group III received 50 mg/kg chloroquine (i.p) every day whereas Group IV received 10 mg/kg penfluridol as well as 50 mg/kg chloroquine every day till day 27. Tumors volume was measured twice a week using vernier caliper. Values were plotted as mean ± SEM. Statistically different at p ≤ 0.05 ( B ) Subcutaneously implanted tumors were removed aseptically after terminating the experiments. Tumors were homogenized, lysed and analyzed for Cl Caspase 3. Actin was used as loading control. Each lane of blot represents tumor from individual mice. ( C ) Blots were quantitated, normalized with actin and represented as bars. Values were plotted as means ± SEM and considered statistically significant at p ≤ 0.05 ( D ) Tumors were sectioned and immunostained for Cl Caspase 3 and TUNEL as described in method section.

    Article Snippet: Cell culture BxPC-3 and AsPC-1 human pancreatic cancer cell lines were procured from ATCC, Manassas, VA. Panc-1 cells were kind gift from Dr. Thomas L. Brown (Wright State University, Dayton, OH).

    Techniques: Injection, Mouse Assay, TUNEL Assay

    Penfluridol induces apoptosis and suppresses survival of pancreatic cancer cells. ( A ) Panc-1, AsPC-1 and BxPC-3 cells were treated with different concentrations of penfluridol for 24, 48 and 72 h. Cell survival was measured by Sulforhodamine B assay to estimate IC 50 values. The experiments were repeated three times with 8 replicates in each experiment. ( B–D ) Approximately 0.3 × 10 6 Panc-1, AsPC-1 and BxPC-3 cells were plated in 6 well plates, treated with 2.5, 5.0 and 10 μM penfluridol for 24 h and processed for AnnexinV/FITC apoptosis assay using Accuri C6 flow cytometer. Values were plotted as means ± SD. Experiment was repeated three times. *Statistically significant at p ≤ 0.05 when compared with control. Panc-1, AsPC-1 and BxPC-3 cells were treated with varying concentrations of penfluridol for 24 h and processed for western blotting. Representative blots showing concentration-dependent effect of penfluridol treatment on Cl Caspase 3 and Cl PARP. Actin was used as loading control. Shown figure is the representative blots of at least three independent experiments.

    Journal: Scientific Reports

    Article Title: Penfluridol suppresses pancreatic tumor growth by autophagy-mediated apoptosis

    doi: 10.1038/srep26165

    Figure Lengend Snippet: Penfluridol induces apoptosis and suppresses survival of pancreatic cancer cells. ( A ) Panc-1, AsPC-1 and BxPC-3 cells were treated with different concentrations of penfluridol for 24, 48 and 72 h. Cell survival was measured by Sulforhodamine B assay to estimate IC 50 values. The experiments were repeated three times with 8 replicates in each experiment. ( B–D ) Approximately 0.3 × 10 6 Panc-1, AsPC-1 and BxPC-3 cells were plated in 6 well plates, treated with 2.5, 5.0 and 10 μM penfluridol for 24 h and processed for AnnexinV/FITC apoptosis assay using Accuri C6 flow cytometer. Values were plotted as means ± SD. Experiment was repeated three times. *Statistically significant at p ≤ 0.05 when compared with control. Panc-1, AsPC-1 and BxPC-3 cells were treated with varying concentrations of penfluridol for 24 h and processed for western blotting. Representative blots showing concentration-dependent effect of penfluridol treatment on Cl Caspase 3 and Cl PARP. Actin was used as loading control. Shown figure is the representative blots of at least three independent experiments.

    Article Snippet: Cell culture BxPC-3 and AsPC-1 human pancreatic cancer cell lines were procured from ATCC, Manassas, VA. Panc-1 cells were kind gift from Dr. Thomas L. Brown (Wright State University, Dayton, OH).

    Techniques: Sulforhodamine B Assay, Apoptosis Assay, Flow Cytometry, Cytometry, Western Blot, Concentration Assay

    Penfluridol treatment does not cause any major side effect in chronic toxicity model. About 1 × 10 6 BxPC-3 cells were implanted subcutaneously on right and left flanks of 4–6 week old female athymic nude mice. Once tumor size was around 70 mm 3 , 10 mg/kg penfluridol by oral route was administered every day to mice. After 59 days, mice were sacrificed; plasma was collected and sent to Texas Veterinary Medical Diagnostic Laboratory System, Amarillo, TX for analysis. ( A ) AST ( B ) ALT ( C ) Total serum ( D ) Albumin ( E ) Calcium ( F ) Phosphorus ( G ) Glucose ( H ) BUN ( I ) ALP ( J ) Total Bilirubin ( K ) A/G ratio ( L ) Chloride ( M ) Sodium ( N ) Potassium ( O ) Na/k ratio. Values were plotted as means ± SD.

    Journal: Scientific Reports

    Article Title: Penfluridol suppresses pancreatic tumor growth by autophagy-mediated apoptosis

    doi: 10.1038/srep26165

    Figure Lengend Snippet: Penfluridol treatment does not cause any major side effect in chronic toxicity model. About 1 × 10 6 BxPC-3 cells were implanted subcutaneously on right and left flanks of 4–6 week old female athymic nude mice. Once tumor size was around 70 mm 3 , 10 mg/kg penfluridol by oral route was administered every day to mice. After 59 days, mice were sacrificed; plasma was collected and sent to Texas Veterinary Medical Diagnostic Laboratory System, Amarillo, TX for analysis. ( A ) AST ( B ) ALT ( C ) Total serum ( D ) Albumin ( E ) Calcium ( F ) Phosphorus ( G ) Glucose ( H ) BUN ( I ) ALP ( J ) Total Bilirubin ( K ) A/G ratio ( L ) Chloride ( M ) Sodium ( N ) Potassium ( O ) Na/k ratio. Values were plotted as means ± SD.

    Article Snippet: Cell culture BxPC-3 and AsPC-1 human pancreatic cancer cell lines were procured from ATCC, Manassas, VA. Panc-1 cells were kind gift from Dr. Thomas L. Brown (Wright State University, Dayton, OH).

    Techniques: Mouse Assay, Diagnostic Assay, AST Assay, ALP Assay

    Assessment of p53-Y220C dependent effect of MB725 . Treatment of HUH-7 (p53-Y220C) and HUH-7 p53-Y220C KO cell lines with MB725 for 72 h underscores the enhanced cytotoxicity of MB725 in the presence of p53-Y220C (left panel). Additionally, p53-target genes were more potently upregulated in the p53-Y220C containing HUH-7 cell line than in the HUH-7 p53-Y220C KO cell line (right panel). These results demonstrate that the anticancer activity of MB725 depends at least partially on p53-Y220C. Cell viability was measured in quadruplicate and normalized against the values of blank (viability = 1) and no cell (viability = 0) controls (left panel). Data are shown as mean ± SEM (Unpaired t -test to test for significance in HUH7 and HUH7 p53 KO viability reduction; *p

    Journal: European Journal of Medicinal Chemistry

    Article Title: Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines

    doi: 10.1016/j.ejmech.2018.04.035

    Figure Lengend Snippet: Assessment of p53-Y220C dependent effect of MB725 . Treatment of HUH-7 (p53-Y220C) and HUH-7 p53-Y220C KO cell lines with MB725 for 72 h underscores the enhanced cytotoxicity of MB725 in the presence of p53-Y220C (left panel). Additionally, p53-target genes were more potently upregulated in the p53-Y220C containing HUH-7 cell line than in the HUH-7 p53-Y220C KO cell line (right panel). These results demonstrate that the anticancer activity of MB725 depends at least partially on p53-Y220C. Cell viability was measured in quadruplicate and normalized against the values of blank (viability = 1) and no cell (viability = 0) controls (left panel). Data are shown as mean ± SEM (Unpaired t -test to test for significance in HUH7 and HUH7 p53 KO viability reduction; *p

    Article Snippet: 4.7 Cell culture and cell viability assays WI-38 and BXPC-3 (p53-Y220C) cell lines were purchased from ATCC and HUH-7 (p53-Y220C+/+), HUH-6 (wild-type p53+/+).

    Techniques: Activity Assay

    Effects of Y220C binders on cancer cell viability. Relative cell viability (Y-axis) of representative cell lines after 72 h treatment with increasing concentrations (X-axis, μM) of 60 (A), MB710 (B), MB725 (C), and previously reported lead compounds PK083 (D), PK7088 (E) and PK5196 (F). The cell line employed in each experiment and their respective p53 status are shown. Aminobenzothiazole MB725 shows strong and selective viability reduction in the p53-Y220C cancer cell lines BXPC-3, HUH-7, and NUGC3 at concentrations below 40 μM, while maintaining relatively low toxicity in the same concentration range in the p53-R273C mutant cell line SW1088, and the p53 WT cell lines WI38 (normal fibroblast cell line) and NUGC4. Cell viability was measured in quadruplicate and normalized against the values of blank (viability = 1) and no cell (viability = 0) controls. Data are shown as mean ± SEM.

    Journal: European Journal of Medicinal Chemistry

    Article Title: Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines

    doi: 10.1016/j.ejmech.2018.04.035

    Figure Lengend Snippet: Effects of Y220C binders on cancer cell viability. Relative cell viability (Y-axis) of representative cell lines after 72 h treatment with increasing concentrations (X-axis, μM) of 60 (A), MB710 (B), MB725 (C), and previously reported lead compounds PK083 (D), PK7088 (E) and PK5196 (F). The cell line employed in each experiment and their respective p53 status are shown. Aminobenzothiazole MB725 shows strong and selective viability reduction in the p53-Y220C cancer cell lines BXPC-3, HUH-7, and NUGC3 at concentrations below 40 μM, while maintaining relatively low toxicity in the same concentration range in the p53-R273C mutant cell line SW1088, and the p53 WT cell lines WI38 (normal fibroblast cell line) and NUGC4. Cell viability was measured in quadruplicate and normalized against the values of blank (viability = 1) and no cell (viability = 0) controls. Data are shown as mean ± SEM.

    Article Snippet: 4.7 Cell culture and cell viability assays WI-38 and BXPC-3 (p53-Y220C) cell lines were purchased from ATCC and HUH-7 (p53-Y220C+/+), HUH-6 (wild-type p53+/+).

    Techniques: Concentration Assay, Mutagenesis

    Heatmap of mRNA fold changes in p53 signaling after treatment with 60 μM MB725 for 18 h in comparison to control. The qPCR array comprised 84 genes related to p53-mediated signal transduction, classified into subgroups for p53 activation and regulation, p53-mediated apoptosis, cell cycle arrest, DNA damage repair, and respective downstream responses [ 47 ]. Changes in mRNA levels were calculated using the ΔΔCt method. A value of 1 indicates no change in relative transcript levels between control and MB725 treated samples (values between 0.66 and 1.5 are shown in white). Increased mRNA levels are shown in green, starting from 1.5 (light green) to 4 (dark green), and decreased mRNA levels are shown in red, ranging from 0.66 (light red) to 0 (dark red). For each gene the average fold-change of two measurements (independent biological replicates) with standard deviation is shown. For GML , TP63 , TP53AIP1 , FASLG , MYOD1 , GML , WT1 , and XRCC5 only one or no ΔΔCt values could be obtained. Especially p53-target genes that are involved in apoptotic signaling (e.g., PUMA ( BBC3 ), FAS , TNF , FOXO3 , BTG2 ) and cell cycle modulation ( p21 ( CDKN1A ), MYC , MLH1 ) were selectively upregulated in NUGC3 (p53-Y220C) cells after MB725 treatment, suggesting Y220C-dependent induction of apoptosis and cell cycle arrest in this cell line.

    Journal: European Journal of Medicinal Chemistry

    Article Title: Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines

    doi: 10.1016/j.ejmech.2018.04.035

    Figure Lengend Snippet: Heatmap of mRNA fold changes in p53 signaling after treatment with 60 μM MB725 for 18 h in comparison to control. The qPCR array comprised 84 genes related to p53-mediated signal transduction, classified into subgroups for p53 activation and regulation, p53-mediated apoptosis, cell cycle arrest, DNA damage repair, and respective downstream responses [ 47 ]. Changes in mRNA levels were calculated using the ΔΔCt method. A value of 1 indicates no change in relative transcript levels between control and MB725 treated samples (values between 0.66 and 1.5 are shown in white). Increased mRNA levels are shown in green, starting from 1.5 (light green) to 4 (dark green), and decreased mRNA levels are shown in red, ranging from 0.66 (light red) to 0 (dark red). For each gene the average fold-change of two measurements (independent biological replicates) with standard deviation is shown. For GML , TP63 , TP53AIP1 , FASLG , MYOD1 , GML , WT1 , and XRCC5 only one or no ΔΔCt values could be obtained. Especially p53-target genes that are involved in apoptotic signaling (e.g., PUMA ( BBC3 ), FAS , TNF , FOXO3 , BTG2 ) and cell cycle modulation ( p21 ( CDKN1A ), MYC , MLH1 ) were selectively upregulated in NUGC3 (p53-Y220C) cells after MB725 treatment, suggesting Y220C-dependent induction of apoptosis and cell cycle arrest in this cell line.

    Article Snippet: 4.7 Cell culture and cell viability assays WI-38 and BXPC-3 (p53-Y220C) cell lines were purchased from ATCC and HUH-7 (p53-Y220C+/+), HUH-6 (wild-type p53+/+).

    Techniques: Real-time Polymerase Chain Reaction, Transduction, Activation Assay, Standard Deviation

    Structures of representative small molecules targeting the p53 cancer mutant Y220C.

    Journal: European Journal of Medicinal Chemistry

    Article Title: Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines

    doi: 10.1016/j.ejmech.2018.04.035

    Figure Lengend Snippet: Structures of representative small molecules targeting the p53 cancer mutant Y220C.

    Article Snippet: 4.7 Cell culture and cell viability assays WI-38 and BXPC-3 (p53-Y220C) cell lines were purchased from ATCC and HUH-7 (p53-Y220C+/+), HUH-6 (wild-type p53+/+).

    Techniques: Mutagenesis