apoptosis Search Results


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  • 99
    Thermo Fisher apoptosis
    Activation of caspases -9, -3 and cleavage of PARP induced by Resveratrol treatment in DLBCL cells. ( A ) SUDHL4 and HBL-1 cells were treated with and without 25 and 50 µM Resveratrol for 24 hours. Cells were lysed and equal amounts of proteins were immunoblotted with antibodies against caspase-9, caspase-3, cleaved caspase-3, PARP and Beta-actin. SUDHL4 and HBL-1 cells were pretreated with either 80 µM z-VAD ( B ) or 10mM NAC ( C ) for 2 hours and subsequently treated with 50 µM Resveratrol for 24 hours. Cells were lysed and equal amounts of proteins were immunoblotted with antibodies against caspase-9, caspase-3 cleaved caspase-3 and beta-actin. ( D ) SUDHL4 and HBL-1 cells were pretreated with either 80 µM of z-VAD-fmk or 10mM NAC for 2 hours and subsequently treated with 50 µM Resveratrol for 24 hours. Following treatment, cells were stained with fluorescein conjugated annexinV/PI and <t>apoptosis</t> was measured by flow cytometry.
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    Millipore apoptosis
    Withanolides induce cellular stress response in NB cells IMR 32 cells were preloaded with ROS indicator CM-H 2 DCFDA prior to withanolides exposure and alteration in oxidation potential was measured. ( A and B ) Fluorescent intensity measurement revelaed the induction of ROS after 4 h of treatment in a dose dependent manner and complete blocking of this effect by 5 mM NAC co-treatment. Immunoblot analysis of the stress response, heat shock proteins demonstrated increased expression levels of HSP32 and HSP70, and decreased expression of HSF1 after 24 h of treatment with increasing concentrations of withanolides. When the cells were pre-treated with NAC, cleavage of PARP that is an indicator of <t>apoptosis</t> was blocked and the increase in the expression levels of the heat shock proteins HSP32 and HSP70 as well as decrease in expression levels of mTOR pathway proteins and Iκ-Bα are blocked after NAC treatment, indicating attenuation of the anti-proliferative properties of withanolides by NAC ( C – E ).
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    93
    BioVision annexin v apoptosis detection kit
    ACF1 depletion increases <t>apoptosis</t> and sensitivity to aphidicolin (APH). ( A ) <t>Annexin</t> V staining of U2OS and HeLa cells 72 h after transfection with siRNA1 against SNF2H or ACF1 measured by FACS analysis. PI staining allowed discarding the necrotic population. The fraction of positive cells for each condition was determined and the values normalized to the corresponding controls, which were set to 1. ( B ) Examples for metaphase chromosomes without (left) or with the types of visible breaks counted to arrive at the numbers in (C) (right). ( C ) Quantification of the number of breaks in ACF1-depleted (ACF1) and control cells (CTRL) after 24 h incubation with 0.1 µM of APH. Two different siRNA pairs where used to deplete ACF1 (black: siRNA1, grey: siRNA2). From each sample 50 cells were counted. ( D ) Clonogenic survival of HeLa cells after ACF1 depletion and controls in response to 0.05, 0.1 or 0.5 µM of APH.
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    94
    Beckman Coulter apoptosis
    The cell cycle population was analyzed in IMC-3 and IMC-3CR cells using flow cytometry after cisplatin treatment (1 μg/ml, 24 h). ( a ) Original data of flow cytometry. Upper and lower panels respectively present results of IMC-3 and IMC-3CR cells. ( b ) <t>Apoptosis</t> (sub-G1) and ( c ) G2/M distributions are shown in bars. * P
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    92
    Becton Dickinson apoptosis
    Pretreatment with salubrinal on brain-death-induced <t>apoptosis</t> in liver as demonstrated by TUNEL. All values shown are mean ± standard deviation. * P
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    93
    Boehringer Mannheim apoptosis
    Immunofluorescent staining with CytoDEATH indicates that overexpression of PS2 and calmyrin increases HeLa cell <t>apoptosis.</t> (A) An example field of four cells shows that two of the three cells overexpressing PS2 are apoptotic according to CytoDEATH positive staining and condensed nuclei. (B) Similarly, an example field of eight cells shows that both cells which overexpress calmyrin also appear apoptotic. (C) 10× field of calmyrin and PS2 cotransfected cells after 16 h. Total cells in the field are indicated by DAPI staining, expressing cells are labeled with anti-PS2 antibody (staining for the presence of PS2 and calmyrin in cotransfected cells showed a near 1:1 correspondence between the overexpression of these two proteins), and apoptotic cells are detected with the CytoDEATH anti-cytokeratin 18 antibody. Note the presence of > 30 apoptotic cells which all also stain positive for PS2 expression. (D) 10× field of calmyrin and PS2 cotransfected cells after 40 h. Note the reduction in total cells and the lower percentage of PS2-expressing cells at this later time point. (E) 10× field of control neurofilament-transfected cells after 40 h. Please note that even at this later time point, a high percentage of anti-neurofilament positive cells remain, while in contrast only one CytoDEATH apoptotic cell can be detected.
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    92
    Cell Signaling Technology Inc apoptosis
    PKCβ-selective inhibition induces <t>apoptosis</t> and transiently inhibits cell cycle progression in BCBL-1 cells
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    92
    Merck & Co apoptosis
    Sept4_i1 induces <t>apoptosis</t> in LX-2 cells as detected by TUNEL staining. Cell nuclei were stained by Hoechst 33342. Apoptotic cells are identified by red spotted staining. Sept4_i1 induced apoptosis in LX-2 cells. Scale, 20 µm.
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    93
    SMAC Corp apoptosis
    Model of tumor killing following treatment with combination oncolytic virotherapy and targeted radionuclide therapy. Initial sites of virus infection often occur in distinct foci surrounding blood vessels (if delivered intravenously) or along the needle track (if delivered intratumorally). Preclinical data indicates that spreading of the virus from these initial sites may be limited. Incomplete transduction of large tumors remains a barrier to effective oncolytic virotherapy. ( a ) Combination oncolytic virotherapy and targeted radionuclide therapy overcomes the barrier of incomplete transduction due to the radiation cross-fire effect. Uninfected cells falling within the area of the path length (depicted by the dashed lines) will be exposed to radiation resulting in DNA damage and subsequent cell death. ( b ) Enlarged view of the mechanism of killing at each foci of infection. Infected cells express the virally encoded receptor (for example, vvDD-SSTR2) at the cell surface. The receptors are specifically bound by their cognate radiolabeled peptide analogue from which radiation is emitted. Radiation is emitted in all three-dimensions from the site of origin with a maximum tissue penetration distance defined by the path length (x). Virally induced oncolysis and radiation-induced <t>apoptosis</t> will result in significantly increased tumor cell death relative to either therapy alone.
    Apoptosis, supplied by SMAC Corp, used in various techniques. Bioz Stars score: 93/100, based on 179 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    4Gene apoptosis
    Model of tumor killing following treatment with combination oncolytic virotherapy and targeted radionuclide therapy. Initial sites of virus infection often occur in distinct foci surrounding blood vessels (if delivered intravenously) or along the needle track (if delivered intratumorally). Preclinical data indicates that spreading of the virus from these initial sites may be limited. Incomplete transduction of large tumors remains a barrier to effective oncolytic virotherapy. ( a ) Combination oncolytic virotherapy and targeted radionuclide therapy overcomes the barrier of incomplete transduction due to the radiation cross-fire effect. Uninfected cells falling within the area of the path length (depicted by the dashed lines) will be exposed to radiation resulting in DNA damage and subsequent cell death. ( b ) Enlarged view of the mechanism of killing at each foci of infection. Infected cells express the virally encoded receptor (for example, vvDD-SSTR2) at the cell surface. The receptors are specifically bound by their cognate radiolabeled peptide analogue from which radiation is emitted. Radiation is emitted in all three-dimensions from the site of origin with a maximum tissue penetration distance defined by the path length (x). Virally induced oncolysis and radiation-induced <t>apoptosis</t> will result in significantly increased tumor cell death relative to either therapy alone.
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    92
    Aven Tools apoptosis
    Model of tumor killing following treatment with combination oncolytic virotherapy and targeted radionuclide therapy. Initial sites of virus infection often occur in distinct foci surrounding blood vessels (if delivered intravenously) or along the needle track (if delivered intratumorally). Preclinical data indicates that spreading of the virus from these initial sites may be limited. Incomplete transduction of large tumors remains a barrier to effective oncolytic virotherapy. ( a ) Combination oncolytic virotherapy and targeted radionuclide therapy overcomes the barrier of incomplete transduction due to the radiation cross-fire effect. Uninfected cells falling within the area of the path length (depicted by the dashed lines) will be exposed to radiation resulting in DNA damage and subsequent cell death. ( b ) Enlarged view of the mechanism of killing at each foci of infection. Infected cells express the virally encoded receptor (for example, vvDD-SSTR2) at the cell surface. The receptors are specifically bound by their cognate radiolabeled peptide analogue from which radiation is emitted. Radiation is emitted in all three-dimensions from the site of origin with a maximum tissue penetration distance defined by the path length (x). Virally induced oncolysis and radiation-induced <t>apoptosis</t> will result in significantly increased tumor cell death relative to either therapy alone.
    Apoptosis, supplied by Aven Tools, used in various techniques. Bioz Stars score: 92/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cytoskeleton Inc apoptosis
    The proposed roles of the c-Jun, Fas, and p53 proteins in <t>apoptosis</t> induced by human amylin in pancreatic beta- cells.
    Apoptosis, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 92/100, based on 87 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Essen Bioscience apoptosis
    Treatment with NVP-BGJ398 does not induce NRH-LS1 cells to undergo <t>apoptosis</t> or senescence in a manner to account for the reduced cell number ( A ) The number of cells with active caspase 3/7 during 96 h of treatment with 100 nM of NVP-BGJ398. ( B ) The percentage of apoptotic cells after treatment with NVP-BGJ398; shown one representative experiment ( n = 3), error bars represent the standard error (SE) of the final measurement. ( C ) Increase in SA-β-galactosidase activity between cells treated with 100 nM of NVP-BGJ398 (red) and untreated (DMSO) cells (blue). Representative flow cytometry histograms of n = 3 biological replicates shown. ( D ) Representative image of SA-β-galactosidase staining after 72 h of treatment with 100 nM NVP-BGJ398. Senescent cells marked with arrows. Scale bars represent 50 μm. ( E ) The percentage of senescent cells after treatment with NVP-BGJ398 based on flow cytometry assay ( n = 3), error bars represent the standard deviation (SD) from three independent experiments.
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    91
    Full Moon BioSystems apoptosis
    Effect of LOC105374325 on the expression of Bax and Bak in podocytes. A, <t>apoptosis</t> antibody array analysis of glomerular tissues of FSGS patients ( n = 3); B, IHC analysis of Bax and Bak in glomerular tissues of FSGS patients ( n = 5); C, Western blot analysis of Bax and Bak in podocytes treated with ADR ( n = 3); D, Western blot analysis of Bax and Bak in podocytes transfected with LOC105374325 plasmid ( n = 3); E, flow cytometric analysis of apoptotic cells in podocytes transfected with Bax or Bak plasmid ( n = 5); F, flow cytometric analysis of apoptotic cells in podocytes treated with ADR, Bax siRNA, and Bak siRNA ( n = 5); G, flow cytometric analysis of apoptotic cells in podocytes transfected with LOC105374325 plasmid, Bax siRNA, and Bak siRNA ( n = 5). For statistical analysis, one-way ANOVA with Tukey's post hoc test was used for E–G . *, p
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    92
    Merck KGaA apoptosis
    Antitumor activity of trastuzumab does not depend on direct inhibition of HER2 signaling but rather on ADCC in HER2-positive SCLC cells. (a) HER2-positive SCLC cells (SBC-3, SBC-3/CDDP, SBC-3/ETP, and SBC-3/SN-38 cells) and HER2-overexpressing breast carcinoma cells (SK-BR-3 cells) were treated with 10 μg/ml of normal human IgG or trastuzumab (Tzmab) for 72 h. The relative numbers of viable cells were quantified using the CCK-8 assay. Points, mean% viable cells; bars, SD of at least three independent experiments performed in triplicate; *, P = 0.018; **, P = 0.004; ***, P = 0.002. (b) SBC-3/ETP and SK-BR-3 cells were treated with 10 μg/ml of trastuzumab for up to 72 h. Phosphorylation and expression of HER2, Akt, and Erk in whole cell lysates were examined by immunoblotting. PARP was also examined to detect <t>apoptosis.</t> Each lane of SBC-3/ETP and SK-BR-3 cell lysates contains 60 μg and 30 μg of total protein, respectively. Representative blots from three independent experiments with similar results are shown. Blots are cropped in the figure and full-length blots are presented in Supplementary information . (c) Induction of CD16 expression on NK cells. NK cells (YTS, NKL, and NK92MI cells) were treated with or without 10 μg/ml of trastuzumab for 4 h. Then, the cells were labeled with an anti-CD16 monoclonal Ab (black shaded) or isotype-matched control (solid line) and analyzed for cell surface expression of CD16 by FACS. (d), (e), and (f) Evaluation of trastuzumab-mediated ADCC. Target cancer cells and effector NK cells were coincubated at various E/T ratios with 10 μg/ml of normal human IgG or trastuzumab (Tzmab) for 4 h. Cytotoxic activity was determined based on the LDH release assay. Representative data from at least three experiments are shown as the means of triplicate cultures.
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    94
    R&D Systems apoptosis
    β-escin induces <t>apoptosis</t> in glioblastoma-initiating cells ( A ) Administration of 10 μM β-escin significantly reduced the number of viable mesenchymal GIC#1, and increased early stage apoptosis compared to DMSO treated controls. ( B ) PARP-1 cleavage was evident 24 hours following β-escin treatment. ( C – D ) Pre-treatment with the pan-caspase inhibitor QVD prior to β-escin administration rescued β-escin induced apoptosis. Data are representative of 3 independent experiments, each in triplicate *** p
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    94
    Roche apoptosis
    ZIKV replication and assessment of <t>apoptosis</t> in various organs in infected Stat1 -/- mice. (A) Liver, spleen, and brain tissues harvested from ZIKV-infected and uninfected Stat1 -/- mice were subjected to immunohistochemistry with an anti-NS1 antibody. (B) Cell death in infected tissues was determined using the TUNEL method. Tissues were collected 3 and 7 days post-infection with 4×10 4 pfu/mouse. TUNEL + signals were examined by fluorescence microscopy and images from 5–10 randomly selected 200X magnification fields were analyzed by ImageJ software (NIH).
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    94
    Trevigen apoptosis
    Loss of HES1 affects BC cell viability. ( A ) BC cells pictured after 72 hours of transient HES1 knock-down. ( B ) <t>Apoptosis</t> in MDA-MB-231 cells after 4 days of transient HES1 knock-down. Error bars - SEM, n = 3; **p
    Apoptosis, supplied by Trevigen, used in various techniques. Bioz Stars score: 94/100, based on 1281 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Beijing Solarbio Science apoptosis
    miR-210 inhibition blocks the protective effect of SWT. (A) Cell viability was determined using an MTS assay (n=4). (B) MDA levels were assessed using the thiobarbituric acid method (n=4). (C) Expression of <t>apoptosis-associated</t> proteins demonstrated by western blot analysis (n=3). *P
    Apoptosis, supplied by Beijing Solarbio Science, used in various techniques. Bioz Stars score: 93/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Beyotime apoptosis
    α -Hederin induces mitochondrial <t>apoptosis</t> in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin at indicated concentrations for 24 h. (a) Hoechst 33258 fluorescence staining. Morphologic changes of apoptotic cells were visualized under a fluorescence microscope (200 x magnification). (b) Flow cytometric analyses of MMP.
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    93
    Mimetics apoptosis
    XIAP plays an important role in mediating TNFα-dependent <t>apoptosis</t> induced by Smac mimetics. A , MDA-MB-231 cell line was transfected with XIAP siRNA for 48 h, followed by the treatment of SM-122 or SM-164 in combination with TNFα (10 ng/mL) for 48 h. Cell viability was determined by trypan blue dye exclusion. B , HCT 116 XIAP +/+ and XIAP −/− cell lines were treated with SM-122 or SM-164 alone or in combination with TNFα (0.1 ng/mL) as indicated. PARP cleavage and activation of caspase-3 were examined by Western blotting and cell growth inhibition by a WST assay. C , Jurkat cell lines were treated with SM-122, SM-164, TNFα (300 ng/mL) alone, or the combination of SM-122 or SM-164 with TNFα for 24 h. Apoptosis was analyzed by propidium iodide staining/Annexin V double staining using flow cytometry.
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    92
    Nexcelom Bioscience apoptosis
    Leptin-Notch signaling axis negatively affects 5-FU cytotoxicity in PC tumorspheres Leptin binding to its receptor (OB-R) expressed by pancreatic cancer tumorspheres induces Notch levels and the number of Notch+ cells that in turn increases proliferation, colony formation, survival, PCSC (CD24+/CD44+/ESA+, c-Met+), EMT (VM+, N-cadherin+), pluripotency (Oct4+, Sox-2+, Nanog+) and ATP-binding cassette proteins (ABCC5+, ABCC11+). Leptin-induced Notch signaling was related to the decrease of 5-FU induced <t>apoptosis</t> (Annexin V+ cells, Caspase 3 activity, Bax, degradation of PARP) and increased levels of anti-apoptotic proteins (Bcl-XL, RIP). Leptin's effects were abrogated by the IONP-LPrA2 leptin signaling inhibitor.
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    Pharmingen apoptosis
    GPI-anchoring has no impact on serum starvation-induced <t>apoptosis</t> in Jurkat cells. Jurkat-7.X and Jurkat-7.P cells were incubated in serum-free medium for 4 days. ▪, Base-line cell titres (day 0, arbitrarily set at 1·0), □, living cells after 4 days of starvation.
    Apoptosis, supplied by Pharmingen, used in various techniques. Bioz Stars score: 92/100, based on 1363 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Promega apoptosis
    PPARα induces <t>apoptosis</t> of HCC cells in vitro Hep3B and Huh-7 cells were transfected with pcDNA3.1 or PPARα for 48 hours; the effect of PPARα overexpression on apoptosis was determined by FACS and annexin V. Apoptotic cells were significantly increased in PPARα-transfected cells compared with pcDNA3.1-transfected cells, in both HepG2 (A1) and in Huh-7 cell lines (A2). Results are mean ± SD from experiments performed in triplicate. (B) Protein expression of cleaved caspase-3 and cleaved caspase-7 in Hep3B and Huh-7 cells as evaluated by western blot. GAPDH was used as loading control.
    Apoptosis, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 9243 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Warner-Lambert apoptosis
    PPARα induces <t>apoptosis</t> of HCC cells in vitro Hep3B and Huh-7 cells were transfected with pcDNA3.1 or PPARα for 48 hours; the effect of PPARα overexpression on apoptosis was determined by FACS and annexin V. Apoptotic cells were significantly increased in PPARα-transfected cells compared with pcDNA3.1-transfected cells, in both HepG2 (A1) and in Huh-7 cell lines (A2). Results are mean ± SD from experiments performed in triplicate. (B) Protein expression of cleaved caspase-3 and cleaved caspase-7 in Hep3B and Huh-7 cells as evaluated by western blot. GAPDH was used as loading control.
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    Activation of caspases -9, -3 and cleavage of PARP induced by Resveratrol treatment in DLBCL cells. ( A ) SUDHL4 and HBL-1 cells were treated with and without 25 and 50 µM Resveratrol for 24 hours. Cells were lysed and equal amounts of proteins were immunoblotted with antibodies against caspase-9, caspase-3, cleaved caspase-3, PARP and Beta-actin. SUDHL4 and HBL-1 cells were pretreated with either 80 µM z-VAD ( B ) or 10mM NAC ( C ) for 2 hours and subsequently treated with 50 µM Resveratrol for 24 hours. Cells were lysed and equal amounts of proteins were immunoblotted with antibodies against caspase-9, caspase-3 cleaved caspase-3 and beta-actin. ( D ) SUDHL4 and HBL-1 cells were pretreated with either 80 µM of z-VAD-fmk or 10mM NAC for 2 hours and subsequently treated with 50 µM Resveratrol for 24 hours. Following treatment, cells were stained with fluorescein conjugated annexinV/PI and apoptosis was measured by flow cytometry.

    Journal: PLoS ONE

    Article Title: Resveratrol Suppresses Constitutive Activation of AKT via Generation of ROS and Induces Apoptosis in Diffuse Large B Cell Lymphoma Cell Lines

    doi: 10.1371/journal.pone.0024703

    Figure Lengend Snippet: Activation of caspases -9, -3 and cleavage of PARP induced by Resveratrol treatment in DLBCL cells. ( A ) SUDHL4 and HBL-1 cells were treated with and without 25 and 50 µM Resveratrol for 24 hours. Cells were lysed and equal amounts of proteins were immunoblotted with antibodies against caspase-9, caspase-3, cleaved caspase-3, PARP and Beta-actin. SUDHL4 and HBL-1 cells were pretreated with either 80 µM z-VAD ( B ) or 10mM NAC ( C ) for 2 hours and subsequently treated with 50 µM Resveratrol for 24 hours. Cells were lysed and equal amounts of proteins were immunoblotted with antibodies against caspase-9, caspase-3 cleaved caspase-3 and beta-actin. ( D ) SUDHL4 and HBL-1 cells were pretreated with either 80 µM of z-VAD-fmk or 10mM NAC for 2 hours and subsequently treated with 50 µM Resveratrol for 24 hours. Following treatment, cells were stained with fluorescein conjugated annexinV/PI and apoptosis was measured by flow cytometry.

    Article Snippet: Live Dead Assay To measure apoptosis, Live-Dead assay (Invitrogen, Eugene, OR) was used as described by the manufacturer.

    Techniques: Activation Assay, Staining, Flow Cytometry, Cytometry

    Resveratrol treatment potentiates TRAIL mediated apoptosis in DLBCL cells. ( A ) SUDHL4 and HBL-1 cells were treated with either 10 µM Resveratrol in the presence and absence of 1 and 5ng TRAIL for 24 hours. Following treatment, cells were stained with fluorescent-conjugated Annexin V/PI and analyzed by flow cytometry. ( B ) SUDHL4 cells were treated with either 10 µM Resveratrol in the presence and absence of 1 and 5ng TRAIL for 24 hours. Following treatment, cells were lysed and equal amounts of proteins were immuno-blotted with antibodies against caspase-8, caspase-3, PARP, and beta- actin. ( C ) SUDHL4 and HBL-1 cells were transfected with either scrambled siRNA (100nM) or DR5 specific siRNA (100nM) for 48 hours and then cells were treated with 10 µM Resveratrol in the presence of either 1 or 5ng TRAIL for 24 hours following which cells were stained with fluorescent-conjugated Annexin V/PI and analyzed by flow cytometry, * denotes statistical significance (p

    Journal: PLoS ONE

    Article Title: Resveratrol Suppresses Constitutive Activation of AKT via Generation of ROS and Induces Apoptosis in Diffuse Large B Cell Lymphoma Cell Lines

    doi: 10.1371/journal.pone.0024703

    Figure Lengend Snippet: Resveratrol treatment potentiates TRAIL mediated apoptosis in DLBCL cells. ( A ) SUDHL4 and HBL-1 cells were treated with either 10 µM Resveratrol in the presence and absence of 1 and 5ng TRAIL for 24 hours. Following treatment, cells were stained with fluorescent-conjugated Annexin V/PI and analyzed by flow cytometry. ( B ) SUDHL4 cells were treated with either 10 µM Resveratrol in the presence and absence of 1 and 5ng TRAIL for 24 hours. Following treatment, cells were lysed and equal amounts of proteins were immuno-blotted with antibodies against caspase-8, caspase-3, PARP, and beta- actin. ( C ) SUDHL4 and HBL-1 cells were transfected with either scrambled siRNA (100nM) or DR5 specific siRNA (100nM) for 48 hours and then cells were treated with 10 µM Resveratrol in the presence of either 1 or 5ng TRAIL for 24 hours following which cells were stained with fluorescent-conjugated Annexin V/PI and analyzed by flow cytometry, * denotes statistical significance (p

    Article Snippet: Live Dead Assay To measure apoptosis, Live-Dead assay (Invitrogen, Eugene, OR) was used as described by the manufacturer.

    Techniques: Staining, Flow Cytometry, Cytometry, Transfection

    Resveratrol suppresses growth and induces apoptosis in DLBCL cells. ( A ) DLBCL cell lines were incubated with 0–100 µM Resveratrol for 24 hours. Cell viability was measured by MTT assays as described in Materials and Methods . The graph displays the mean +/− SD (standard deviation) of three independent experiments, * p

    Journal: PLoS ONE

    Article Title: Resveratrol Suppresses Constitutive Activation of AKT via Generation of ROS and Induces Apoptosis in Diffuse Large B Cell Lymphoma Cell Lines

    doi: 10.1371/journal.pone.0024703

    Figure Lengend Snippet: Resveratrol suppresses growth and induces apoptosis in DLBCL cells. ( A ) DLBCL cell lines were incubated with 0–100 µM Resveratrol for 24 hours. Cell viability was measured by MTT assays as described in Materials and Methods . The graph displays the mean +/− SD (standard deviation) of three independent experiments, * p

    Article Snippet: Live Dead Assay To measure apoptosis, Live-Dead assay (Invitrogen, Eugene, OR) was used as described by the manufacturer.

    Techniques: Incubation, MTT Assay, Standard Deviation

    Schematic representation of Resveratrol-induced apoptosis in DLBCL.

    Journal: PLoS ONE

    Article Title: Resveratrol Suppresses Constitutive Activation of AKT via Generation of ROS and Induces Apoptosis in Diffuse Large B Cell Lymphoma Cell Lines

    doi: 10.1371/journal.pone.0024703

    Figure Lengend Snippet: Schematic representation of Resveratrol-induced apoptosis in DLBCL.

    Article Snippet: Live Dead Assay To measure apoptosis, Live-Dead assay (Invitrogen, Eugene, OR) was used as described by the manufacturer.

    Techniques:

    Withanolides induce cellular stress response in NB cells IMR 32 cells were preloaded with ROS indicator CM-H 2 DCFDA prior to withanolides exposure and alteration in oxidation potential was measured. ( A and B ) Fluorescent intensity measurement revelaed the induction of ROS after 4 h of treatment in a dose dependent manner and complete blocking of this effect by 5 mM NAC co-treatment. Immunoblot analysis of the stress response, heat shock proteins demonstrated increased expression levels of HSP32 and HSP70, and decreased expression of HSF1 after 24 h of treatment with increasing concentrations of withanolides. When the cells were pre-treated with NAC, cleavage of PARP that is an indicator of apoptosis was blocked and the increase in the expression levels of the heat shock proteins HSP32 and HSP70 as well as decrease in expression levels of mTOR pathway proteins and Iκ-Bα are blocked after NAC treatment, indicating attenuation of the anti-proliferative properties of withanolides by NAC ( C – E ).

    Journal: Oncotarget

    Article Title: Novel natural withanolides induce apoptosis and inhibit migration of neuroblastoma cells through down regulation of N-myc and suppression of Akt/mTOR/NF-κB activation

    doi: 10.18632/oncotarget.24429

    Figure Lengend Snippet: Withanolides induce cellular stress response in NB cells IMR 32 cells were preloaded with ROS indicator CM-H 2 DCFDA prior to withanolides exposure and alteration in oxidation potential was measured. ( A and B ) Fluorescent intensity measurement revelaed the induction of ROS after 4 h of treatment in a dose dependent manner and complete blocking of this effect by 5 mM NAC co-treatment. Immunoblot analysis of the stress response, heat shock proteins demonstrated increased expression levels of HSP32 and HSP70, and decreased expression of HSF1 after 24 h of treatment with increasing concentrations of withanolides. When the cells were pre-treated with NAC, cleavage of PARP that is an indicator of apoptosis was blocked and the increase in the expression levels of the heat shock proteins HSP32 and HSP70 as well as decrease in expression levels of mTOR pathway proteins and Iκ-Bα are blocked after NAC treatment, indicating attenuation of the anti-proliferative properties of withanolides by NAC ( C – E ).

    Article Snippet: Reagents used in the flow cytometry analysis for cell cycle and apoptosis such as propidium idodide (PI), RNase were obtained from Sigma-Aldrich ((St. Louis, MO) and Annexin V-FITC was obtained from BD biosciences (San Diego, CA).

    Techniques: Blocking Assay, Expressing

    Induction of apoptosis after novel withanolides treatment in NB cells ( A and D ) IMR 32 and GOTO cells were stained with PI and annexin V-FITC and then analyzed by flow cytometry after treatment with increasing amounts of each withanolides. ( B and E ) Graphic representation of induction of apoptosis and necrosis after treatment of IMR 32 and GOTO cells with increasing concentrations of withanolides. Mean ± standard deviation results from three independent experiments are shown. ( C and F ) Western blot analysis of cleavage of PARP and caspases 3 and 7 after treatment of NB cells, IMR 32 and GOTO with novel withanolides for 24 h confirms induction of apoptosis. As a loading control actin was used.

    Journal: Oncotarget

    Article Title: Novel natural withanolides induce apoptosis and inhibit migration of neuroblastoma cells through down regulation of N-myc and suppression of Akt/mTOR/NF-κB activation

    doi: 10.18632/oncotarget.24429

    Figure Lengend Snippet: Induction of apoptosis after novel withanolides treatment in NB cells ( A and D ) IMR 32 and GOTO cells were stained with PI and annexin V-FITC and then analyzed by flow cytometry after treatment with increasing amounts of each withanolides. ( B and E ) Graphic representation of induction of apoptosis and necrosis after treatment of IMR 32 and GOTO cells with increasing concentrations of withanolides. Mean ± standard deviation results from three independent experiments are shown. ( C and F ) Western blot analysis of cleavage of PARP and caspases 3 and 7 after treatment of NB cells, IMR 32 and GOTO with novel withanolides for 24 h confirms induction of apoptosis. As a loading control actin was used.

    Article Snippet: Reagents used in the flow cytometry analysis for cell cycle and apoptosis such as propidium idodide (PI), RNase were obtained from Sigma-Aldrich ((St. Louis, MO) and Annexin V-FITC was obtained from BD biosciences (San Diego, CA).

    Techniques: Staining, Flow Cytometry, Cytometry, Standard Deviation, Western Blot

    ACF1 depletion increases apoptosis and sensitivity to aphidicolin (APH). ( A ) Annexin V staining of U2OS and HeLa cells 72 h after transfection with siRNA1 against SNF2H or ACF1 measured by FACS analysis. PI staining allowed discarding the necrotic population. The fraction of positive cells for each condition was determined and the values normalized to the corresponding controls, which were set to 1. ( B ) Examples for metaphase chromosomes without (left) or with the types of visible breaks counted to arrive at the numbers in (C) (right). ( C ) Quantification of the number of breaks in ACF1-depleted (ACF1) and control cells (CTRL) after 24 h incubation with 0.1 µM of APH. Two different siRNA pairs where used to deplete ACF1 (black: siRNA1, grey: siRNA2). From each sample 50 cells were counted. ( D ) Clonogenic survival of HeLa cells after ACF1 depletion and controls in response to 0.05, 0.1 or 0.5 µM of APH.

    Journal: Nucleic Acids Research

    Article Title: Role for hACF1 in the G2/M damage checkpoint

    doi: 10.1093/nar/gkr435

    Figure Lengend Snippet: ACF1 depletion increases apoptosis and sensitivity to aphidicolin (APH). ( A ) Annexin V staining of U2OS and HeLa cells 72 h after transfection with siRNA1 against SNF2H or ACF1 measured by FACS analysis. PI staining allowed discarding the necrotic population. The fraction of positive cells for each condition was determined and the values normalized to the corresponding controls, which were set to 1. ( B ) Examples for metaphase chromosomes without (left) or with the types of visible breaks counted to arrive at the numbers in (C) (right). ( C ) Quantification of the number of breaks in ACF1-depleted (ACF1) and control cells (CTRL) after 24 h incubation with 0.1 µM of APH. Two different siRNA pairs where used to deplete ACF1 (black: siRNA1, grey: siRNA2). From each sample 50 cells were counted. ( D ) Clonogenic survival of HeLa cells after ACF1 depletion and controls in response to 0.05, 0.1 or 0.5 µM of APH.

    Article Snippet: Flow cytometry Apoptotic cells were detected with an Annexin V Apoptosis Detection Kit (Biovision).

    Techniques: Staining, Transfection, FACS, Incubation

    The cell cycle population was analyzed in IMC-3 and IMC-3CR cells using flow cytometry after cisplatin treatment (1 μg/ml, 24 h). ( a ) Original data of flow cytometry. Upper and lower panels respectively present results of IMC-3 and IMC-3CR cells. ( b ) Apoptosis (sub-G1) and ( c ) G2/M distributions are shown in bars. * P

    Journal: Scientific Reports

    Article Title: Suppression of Poly(rC)-Binding Protein 4 (PCBP4) reduced cisplatin resistance in human maxillary cancer cells

    doi: 10.1038/srep12360

    Figure Lengend Snippet: The cell cycle population was analyzed in IMC-3 and IMC-3CR cells using flow cytometry after cisplatin treatment (1 μg/ml, 24 h). ( a ) Original data of flow cytometry. Upper and lower panels respectively present results of IMC-3 and IMC-3CR cells. ( b ) Apoptosis (sub-G1) and ( c ) G2/M distributions are shown in bars. * P

    Article Snippet: Furthermore, analysis of apoptotic cells was performed by the same systems, using an Annexin V-FITC Kit System for the Detection of Apoptosis (Beckman Coulter Inc., Brea, CA, USA) according to the manufacturer’s instructions.

    Techniques: Flow Cytometry, Cytometry

    Pretreatment with salubrinal on brain-death-induced apoptosis in liver as demonstrated by TUNEL. All values shown are mean ± standard deviation. * P

    Journal: Chinese Medical Journal

    Article Title: Protective Effects of Salubrinal on Liver Injury in Rat Models of Brain Death

    doi: 10.4103/0366-6999.157684

    Figure Lengend Snippet: Pretreatment with salubrinal on brain-death-induced apoptosis in liver as demonstrated by TUNEL. All values shown are mean ± standard deviation. * P

    Article Snippet: Previous studies have indicated that endoplasmic reticulum stress participates in and mediates liver injury and apoptosis in brain-dead (BD) rats.

    Techniques: TUNEL Assay, Standard Deviation

    Immunofluorescent staining with CytoDEATH indicates that overexpression of PS2 and calmyrin increases HeLa cell apoptosis. (A) An example field of four cells shows that two of the three cells overexpressing PS2 are apoptotic according to CytoDEATH positive staining and condensed nuclei. (B) Similarly, an example field of eight cells shows that both cells which overexpress calmyrin also appear apoptotic. (C) 10× field of calmyrin and PS2 cotransfected cells after 16 h. Total cells in the field are indicated by DAPI staining, expressing cells are labeled with anti-PS2 antibody (staining for the presence of PS2 and calmyrin in cotransfected cells showed a near 1:1 correspondence between the overexpression of these two proteins), and apoptotic cells are detected with the CytoDEATH anti-cytokeratin 18 antibody. Note the presence of > 30 apoptotic cells which all also stain positive for PS2 expression. (D) 10× field of calmyrin and PS2 cotransfected cells after 40 h. Note the reduction in total cells and the lower percentage of PS2-expressing cells at this later time point. (E) 10× field of control neurofilament-transfected cells after 40 h. Please note that even at this later time point, a high percentage of anti-neurofilament positive cells remain, while in contrast only one CytoDEATH apoptotic cell can be detected.

    Journal: The Journal of Cell Biology

    Article Title: A Myristoylated Calcium-binding Protein that Preferentially Interacts with the Alzheimer's Disease Presenilin 2 Protein

    doi:

    Figure Lengend Snippet: Immunofluorescent staining with CytoDEATH indicates that overexpression of PS2 and calmyrin increases HeLa cell apoptosis. (A) An example field of four cells shows that two of the three cells overexpressing PS2 are apoptotic according to CytoDEATH positive staining and condensed nuclei. (B) Similarly, an example field of eight cells shows that both cells which overexpress calmyrin also appear apoptotic. (C) 10× field of calmyrin and PS2 cotransfected cells after 16 h. Total cells in the field are indicated by DAPI staining, expressing cells are labeled with anti-PS2 antibody (staining for the presence of PS2 and calmyrin in cotransfected cells showed a near 1:1 correspondence between the overexpression of these two proteins), and apoptotic cells are detected with the CytoDEATH anti-cytokeratin 18 antibody. Note the presence of > 30 apoptotic cells which all also stain positive for PS2 expression. (D) 10× field of calmyrin and PS2 cotransfected cells after 40 h. Note the reduction in total cells and the lower percentage of PS2-expressing cells at this later time point. (E) 10× field of control neurofilament-transfected cells after 40 h. Please note that even at this later time point, a high percentage of anti-neurofilament positive cells remain, while in contrast only one CytoDEATH apoptotic cell can be detected.

    Article Snippet: This mouse monoclonal binds an epitope of cytokeratin 18 which is exposed only after caspase cleavage, an early event in apoptosis ( ; Boehringer Mannheim ).

    Techniques: Staining, Over Expression, Expressing, Labeling, Transfection

    PKCβ-selective inhibition induces apoptosis and transiently inhibits cell cycle progression in BCBL-1 cells

    Journal: Journal of investigative medicine : the official publication of the American Federation for Clinical Research

    Article Title: Protein kinase C-beta inhibition induces apoptosis and inhibits cell cycle progression in AIDS-related Non-Hodgkin lymphoma cells

    doi: 10.231/JIM.0b013e318237eb55

    Figure Lengend Snippet: PKCβ-selective inhibition induces apoptosis and transiently inhibits cell cycle progression in BCBL-1 cells

    Article Snippet: Apoptosis, Cell Signaling and Human Disease.

    Techniques: Inhibition

    PKCβ-selective inhibition at high concentration induces apoptosis but does not inhibit cell cycle progression in UMCL01-101 cells

    Journal: Journal of investigative medicine : the official publication of the American Federation for Clinical Research

    Article Title: Protein kinase C-beta inhibition induces apoptosis and inhibits cell cycle progression in AIDS-related Non-Hodgkin lymphoma cells

    doi: 10.231/JIM.0b013e318237eb55

    Figure Lengend Snippet: PKCβ-selective inhibition at high concentration induces apoptosis but does not inhibit cell cycle progression in UMCL01-101 cells

    Article Snippet: Apoptosis, Cell Signaling and Human Disease.

    Techniques: Inhibition, Concentration Assay

    PKCβ-selective inhibition induces apoptosis and inhibits cell cycle progression in 2F7 cells

    Journal: Journal of investigative medicine : the official publication of the American Federation for Clinical Research

    Article Title: Protein kinase C-beta inhibition induces apoptosis and inhibits cell cycle progression in AIDS-related Non-Hodgkin lymphoma cells

    doi: 10.231/JIM.0b013e318237eb55

    Figure Lengend Snippet: PKCβ-selective inhibition induces apoptosis and inhibits cell cycle progression in 2F7 cells

    Article Snippet: Apoptosis, Cell Signaling and Human Disease.

    Techniques: Inhibition

    Sept4_i1 induces apoptosis in LX-2 cells as detected by TUNEL staining. Cell nuclei were stained by Hoechst 33342. Apoptotic cells are identified by red spotted staining. Sept4_i1 induced apoptosis in LX-2 cells. Scale, 20 µm.

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: Septin4_i1 Regulates Apoptosis in Hepatic Stellate Cells through Peroxisome Proliferator-Activated Receptor-γ/Akt/B-Cell Lymphoma 2 Pathway

    doi: 10.1369/0022155414567230

    Figure Lengend Snippet: Sept4_i1 induces apoptosis in LX-2 cells as detected by TUNEL staining. Cell nuclei were stained by Hoechst 33342. Apoptotic cells are identified by red spotted staining. Sept4_i1 induced apoptosis in LX-2 cells. Scale, 20 µm.

    Article Snippet: Annexin V-FITC staining kit was also used to observe apoptosis and purchased from Merck/EMD Millipore (Billerica, MA).

    Techniques: TUNEL Assay, Staining

    Sept4_i1 induces apoptosis in LX-2 cells. (A) Western blotting shows upregulation in the expression levels PPAR-γ and cleaved-caspase-3 in cells transfected with pIRES2-EGFP-Sept4_i1. The expression of α-SMA was inhibited in transfected

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: Septin4_i1 Regulates Apoptosis in Hepatic Stellate Cells through Peroxisome Proliferator-Activated Receptor-γ/Akt/B-Cell Lymphoma 2 Pathway

    doi: 10.1369/0022155414567230

    Figure Lengend Snippet: Sept4_i1 induces apoptosis in LX-2 cells. (A) Western blotting shows upregulation in the expression levels PPAR-γ and cleaved-caspase-3 in cells transfected with pIRES2-EGFP-Sept4_i1. The expression of α-SMA was inhibited in transfected

    Article Snippet: Annexin V-FITC staining kit was also used to observe apoptosis and purchased from Merck/EMD Millipore (Billerica, MA).

    Techniques: Western Blot, Expressing, Transfection

    Sept4_i1-induced apoptosis in LX-2 cells is dependent on Akt/Bcl-2 expression. (A) Cells were transfected with pIRES2-EGFP-Sept4_i1 or pIRES2-EGFP vector. The expression levels of Akt, p53, DR5 and Bcl-2 were detected by western blotting. Over-expression

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: Septin4_i1 Regulates Apoptosis in Hepatic Stellate Cells through Peroxisome Proliferator-Activated Receptor-γ/Akt/B-Cell Lymphoma 2 Pathway

    doi: 10.1369/0022155414567230

    Figure Lengend Snippet: Sept4_i1-induced apoptosis in LX-2 cells is dependent on Akt/Bcl-2 expression. (A) Cells were transfected with pIRES2-EGFP-Sept4_i1 or pIRES2-EGFP vector. The expression levels of Akt, p53, DR5 and Bcl-2 were detected by western blotting. Over-expression

    Article Snippet: Annexin V-FITC staining kit was also used to observe apoptosis and purchased from Merck/EMD Millipore (Billerica, MA).

    Techniques: Expressing, Transfection, Plasmid Preparation, Western Blot, Over Expression

    Model of tumor killing following treatment with combination oncolytic virotherapy and targeted radionuclide therapy. Initial sites of virus infection often occur in distinct foci surrounding blood vessels (if delivered intravenously) or along the needle track (if delivered intratumorally). Preclinical data indicates that spreading of the virus from these initial sites may be limited. Incomplete transduction of large tumors remains a barrier to effective oncolytic virotherapy. ( a ) Combination oncolytic virotherapy and targeted radionuclide therapy overcomes the barrier of incomplete transduction due to the radiation cross-fire effect. Uninfected cells falling within the area of the path length (depicted by the dashed lines) will be exposed to radiation resulting in DNA damage and subsequent cell death. ( b ) Enlarged view of the mechanism of killing at each foci of infection. Infected cells express the virally encoded receptor (for example, vvDD-SSTR2) at the cell surface. The receptors are specifically bound by their cognate radiolabeled peptide analogue from which radiation is emitted. Radiation is emitted in all three-dimensions from the site of origin with a maximum tissue penetration distance defined by the path length (x). Virally induced oncolysis and radiation-induced apoptosis will result in significantly increased tumor cell death relative to either therapy alone.

    Journal: Molecular Therapy

    Article Title: Intelligent Design: Combination Therapy With Oncolytic Viruses

    doi: 10.1038/mt.2009.283

    Figure Lengend Snippet: Model of tumor killing following treatment with combination oncolytic virotherapy and targeted radionuclide therapy. Initial sites of virus infection often occur in distinct foci surrounding blood vessels (if delivered intravenously) or along the needle track (if delivered intratumorally). Preclinical data indicates that spreading of the virus from these initial sites may be limited. Incomplete transduction of large tumors remains a barrier to effective oncolytic virotherapy. ( a ) Combination oncolytic virotherapy and targeted radionuclide therapy overcomes the barrier of incomplete transduction due to the radiation cross-fire effect. Uninfected cells falling within the area of the path length (depicted by the dashed lines) will be exposed to radiation resulting in DNA damage and subsequent cell death. ( b ) Enlarged view of the mechanism of killing at each foci of infection. Infected cells express the virally encoded receptor (for example, vvDD-SSTR2) at the cell surface. The receptors are specifically bound by their cognate radiolabeled peptide analogue from which radiation is emitted. Radiation is emitted in all three-dimensions from the site of origin with a maximum tissue penetration distance defined by the path length (x). Virally induced oncolysis and radiation-induced apoptosis will result in significantly increased tumor cell death relative to either therapy alone.

    Article Snippet: Two other E1B 55kD-deleted adenoviruses, encoding activators of apoptosis (ZD55-TRAIL and ZD55-SMAC), also showed increased cytotoxicity in tumor cells when combined with cisplatin., The combination therapy showed dose-dependent cytotoxicity in normal cell lines; however it was not significantly greater than the drug-induced cytotoxicity.

    Techniques: Infection, Transduction

    The proposed roles of the c-Jun, Fas, and p53 proteins in apoptosis induced by human amylin in pancreatic beta- cells.

    Journal: BioMed Research International

    Article Title: Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

    doi: 10.1155/2013/826706

    Figure Lengend Snippet: The proposed roles of the c-Jun, Fas, and p53 proteins in apoptosis induced by human amylin in pancreatic beta- cells.

    Article Snippet: Apoptosis is defined as programmed cell death and is characterised by cell shrinkage, membrane blebbing (detachment of the cell membrane from the cytoskeleton), disruption of nuclear architecture, and DNA laddering (breaking of chromosomal DNA into fragments containing 180 base pairs) [ ].

    Techniques:

    Treatment with NVP-BGJ398 does not induce NRH-LS1 cells to undergo apoptosis or senescence in a manner to account for the reduced cell number ( A ) The number of cells with active caspase 3/7 during 96 h of treatment with 100 nM of NVP-BGJ398. ( B ) The percentage of apoptotic cells after treatment with NVP-BGJ398; shown one representative experiment ( n = 3), error bars represent the standard error (SE) of the final measurement. ( C ) Increase in SA-β-galactosidase activity between cells treated with 100 nM of NVP-BGJ398 (red) and untreated (DMSO) cells (blue). Representative flow cytometry histograms of n = 3 biological replicates shown. ( D ) Representative image of SA-β-galactosidase staining after 72 h of treatment with 100 nM NVP-BGJ398. Senescent cells marked with arrows. Scale bars represent 50 μm. ( E ) The percentage of senescent cells after treatment with NVP-BGJ398 based on flow cytometry assay ( n = 3), error bars represent the standard deviation (SD) from three independent experiments.

    Journal: Oncotarget

    Article Title: Preclinical evaluation of potential therapeutic targets in dedifferentiated liposarcoma

    doi: 10.18632/oncotarget.10518

    Figure Lengend Snippet: Treatment with NVP-BGJ398 does not induce NRH-LS1 cells to undergo apoptosis or senescence in a manner to account for the reduced cell number ( A ) The number of cells with active caspase 3/7 during 96 h of treatment with 100 nM of NVP-BGJ398. ( B ) The percentage of apoptotic cells after treatment with NVP-BGJ398; shown one representative experiment ( n = 3), error bars represent the standard error (SE) of the final measurement. ( C ) Increase in SA-β-galactosidase activity between cells treated with 100 nM of NVP-BGJ398 (red) and untreated (DMSO) cells (blue). Representative flow cytometry histograms of n = 3 biological replicates shown. ( D ) Representative image of SA-β-galactosidase staining after 72 h of treatment with 100 nM NVP-BGJ398. Senescent cells marked with arrows. Scale bars represent 50 μm. ( E ) The percentage of senescent cells after treatment with NVP-BGJ398 based on flow cytometry assay ( n = 3), error bars represent the standard deviation (SD) from three independent experiments.

    Article Snippet: Apoptosis The apoptosis assay was performed using a live-cell imaging system, IncuCyte ZOOM (Essen Bioscience, Birmingham, UK).

    Techniques: Activity Assay, Flow Cytometry, Cytometry, Staining, Standard Deviation

    Effect of LOC105374325 on the expression of Bax and Bak in podocytes. A, apoptosis antibody array analysis of glomerular tissues of FSGS patients ( n = 3); B, IHC analysis of Bax and Bak in glomerular tissues of FSGS patients ( n = 5); C, Western blot analysis of Bax and Bak in podocytes treated with ADR ( n = 3); D, Western blot analysis of Bax and Bak in podocytes transfected with LOC105374325 plasmid ( n = 3); E, flow cytometric analysis of apoptotic cells in podocytes transfected with Bax or Bak plasmid ( n = 5); F, flow cytometric analysis of apoptotic cells in podocytes treated with ADR, Bax siRNA, and Bak siRNA ( n = 5); G, flow cytometric analysis of apoptotic cells in podocytes transfected with LOC105374325 plasmid, Bax siRNA, and Bak siRNA ( n = 5). For statistical analysis, one-way ANOVA with Tukey's post hoc test was used for E–G . *, p

    Journal: The Journal of Biological Chemistry

    Article Title: The long noncoding RNA LOC105374325 causes podocyte injury in individuals with focal segmental glomerulosclerosis

    doi: 10.1074/jbc.RA118.005579

    Figure Lengend Snippet: Effect of LOC105374325 on the expression of Bax and Bak in podocytes. A, apoptosis antibody array analysis of glomerular tissues of FSGS patients ( n = 3); B, IHC analysis of Bax and Bak in glomerular tissues of FSGS patients ( n = 5); C, Western blot analysis of Bax and Bak in podocytes treated with ADR ( n = 3); D, Western blot analysis of Bax and Bak in podocytes transfected with LOC105374325 plasmid ( n = 3); E, flow cytometric analysis of apoptotic cells in podocytes transfected with Bax or Bak plasmid ( n = 5); F, flow cytometric analysis of apoptotic cells in podocytes treated with ADR, Bax siRNA, and Bak siRNA ( n = 5); G, flow cytometric analysis of apoptotic cells in podocytes transfected with LOC105374325 plasmid, Bax siRNA, and Bak siRNA ( n = 5). For statistical analysis, one-way ANOVA with Tukey's post hoc test was used for E–G . *, p

    Article Snippet: Apoptosis antibody array featured highly specific and well-characterized antibodies related to apoptosis (APP069, Full Moon BioSystems).

    Techniques: Expressing, Ab Array, Immunohistochemistry, Western Blot, Transfection, Plasmid Preparation, Flow Cytometry

    Antitumor activity of trastuzumab does not depend on direct inhibition of HER2 signaling but rather on ADCC in HER2-positive SCLC cells. (a) HER2-positive SCLC cells (SBC-3, SBC-3/CDDP, SBC-3/ETP, and SBC-3/SN-38 cells) and HER2-overexpressing breast carcinoma cells (SK-BR-3 cells) were treated with 10 μg/ml of normal human IgG or trastuzumab (Tzmab) for 72 h. The relative numbers of viable cells were quantified using the CCK-8 assay. Points, mean% viable cells; bars, SD of at least three independent experiments performed in triplicate; *, P = 0.018; **, P = 0.004; ***, P = 0.002. (b) SBC-3/ETP and SK-BR-3 cells were treated with 10 μg/ml of trastuzumab for up to 72 h. Phosphorylation and expression of HER2, Akt, and Erk in whole cell lysates were examined by immunoblotting. PARP was also examined to detect apoptosis. Each lane of SBC-3/ETP and SK-BR-3 cell lysates contains 60 μg and 30 μg of total protein, respectively. Representative blots from three independent experiments with similar results are shown. Blots are cropped in the figure and full-length blots are presented in Supplementary information . (c) Induction of CD16 expression on NK cells. NK cells (YTS, NKL, and NK92MI cells) were treated with or without 10 μg/ml of trastuzumab for 4 h. Then, the cells were labeled with an anti-CD16 monoclonal Ab (black shaded) or isotype-matched control (solid line) and analyzed for cell surface expression of CD16 by FACS. (d), (e), and (f) Evaluation of trastuzumab-mediated ADCC. Target cancer cells and effector NK cells were coincubated at various E/T ratios with 10 μg/ml of normal human IgG or trastuzumab (Tzmab) for 4 h. Cytotoxic activity was determined based on the LDH release assay. Representative data from at least three experiments are shown as the means of triplicate cultures.

    Journal: Scientific Reports

    Article Title: Overcoming chemoresistance of small-cell lung cancer through stepwise HER2-targeted antibody-dependent cell-mediated cytotoxicity and VEGF-targeted antiangiogenesis

    doi: 10.1038/srep02669

    Figure Lengend Snippet: Antitumor activity of trastuzumab does not depend on direct inhibition of HER2 signaling but rather on ADCC in HER2-positive SCLC cells. (a) HER2-positive SCLC cells (SBC-3, SBC-3/CDDP, SBC-3/ETP, and SBC-3/SN-38 cells) and HER2-overexpressing breast carcinoma cells (SK-BR-3 cells) were treated with 10 μg/ml of normal human IgG or trastuzumab (Tzmab) for 72 h. The relative numbers of viable cells were quantified using the CCK-8 assay. Points, mean% viable cells; bars, SD of at least three independent experiments performed in triplicate; *, P = 0.018; **, P = 0.004; ***, P = 0.002. (b) SBC-3/ETP and SK-BR-3 cells were treated with 10 μg/ml of trastuzumab for up to 72 h. Phosphorylation and expression of HER2, Akt, and Erk in whole cell lysates were examined by immunoblotting. PARP was also examined to detect apoptosis. Each lane of SBC-3/ETP and SK-BR-3 cell lysates contains 60 μg and 30 μg of total protein, respectively. Representative blots from three independent experiments with similar results are shown. Blots are cropped in the figure and full-length blots are presented in Supplementary information . (c) Induction of CD16 expression on NK cells. NK cells (YTS, NKL, and NK92MI cells) were treated with or without 10 μg/ml of trastuzumab for 4 h. Then, the cells were labeled with an anti-CD16 monoclonal Ab (black shaded) or isotype-matched control (solid line) and analyzed for cell surface expression of CD16 by FACS. (d), (e), and (f) Evaluation of trastuzumab-mediated ADCC. Target cancer cells and effector NK cells were coincubated at various E/T ratios with 10 μg/ml of normal human IgG or trastuzumab (Tzmab) for 4 h. Cytotoxic activity was determined based on the LDH release assay. Representative data from at least three experiments are shown as the means of triplicate cultures.

    Article Snippet: TUNEL staining TUNEL staining was performed to measure apoptosis in paraffin-embedded tumor sections using ApopTag Peroxidase In Situ Apoptosis Detection kit according to the manufacturer's instructions (Merck Millipore, Billerica, MA).

    Techniques: Activity Assay, Inhibition, CCK-8 Assay, Expressing, Labeling, FACS, Lactate Dehydrogenase Assay

    β-escin induces apoptosis in glioblastoma-initiating cells ( A ) Administration of 10 μM β-escin significantly reduced the number of viable mesenchymal GIC#1, and increased early stage apoptosis compared to DMSO treated controls. ( B ) PARP-1 cleavage was evident 24 hours following β-escin treatment. ( C – D ) Pre-treatment with the pan-caspase inhibitor QVD prior to β-escin administration rescued β-escin induced apoptosis. Data are representative of 3 independent experiments, each in triplicate *** p

    Journal: Oncotarget

    Article Title: β-escin selectively targets the glioblastoma-initiating cell population and reduces cell viability

    doi: 10.18632/oncotarget.11784

    Figure Lengend Snippet: β-escin induces apoptosis in glioblastoma-initiating cells ( A ) Administration of 10 μM β-escin significantly reduced the number of viable mesenchymal GIC#1, and increased early stage apoptosis compared to DMSO treated controls. ( B ) PARP-1 cleavage was evident 24 hours following β-escin treatment. ( C – D ) Pre-treatment with the pan-caspase inhibitor QVD prior to β-escin administration rescued β-escin induced apoptosis. Data are representative of 3 independent experiments, each in triplicate *** p

    Article Snippet: The pan caspase OPH inhibitor, QVD was used to inhibit apoptosis (R & D systems).

    Techniques:

    Preventing apoptosis does not halt β-escin action on glioblastoma-initiating cells ( A ) Pre-treatment of mesenchymal GIC#1 with the caspase inhibitor QVD does not alter β-escin induced decreases in TS formation. ( B ) TS size in response to QVD and β-escin treatment. ( C – D ) Addition of QVD in combination with β-escin did not rescue the β-escin induced reduction in TS formation or ALDH activity. Data are representative of 3 independent experiments, * p

    Journal: Oncotarget

    Article Title: β-escin selectively targets the glioblastoma-initiating cell population and reduces cell viability

    doi: 10.18632/oncotarget.11784

    Figure Lengend Snippet: Preventing apoptosis does not halt β-escin action on glioblastoma-initiating cells ( A ) Pre-treatment of mesenchymal GIC#1 with the caspase inhibitor QVD does not alter β-escin induced decreases in TS formation. ( B ) TS size in response to QVD and β-escin treatment. ( C – D ) Addition of QVD in combination with β-escin did not rescue the β-escin induced reduction in TS formation or ALDH activity. Data are representative of 3 independent experiments, * p

    Article Snippet: The pan caspase OPH inhibitor, QVD was used to inhibit apoptosis (R & D systems).

    Techniques: Activity Assay

    ZIKV replication and assessment of apoptosis in various organs in infected Stat1 -/- mice. (A) Liver, spleen, and brain tissues harvested from ZIKV-infected and uninfected Stat1 -/- mice were subjected to immunohistochemistry with an anti-NS1 antibody. (B) Cell death in infected tissues was determined using the TUNEL method. Tissues were collected 3 and 7 days post-infection with 4×10 4 pfu/mouse. TUNEL + signals were examined by fluorescence microscopy and images from 5–10 randomly selected 200X magnification fields were analyzed by ImageJ software (NIH).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Establishment of a mouse model for the complete mosquito-mediated transmission cycle of Zika virus

    doi: 10.1371/journal.pntd.0006417

    Figure Lengend Snippet: ZIKV replication and assessment of apoptosis in various organs in infected Stat1 -/- mice. (A) Liver, spleen, and brain tissues harvested from ZIKV-infected and uninfected Stat1 -/- mice were subjected to immunohistochemistry with an anti-NS1 antibody. (B) Cell death in infected tissues was determined using the TUNEL method. Tissues were collected 3 and 7 days post-infection with 4×10 4 pfu/mouse. TUNEL + signals were examined by fluorescence microscopy and images from 5–10 randomly selected 200X magnification fields were analyzed by ImageJ software (NIH).

    Article Snippet: Apoptosis in tissue sections was detected using the In Situ Cell Death detection kit (Roche, Indianapolis, IN).

    Techniques: Infection, Mouse Assay, Immunohistochemistry, TUNEL Assay, Fluorescence, Microscopy, Software

    Loss of HES1 affects BC cell viability. ( A ) BC cells pictured after 72 hours of transient HES1 knock-down. ( B ) Apoptosis in MDA-MB-231 cells after 4 days of transient HES1 knock-down. Error bars - SEM, n = 3; **p

    Journal: Scientific Reports

    Article Title: O-GlcNAc Transferase Inhibition Differentially Affects Breast Cancer Subtypes

    doi: 10.1038/s41598-019-42153-6

    Figure Lengend Snippet: Loss of HES1 affects BC cell viability. ( A ) BC cells pictured after 72 hours of transient HES1 knock-down. ( B ) Apoptosis in MDA-MB-231 cells after 4 days of transient HES1 knock-down. Error bars - SEM, n = 3; **p

    Article Snippet: Annexin V flow-cytometry based assay was also used to measure the proportion of cells undergoing apoptosis (Trevigen®, Gaithersburg, MD).

    Techniques: Multiple Displacement Amplification

    miR-210 inhibition blocks the protective effect of SWT. (A) Cell viability was determined using an MTS assay (n=4). (B) MDA levels were assessed using the thiobarbituric acid method (n=4). (C) Expression of apoptosis-associated proteins demonstrated by western blot analysis (n=3). *P

    Journal: Molecular Medicine Reports

    Article Title: Cardiac shock wave therapy protects cardiomyocytes from hypoxia-induced injury by modulating miR-210

    doi: 10.3892/mmr.2019.10892

    Figure Lengend Snippet: miR-210 inhibition blocks the protective effect of SWT. (A) Cell viability was determined using an MTS assay (n=4). (B) MDA levels were assessed using the thiobarbituric acid method (n=4). (C) Expression of apoptosis-associated proteins demonstrated by western blot analysis (n=3). *P

    Article Snippet: Fluorescent assays for apoptosis was from Beijing Solarbio Science & Technology Co., Ltd.

    Techniques: Inhibition, MTS Assay, Multiple Displacement Amplification, Expressing, Western Blot

    α -Hederin induces mitochondrial apoptosis in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin at indicated concentrations for 24 h. (a) Hoechst 33258 fluorescence staining. Morphologic changes of apoptotic cells were visualized under a fluorescence microscope (200 x magnification). (b) Flow cytometric analyses of MMP.

    Journal: BioMed Research International

    Article Title: α-Hederin Arrests Cell Cycle at G2/M Checkpoint and Promotes Mitochondrial Apoptosis by Blocking Nuclear Factor-κB Signaling in Colon Cancer Cells

    doi: 10.1155/2018/2548378

    Figure Lengend Snippet: α -Hederin induces mitochondrial apoptosis in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin at indicated concentrations for 24 h. (a) Hoechst 33258 fluorescence staining. Morphologic changes of apoptotic cells were visualized under a fluorescence microscope (200 x magnification). (b) Flow cytometric analyses of MMP.

    Article Snippet: SW620 cells were seeded in 6-well plates and then treated with vehicle, IL-6, and/or α -hederin, or PDTC at different concentrations for 24 h. Apoptosis was evaluated using a Hoechst 33258 staining kit provided by Beyotime Institute of Biotechnology (Haimen, China) according to the protocol.

    Techniques: Fluorescence, Staining, Microscopy, Flow Cytometry

    α -Hederin regulates mitochondrial apoptosis-related proteins in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin at indicated concentrations for 24 h. (a) Western blot analyses of protein expression of Bcl-2 and Bax with quantification. Significance: ∗∗P

    Journal: BioMed Research International

    Article Title: α-Hederin Arrests Cell Cycle at G2/M Checkpoint and Promotes Mitochondrial Apoptosis by Blocking Nuclear Factor-κB Signaling in Colon Cancer Cells

    doi: 10.1155/2018/2548378

    Figure Lengend Snippet: α -Hederin regulates mitochondrial apoptosis-related proteins in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin at indicated concentrations for 24 h. (a) Western blot analyses of protein expression of Bcl-2 and Bax with quantification. Significance: ∗∗P

    Article Snippet: SW620 cells were seeded in 6-well plates and then treated with vehicle, IL-6, and/or α -hederin, or PDTC at different concentrations for 24 h. Apoptosis was evaluated using a Hoechst 33258 staining kit provided by Beyotime Institute of Biotechnology (Haimen, China) according to the protocol.

    Techniques: Western Blot, Expressing

    Blockade of NF- κ B signaling is required for α -hederin induction of mitochondrial apoptosis in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin or PDTC at indicated concentrations for 24 h. (a) Hoechst 33258 fluorescence staining. Morphologic changes of apoptotic cells were visualized under a fluorescence microscope (200 x magnification). (b) Western blot analysis of protein abundance of cleaved-caspase-9, cleaved-caspase-3, and cleaved-PARP with quantification. Significance: ∗∗P

    Journal: BioMed Research International

    Article Title: α-Hederin Arrests Cell Cycle at G2/M Checkpoint and Promotes Mitochondrial Apoptosis by Blocking Nuclear Factor-κB Signaling in Colon Cancer Cells

    doi: 10.1155/2018/2548378

    Figure Lengend Snippet: Blockade of NF- κ B signaling is required for α -hederin induction of mitochondrial apoptosis in IL-6-stimulated SW620 cells. SW620 cells were treated with vehicle, IL-6, and/or α -hederin or PDTC at indicated concentrations for 24 h. (a) Hoechst 33258 fluorescence staining. Morphologic changes of apoptotic cells were visualized under a fluorescence microscope (200 x magnification). (b) Western blot analysis of protein abundance of cleaved-caspase-9, cleaved-caspase-3, and cleaved-PARP with quantification. Significance: ∗∗P

    Article Snippet: SW620 cells were seeded in 6-well plates and then treated with vehicle, IL-6, and/or α -hederin, or PDTC at different concentrations for 24 h. Apoptosis was evaluated using a Hoechst 33258 staining kit provided by Beyotime Institute of Biotechnology (Haimen, China) according to the protocol.

    Techniques: Fluorescence, Staining, Microscopy, Western Blot

    XIAP plays an important role in mediating TNFα-dependent apoptosis induced by Smac mimetics. A , MDA-MB-231 cell line was transfected with XIAP siRNA for 48 h, followed by the treatment of SM-122 or SM-164 in combination with TNFα (10 ng/mL) for 48 h. Cell viability was determined by trypan blue dye exclusion. B , HCT 116 XIAP +/+ and XIAP −/− cell lines were treated with SM-122 or SM-164 alone or in combination with TNFα (0.1 ng/mL) as indicated. PARP cleavage and activation of caspase-3 were examined by Western blotting and cell growth inhibition by a WST assay. C , Jurkat cell lines were treated with SM-122, SM-164, TNFα (300 ng/mL) alone, or the combination of SM-122 or SM-164 with TNFα for 24 h. Apoptosis was analyzed by propidium iodide staining/Annexin V double staining using flow cytometry.

    Journal: Cancer research

    Article Title: SM-164: A Novel, Bivalent Smac Mimetic That Induces Apoptosis and Tumor Regression by Concurrent Removal of the Blockade of cIAP-1/2 and XIAP

    doi: 10.1158/0008-5472.CAN-08-2655

    Figure Lengend Snippet: XIAP plays an important role in mediating TNFα-dependent apoptosis induced by Smac mimetics. A , MDA-MB-231 cell line was transfected with XIAP siRNA for 48 h, followed by the treatment of SM-122 or SM-164 in combination with TNFα (10 ng/mL) for 48 h. Cell viability was determined by trypan blue dye exclusion. B , HCT 116 XIAP +/+ and XIAP −/− cell lines were treated with SM-122 or SM-164 alone or in combination with TNFα (0.1 ng/mL) as indicated. PARP cleavage and activation of caspase-3 were examined by Western blotting and cell growth inhibition by a WST assay. C , Jurkat cell lines were treated with SM-122, SM-164, TNFα (300 ng/mL) alone, or the combination of SM-122 or SM-164 with TNFα for 24 h. Apoptosis was analyzed by propidium iodide staining/Annexin V double staining using flow cytometry.

    Article Snippet: Recent studies have shown that Smac mimetics induce apoptosis in tumor cells through a TNFα-dependent pathway ( , , , ).

    Techniques: Multiple Displacement Amplification, Transfection, Activation Assay, Western Blot, Inhibition, WST Assay, Staining, Double Staining, Flow Cytometry, Cytometry

    Monovalent and bivalent Smac mimetics induce apoptosis in the MDA-MB-231 cancer cell line in a caspase-3– and caspase-8–dependent manner. MDA-MB-231 cells were treated as indicated. Apoptosis was analyzed by propidium iodide ( PI )/Annexin V double staining using flow cytometry ( A ); cell viability was determined by trypan blue dye exclusion assay ( B ); and cleavage of caspases and PARP was analyzed by Western blotting ( C ). D , cells were transfected with siRNA against caspase-3, caspase-8, and caspase-9 for 48 h, followed by treatment with SM-164 ( middle ) or SM-122 ( right ) for 48 h. Knockdown efficacy was examined by Western blotting and cell growth inhibitory activity by a WST assay. E , cells were treated with Z-DEVD-FMK (25 μmol/L) or Z-IETD-FMK (25 μmol/L) for 1 h, followed by treatment with a Smac mimetic for 48 h. Cell growth inhibitory activity was examined by a WST assay. Points , mean of triplicates; bars , SD.

    Journal: Cancer research

    Article Title: SM-164: A Novel, Bivalent Smac Mimetic That Induces Apoptosis and Tumor Regression by Concurrent Removal of the Blockade of cIAP-1/2 and XIAP

    doi: 10.1158/0008-5472.CAN-08-2655

    Figure Lengend Snippet: Monovalent and bivalent Smac mimetics induce apoptosis in the MDA-MB-231 cancer cell line in a caspase-3– and caspase-8–dependent manner. MDA-MB-231 cells were treated as indicated. Apoptosis was analyzed by propidium iodide ( PI )/Annexin V double staining using flow cytometry ( A ); cell viability was determined by trypan blue dye exclusion assay ( B ); and cleavage of caspases and PARP was analyzed by Western blotting ( C ). D , cells were transfected with siRNA against caspase-3, caspase-8, and caspase-9 for 48 h, followed by treatment with SM-164 ( middle ) or SM-122 ( right ) for 48 h. Knockdown efficacy was examined by Western blotting and cell growth inhibitory activity by a WST assay. E , cells were treated with Z-DEVD-FMK (25 μmol/L) or Z-IETD-FMK (25 μmol/L) for 1 h, followed by treatment with a Smac mimetic for 48 h. Cell growth inhibitory activity was examined by a WST assay. Points , mean of triplicates; bars , SD.

    Article Snippet: Recent studies have shown that Smac mimetics induce apoptosis in tumor cells through a TNFα-dependent pathway ( , , , ).

    Techniques: Multiple Displacement Amplification, Double Staining, Flow Cytometry, Cytometry, Exclusion Assay, Western Blot, Transfection, Activity Assay, WST Assay

    Smac mimetics induce TNFα-dependent apoptosis and cIAP-1 degradation. A , MDA-MB-231 cells were pretreated with or without TNFα-or TRAIL- blocking antibody, followed by treatment with Smac mimetics. Cell viability was determined with trypan blue assay. B , HCT116 colon cancer cells were treated with SM-164 alone, TNFα alone, or the combination for 48 h. Cell growth inhibition was determined by a WST assay. C and D , MDA-MB-231 cells were treated with Smac mimetics as indicated and the levels of cIAP-1 and XIAP were examined by Western blotting. E , MDA-MB-231 or HCT116 cells treated with or without MG-132, followed by the treatment with 100 nmol/L of SM-122 or SM-164. The levels of cIAP-1 were examined by Western blotting.

    Journal: Cancer research

    Article Title: SM-164: A Novel, Bivalent Smac Mimetic That Induces Apoptosis and Tumor Regression by Concurrent Removal of the Blockade of cIAP-1/2 and XIAP

    doi: 10.1158/0008-5472.CAN-08-2655

    Figure Lengend Snippet: Smac mimetics induce TNFα-dependent apoptosis and cIAP-1 degradation. A , MDA-MB-231 cells were pretreated with or without TNFα-or TRAIL- blocking antibody, followed by treatment with Smac mimetics. Cell viability was determined with trypan blue assay. B , HCT116 colon cancer cells were treated with SM-164 alone, TNFα alone, or the combination for 48 h. Cell growth inhibition was determined by a WST assay. C and D , MDA-MB-231 cells were treated with Smac mimetics as indicated and the levels of cIAP-1 and XIAP were examined by Western blotting. E , MDA-MB-231 or HCT116 cells treated with or without MG-132, followed by the treatment with 100 nmol/L of SM-122 or SM-164. The levels of cIAP-1 were examined by Western blotting.

    Article Snippet: Recent studies have shown that Smac mimetics induce apoptosis in tumor cells through a TNFα-dependent pathway ( , , , ).

    Techniques: Multiple Displacement Amplification, Blocking Assay, Inhibition, WST Assay, Western Blot

    Removal of cIAP-1/2 alone is not sufficient to induce robust TNFα-dependent apoptosis. MDA-MB-231 ( A ) and SK-OV-3 ( B ) cell lines were treated with SM-122 alone, TNFα alone, or the combination for 24 h. The levels of cIAP-1 and cIAP-2 were examined by Western blotting and cell viability was determined by trypan blue assay. MDA-MB-231 ( C ) and SK-OV-3 ( D ) cell lines were transfected with siRNA against cIAP-1, cIAP-2, both cIAP-1 and cIAP-2, or control siRNA for 48 h, followed by treatment with TNFα for 24 h. The levels of cIAP-1 and cIAP-2 were examined by Western blotting and cell viability was determined by trypan blue assay.

    Journal: Cancer research

    Article Title: SM-164: A Novel, Bivalent Smac Mimetic That Induces Apoptosis and Tumor Regression by Concurrent Removal of the Blockade of cIAP-1/2 and XIAP

    doi: 10.1158/0008-5472.CAN-08-2655

    Figure Lengend Snippet: Removal of cIAP-1/2 alone is not sufficient to induce robust TNFα-dependent apoptosis. MDA-MB-231 ( A ) and SK-OV-3 ( B ) cell lines were treated with SM-122 alone, TNFα alone, or the combination for 24 h. The levels of cIAP-1 and cIAP-2 were examined by Western blotting and cell viability was determined by trypan blue assay. MDA-MB-231 ( C ) and SK-OV-3 ( D ) cell lines were transfected with siRNA against cIAP-1, cIAP-2, both cIAP-1 and cIAP-2, or control siRNA for 48 h, followed by treatment with TNFα for 24 h. The levels of cIAP-1 and cIAP-2 were examined by Western blotting and cell viability was determined by trypan blue assay.

    Article Snippet: Recent studies have shown that Smac mimetics induce apoptosis in tumor cells through a TNFα-dependent pathway ( , , , ).

    Techniques: Multiple Displacement Amplification, Western Blot, Transfection

    SM-164 induces rapid cIAP-1 degradation and robust apoptosis in tumor tissues and achieves tumor regression, but causes minimal toxicity to mouse tissues. A , SCID mice (two mice per group) bearing established MDA-MB-231 xenograft tumors were treated with a single i.v. dose of SM-164, Taxotere ( TXT ), or vehicle ( VEH ). Tumor tissues were harvested at the indicated time points. Degradation of cIAP-1 and XIAP, activation of caspases, and PARP cleavage in tumor tissues were analyzed by Western blotting. B , SCID mice (two mice per group) bearing established MDA-MB-231 xenograft tumors were treated with a single i.v. dose of SM-122 or vehicle. Tumor tissues were harvested at the indicated time points. cIAP-1 degradation and PARP cleavage in tumor tissues were analyzed by Western blotting. Tumor tissues harvested from mice treated with SM-164 were included as controls. C , apoptosis by TUNEL staining. To score apoptosis, at least 1,000 cells were counted under a microscope. D , SCID mice (two to three mice per group) bearing established MDA-MB-231 xenograft tumors were treated with a single dose of SM-164 (5 mg/kg, i.v.) or vehicle. Tumor and mouse tissues were harvested at the 24-h time point and examined by H E staining. Xenograft tumor tissues treated with SM-164 were shown with cell shrinkage, nuclear pyknosis, and chromatin condensation. E , SCID mice (8–10 per group) bearing established MDA-MB-231 xenograft tumors were treated i.v. with SM-164, Taxotere, or vehicle. Points , mean tumor volume; bars , SE.

    Journal: Cancer research

    Article Title: SM-164: A Novel, Bivalent Smac Mimetic That Induces Apoptosis and Tumor Regression by Concurrent Removal of the Blockade of cIAP-1/2 and XIAP

    doi: 10.1158/0008-5472.CAN-08-2655

    Figure Lengend Snippet: SM-164 induces rapid cIAP-1 degradation and robust apoptosis in tumor tissues and achieves tumor regression, but causes minimal toxicity to mouse tissues. A , SCID mice (two mice per group) bearing established MDA-MB-231 xenograft tumors were treated with a single i.v. dose of SM-164, Taxotere ( TXT ), or vehicle ( VEH ). Tumor tissues were harvested at the indicated time points. Degradation of cIAP-1 and XIAP, activation of caspases, and PARP cleavage in tumor tissues were analyzed by Western blotting. B , SCID mice (two mice per group) bearing established MDA-MB-231 xenograft tumors were treated with a single i.v. dose of SM-122 or vehicle. Tumor tissues were harvested at the indicated time points. cIAP-1 degradation and PARP cleavage in tumor tissues were analyzed by Western blotting. Tumor tissues harvested from mice treated with SM-164 were included as controls. C , apoptosis by TUNEL staining. To score apoptosis, at least 1,000 cells were counted under a microscope. D , SCID mice (two to three mice per group) bearing established MDA-MB-231 xenograft tumors were treated with a single dose of SM-164 (5 mg/kg, i.v.) or vehicle. Tumor and mouse tissues were harvested at the 24-h time point and examined by H E staining. Xenograft tumor tissues treated with SM-164 were shown with cell shrinkage, nuclear pyknosis, and chromatin condensation. E , SCID mice (8–10 per group) bearing established MDA-MB-231 xenograft tumors were treated i.v. with SM-164, Taxotere, or vehicle. Points , mean tumor volume; bars , SE.

    Article Snippet: Recent studies have shown that Smac mimetics induce apoptosis in tumor cells through a TNFα-dependent pathway ( , , , ).

    Techniques: Mouse Assay, Multiple Displacement Amplification, Activation Assay, Western Blot, TUNEL Assay, Staining, Microscopy

    Leptin-Notch signaling axis negatively affects 5-FU cytotoxicity in PC tumorspheres Leptin binding to its receptor (OB-R) expressed by pancreatic cancer tumorspheres induces Notch levels and the number of Notch+ cells that in turn increases proliferation, colony formation, survival, PCSC (CD24+/CD44+/ESA+, c-Met+), EMT (VM+, N-cadherin+), pluripotency (Oct4+, Sox-2+, Nanog+) and ATP-binding cassette proteins (ABCC5+, ABCC11+). Leptin-induced Notch signaling was related to the decrease of 5-FU induced apoptosis (Annexin V+ cells, Caspase 3 activity, Bax, degradation of PARP) and increased levels of anti-apoptotic proteins (Bcl-XL, RIP). Leptin's effects were abrogated by the IONP-LPrA2 leptin signaling inhibitor.

    Journal: Oncotarget

    Article Title: Leptin-Notch axis impairs 5-fluorouracil effects on pancreatic cancer

    doi: 10.18632/oncotarget.24435

    Figure Lengend Snippet: Leptin-Notch signaling axis negatively affects 5-FU cytotoxicity in PC tumorspheres Leptin binding to its receptor (OB-R) expressed by pancreatic cancer tumorspheres induces Notch levels and the number of Notch+ cells that in turn increases proliferation, colony formation, survival, PCSC (CD24+/CD44+/ESA+, c-Met+), EMT (VM+, N-cadherin+), pluripotency (Oct4+, Sox-2+, Nanog+) and ATP-binding cassette proteins (ABCC5+, ABCC11+). Leptin-induced Notch signaling was related to the decrease of 5-FU induced apoptosis (Annexin V+ cells, Caspase 3 activity, Bax, degradation of PARP) and increased levels of anti-apoptotic proteins (Bcl-XL, RIP). Leptin's effects were abrogated by the IONP-LPrA2 leptin signaling inhibitor.

    Article Snippet: Annexin V-FITC, Annexin-V binding buffer and ViaStain PI staining solution for apoptosis were from Nexcelom Bioscience (Lawrence, MA).

    Techniques: Binding Assay, Activity Assay

    Leptin impairs 5-FU induced Caspase-3 activity and apoptosis- related proteins in 5-FU treated- tumorspheres Caspase-3 activity in BxPC-3 (A) and MiaPaCa-2 (D) tumorspheres after treatment; Representative western blot results from PARP, RIP, Bax and Bcl-XL expression in BxPC-3 (B) and MiaPaCa-2 (E) derived tumorspheres; Quantitative determination of PARP, RIP, Bax and Bcl-XL in BxPC-3 (C) and MiaPaCa-2 (F) tumorspheres after treatment. PC tumorspheres were cultured in 6 wells low-attachment plates in Mammocult medium containing 5-FU (20 μg/ml), leptin (L; 1.2 nM), IONP-LPrA2 (I; 0.0036 pM) and DAPT (D, γ-secretase inhibitor; 20 μM) for 1-2 days. Untreated cells were used as control (Basal, B). Effects of treatment on cell number were expressed as % of control. Experiments were performed three times. a: p≤0.05 compared to control; b: p≤0.05 compared to 5-FU; c: p≤0.05 compared to D; d: p≤0.05 compared to 5-FU+L.

    Journal: Oncotarget

    Article Title: Leptin-Notch axis impairs 5-fluorouracil effects on pancreatic cancer

    doi: 10.18632/oncotarget.24435

    Figure Lengend Snippet: Leptin impairs 5-FU induced Caspase-3 activity and apoptosis- related proteins in 5-FU treated- tumorspheres Caspase-3 activity in BxPC-3 (A) and MiaPaCa-2 (D) tumorspheres after treatment; Representative western blot results from PARP, RIP, Bax and Bcl-XL expression in BxPC-3 (B) and MiaPaCa-2 (E) derived tumorspheres; Quantitative determination of PARP, RIP, Bax and Bcl-XL in BxPC-3 (C) and MiaPaCa-2 (F) tumorspheres after treatment. PC tumorspheres were cultured in 6 wells low-attachment plates in Mammocult medium containing 5-FU (20 μg/ml), leptin (L; 1.2 nM), IONP-LPrA2 (I; 0.0036 pM) and DAPT (D, γ-secretase inhibitor; 20 μM) for 1-2 days. Untreated cells were used as control (Basal, B). Effects of treatment on cell number were expressed as % of control. Experiments were performed three times. a: p≤0.05 compared to control; b: p≤0.05 compared to 5-FU; c: p≤0.05 compared to D; d: p≤0.05 compared to 5-FU+L.

    Article Snippet: Annexin V-FITC, Annexin-V binding buffer and ViaStain PI staining solution for apoptosis were from Nexcelom Bioscience (Lawrence, MA).

    Techniques: Activity Assay, Western Blot, Expressing, Derivative Assay, Cell Culture

    Leptin- induced survival of 5-FU treated- tumorspheres involves ABCC proteins Effects of 5-FU on survival of (A) BxPC-3 and (B) MiaPaCa-2 tumorspheres. Effects of 5-FU, leptin, DAPT and Probenecid on survival of (C) BxPC-3 and (D) MiaPaCa-2 cells forming tumorspheres. Cell numbers (live, apoptotic and necrotic) were determined after 1-2 days of treatment. PC tumorspheres were cultured (20,000 cells/well) in 6 wells low attachment plates in Mammocult medium containing 5-FU (20 μg/ml), leptin (L; 1.2 nM), IONP-LPrA2 (I; 0.0036 pM), DAPT (D, γ-secretase inhibitor; 20 μM) and Probenecid (P, ABCC inhibitor; 2 mmol/ml) for one week. Untreated cells were used as control (Basal, B). Apoptosis was determined via Annexin V assay. Effects of treatment on cell number were expressed as % of control for live, apoptotic and necrotic cells in basal conditions. Experiments were repeated three times. a: p≤0.05 compared to control; b: p≤0.05 compared to 5-FU; c: p≤0.05 compared to 5-FU+L; d: p≤0.05 compared to L.

    Journal: Oncotarget

    Article Title: Leptin-Notch axis impairs 5-fluorouracil effects on pancreatic cancer

    doi: 10.18632/oncotarget.24435

    Figure Lengend Snippet: Leptin- induced survival of 5-FU treated- tumorspheres involves ABCC proteins Effects of 5-FU on survival of (A) BxPC-3 and (B) MiaPaCa-2 tumorspheres. Effects of 5-FU, leptin, DAPT and Probenecid on survival of (C) BxPC-3 and (D) MiaPaCa-2 cells forming tumorspheres. Cell numbers (live, apoptotic and necrotic) were determined after 1-2 days of treatment. PC tumorspheres were cultured (20,000 cells/well) in 6 wells low attachment plates in Mammocult medium containing 5-FU (20 μg/ml), leptin (L; 1.2 nM), IONP-LPrA2 (I; 0.0036 pM), DAPT (D, γ-secretase inhibitor; 20 μM) and Probenecid (P, ABCC inhibitor; 2 mmol/ml) for one week. Untreated cells were used as control (Basal, B). Apoptosis was determined via Annexin V assay. Effects of treatment on cell number were expressed as % of control for live, apoptotic and necrotic cells in basal conditions. Experiments were repeated three times. a: p≤0.05 compared to control; b: p≤0.05 compared to 5-FU; c: p≤0.05 compared to 5-FU+L; d: p≤0.05 compared to L.

    Article Snippet: Annexin V-FITC, Annexin-V binding buffer and ViaStain PI staining solution for apoptosis were from Nexcelom Bioscience (Lawrence, MA).

    Techniques: Cell Culture, Annexin V Assay

    GPI-anchoring has no impact on serum starvation-induced apoptosis in Jurkat cells. Jurkat-7.X and Jurkat-7.P cells were incubated in serum-free medium for 4 days. ▪, Base-line cell titres (day 0, arbitrarily set at 1·0), □, living cells after 4 days of starvation.

    Journal: Clinical and Experimental Immunology

    Article Title: Glycosylphosphatidylinositol (GPI)-deficient Jurkat T cells as a model to study functions of GPI-anchored proteins

    doi: 10.1046/j.1365-2249.2000.01350.x

    Figure Lengend Snippet: GPI-anchoring has no impact on serum starvation-induced apoptosis in Jurkat cells. Jurkat-7.X and Jurkat-7.P cells were incubated in serum-free medium for 4 days. ▪, Base-line cell titres (day 0, arbitrarily set at 1·0), □, living cells after 4 days of starvation.

    Article Snippet: Jurkat-7 cells transfected with pL- PIG-A -SN or pLXSN (vector control) were subjected to apoptosis induction by the following methods: (i) serum removal for 1–4 days; (ii) addition of 200 ng/ml camptothecin (Sigma, Munich, Germany) for 2–6 h; (iii) incubation with CD95 MoAb for 1 h. To measure apoptosis, 106 washed cells were resuspended in 1 ml binding buffer (10 m m HEPES/NaOH pH 7·4, 140 m m NaCl, 2·5 m m CaCl2 ) and incubated in buffer alone or buffer with 5% (v/v) annexin V–PE (PharMingen), 5% 7-AAD or 5% annexin plus 5% 7-AAD for 15 min. After addition of 4 volumes of binding buffer, cells were analysed by fluorimetry.

    Techniques: Incubation

    GPI-anchoring has no impact on camptothecin-induced apoptosis in Jurkat cells. Jurkat-7.X and Jurkat-7.P cells were incubated with camptothecin for 2 h and subsequently stained with annexin V-PE (abscissa, apoptotic and dead cells) and 7-AAD (ordinate, dead cells). Cells positive for annexin, but negative for 7-AAD were regarded as apoptotic (right lower quadrant). In four separate experiments, these were not significantly different for Jurkat-7.X and Jurkat-7.P cells.

    Journal: Clinical and Experimental Immunology

    Article Title: Glycosylphosphatidylinositol (GPI)-deficient Jurkat T cells as a model to study functions of GPI-anchored proteins

    doi: 10.1046/j.1365-2249.2000.01350.x

    Figure Lengend Snippet: GPI-anchoring has no impact on camptothecin-induced apoptosis in Jurkat cells. Jurkat-7.X and Jurkat-7.P cells were incubated with camptothecin for 2 h and subsequently stained with annexin V-PE (abscissa, apoptotic and dead cells) and 7-AAD (ordinate, dead cells). Cells positive for annexin, but negative for 7-AAD were regarded as apoptotic (right lower quadrant). In four separate experiments, these were not significantly different for Jurkat-7.X and Jurkat-7.P cells.

    Article Snippet: Jurkat-7 cells transfected with pL- PIG-A -SN or pLXSN (vector control) were subjected to apoptosis induction by the following methods: (i) serum removal for 1–4 days; (ii) addition of 200 ng/ml camptothecin (Sigma, Munich, Germany) for 2–6 h; (iii) incubation with CD95 MoAb for 1 h. To measure apoptosis, 106 washed cells were resuspended in 1 ml binding buffer (10 m m HEPES/NaOH pH 7·4, 140 m m NaCl, 2·5 m m CaCl2 ) and incubated in buffer alone or buffer with 5% (v/v) annexin V–PE (PharMingen), 5% 7-AAD or 5% annexin plus 5% 7-AAD for 15 min. After addition of 4 volumes of binding buffer, cells were analysed by fluorimetry.

    Techniques: Incubation, Staining

    PPARα induces apoptosis of HCC cells in vitro Hep3B and Huh-7 cells were transfected with pcDNA3.1 or PPARα for 48 hours; the effect of PPARα overexpression on apoptosis was determined by FACS and annexin V. Apoptotic cells were significantly increased in PPARα-transfected cells compared with pcDNA3.1-transfected cells, in both HepG2 (A1) and in Huh-7 cell lines (A2). Results are mean ± SD from experiments performed in triplicate. (B) Protein expression of cleaved caspase-3 and cleaved caspase-7 in Hep3B and Huh-7 cells as evaluated by western blot. GAPDH was used as loading control.

    Journal: Oncotarget

    Article Title: Peroxisome proliferator activated receptor alpha inhibits hepatocarcinogenesis through mediating NF-κB signaling pathway

    doi:

    Figure Lengend Snippet: PPARα induces apoptosis of HCC cells in vitro Hep3B and Huh-7 cells were transfected with pcDNA3.1 or PPARα for 48 hours; the effect of PPARα overexpression on apoptosis was determined by FACS and annexin V. Apoptotic cells were significantly increased in PPARα-transfected cells compared with pcDNA3.1-transfected cells, in both HepG2 (A1) and in Huh-7 cell lines (A2). Results are mean ± SD from experiments performed in triplicate. (B) Protein expression of cleaved caspase-3 and cleaved caspase-7 in Hep3B and Huh-7 cells as evaluated by western blot. GAPDH was used as loading control.

    Article Snippet: Terminal deoxynucleotidyl transferase-mediated nick-end labeling (TUNEL) staining TUNEL staining was employed for detection of apoptosis in liver sections (Promega, Madison, WI).

    Techniques: In Vitro, Transfection, Over Expression, FACS, Expressing, Western Blot

    PPARα loss increases susceptibility to DEN-induced hepatocarcinogenesis (A1) Gross morphology of typical liver tumors from DEN-treated wild-type (WT) and PPARα knock out (PPARα -/- ) male mice at 6 months. (A2) Representative microscopic features of HCC in H E-stained liver sections of mice. T, tumor; N, adjacent non-tumor tissue. (A3) HCC incidence, and (A4) Number of HCCs per mouse in PPARα -/- and WT mice at 6 months were counted and expressed as mean ± SD, 7-10 mice/group. (B) Cell proliferation in HCCs of PPARα -/- and WT mice by Ki-67 immuno-staining (left panel). Quantitative assessment of cell proliferative index by Ki-67 positive cells (right panel). Data expressed as mean ± SD, 7-10 mice/group. (C) Apoptosis in HCCs of PPARα -/- and WT mice by TUNEL staining (left panel). Quantitative assessment of apoptosis determined by TUNEL positive cells (right panel). Data are means ± SD, 7-10 mice/group. (D) Protein expression of cyclin D1, p15, cleaved caspase-7, cleaved caspase-3 and PPARα in HCCs from PPARα -/- and WT mice determined by western blot. GAPDH was used as a loading control.

    Journal: Oncotarget

    Article Title: Peroxisome proliferator activated receptor alpha inhibits hepatocarcinogenesis through mediating NF-κB signaling pathway

    doi:

    Figure Lengend Snippet: PPARα loss increases susceptibility to DEN-induced hepatocarcinogenesis (A1) Gross morphology of typical liver tumors from DEN-treated wild-type (WT) and PPARα knock out (PPARα -/- ) male mice at 6 months. (A2) Representative microscopic features of HCC in H E-stained liver sections of mice. T, tumor; N, adjacent non-tumor tissue. (A3) HCC incidence, and (A4) Number of HCCs per mouse in PPARα -/- and WT mice at 6 months were counted and expressed as mean ± SD, 7-10 mice/group. (B) Cell proliferation in HCCs of PPARα -/- and WT mice by Ki-67 immuno-staining (left panel). Quantitative assessment of cell proliferative index by Ki-67 positive cells (right panel). Data expressed as mean ± SD, 7-10 mice/group. (C) Apoptosis in HCCs of PPARα -/- and WT mice by TUNEL staining (left panel). Quantitative assessment of apoptosis determined by TUNEL positive cells (right panel). Data are means ± SD, 7-10 mice/group. (D) Protein expression of cyclin D1, p15, cleaved caspase-7, cleaved caspase-3 and PPARα in HCCs from PPARα -/- and WT mice determined by western blot. GAPDH was used as a loading control.

    Article Snippet: Terminal deoxynucleotidyl transferase-mediated nick-end labeling (TUNEL) staining TUNEL staining was employed for detection of apoptosis in liver sections (Promega, Madison, WI).

    Techniques: Knock-Out, Mouse Assay, Staining, Immunostaining, TUNEL Assay, Expressing, Western Blot