caspase 3 Search Results


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    Synonyms CPP 32 Apopain Yama SCA 1 Capase3 Price 325 00 Host rabbit Immunogen Synthetic peptide corresponding to AA 170 to 175 from mouse Caspase3 UniProt Id P70677 Reactivity human
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    93
    Millipore caspase 3
    Protein expression levels of Bax, Bcl-2, <t>caspase-3,</t> GRP78, IREα, PERK were detected by western blot analysis. (A) Expression of apoptotic proteins. (B) Expression of ERS proteins. 1, X-ray; 2, C225/X-ray; 3, GNPs/X-ray; 4, C225-GNPs/X-ray. Drug concentrations of C225, C225-GNPs and GNPs were one fifth of each 50% inhibition concentration and the radiation dose was 2 Gy. GNPs, gold nanoparticles; C225, cetuximab; Bcl-2, B-cell lymphoma 2; Bax, Bcl-2-associated X protein; GRP78, glucose-regulated protein 78; IRE1α, inositol-requiring enzyme α; PERK, PRKR-like endoplasmic reticulum kinase.
    Caspase 3, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 2538 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc cleaved caspase 3
    REV-ERB agonist SR9011 inhibit autophagy a–b, SR90011 treatment reduces the number of autophagosomes both in MCF7 and T47D, n= biological independent samples MCF7 20µM 24h n=9 (mock), n=4 (SR9011) ** P =0.0056, T47D 48h 20µM n=5 (mock), n=4 (SR9011) ** P =0.0079; c–d, SR9011 induces accumulation of p62 as shown by immunofluorescence both in MCF7 and T47D n= biological independent samples 48h MCF7 p62 n=3 (mock), n=4 (SR9011) * P =0.0286; 48h T47D n=5 (mock, SR9011) ** P =0.004; e, Accumulation of p62 is confirmed by immunoblot (48h, 20µM A375); f–g, Inhibition of autophagy precedes apoptosis induction as shown by immunofluorescence of p62, cleaved <t>Caspase</t> 3 and TUNEL assay (n= biological independent samples n=4 mock 48h, n=5 SR9011 p62, n=3 48h SR9011; n=6 (mock, SR9011 72h p62), n=10 (mock 72h), n=8 (SR9011 72h) A375 20µM, Cl. Casp. 3 48h * P =0.0286; Cl. Casp. 3 72h **** P
    Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 38170 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc caspase 3
    Evaluation of V-9302  in vivo  in HCC1806 cell line xenograft-bearing mice ( A ) Tumor volumetric analysis of mice treated with vehicle or V-9302 (75 mg/kg per day) for 10 days.  n  = 5 mice per group. Treatment started 9 days post injection. P value at day 10 determined by Student’s  t  test. ( B ) Immunofluorescence analysis of tumor tissues harvested from vehicle- or V-9302-treated mice; LC3B and pAKT (Ser473) shown (pink). CD-31 positive vessels shown in green and nuclei in blue (DAPI). 20× magnification. P values determined by Student’s  t  test. ( C ) Effects of V-9302 treatment on pS6-positive cells and caspase 3-positive cells by immunohistochemistry. Quantitative analysis consisted of the mean counts of at least three representative fields from three vehicle and three V-9302-treated mice. For box plots, center line is plotted at the median; the box spans from the first quartile to the third quartile; whiskers represent min to max. Error bars represent ± std. dev.
    Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 27987 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc anti caspase 3
    MLKL encoding mRNA induces cell death in vitro and in vivo. a – f In vitro cell death characterization. B16-OVA cells were transfected with PBS or with Fluc-, tBid-, or MLKL-mRNA. a At different time points after transfection, cells were collected and analyzed by flow cytometry. Graph showing the percentages of sytox + cells (left). Representative flow cytometric plots 24 h after transfection (right). b Impact of the pan-caspase inhibitor zVAD-fmk on cell death induction (top) and caspase activity (bottom) upon transfection of B16-OVA cells with tBID- or MLKL-mRNA. c Western blot analysis of the expression of MLKL, <t>caspase-3,</t> and cleaved caspase-3 in cell lysates prepared 24 h after mRNA transfection. Tubulin served as a loading control. d B16 cells were co-transfected with luciferase NF-κB reporter plasmid and a plasmid expressing β-galactosidase. Twenty four hours later, the cells were transfected with PBS, GFP-, tBid-, or MLKL-mRNA or, as a positive control for NF-κB activation, with TRAF6 expression vector or they were stimulated with TNF. The normalized luciferase activity in the lysates determined at different time points after mRNA transfection is depicted. e B16 cells were transfected with a GFP expression plasmid. Twenty four hours later, the cells were transfected with PBS, Fluc-, tBid-, or MLKL-mRNA and the cells were treated or not with actinomycin D as indicated. Twenty four hours after mRNA transfection, cell death and GFP expression were quantified using flow cytometry. Horizontal lines indicate the mean. f Still images of B16-OVA cells at 0 and 24 h after transfection with tBid- or MLKL-mRNA visualized by time-lapse microscopy (scale bar = 10 µm). g In vivo cell death characterization. Subcutaneously growing B16-OVA tumors were injected with PBS or with 10 µg mRNA encoding Fluc, tBid, or MLKL followed by electroporation. Twenty four hours later, the tumor cells were isolated and analyzed by flow cytometry for sytox uptake. Graph showing the percentages of sytox + cells (left) and representative flow cytometry plots (right). Horizontal lines indicate the mean
    Anti Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 7327 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology caspase 3
    Western blot analysis of <t>caspase-3</t> from lysates of rat periodontal ligament fibroblasts exposed to different concentrations of CSE. Rat PDL fibroblasts cultured and grown to 70–80% confluence in an incubator at 37°C. The cells were exposed to different concentrations of CSE (5%, 10% and 15%) (v/v) in serum free media for 60 min keeping controls which were not exposed to CSE. (A) Lane 1: cell lysates not exposed to CSE. Lane 2: cell lysates exposed to 5% CSE. Lane 3: Cell lysates exposed to 10% CSE. Lane 4: Cell lysates exposed to 15% CSE. (B) Densitometric analysis of band intensity shows each bar represents the mean ± SEM of three experiments. A β-actin loading control is shown beneath the plot.
    Caspase 3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 7189 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam caspase 3
    p-ERK1/2 inhibitor downregulated light-induced p-ERK1/2 overexpression and <t>caspase</t> 3 activating. The level of p-ERK1/2 and caspase 3 expression was detected with Western blotting. (a) Light injury significantly increased the expression of p-ERK1/2 compared with normal group. The p-ERK1/2 inhibitor significantly reduced p-ERK1/2 overexpression compared with light injury group. (b) Light injury significantly induced caspase 3 activating compared with normal group. The p-ERK1/2 inhibitor significantly downregulated caspase 3 activating compared with light injury group. (c) No significant change in the total level of caspase 3 was seen in different groups ( F = 0.56, P = 0.75). * P
    Caspase 3, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 4895 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc anti cleaved caspase 3
    Tn affects DIAP1 and <t>Caspase-3</t> activity during DEOM histolysis at 12 h APF. a – c In vivo labeling of Caspase-3 (green) in mef2-Gal4/+ control or mef2 > tn RNAi DEOMs co-labeled with phalloidin (red). a Puncta corresponding to Caspase-3 are present in degenerating DEOM controls (white arrows in inset). b No Caspase-3(+) puncta are present in tn RNAi muscles. c Quantification of the relative fluorescence intensities of Caspase-3 in DEOMs reflects the general decrease observed upon a reduction in Tn. d – f Immunostaining for DIAP1 (green) and F-actin (red) is higher upon disruption of Tn function ( e , white arrows in inset) than in mef2-Gal4/+ control muscles ( d ). f Bar graph showing that the relative DIAP1 fluorescence levels are increased upon reduced Tn function. g – i Overall p35 (green) levels in DEOMs labeled with F-actin (red) are not changed upon a reduction in Tn. mef2 > p35 appears similar when co-expressed in a WT ( g ) or tn RNAi ( h ) background. Quantification of fluorescence intensity reveals no significant difference between WT or experimental DEOMs ( i ). Mean ± SEM (n.s., not significant, ** p
    Anti Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 11428 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti cleaved caspase 3
    AgNP-induced occurrence of systemic apoptosis. Immunofluorescent signals of the apoptotic biomarker “active caspase 3” in multiple tissues (brain, salivary gland, wing disc and gut) dissected from AgNP-exposed 3 rd -instar wandering larvae.
    Rabbit Anti Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 5764 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam cleaved caspase 3
    Everolimus attenuated and enhanced palbociclib sensitivity of MCF-7 cells. ( A ) MCF-7-P cells were treated with palbociclib with or without everolimus, and followed by cell viability assay. ( B ) Expression of the apoptosis executors, cleaved <t>caspase-3</t> and cleaved PARP, was detected in cells depicted in ( A ). ( C, D ) Expression of drug resistance genes ABCG2 and MDR1 was examined in cells depicted in ( A ). (E) MCF-7 cells were treated with palbociclib with or without everolimus and followed by detecting cell viability after 24, 48, and 72 hours. ( F ) Expression of the executors cleaved caspase-3 and cleaved PARP was detected in cells depicted in ( E ). Data were presented as mean ± standard deviation; ** P
    Cleaved Caspase 3, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 2633 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore caspase 3 activity
    Activity of <t>caspase-3</t> in human lymphocytes following PFOS treatment. The effect of PFOS on activity of caspase-3 in cultured human lymphocytes. Caspase-3 activity was assessed after treatment of human lymphocytes with IC 50 (150 µM) of PFOS for 6 and 12 h. PFOS (150 µM), significantly ( P
    Caspase 3 Activity, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1989 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson caspase 3
    The activation of <t>caspase-3</t> occurs in early activated cells before the emergence of fully differentiated effector cells. C57BL/6 mice were initially parked with 10 4 OT1 spleen cells. After infection with 10 4 LM-OVA, mice were sacrificed at various time points and spleens were harvested. Single cell suspensions were co-stained for CD8 + , OVA-Tetramer, CD62L, IL7Rα and active caspase-3. (A) Scatter plots show the relative staining of OVA-tetramer + CD8 + cells for activation markers and active caspase-3. Data is representative for at least 3 mice per time point. (B) OVA-tetramer + CD8 + T cells were examined for active intracellular active caspase-3 and surface CD62L between days 0–15 of LM-OVA infection. (data is representative for 3 mice per timepoint).
    Caspase 3, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 2249 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc active caspase 3
    The activation of <t>caspase-3</t> occurs in early activated cells before the emergence of fully differentiated effector cells. C57BL/6 mice were initially parked with 10 4 OT1 spleen cells. After infection with 10 4 LM-OVA, mice were sacrificed at various time points and spleens were harvested. Single cell suspensions were co-stained for CD8 + , OVA-Tetramer, CD62L, IL7Rα and active caspase-3. (A) Scatter plots show the relative staining of OVA-tetramer + CD8 + cells for activation markers and active caspase-3. Data is representative for at least 3 mice per time point. (B) OVA-tetramer + CD8 + T cells were examined for active intracellular active caspase-3 and surface CD62L between days 0–15 of LM-OVA infection. (data is representative for 3 mice per timepoint).
    Active Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1921 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology cleaved caspase 3
    Mediating role of PIM 1 in the antitumor effect of hispidulin in colorectal cancer ( CRC ) cells. A, Modulation of PIM 1 mRNA expression by hispidulin in CRC cells. B, Modulation of PIM 1 protein by hispidulin in CRC cells. C–G, Effect of PIM 1 overexpression or knockdown on hispidulin‐induced growth inhibition (C), apoptosis (D), activation of <t>caspase‐3</t> and poly( ADP ‐ribose) polymerase ( PARP ) (E), suppression of cell invasion (F), and repression of MMP ‐2 and MMP ‐9 expression (G). ** P
    Cleaved Caspase 3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1672 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti active caspase 3 antibody
    LncRNA PART1 regulated cell growth, apoptosis and ECM-related genes through targeting miR-93-5p. (A) Images of NP cell colonies. The colony formation rates are shown on the right. (B) The apoptosis of NP cells was measured by flow cytometry. The apoptosis rates of NP cells are shown on the right. (C and D) The expression levels of Ki67 and <t>C-caspase-3</t> in NP cells were measured by western blotting. (E-G) The expression levels of aggrecan, ADAMTS4, collagen II and MMP13 in NP cells were measured by (E and F) western blotting and (G) reverse transcription-quantitative PCR analysis. ** P
    Anti Active Caspase 3 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 692 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti caspase 3
    Knockout of DFNA5 reduces secondary necrosis in macrophages. ( a ) Immunoblots of S100 lysates from DFNA5 +/+ (WT) and DFNA5 −/− (DFNA5-KO) macrophages stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 (upper), <t>anti-caspase-3</t> (middle) or anti-β-actin (lower) antibodies. Asterisk indicate non-specific band (NS). ( b , c ) Cytotoxicity of VSV ( b ) ( n =3) and etoposide ( c ) ( n =3) as measured by LDH release in the culture supernatants of DFNA5 +/+ (WT) and DFNA5 −/− (DFNA5-KO) macrophages infected with VSV or treated with etoposide for 8 h. * P
    Anti Caspase 3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1918 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    R&D Systems caspase 3
    Changes in the small intestinal epithelium of acute and chronic TNF-mediated injury mouse models. a Schematic of experimental treatment and sampling timeline for acute and chronic TNF-mediated inflammatory injury. b Morphology of duodenal sections illustrating epithelial disruption 1–4 h following a high-dose pulse of TNF (acute model) with concomitant BrdU administration (brown staining), counterstained with Haematoxylin (blue/purple). Arrows indicate the hollow villus tips following stromal retraction induced by TNF and the constriction of the epithelium over the stroma preceding the shedding of the tip, which is re-epithelised at 4 h post-TNF. The epithelium in healthy and chronic inflammation models exhibits standard morphological appearance. Progression of BrdU-labelled cells on the CVEU over time was used to quantify cell dynamics in later analyses. c Images of TUNEL and <t>cleaved-Caspase-3</t> (CC3) labelled duodenum sections illustrating labelling similarity and differences in cell death intensity along the CVEU of healthy and inflammation mouse models. d Representative images and quantification of cells staining positive for goblet cell mucin (MUC2) in small intestine of control and acute inflammation mouse model at 1, 1.5, and 12 h post-TNF delivery. e Plot symbols show the decrease and recovery of the CVEU length (average number of cells ± standard deviation) in duodenum and ileum over time following the administration of one high-dose pulse of TNF (acute inflammation). Continuous blue and red bands show the average ± standard deviation of the CVEU length in control conditions and the chronic inflammation model, respectively
    Caspase 3, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 1282 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega apo one homogeneous caspase 3 7 assay
    Changes in the small intestinal epithelium of acute and chronic TNF-mediated injury mouse models. a Schematic of experimental treatment and sampling timeline for acute and chronic TNF-mediated inflammatory injury. b Morphology of duodenal sections illustrating epithelial disruption 1–4 h following a high-dose pulse of TNF (acute model) with concomitant BrdU administration (brown staining), counterstained with Haematoxylin (blue/purple). Arrows indicate the hollow villus tips following stromal retraction induced by TNF and the constriction of the epithelium over the stroma preceding the shedding of the tip, which is re-epithelised at 4 h post-TNF. The epithelium in healthy and chronic inflammation models exhibits standard morphological appearance. Progression of BrdU-labelled cells on the CVEU over time was used to quantify cell dynamics in later analyses. c Images of TUNEL and <t>cleaved-Caspase-3</t> (CC3) labelled duodenum sections illustrating labelling similarity and differences in cell death intensity along the CVEU of healthy and inflammation mouse models. d Representative images and quantification of cells staining positive for goblet cell mucin (MUC2) in small intestine of control and acute inflammation mouse model at 1, 1.5, and 12 h post-TNF delivery. e Plot symbols show the decrease and recovery of the CVEU length (average number of cells ± standard deviation) in duodenum and ileum over time following the administration of one high-dose pulse of TNF (acute inflammation). Continuous blue and red bands show the average ± standard deviation of the CVEU length in control conditions and the chronic inflammation model, respectively
    Apo One Homogeneous Caspase 3 7 Assay, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 1320 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    This peptide was used as an antigen for production of Cayman s Caspase 3 human Polyclonal Antibody Catalog No 160745 and can be used in conjunction with this antibody to
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    N/A
    Apoptosis is associated with many diseases and is induced by a family of cell death receptors and their ligands Cell death signals are transduced by death domain containing adapter molecules
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    Image Search Results


    Protein expression levels of Bax, Bcl-2, caspase-3, GRP78, IREα, PERK were detected by western blot analysis. (A) Expression of apoptotic proteins. (B) Expression of ERS proteins. 1, X-ray; 2, C225/X-ray; 3, GNPs/X-ray; 4, C225-GNPs/X-ray. Drug concentrations of C225, C225-GNPs and GNPs were one fifth of each 50% inhibition concentration and the radiation dose was 2 Gy. GNPs, gold nanoparticles; C225, cetuximab; Bcl-2, B-cell lymphoma 2; Bax, Bcl-2-associated X protein; GRP78, glucose-regulated protein 78; IRE1α, inositol-requiring enzyme α; PERK, PRKR-like endoplasmic reticulum kinase.

    Journal: Oncology Letters

    Article Title: Enhanced radiation effect on SMCC7721 cells through endoplasmic reticulum stress induced by C225-GNPs in vitro and in vivo

    doi: 10.3892/ol.2018.7864

    Figure Lengend Snippet: Protein expression levels of Bax, Bcl-2, caspase-3, GRP78, IREα, PERK were detected by western blot analysis. (A) Expression of apoptotic proteins. (B) Expression of ERS proteins. 1, X-ray; 2, C225/X-ray; 3, GNPs/X-ray; 4, C225-GNPs/X-ray. Drug concentrations of C225, C225-GNPs and GNPs were one fifth of each 50% inhibition concentration and the radiation dose was 2 Gy. GNPs, gold nanoparticles; C225, cetuximab; Bcl-2, B-cell lymphoma 2; Bax, Bcl-2-associated X protein; GRP78, glucose-regulated protein 78; IRE1α, inositol-requiring enzyme α; PERK, PRKR-like endoplasmic reticulum kinase.

    Article Snippet: The membrane was probed with specific antibodies against B-cell lymphoma 2 (Bcl-2; 1:500; cat no. SAB1306605), Bcl-2-associated X protein (Bax; 1:500; cat no. SAB2108447), caspase-3 (1:500; cat no. C5737), glucose-regulated protein 78 (GRP78; 1:800; cat no. G9043), inositol-requiring enzyme (IRE1α; 1:800; cat no. I6785) and PRKR-like endoplasmic reticulum kinase (PERK; 1:800; cat no. P7704), all from Sigma; Merck Millipore (Darmstadt, Germany) diluted with TBST [10 mM Tris-HCl (pH 7.4), 0.1 M NaCl and 0.1% Tween-20] containing 5% non-fat skim milk overnight at 4°C.

    Techniques: Expressing, Western Blot, Inhibition, Concentration Assay

    REV-ERB agonist SR9011 inhibit autophagy a–b, SR90011 treatment reduces the number of autophagosomes both in MCF7 and T47D, n= biological independent samples MCF7 20µM 24h n=9 (mock), n=4 (SR9011) ** P =0.0056, T47D 48h 20µM n=5 (mock), n=4 (SR9011) ** P =0.0079; c–d, SR9011 induces accumulation of p62 as shown by immunofluorescence both in MCF7 and T47D n= biological independent samples 48h MCF7 p62 n=3 (mock), n=4 (SR9011) * P =0.0286; 48h T47D n=5 (mock, SR9011) ** P =0.004; e, Accumulation of p62 is confirmed by immunoblot (48h, 20µM A375); f–g, Inhibition of autophagy precedes apoptosis induction as shown by immunofluorescence of p62, cleaved Caspase 3 and TUNEL assay (n= biological independent samples n=4 mock 48h, n=5 SR9011 p62, n=3 48h SR9011; n=6 (mock, SR9011 72h p62), n=10 (mock 72h), n=8 (SR9011 72h) A375 20µM, Cl. Casp. 3 48h * P =0.0286; Cl. Casp. 3 72h **** P

    Journal: Nature

    Article Title: Pharmacological activation of REV-ERBs is lethal in cancer and oncogene induced senescence

    doi: 10.1038/nature25170

    Figure Lengend Snippet: REV-ERB agonist SR9011 inhibit autophagy a–b, SR90011 treatment reduces the number of autophagosomes both in MCF7 and T47D, n= biological independent samples MCF7 20µM 24h n=9 (mock), n=4 (SR9011) ** P =0.0056, T47D 48h 20µM n=5 (mock), n=4 (SR9011) ** P =0.0079; c–d, SR9011 induces accumulation of p62 as shown by immunofluorescence both in MCF7 and T47D n= biological independent samples 48h MCF7 p62 n=3 (mock), n=4 (SR9011) * P =0.0286; 48h T47D n=5 (mock, SR9011) ** P =0.004; e, Accumulation of p62 is confirmed by immunoblot (48h, 20µM A375); f–g, Inhibition of autophagy precedes apoptosis induction as shown by immunofluorescence of p62, cleaved Caspase 3 and TUNEL assay (n= biological independent samples n=4 mock 48h, n=5 SR9011 p62, n=3 48h SR9011; n=6 (mock, SR9011 72h p62), n=10 (mock 72h), n=8 (SR9011 72h) A375 20µM, Cl. Casp. 3 48h * P =0.0286; Cl. Casp. 3 72h **** P

    Article Snippet: Apoptosis was evaluated by immunostaining of cleaved caspase 3 (Cell signaling #9664 1:200) and by TUNEL assay using In Situ Cell Death Detection Kit, Fluoresceine or TMR red (Roche).

    Techniques: Immunofluorescence, Inhibition, TUNEL Assay

    SR9009 and SR9011 treatment evokes an apoptotic response and induces inhibition of autophagy in OIS cells a, Proliferation assay shows that REV-ERBs agonists impair viability of OIS cells (6 days, 20µM). b–c, Immunofluorescence assay for cleaved Caspase 3 and TUNEL assay shows apoptosis induction specifically in OIS (n=biological independent samples, n=7 mock, n=9 SR9009, n=14 SR9011, 72h, 20µM; one-way ANOVA, Cl. Casp 3 **** P

    Journal: Nature

    Article Title: Pharmacological activation of REV-ERBs is lethal in cancer and oncogene induced senescence

    doi: 10.1038/nature25170

    Figure Lengend Snippet: SR9009 and SR9011 treatment evokes an apoptotic response and induces inhibition of autophagy in OIS cells a, Proliferation assay shows that REV-ERBs agonists impair viability of OIS cells (6 days, 20µM). b–c, Immunofluorescence assay for cleaved Caspase 3 and TUNEL assay shows apoptosis induction specifically in OIS (n=biological independent samples, n=7 mock, n=9 SR9009, n=14 SR9011, 72h, 20µM; one-way ANOVA, Cl. Casp 3 **** P

    Article Snippet: Apoptosis was evaluated by immunostaining of cleaved caspase 3 (Cell signaling #9664 1:200) and by TUNEL assay using In Situ Cell Death Detection Kit, Fluoresceine or TMR red (Roche).

    Techniques: Inhibition, Proliferation Assay, Immunofluorescence, TUNEL Assay

    REV-ERBs agonist SR9009 inhibits autophagy a–b , SR9009 treatment reduces the number of autophagosomes, as shown by immunofluorescence of LC3B, (n=biological independent samples MCF7 (n=6 mock), (n=5 SR9009) and T47D (n=5 mock) (n=4 SR9009) Mann–Whitney test one-tailed MCF7 20µM 24h * P =0.0152, T47D 20µM 48h ** P =0.0079; c–d SR9009 induces accumulation of p62 as shown by immunofluorescence; n= biological independent samples MCF7 (n=3 mock), (n=8 SR9009) and T47D (n=5 mock), (n=4 SR9009) Mann–Whitney test one-tailed 48h MCF7 p62 ** P =0.0061; 48h T47D ** P =0.0079; e, Inhibition of autophagy is confirmed by the immunoblot for p62 (20µM 48h, A375); f–g, Inhibition of autophagy precedes apoptosis induction as shown by immunofluorescence of p62, cleaved Caspase 3 and TUNEL assay; n=biological independent samples, Mann–Whitney test one-tailed, A375 20µM Cl. Casp. 3 48h (n=3) * P =0.0179; Cl. Casp. 3 72h (n=7) **** P

    Journal: Nature

    Article Title: Pharmacological activation of REV-ERBs is lethal in cancer and oncogene induced senescence

    doi: 10.1038/nature25170

    Figure Lengend Snippet: REV-ERBs agonist SR9009 inhibits autophagy a–b , SR9009 treatment reduces the number of autophagosomes, as shown by immunofluorescence of LC3B, (n=biological independent samples MCF7 (n=6 mock), (n=5 SR9009) and T47D (n=5 mock) (n=4 SR9009) Mann–Whitney test one-tailed MCF7 20µM 24h * P =0.0152, T47D 20µM 48h ** P =0.0079; c–d SR9009 induces accumulation of p62 as shown by immunofluorescence; n= biological independent samples MCF7 (n=3 mock), (n=8 SR9009) and T47D (n=5 mock), (n=4 SR9009) Mann–Whitney test one-tailed 48h MCF7 p62 ** P =0.0061; 48h T47D ** P =0.0079; e, Inhibition of autophagy is confirmed by the immunoblot for p62 (20µM 48h, A375); f–g, Inhibition of autophagy precedes apoptosis induction as shown by immunofluorescence of p62, cleaved Caspase 3 and TUNEL assay; n=biological independent samples, Mann–Whitney test one-tailed, A375 20µM Cl. Casp. 3 48h (n=3) * P =0.0179; Cl. Casp. 3 72h (n=7) **** P

    Article Snippet: Apoptosis was evaluated by immunostaining of cleaved caspase 3 (Cell signaling #9664 1:200) and by TUNEL assay using In Situ Cell Death Detection Kit, Fluoresceine or TMR red (Roche).

    Techniques: Immunofluorescence, MANN-WHITNEY, One-tailed Test, Inhibition, TUNEL Assay

    Evaluation of V-9302  in vivo  in HCC1806 cell line xenograft-bearing mice ( A ) Tumor volumetric analysis of mice treated with vehicle or V-9302 (75 mg/kg per day) for 10 days.  n  = 5 mice per group. Treatment started 9 days post injection. P value at day 10 determined by Student’s  t  test. ( B ) Immunofluorescence analysis of tumor tissues harvested from vehicle- or V-9302-treated mice; LC3B and pAKT (Ser473) shown (pink). CD-31 positive vessels shown in green and nuclei in blue (DAPI). 20× magnification. P values determined by Student’s  t  test. ( C ) Effects of V-9302 treatment on pS6-positive cells and caspase 3-positive cells by immunohistochemistry. Quantitative analysis consisted of the mean counts of at least three representative fields from three vehicle and three V-9302-treated mice. For box plots, center line is plotted at the median; the box spans from the first quartile to the third quartile; whiskers represent min to max. Error bars represent ± std. dev.

    Journal: Nature medicine

    Article Title: Pharmacological Blockade of ASCT2-dependent Glutamine Transport Leads To Anti-tumor Efficacy in Preclinical Models

    doi: 10.1038/nm.4464

    Figure Lengend Snippet: Evaluation of V-9302 in vivo in HCC1806 cell line xenograft-bearing mice ( A ) Tumor volumetric analysis of mice treated with vehicle or V-9302 (75 mg/kg per day) for 10 days. n = 5 mice per group. Treatment started 9 days post injection. P value at day 10 determined by Student’s t test. ( B ) Immunofluorescence analysis of tumor tissues harvested from vehicle- or V-9302-treated mice; LC3B and pAKT (Ser473) shown (pink). CD-31 positive vessels shown in green and nuclei in blue (DAPI). 20× magnification. P values determined by Student’s t test. ( C ) Effects of V-9302 treatment on pS6-positive cells and caspase 3-positive cells by immunohistochemistry. Quantitative analysis consisted of the mean counts of at least three representative fields from three vehicle and three V-9302-treated mice. For box plots, center line is plotted at the median; the box spans from the first quartile to the third quartile; whiskers represent min to max. Error bars represent ± std. dev.

    Article Snippet: Tissues were sectioned (5 µm thickness) and stained for pS6 (Cell Signaling, #4858) and caspase 3 (Cell Signaling #9661).

    Techniques: In Vivo, Mouse Assay, Injection, Immunofluorescence, Immunohistochemistry

    Evaluation of V-9302 in vivo ( A ) Pharmacodynamic [ 18 F]-4F-Gln PET imaging prior to and 4 h following a single administration of V-9302 (75 mg/kg) in HCC1806 cell line xenograft-bearing mice (arrows indicate xenograft tumor on right flank*). ( B ) Mean time activity curves (TACs) from tumor regions of interest ( n = 4 measurements per condition); data prior to and 4 hrs following V-9302 administration. ( C ) P values determined by Student’s t test. Quantified tracer accumulation in xenograft tumors, muscle, and liver ( n = 4 measurements per condition). Volumetric analysis over 21 day treatment regimen (Vehicle or V-9302; 75 mg/kg, daily) of HCT-116 ( D ) and HT29 ( F ) cell line xenografts propagated in athymic nude mice ( n = 10 mice per group). Treatment started 12 days post tumor injection for HCT-116 and 4 days post injection for HT29. P values on day 21 determined by Student’s t test. Immunohistochemistry for pS6 and caspase 3 in vehicle-treated or V-9302-treated HCT-116 ( E ) and HT29 ( G ) xenografts. Representative photomicrographs and quantitation shown; magnification 20×. P values determined by Student’s t test. ( H ) Volumetric analysis over 31 day treatment regimen (Vehicle or V-9302; 75 mg/kg, daily) on athymic nude mice bearing patient-derived xenograft tumors (PDX A 008, F3 generation, treatment started 28 days post implantation, KRAS G12V ;p53 R248Q ;PTEN L140Y ; n = 10 mice per group) P value on day 31 determined by Student’s t test. ( I ) Photographs of A 008 PDX-bearing mice treated with V-9302 or vehicle; day 16 of 31. (Error bars represent ± std. dev. *Central photopenia observed.

    Journal: Nature medicine

    Article Title: Pharmacological Blockade of ASCT2-dependent Glutamine Transport Leads To Anti-tumor Efficacy in Preclinical Models

    doi: 10.1038/nm.4464

    Figure Lengend Snippet: Evaluation of V-9302 in vivo ( A ) Pharmacodynamic [ 18 F]-4F-Gln PET imaging prior to and 4 h following a single administration of V-9302 (75 mg/kg) in HCC1806 cell line xenograft-bearing mice (arrows indicate xenograft tumor on right flank*). ( B ) Mean time activity curves (TACs) from tumor regions of interest ( n = 4 measurements per condition); data prior to and 4 hrs following V-9302 administration. ( C ) P values determined by Student’s t test. Quantified tracer accumulation in xenograft tumors, muscle, and liver ( n = 4 measurements per condition). Volumetric analysis over 21 day treatment regimen (Vehicle or V-9302; 75 mg/kg, daily) of HCT-116 ( D ) and HT29 ( F ) cell line xenografts propagated in athymic nude mice ( n = 10 mice per group). Treatment started 12 days post tumor injection for HCT-116 and 4 days post injection for HT29. P values on day 21 determined by Student’s t test. Immunohistochemistry for pS6 and caspase 3 in vehicle-treated or V-9302-treated HCT-116 ( E ) and HT29 ( G ) xenografts. Representative photomicrographs and quantitation shown; magnification 20×. P values determined by Student’s t test. ( H ) Volumetric analysis over 31 day treatment regimen (Vehicle or V-9302; 75 mg/kg, daily) on athymic nude mice bearing patient-derived xenograft tumors (PDX A 008, F3 generation, treatment started 28 days post implantation, KRAS G12V ;p53 R248Q ;PTEN L140Y ; n = 10 mice per group) P value on day 31 determined by Student’s t test. ( I ) Photographs of A 008 PDX-bearing mice treated with V-9302 or vehicle; day 16 of 31. (Error bars represent ± std. dev. *Central photopenia observed.

    Article Snippet: Tissues were sectioned (5 µm thickness) and stained for pS6 (Cell Signaling, #4858) and caspase 3 (Cell Signaling #9661).

    Techniques: In Vivo, Positron Emission Tomography, Imaging, Mouse Assay, Activity Assay, Injection, Immunohistochemistry, Quantitation Assay, Derivative Assay

    Haematopoietic and gastrointestinal failure in AIMP3 mKO mouse. ( A ) Hypotrophy of haematopoietic and intestinal organs in AIMP3 mKO. At day 30, the thymus, spleen, bone marrow and intestine from AIMP3 CON (left column) and AIMP3 mKO (right column) were isolated, and tissue sections were stained with haematoxylin-eosin (HE). The inset shows a low-resolution image of the HE-stained tissue. Dotted lines mark the boundary between the cortex (C) and medulla (M) in the thymic lobe and between the white pulp (WP) and red pulp (RP) in the spleen, respectively. Arrows and arrowheads in the intestine indicate elongated crypts and blunted villi, respectively, in AIMP3 mKO mice. ( B ) Bone marrow isolated from AIMP3 CON and AIMP3 mKO mice were immunostained with antibodies against cleaved caspase-3. ( C ) Splenocytes from AIMP3 CON (left) and AIMP3 mKO (right) mice were analysed by FACS cytometry using the markers CD3ε (pan-T cells) and CD45R (pan-B cells). The number indicates the percentage of the cells in the quadrant. Representative results from three animals are shown. ( D ) CD3ε–(left), CD45R- (middle) and CD11b- (right) positive cells were analysed by FACS in spleen and bone marrow from AIMP3 CON and AIMP3 mKO mice. Three to five animals per group were used. Error bars indicate standard error. Asterisks denote significant difference between groups by Student’s t-test (*p

    Journal: Scientific Reports

    Article Title: AIMP3 Deletion Induces Acute Radiation Syndrome-like Phenotype in Mice

    doi: 10.1038/s41598-018-33303-3

    Figure Lengend Snippet: Haematopoietic and gastrointestinal failure in AIMP3 mKO mouse. ( A ) Hypotrophy of haematopoietic and intestinal organs in AIMP3 mKO. At day 30, the thymus, spleen, bone marrow and intestine from AIMP3 CON (left column) and AIMP3 mKO (right column) were isolated, and tissue sections were stained with haematoxylin-eosin (HE). The inset shows a low-resolution image of the HE-stained tissue. Dotted lines mark the boundary between the cortex (C) and medulla (M) in the thymic lobe and between the white pulp (WP) and red pulp (RP) in the spleen, respectively. Arrows and arrowheads in the intestine indicate elongated crypts and blunted villi, respectively, in AIMP3 mKO mice. ( B ) Bone marrow isolated from AIMP3 CON and AIMP3 mKO mice were immunostained with antibodies against cleaved caspase-3. ( C ) Splenocytes from AIMP3 CON (left) and AIMP3 mKO (right) mice were analysed by FACS cytometry using the markers CD3ε (pan-T cells) and CD45R (pan-B cells). The number indicates the percentage of the cells in the quadrant. Representative results from three animals are shown. ( D ) CD3ε–(left), CD45R- (middle) and CD11b- (right) positive cells were analysed by FACS in spleen and bone marrow from AIMP3 CON and AIMP3 mKO mice. Three to five animals per group were used. Error bars indicate standard error. Asterisks denote significant difference between groups by Student’s t-test (*p

    Article Snippet: Cleaved caspase-3 antibody (Cell signalling #9661, 1:200) and Dako system for rabbit was used for colorimetric development.

    Techniques: Isolation, Staining, Mouse Assay, FACS, Cytometry

    MLKL encoding mRNA induces cell death in vitro and in vivo. a – f In vitro cell death characterization. B16-OVA cells were transfected with PBS or with Fluc-, tBid-, or MLKL-mRNA. a At different time points after transfection, cells were collected and analyzed by flow cytometry. Graph showing the percentages of sytox + cells (left). Representative flow cytometric plots 24 h after transfection (right). b Impact of the pan-caspase inhibitor zVAD-fmk on cell death induction (top) and caspase activity (bottom) upon transfection of B16-OVA cells with tBID- or MLKL-mRNA. c Western blot analysis of the expression of MLKL, caspase-3, and cleaved caspase-3 in cell lysates prepared 24 h after mRNA transfection. Tubulin served as a loading control. d B16 cells were co-transfected with luciferase NF-κB reporter plasmid and a plasmid expressing β-galactosidase. Twenty four hours later, the cells were transfected with PBS, GFP-, tBid-, or MLKL-mRNA or, as a positive control for NF-κB activation, with TRAF6 expression vector or they were stimulated with TNF. The normalized luciferase activity in the lysates determined at different time points after mRNA transfection is depicted. e B16 cells were transfected with a GFP expression plasmid. Twenty four hours later, the cells were transfected with PBS, Fluc-, tBid-, or MLKL-mRNA and the cells were treated or not with actinomycin D as indicated. Twenty four hours after mRNA transfection, cell death and GFP expression were quantified using flow cytometry. Horizontal lines indicate the mean. f Still images of B16-OVA cells at 0 and 24 h after transfection with tBid- or MLKL-mRNA visualized by time-lapse microscopy (scale bar = 10 µm). g In vivo cell death characterization. Subcutaneously growing B16-OVA tumors were injected with PBS or with 10 µg mRNA encoding Fluc, tBid, or MLKL followed by electroporation. Twenty four hours later, the tumor cells were isolated and analyzed by flow cytometry for sytox uptake. Graph showing the percentages of sytox + cells (left) and representative flow cytometry plots (right). Horizontal lines indicate the mean

    Journal: Nature Communications

    Article Title: Treatment with mRNA coding for the necroptosis mediator MLKL induces antitumor immunity directed against neo-epitopes

    doi: 10.1038/s41467-018-05979-8

    Figure Lengend Snippet: MLKL encoding mRNA induces cell death in vitro and in vivo. a – f In vitro cell death characterization. B16-OVA cells were transfected with PBS or with Fluc-, tBid-, or MLKL-mRNA. a At different time points after transfection, cells were collected and analyzed by flow cytometry. Graph showing the percentages of sytox + cells (left). Representative flow cytometric plots 24 h after transfection (right). b Impact of the pan-caspase inhibitor zVAD-fmk on cell death induction (top) and caspase activity (bottom) upon transfection of B16-OVA cells with tBID- or MLKL-mRNA. c Western blot analysis of the expression of MLKL, caspase-3, and cleaved caspase-3 in cell lysates prepared 24 h after mRNA transfection. Tubulin served as a loading control. d B16 cells were co-transfected with luciferase NF-κB reporter plasmid and a plasmid expressing β-galactosidase. Twenty four hours later, the cells were transfected with PBS, GFP-, tBid-, or MLKL-mRNA or, as a positive control for NF-κB activation, with TRAF6 expression vector or they were stimulated with TNF. The normalized luciferase activity in the lysates determined at different time points after mRNA transfection is depicted. e B16 cells were transfected with a GFP expression plasmid. Twenty four hours later, the cells were transfected with PBS, Fluc-, tBid-, or MLKL-mRNA and the cells were treated or not with actinomycin D as indicated. Twenty four hours after mRNA transfection, cell death and GFP expression were quantified using flow cytometry. Horizontal lines indicate the mean. f Still images of B16-OVA cells at 0 and 24 h after transfection with tBid- or MLKL-mRNA visualized by time-lapse microscopy (scale bar = 10 µm). g In vivo cell death characterization. Subcutaneously growing B16-OVA tumors were injected with PBS or with 10 µg mRNA encoding Fluc, tBid, or MLKL followed by electroporation. Twenty four hours later, the tumor cells were isolated and analyzed by flow cytometry for sytox uptake. Graph showing the percentages of sytox + cells (left) and representative flow cytometry plots (right). Horizontal lines indicate the mean

    Article Snippet: Twenty four hours after transfection, the lysates were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (10% acrylamide) and MLKL and caspase-3 were visualized by western blotting with, respectively, anti-MLKL (1000× dilution) (Millipore, Cat. No. MABC604) and anti-caspase 3 (1000× dilution) (Cell Signaling Technology, Cat. No. 9662S) antibodies.

    Techniques: In Vitro, In Vivo, Transfection, Flow Cytometry, Cytometry, Activity Assay, Western Blot, Expressing, Luciferase, Plasmid Preparation, Positive Control, Activation Assay, Time-lapse Microscopy, Injection, Electroporation, Isolation

     Characterization of legumain-activatable liposomes (aLip). (A)  Size and TEM of aLip.  (B) In vitro  release of PTX.  (C)  Representative confocal imaging (scale bar, 20 μm) and  (D)  flow cytometry analysis of aLip uptake in A549T cells with or without pretreatment with M2Φ. The cell-penetrating R9/Lip was used as a positive control, while PEG/Lip was the negative control.  (E)  Quantitative analysis of the uptake efficiency in A549T cells.  (F)  Penetration of the pre-cleaved (top panel) or uncleaved (bottom panel) aLip in the cultured tumor spheroids. The aLip pretreated with legumain-containing M2 lysis would have activated cell-penetrating peptide-assisted intratumor penetration. Z-axis continuous top-down scanning layers by confocal microscopy of the spheroids. Scale bar, 200 μm.  (G)  Analysis of intratumor penetration depth in tumor spheroids.  (H)  MTT assay of free PTX/SV, PEG/Lip, and pre-cleaved aLip by M2Φ in A549T cells.  (I)  Cell apoptosis assay of free drug and aLip in A549T cells.  (J)  Western blot analysis of caspase 3 in A549T cells. aLip enhanced the level of activated caspase 3.  (K)  Western blot analysis of EMT reversal after drug treatment.

    Journal: Theranostics

    Article Title: Targeting lipid metabolism to overcome EMT-associated drug resistance via integrin β3/FAK pathway and tumor-associated macrophage repolarization using legumain-activatable delivery

    doi: 10.7150/thno.27246

    Figure Lengend Snippet: Characterization of legumain-activatable liposomes (aLip). (A) Size and TEM of aLip. (B) In vitro release of PTX. (C) Representative confocal imaging (scale bar, 20 μm) and (D) flow cytometry analysis of aLip uptake in A549T cells with or without pretreatment with M2Φ. The cell-penetrating R9/Lip was used as a positive control, while PEG/Lip was the negative control. (E) Quantitative analysis of the uptake efficiency in A549T cells. (F) Penetration of the pre-cleaved (top panel) or uncleaved (bottom panel) aLip in the cultured tumor spheroids. The aLip pretreated with legumain-containing M2 lysis would have activated cell-penetrating peptide-assisted intratumor penetration. Z-axis continuous top-down scanning layers by confocal microscopy of the spheroids. Scale bar, 200 μm. (G) Analysis of intratumor penetration depth in tumor spheroids. (H) MTT assay of free PTX/SV, PEG/Lip, and pre-cleaved aLip by M2Φ in A549T cells. (I) Cell apoptosis assay of free drug and aLip in A549T cells. (J) Western blot analysis of caspase 3 in A549T cells. aLip enhanced the level of activated caspase 3. (K) Western blot analysis of EMT reversal after drug treatment.

    Article Snippet: E-CAD, vimentin, ERK (p42/44), P-ERK (Thr202/Tyr204), AKT, P-AKT (Ser473), and caspase-3 antibodies were obtained from CST (Boston, USA).

    Techniques: Transmission Electron Microscopy, In Vitro, Imaging, Flow Cytometry, Cytometry, Positive Control, Negative Control, Cell Culture, Lysis, Confocal Microscopy, MTT Assay, Apoptosis Assay, Western Blot

    Western blot analysis of caspase-3 from lysates of rat periodontal ligament fibroblasts exposed to different concentrations of CSE. Rat PDL fibroblasts cultured and grown to 70–80% confluence in an incubator at 37°C. The cells were exposed to different concentrations of CSE (5%, 10% and 15%) (v/v) in serum free media for 60 min keeping controls which were not exposed to CSE. (A) Lane 1: cell lysates not exposed to CSE. Lane 2: cell lysates exposed to 5% CSE. Lane 3: Cell lysates exposed to 10% CSE. Lane 4: Cell lysates exposed to 15% CSE. (B) Densitometric analysis of band intensity shows each bar represents the mean ± SEM of three experiments. A β-actin loading control is shown beneath the plot.

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Western blot analysis of caspase-3 from lysates of rat periodontal ligament fibroblasts exposed to different concentrations of CSE. Rat PDL fibroblasts cultured and grown to 70–80% confluence in an incubator at 37°C. The cells were exposed to different concentrations of CSE (5%, 10% and 15%) (v/v) in serum free media for 60 min keeping controls which were not exposed to CSE. (A) Lane 1: cell lysates not exposed to CSE. Lane 2: cell lysates exposed to 5% CSE. Lane 3: Cell lysates exposed to 10% CSE. Lane 4: Cell lysates exposed to 15% CSE. (B) Densitometric analysis of band intensity shows each bar represents the mean ± SEM of three experiments. A β-actin loading control is shown beneath the plot.

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Western Blot, Cell Culture

    Western blot analysis of caspase-3 from lysates of isolated fetal rat lung fibroblasts exposed to different concentrations of CSE. Fetal rat lung fibroblasts were isolated on the 21st day of gestation and grown to 70–80% confluence in an incubator at 37°C. The cells were exposed to different concentrations of CSE (5%, 10% and 15%) (v/v) in serum free media for 60 min keeping controls which were not exposed to CSE. (A) Lane 1: cell lysates not exposed to CSE. Lane 2: cell lysates exposed to 5% CSE. Lane 3: Cell lysates exposed to 10% CSE. Lane 4: Cell lysates exposed to 15% CSE. (B) Densitometric analysis of band intensity shows each bar represents the mean ± SEM of three experiments. (*) indicates significantly different from the corresponding controls (p

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Western blot analysis of caspase-3 from lysates of isolated fetal rat lung fibroblasts exposed to different concentrations of CSE. Fetal rat lung fibroblasts were isolated on the 21st day of gestation and grown to 70–80% confluence in an incubator at 37°C. The cells were exposed to different concentrations of CSE (5%, 10% and 15%) (v/v) in serum free media for 60 min keeping controls which were not exposed to CSE. (A) Lane 1: cell lysates not exposed to CSE. Lane 2: cell lysates exposed to 5% CSE. Lane 3: Cell lysates exposed to 10% CSE. Lane 4: Cell lysates exposed to 15% CSE. (B) Densitometric analysis of band intensity shows each bar represents the mean ± SEM of three experiments. (*) indicates significantly different from the corresponding controls (p

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Western Blot, Isolation

    Immunofluorescence staining for detection of caspase 3 expression in isolated fetal rat lung fibroblasts. Isolated fetal rat lung fibroblasts were exposed to CSE (15% v/v) for three hours. Immunofluorescence was performed using caspase 3 rabbit polyclonal IGg antibody. Caspase 3 was visualized using donkey anti-rabbit IGg-FITC (green fluorescence) and counter stained with Hoescht 33342 (nuclear staining - blue). Image (A) shows controls not exposed to CSE. Image (B) shows expression of caspase 3 (green) primarily localized in the cytoplasm. Image (C) shows an enlarged image of a single cell.

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Immunofluorescence staining for detection of caspase 3 expression in isolated fetal rat lung fibroblasts. Isolated fetal rat lung fibroblasts were exposed to CSE (15% v/v) for three hours. Immunofluorescence was performed using caspase 3 rabbit polyclonal IGg antibody. Caspase 3 was visualized using donkey anti-rabbit IGg-FITC (green fluorescence) and counter stained with Hoescht 33342 (nuclear staining - blue). Image (A) shows controls not exposed to CSE. Image (B) shows expression of caspase 3 (green) primarily localized in the cytoplasm. Image (C) shows an enlarged image of a single cell.

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Immunofluorescence, Staining, Expressing, Isolation, Fluorescence

    Effect of CSE on caspase 3 activity in rat periodontal ligament fibroblasts. Fluorometric assay to assess the activity of caspase-3 in rat periodontal ligament fibroblasts exposed to different concentrations of CSE (5%, 10% or 15%) (v/v) for 60 minutes in 37°C incubator. Cells not exposed to CSE were considered as controls. Each bar represents the mean ± SEM of three experiments of 16 samples in each. No significant differences were noted.

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Effect of CSE on caspase 3 activity in rat periodontal ligament fibroblasts. Fluorometric assay to assess the activity of caspase-3 in rat periodontal ligament fibroblasts exposed to different concentrations of CSE (5%, 10% or 15%) (v/v) for 60 minutes in 37°C incubator. Cells not exposed to CSE were considered as controls. Each bar represents the mean ± SEM of three experiments of 16 samples in each. No significant differences were noted.

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Activity Assay

    Effect of Z-VAD-fmk and caspase 3 activity in isolated fetal rat lung fibroblast cells exposed to CSE. Caspase 3 activity and effect of Z-VAD-fmk was measured using caspase 3 fluorometric assay in isolated fetal rat lung fibroblast cells exposed to 5%, 10% or 15% (v/v) CSE for 60 minutes. Each bar represents the mean of ± SEM of three experiments of 16 samples each. (*) indicates significantly (p

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Effect of Z-VAD-fmk and caspase 3 activity in isolated fetal rat lung fibroblast cells exposed to CSE. Caspase 3 activity and effect of Z-VAD-fmk was measured using caspase 3 fluorometric assay in isolated fetal rat lung fibroblast cells exposed to 5%, 10% or 15% (v/v) CSE for 60 minutes. Each bar represents the mean of ± SEM of three experiments of 16 samples each. (*) indicates significantly (p

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Activity Assay, Isolation

    Effect of Z-VAD-fmk and caspase 3 activity in rat PDL fibroblasts exposed to CSE. Caspase 3 activity and effect of Z-VAD-fmk was measured using caspase 3 fluorometric assay in rat PDL fibroblast cells exposed to 5%, 10% or 15% (v/v) CSE for 60 minutes. Each bar represents the mean of ± SEM of three experiments of 16 samples each. No significant differences were noted.

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Effect of Z-VAD-fmk and caspase 3 activity in rat PDL fibroblasts exposed to CSE. Caspase 3 activity and effect of Z-VAD-fmk was measured using caspase 3 fluorometric assay in rat PDL fibroblast cells exposed to 5%, 10% or 15% (v/v) CSE for 60 minutes. Each bar represents the mean of ± SEM of three experiments of 16 samples each. No significant differences were noted.

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Activity Assay

    Effect of CSE on caspase 3 activity in fetal rat lung fibroblasts. Fluorometric assay to assess the activity of caspase-3 in fetal rat lung fibroblasts exposed to different concentrations of CSE (5%, 10% or 15%) (v/v) for 60 minutes in 37°C incubator. Cells not exposed to CSE were considered as controls. Each bar represents the mean ± SEM of three experiments of 16 samples in each. (*) indicates (p

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Effect of CSE on caspase 3 activity in fetal rat lung fibroblasts. Fluorometric assay to assess the activity of caspase-3 in fetal rat lung fibroblasts exposed to different concentrations of CSE (5%, 10% or 15%) (v/v) for 60 minutes in 37°C incubator. Cells not exposed to CSE were considered as controls. Each bar represents the mean ± SEM of three experiments of 16 samples in each. (*) indicates (p

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Activity Assay

    Immunofluorescence staining for detection of caspase 3 expression in rat PDL cells. Rat PDL cells were exposed to CSE (15% v/v) for three hours. Immunofluorescence was performed using caspase 3 rabbit polyclonal IGg antibody. Caspase 3 was visualized using donkey anti-rabbit IGg-FITC (green fluorescence) and counter stained with Hoescht 33342 (nuclear staining - blue). Image (A) shows controls not exposed to CSE. Image (B) shows expression of caspase 3 (green) primarily localized in the cytoplasm. Image (C) shows enlarged image of a single cell.

    Journal: Tobacco Induced Diseases

    Article Title: Caspase 3 activity in isolated fetal rat lung fibroblasts and rat periodontal ligament fibroblasts: cigarette smoke induced alterations

    doi: 10.1186/1617-9625-11-25

    Figure Lengend Snippet: Immunofluorescence staining for detection of caspase 3 expression in rat PDL cells. Rat PDL cells were exposed to CSE (15% v/v) for three hours. Immunofluorescence was performed using caspase 3 rabbit polyclonal IGg antibody. Caspase 3 was visualized using donkey anti-rabbit IGg-FITC (green fluorescence) and counter stained with Hoescht 33342 (nuclear staining - blue). Image (A) shows controls not exposed to CSE. Image (B) shows expression of caspase 3 (green) primarily localized in the cytoplasm. Image (C) shows enlarged image of a single cell.

    Article Snippet: Sub-cellular localization of caspase-3 using immunofluorescence Sub-cellular localization of caspase-3 in cells exposed to CSE was observed using immunofluorescence microcopy.

    Techniques: Immunofluorescence, Staining, Expressing, Fluorescence

    p-ERK1/2 inhibitor downregulated light-induced p-ERK1/2 overexpression and caspase 3 activating. The level of p-ERK1/2 and caspase 3 expression was detected with Western blotting. (a) Light injury significantly increased the expression of p-ERK1/2 compared with normal group. The p-ERK1/2 inhibitor significantly reduced p-ERK1/2 overexpression compared with light injury group. (b) Light injury significantly induced caspase 3 activating compared with normal group. The p-ERK1/2 inhibitor significantly downregulated caspase 3 activating compared with light injury group. (c) No significant change in the total level of caspase 3 was seen in different groups ( F = 0.56, P = 0.75). * P

    Journal: Chinese Medical Journal

    Article Title: Effect of Phosphorylated-Extracellular Regulated Kinase 1/2 Inhibitor on Retina from Light-induced Photoreceptor Degeneration

    doi: 10.4103/0366-6999.246064

    Figure Lengend Snippet: p-ERK1/2 inhibitor downregulated light-induced p-ERK1/2 overexpression and caspase 3 activating. The level of p-ERK1/2 and caspase 3 expression was detected with Western blotting. (a) Light injury significantly increased the expression of p-ERK1/2 compared with normal group. The p-ERK1/2 inhibitor significantly reduced p-ERK1/2 overexpression compared with light injury group. (b) Light injury significantly induced caspase 3 activating compared with normal group. The p-ERK1/2 inhibitor significantly downregulated caspase 3 activating compared with light injury group. (c) No significant change in the total level of caspase 3 was seen in different groups ( F = 0.56, P = 0.75). * P

    Article Snippet: The membranes were blocked with 5% nonfat milk in Tris-buffered saline containing Tween-20 for 1 h and then incubated with antibodies directed against the following proteins: p-ERK1/2 (1:100, Cat #4370, CST, Boston, MA, USA), TNF-α (1:1000, Cat #ab6671, Abcam, Cambridge, MA, USA), IL-1β (1:1000, Cat #ab9722, Abcam, Cambridge, MA, USA), caspase 3 (1:1000, Cat #ab13847, Abcam, Cambridge, MA, USA), and activated caspase 3 (1:1000, Cat #ab2302, Abcam, Cambridge, MA, USA).

    Techniques: Over Expression, Expressing, Western Blot

    Tn affects DIAP1 and Caspase-3 activity during DEOM histolysis at 12 h APF. a – c In vivo labeling of Caspase-3 (green) in mef2-Gal4/+ control or mef2 > tn RNAi DEOMs co-labeled with phalloidin (red). a Puncta corresponding to Caspase-3 are present in degenerating DEOM controls (white arrows in inset). b No Caspase-3(+) puncta are present in tn RNAi muscles. c Quantification of the relative fluorescence intensities of Caspase-3 in DEOMs reflects the general decrease observed upon a reduction in Tn. d – f Immunostaining for DIAP1 (green) and F-actin (red) is higher upon disruption of Tn function ( e , white arrows in inset) than in mef2-Gal4/+ control muscles ( d ). f Bar graph showing that the relative DIAP1 fluorescence levels are increased upon reduced Tn function. g – i Overall p35 (green) levels in DEOMs labeled with F-actin (red) are not changed upon a reduction in Tn. mef2 > p35 appears similar when co-expressed in a WT ( g ) or tn RNAi ( h ) background. Quantification of fluorescence intensity reveals no significant difference between WT or experimental DEOMs ( i ). Mean ± SEM (n.s., not significant, ** p

    Journal: Cell Death & Disease

    Article Title: Thin is required for cell death in the Drosophila abdominal muscles by targeting DIAP1

    doi: 10.1038/s41419-018-0756-x

    Figure Lengend Snippet: Tn affects DIAP1 and Caspase-3 activity during DEOM histolysis at 12 h APF. a – c In vivo labeling of Caspase-3 (green) in mef2-Gal4/+ control or mef2 > tn RNAi DEOMs co-labeled with phalloidin (red). a Puncta corresponding to Caspase-3 are present in degenerating DEOM controls (white arrows in inset). b No Caspase-3(+) puncta are present in tn RNAi muscles. c Quantification of the relative fluorescence intensities of Caspase-3 in DEOMs reflects the general decrease observed upon a reduction in Tn. d – f Immunostaining for DIAP1 (green) and F-actin (red) is higher upon disruption of Tn function ( e , white arrows in inset) than in mef2-Gal4/+ control muscles ( d ). f Bar graph showing that the relative DIAP1 fluorescence levels are increased upon reduced Tn function. g – i Overall p35 (green) levels in DEOMs labeled with F-actin (red) are not changed upon a reduction in Tn. mef2 > p35 appears similar when co-expressed in a WT ( g ) or tn RNAi ( h ) background. Quantification of fluorescence intensity reveals no significant difference between WT or experimental DEOMs ( i ). Mean ± SEM (n.s., not significant, ** p

    Article Snippet: The following primary antibodies were used: rabbit anti-Caspase-3 (1:100, Cell Signaling Technology, Danvers, MA,USA), mouse anti-DIAP1 (1:200, B. Hay) , guinea pig anti-p35 (1:10, P. Meier) , and guinea pig anti-Tn .

    Techniques: Activity Assay, In Vivo, Labeling, Fluorescence, Immunostaining

    AgNP-induced occurrence of systemic apoptosis. Immunofluorescent signals of the apoptotic biomarker “active caspase 3” in multiple tissues (brain, salivary gland, wing disc and gut) dissected from AgNP-exposed 3 rd -instar wandering larvae.

    Journal: Scientific Reports

    Article Title: Silver nanoparticles have lethal and sublethal adverse effects on development and longevity by inducing ROS-mediated stress responses

    doi: 10.1038/s41598-018-20728-z

    Figure Lengend Snippet: AgNP-induced occurrence of systemic apoptosis. Immunofluorescent signals of the apoptotic biomarker “active caspase 3” in multiple tissues (brain, salivary gland, wing disc and gut) dissected from AgNP-exposed 3 rd -instar wandering larvae.

    Article Snippet: The rabbit anti-cleaved caspase 3 (1:250, Cell Signaling Technology, MA, USA) and rabbit anti-phosphorylated H2AX (1:500, Rockland, PA, USA) primary antibodies were used to quantitate the levels of AgNP-induced apoptosis and DNA damage (double-stranded breaks), respectively.

    Techniques: Biomarker Assay

    Everolimus attenuated and enhanced palbociclib sensitivity of MCF-7 cells. ( A ) MCF-7-P cells were treated with palbociclib with or without everolimus, and followed by cell viability assay. ( B ) Expression of the apoptosis executors, cleaved caspase-3 and cleaved PARP, was detected in cells depicted in ( A ). ( C, D ) Expression of drug resistance genes ABCG2 and MDR1 was examined in cells depicted in ( A ). (E) MCF-7 cells were treated with palbociclib with or without everolimus and followed by detecting cell viability after 24, 48, and 72 hours. ( F ) Expression of the executors cleaved caspase-3 and cleaved PARP was detected in cells depicted in ( E ). Data were presented as mean ± standard deviation; ** P

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Everolimus Reverses Palbociclib Resistance in ER+ Human Breast Cancer Cells by Inhibiting Phosphatidylinositol 3-Kinase(PI3K)/Akt/Mammalian Target of Rapamycin (mTOR) Pathway

    doi: 10.12659/MSM.912929

    Figure Lengend Snippet: Everolimus attenuated and enhanced palbociclib sensitivity of MCF-7 cells. ( A ) MCF-7-P cells were treated with palbociclib with or without everolimus, and followed by cell viability assay. ( B ) Expression of the apoptosis executors, cleaved caspase-3 and cleaved PARP, was detected in cells depicted in ( A ). ( C, D ) Expression of drug resistance genes ABCG2 and MDR1 was examined in cells depicted in ( A ). (E) MCF-7 cells were treated with palbociclib with or without everolimus and followed by detecting cell viability after 24, 48, and 72 hours. ( F ) Expression of the executors cleaved caspase-3 and cleaved PARP was detected in cells depicted in ( E ). Data were presented as mean ± standard deviation; ** P

    Article Snippet: The primary antibodies against ALDH1 (ab129815), Nanog (ab80892), ABCG2 (ab203397), MDR1 (ab3366), p-mTOR (ab84400), cleaved caspase-3 (ab32042), and cleaved PARP (ab32064) were purchased from Abcam.

    Techniques: Viability Assay, Expressing, Standard Deviation

    Activity of caspase-3 in human lymphocytes following PFOS treatment. The effect of PFOS on activity of caspase-3 in cultured human lymphocytes. Caspase-3 activity was assessed after treatment of human lymphocytes with IC 50 (150 µM) of PFOS for 6 and 12 h. PFOS (150 µM), significantly ( P

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Perfluorooctanesulfonate (PFOS) Induces Apoptosis Signaling and Proteolysis in Human Lymphocytes through ROS Mediated Mitochondrial Dysfunction and Lysosomal Membrane Labialization

    doi:

    Figure Lengend Snippet: Activity of caspase-3 in human lymphocytes following PFOS treatment. The effect of PFOS on activity of caspase-3 in cultured human lymphocytes. Caspase-3 activity was assessed after treatment of human lymphocytes with IC 50 (150 µM) of PFOS for 6 and 12 h. PFOS (150 µM), significantly ( P

    Article Snippet: Measurment of caspase-3 activity After treatment of human lymphocytes with IC50 of PFOS for 6 and 12 h, activity of caspase3 was determined by use of “Sigma’s caspase-3 assay kit (CASP-3-C)”.

    Techniques: Activity Assay, Cell Culture

    The activation of caspase-3 occurs in early activated cells before the emergence of fully differentiated effector cells. C57BL/6 mice were initially parked with 10 4 OT1 spleen cells. After infection with 10 4 LM-OVA, mice were sacrificed at various time points and spleens were harvested. Single cell suspensions were co-stained for CD8 + , OVA-Tetramer, CD62L, IL7Rα and active caspase-3. (A) Scatter plots show the relative staining of OVA-tetramer + CD8 + cells for activation markers and active caspase-3. Data is representative for at least 3 mice per time point. (B) OVA-tetramer + CD8 + T cells were examined for active intracellular active caspase-3 and surface CD62L between days 0–15 of LM-OVA infection. (data is representative for 3 mice per timepoint).

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: The activation of caspase-3 occurs in early activated cells before the emergence of fully differentiated effector cells. C57BL/6 mice were initially parked with 10 4 OT1 spleen cells. After infection with 10 4 LM-OVA, mice were sacrificed at various time points and spleens were harvested. Single cell suspensions were co-stained for CD8 + , OVA-Tetramer, CD62L, IL7Rα and active caspase-3. (A) Scatter plots show the relative staining of OVA-tetramer + CD8 + cells for activation markers and active caspase-3. Data is representative for at least 3 mice per time point. (B) OVA-tetramer + CD8 + T cells were examined for active intracellular active caspase-3 and surface CD62L between days 0–15 of LM-OVA infection. (data is representative for 3 mice per timepoint).

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: Activation Assay, Mouse Assay, Infection, Staining

    Rapidly proliferating CD8 + T cells have an apoptotic like phenotype in vivo . C57BL6/J mice were injected with 10 4 OT1 cells and infected with 10 4 LM-OVA. At various time points mice were sacrificed and splenic cells were stained and analyzed by FACS. Scatterplots show OVA-tetramer binding versus (A) active caspase, (B) PhiPhiLux cleavage by caspase-3 (PPL), (C) Annexin V binding and (d) PD-1, in cells over days 3, 4 and 7 of LM-OVA infection. The % of OVA-tetramer + CD8 + cells expressing a high level of (E▴) caspase-3, (F•) PPL cleavage, (G Δ) Annexin V binding, and (H ○) PD-1 are shown over the course of an acute OVA specific CD8 + T cell response (▪). *The decrease in apoptotic staining between day 3 and 7 shows significant linear correlation (by Pearson analysis) between active caspase-3 antibody staining and (E) PPL cleavage activity, (F) annexin V binding and (G) PD-1 expression (P

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Rapidly proliferating CD8 + T cells have an apoptotic like phenotype in vivo . C57BL6/J mice were injected with 10 4 OT1 cells and infected with 10 4 LM-OVA. At various time points mice were sacrificed and splenic cells were stained and analyzed by FACS. Scatterplots show OVA-tetramer binding versus (A) active caspase, (B) PhiPhiLux cleavage by caspase-3 (PPL), (C) Annexin V binding and (d) PD-1, in cells over days 3, 4 and 7 of LM-OVA infection. The % of OVA-tetramer + CD8 + cells expressing a high level of (E▴) caspase-3, (F•) PPL cleavage, (G Δ) Annexin V binding, and (H ○) PD-1 are shown over the course of an acute OVA specific CD8 + T cell response (▪). *The decrease in apoptotic staining between day 3 and 7 shows significant linear correlation (by Pearson analysis) between active caspase-3 antibody staining and (E) PPL cleavage activity, (F) annexin V binding and (G) PD-1 expression (P

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: In Vivo, Mouse Assay, Injection, Infection, Staining, FACS, Binding Assay, Expressing, Activity Assay

    The majority of active caspase-3 hi cells do not progress to cell death during early antigen induced proliferation in vivo . Mice were parked with 10 4 CD45.1 + OT1 spleen cells and challenged with 10 4 LM-OVA (iv). Mice were sacrificed at day 5 post LM-OVA infection and CD8 + T cells were magnetically isolated by negative selection. Cells were stained with anti-CD45.1 antibody and PhiPhiLux. (A) Cells were sorted into CD45.1 + caspase-3 activity high and CD45.1 + caspase-3 activity low fractions. (B) Sorted cells were then plated at low cell densities (∼12.5 cells/well) and examined for viability during proliferation over several days using TMRE staining. (C) The total number and number of dead cells were counted directly in at least 6 replicate wells and the changes observed over 72 hours in the plates. (D) Cells were also maintained at higher concentrations (∼100 000/well) and stained for DNA cleavage (TUNEL) after 1 day in culture.

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: The majority of active caspase-3 hi cells do not progress to cell death during early antigen induced proliferation in vivo . Mice were parked with 10 4 CD45.1 + OT1 spleen cells and challenged with 10 4 LM-OVA (iv). Mice were sacrificed at day 5 post LM-OVA infection and CD8 + T cells were magnetically isolated by negative selection. Cells were stained with anti-CD45.1 antibody and PhiPhiLux. (A) Cells were sorted into CD45.1 + caspase-3 activity high and CD45.1 + caspase-3 activity low fractions. (B) Sorted cells were then plated at low cell densities (∼12.5 cells/well) and examined for viability during proliferation over several days using TMRE staining. (C) The total number and number of dead cells were counted directly in at least 6 replicate wells and the changes observed over 72 hours in the plates. (D) Cells were also maintained at higher concentrations (∼100 000/well) and stained for DNA cleavage (TUNEL) after 1 day in culture.

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: In Vivo, Mouse Assay, Infection, Isolation, Selection, Staining, Activity Assay, TUNEL Assay

    Elevated active caspase-3 is found primarily in secondary lymphoid tissues early in T cell activation. Mice parked with 10 4 OT1 cells were challenged with 10 4 LM-OVA. At various time points, mice were perfused and organs removed. Single cell suspensions were stained and analyzed by FACS. (A) Scatterplots show OVA-tetramer binding versus active caspase-3 expression in CD8 + T cells. Plots are representative of 3 mice analyzed. (B) The % of OVA-tetramer + cells in each organ (upper right) and the change in the level of active caspase-3 expression in OVA specific CD8 + T cells (lower right) from each organ is shown. There is a significantly higher proportion of active caspase-3 high cells in the spleen when compared to PBL, lungs or brain at day 4 (*P

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Elevated active caspase-3 is found primarily in secondary lymphoid tissues early in T cell activation. Mice parked with 10 4 OT1 cells were challenged with 10 4 LM-OVA. At various time points, mice were perfused and organs removed. Single cell suspensions were stained and analyzed by FACS. (A) Scatterplots show OVA-tetramer binding versus active caspase-3 expression in CD8 + T cells. Plots are representative of 3 mice analyzed. (B) The % of OVA-tetramer + cells in each organ (upper right) and the change in the level of active caspase-3 expression in OVA specific CD8 + T cells (lower right) from each organ is shown. There is a significantly higher proportion of active caspase-3 high cells in the spleen when compared to PBL, lungs or brain at day 4 (*P

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: Activation Assay, Mouse Assay, Staining, FACS, Binding Assay, Expressing

    ST-OVA infection induces a lower and protracted increase in the expression of active caspase-3 consistent with delayed and muted antigen induced CD8 + T cell proliferation. B6129F1 mice that resist infection with ST were parked with 10 4 OT1 cells and challenged with either 10 3 LM-OVA or 10 3 ST-OVA iv and sacrificed at various time points after infection. Single cell suspensions were obtained from spleens and stained with various markers indicated in the figure. Relative expression of various markers on OVA-tetramer + CD8 + T cells was evaluated (A). Cells were also co-stained for DNA cleavage (TUNEL) vs. active caspase-3 expression (B). (n≥3 per timepoint).

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: ST-OVA infection induces a lower and protracted increase in the expression of active caspase-3 consistent with delayed and muted antigen induced CD8 + T cell proliferation. B6129F1 mice that resist infection with ST were parked with 10 4 OT1 cells and challenged with either 10 3 LM-OVA or 10 3 ST-OVA iv and sacrificed at various time points after infection. Single cell suspensions were obtained from spleens and stained with various markers indicated in the figure. Relative expression of various markers on OVA-tetramer + CD8 + T cells was evaluated (A). Cells were also co-stained for DNA cleavage (TUNEL) vs. active caspase-3 expression (B). (n≥3 per timepoint).

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: Infection, Expressing, Mouse Assay, Staining, TUNEL Assay

    Active caspase-3 in antigen activated T cells is expressed in live proliferating cells. OT1 spleen cells were stimulated in vitro for 48 hours with varying amounts of antigen. Apoptotic control cells were treated with 1 µg/ml staurospaurine. Cells were then stained with anti-CD8 antibody and fixed and permeabilized before TUNEL and caspase-3 staining. Cells were mounted on slides and examinated by fluorescence microscopy. Images show TUNEL staining (green), and active caspase-3 (red) in CD8 labeled T cells (blue). The images are representative of 3 repeated examinations for each differentially stimulated culture. Arrows shown identify cells with positive staining for both caspase-3 and TUNEL.

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Active caspase-3 in antigen activated T cells is expressed in live proliferating cells. OT1 spleen cells were stimulated in vitro for 48 hours with varying amounts of antigen. Apoptotic control cells were treated with 1 µg/ml staurospaurine. Cells were then stained with anti-CD8 antibody and fixed and permeabilized before TUNEL and caspase-3 staining. Cells were mounted on slides and examinated by fluorescence microscopy. Images show TUNEL staining (green), and active caspase-3 (red) in CD8 labeled T cells (blue). The images are representative of 3 repeated examinations for each differentially stimulated culture. Arrows shown identify cells with positive staining for both caspase-3 and TUNEL.

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: In Vitro, Staining, TUNEL Assay, Fluorescence, Microscopy, Labeling

    Caspase-3 activation does not occur during rapid homeostatic proliferation in vivo. Rag1-/- mice were injected with 10 4 CFSE stained OT1 cells. WT mice were injected with 10 5 CFSE stained OT1 cells concurrent with PBS, LM or LM-OVA (10 4 , iv). Four days later mice were sacrificed and spleen cell suspensions stained with anti-CD8 antibody, OVA-tetramer, followed by intracellular staining with anti-caspase-3 antibody. Scatterplots show data obtained from gated OVA specific CD8 + T cells and is representative of 3 mice per group.

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Caspase-3 activation does not occur during rapid homeostatic proliferation in vivo. Rag1-/- mice were injected with 10 4 CFSE stained OT1 cells. WT mice were injected with 10 5 CFSE stained OT1 cells concurrent with PBS, LM or LM-OVA (10 4 , iv). Four days later mice were sacrificed and spleen cell suspensions stained with anti-CD8 antibody, OVA-tetramer, followed by intracellular staining with anti-caspase-3 antibody. Scatterplots show data obtained from gated OVA specific CD8 + T cells and is representative of 3 mice per group.

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: Activation Assay, In Vivo, Mouse Assay, Injection, Staining

    Actively proliferating cells in vivo co-express markers for apoptosis and proliferation with little apparent cell death. C57BL/6 mice were parked with 10 4 OT1 cells and challenged with 10 4 LM-OVA. Splenic cells were obtained from infected C57BL/6 mice at various time points after infection and stained for CD8 and OVA-tatramer binding as well (A) proliferation marker Ki67 vs. active caspase-3. (B) Cells were also co-stained for DNA cleavage (TUNEL) vs. active caspase-3 expression.

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Actively proliferating cells in vivo co-express markers for apoptosis and proliferation with little apparent cell death. C57BL/6 mice were parked with 10 4 OT1 cells and challenged with 10 4 LM-OVA. Splenic cells were obtained from infected C57BL/6 mice at various time points after infection and stained for CD8 and OVA-tatramer binding as well (A) proliferation marker Ki67 vs. active caspase-3. (B) Cells were also co-stained for DNA cleavage (TUNEL) vs. active caspase-3 expression.

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: In Vivo, Mouse Assay, Infection, Staining, Binding Assay, Marker, TUNEL Assay, Expressing

    Caspase 3 and CD62L expression is progressively lost as proliferation proceeds. 10 4 OT1 splenocytes were stained with CFSE and injected in C57BL/6 recipient mice concurrently with LM-OVA challenge. After 3, 4 and 5 days, mice were sacrificed (3 per time point) and spleen cells stained for expression markers. (A) Scatterplots show expression of active caspase-3 versus CFSE and CD62L in OVA-tetramer + CD8 + T cells after 4 days in vivo. (B) OVA specific CD8 + T cells were gated for division number based on CFSE dilution. Cells show a significant, coordinate decrease in the expression of active caspase-3 and CD62L/IL7Rα as cell proliferation proceeds (***P

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Caspase 3 and CD62L expression is progressively lost as proliferation proceeds. 10 4 OT1 splenocytes were stained with CFSE and injected in C57BL/6 recipient mice concurrently with LM-OVA challenge. After 3, 4 and 5 days, mice were sacrificed (3 per time point) and spleen cells stained for expression markers. (A) Scatterplots show expression of active caspase-3 versus CFSE and CD62L in OVA-tetramer + CD8 + T cells after 4 days in vivo. (B) OVA specific CD8 + T cells were gated for division number based on CFSE dilution. Cells show a significant, coordinate decrease in the expression of active caspase-3 and CD62L/IL7Rα as cell proliferation proceeds (***P

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: Expressing, Staining, Injection, Mouse Assay, In Vivo

    Significant increase in active caspase-3 during T cell activation correlates directly with an increase in proliferation. A single cell suspension of OT1 splenocytes, some of which were first CFSE stained, were placed in culture with varying concentrations of SIINFEKL peptide for 48 hours and analyzed by intracellular flow cytometry (n≥3). Cells were stained with anti-CD8 antibody and OVA-tetramer, then fixed and permeabilized before staining with anti- active caspase-3 antibody and Ki67. Graphs show the mean fluorescence intensity (MFI) of CD8 + OVA-tetramer + gated cells. (A) MFI of active caspase-3 versus Ki67 show a high amount of linear correlation in their expression levels (P

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Significant increase in active caspase-3 during T cell activation correlates directly with an increase in proliferation. A single cell suspension of OT1 splenocytes, some of which were first CFSE stained, were placed in culture with varying concentrations of SIINFEKL peptide for 48 hours and analyzed by intracellular flow cytometry (n≥3). Cells were stained with anti-CD8 antibody and OVA-tetramer, then fixed and permeabilized before staining with anti- active caspase-3 antibody and Ki67. Graphs show the mean fluorescence intensity (MFI) of CD8 + OVA-tetramer + gated cells. (A) MFI of active caspase-3 versus Ki67 show a high amount of linear correlation in their expression levels (P

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: Activation Assay, Staining, Flow Cytometry, Cytometry, Fluorescence, Expressing

    Caspase-3 is induced by antigen, not inflammation in vivo . B6129F1 mice were parked with 10 4 OT1 spleen cells, then infected with ST-OVA or LM-OVA (10 3 , iv) and sacrificed at several time points between days 4 and 60 post-infection. Splenic suspensions were analyzed for (A) bacterial load by CFU, (B) bacterial OVA mRNA expression by qRT-PCR, and (C) the relative induction of 40 cytokines/chemokines by cytokine proteome array (day 6). (D) CFSE labeled OT1 cells were injected into B6129F1 mice that were challenged with LM-OVA or ST-OVA, and the proliferation and caspase 3 expression of OVA-specific evaluated at day 5 after infection. Scatter plots show data obtained from gated OVA specific CD8 + T cells. Data shown is representative for at least 3 mice per timepoint.

    Journal: PLoS ONE

    Article Title: Caspase-3 Is Transiently Activated without Cell Death during Early Antigen Driven Expansion of CD8+ T Cells In Vivo

    doi: 10.1371/journal.pone.0015328

    Figure Lengend Snippet: Caspase-3 is induced by antigen, not inflammation in vivo . B6129F1 mice were parked with 10 4 OT1 spleen cells, then infected with ST-OVA or LM-OVA (10 3 , iv) and sacrificed at several time points between days 4 and 60 post-infection. Splenic suspensions were analyzed for (A) bacterial load by CFU, (B) bacterial OVA mRNA expression by qRT-PCR, and (C) the relative induction of 40 cytokines/chemokines by cytokine proteome array (day 6). (D) CFSE labeled OT1 cells were injected into B6129F1 mice that were challenged with LM-OVA or ST-OVA, and the proliferation and caspase 3 expression of OVA-specific evaluated at day 5 after infection. Scatter plots show data obtained from gated OVA specific CD8 + T cells. Data shown is representative for at least 3 mice per timepoint.

    Article Snippet: In order to stain cells for active caspase-3, cells were then washed, fix/permeabilized (BD – Cat #554714) and stained with a biotin conjugated antibody against active caspase-3 (BD - Cat#550557), before streptavidin labeling.

    Techniques: In Vivo, Mouse Assay, Infection, Expressing, Quantitative RT-PCR, Labeling, Injection

    Mediating role of PIM 1 in the antitumor effect of hispidulin in colorectal cancer ( CRC ) cells. A, Modulation of PIM 1 mRNA expression by hispidulin in CRC cells. B, Modulation of PIM 1 protein by hispidulin in CRC cells. C–G, Effect of PIM 1 overexpression or knockdown on hispidulin‐induced growth inhibition (C), apoptosis (D), activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ) (E), suppression of cell invasion (F), and repression of MMP ‐2 and MMP ‐9 expression (G). ** P

    Journal: Cancer Science

    Article Title: Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/ STAT3 signaling in colorectal cancer, et al. Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/STAT3 signaling in colorectal cancer

    doi: 10.1111/cas.13575

    Figure Lengend Snippet: Mediating role of PIM 1 in the antitumor effect of hispidulin in colorectal cancer ( CRC ) cells. A, Modulation of PIM 1 mRNA expression by hispidulin in CRC cells. B, Modulation of PIM 1 protein by hispidulin in CRC cells. C–G, Effect of PIM 1 overexpression or knockdown on hispidulin‐induced growth inhibition (C), apoptosis (D), activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ) (E), suppression of cell invasion (F), and repression of MMP ‐2 and MMP ‐9 expression (G). ** P

    Article Snippet: The sections were incubated overnight at 4°C with primary antibodies (human PIM1 [1:100], Ki‐67 [3 μg/mL], cleaved caspase‐3 [1:200] from Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: Expressing, Over Expression, Inhibition, Activation Assay

    Correlation of PIM 1 expression with Ki‐67 and cleaved caspase‐3 expression in colorectal cancer tissue. A, Positive association between PIM 1 and Ki‐67 expression. B, Inverse association between PIM 1 and cleaved caspase‐3 expression. ** P

    Journal: Cancer Science

    Article Title: Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/ STAT3 signaling in colorectal cancer, et al. Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/STAT3 signaling in colorectal cancer

    doi: 10.1111/cas.13575

    Figure Lengend Snippet: Correlation of PIM 1 expression with Ki‐67 and cleaved caspase‐3 expression in colorectal cancer tissue. A, Positive association between PIM 1 and Ki‐67 expression. B, Inverse association between PIM 1 and cleaved caspase‐3 expression. ** P

    Article Snippet: The sections were incubated overnight at 4°C with primary antibodies (human PIM1 [1:100], Ki‐67 [3 μg/mL], cleaved caspase‐3 [1:200] from Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: Expressing

    Anticancer effect of hispidulin against colorectal cancer ( CRC ). A, HT ‐29 and SW 480 cells were treated with hispidulin (10 or 20 μmol/L) for 24 and 48 hours, the antigrowth effect of hispidulin on CRC cells was measured by CCK ‐8 assay. B, Cell apoptosis was quantified by flow cytometry after CRC cells were treated with different concentrations of hispidulin (10 or 20 μmol/L) for 24 hours. C, Effect of hispidulin on activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ). D, After cells were incubated with hispidulin for 24 hours, the effect of hispidulin (10 or 20 μmol/L) on cell invasion ability was analyzed using Transwell invasion assay. E, HT ‐29 and SW 480 cells were treated with hispidulin (10 or 20 μmol/L) for 24 h. Western blot analysis was used to detect the expression of MMP ‐2 and MMP ‐9 using indicated the antibodies. ** P

    Journal: Cancer Science

    Article Title: Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/ STAT3 signaling in colorectal cancer, et al. Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/STAT3 signaling in colorectal cancer

    doi: 10.1111/cas.13575

    Figure Lengend Snippet: Anticancer effect of hispidulin against colorectal cancer ( CRC ). A, HT ‐29 and SW 480 cells were treated with hispidulin (10 or 20 μmol/L) for 24 and 48 hours, the antigrowth effect of hispidulin on CRC cells was measured by CCK ‐8 assay. B, Cell apoptosis was quantified by flow cytometry after CRC cells were treated with different concentrations of hispidulin (10 or 20 μmol/L) for 24 hours. C, Effect of hispidulin on activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ). D, After cells were incubated with hispidulin for 24 hours, the effect of hispidulin (10 or 20 μmol/L) on cell invasion ability was analyzed using Transwell invasion assay. E, HT ‐29 and SW 480 cells were treated with hispidulin (10 or 20 μmol/L) for 24 h. Western blot analysis was used to detect the expression of MMP ‐2 and MMP ‐9 using indicated the antibodies. ** P

    Article Snippet: The sections were incubated overnight at 4°C with primary antibodies (human PIM1 [1:100], Ki‐67 [3 μg/mL], cleaved caspase‐3 [1:200] from Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: CCK-8 Assay, Flow Cytometry, Cytometry, Activation Assay, Incubation, Transwell Invasion Assay, Western Blot, Expressing

    Oncogenic role of PIM 1 in colorectal cancer. A, Knockdown of PIM 1 in HT 29 and SW 480 cells using si RNA . B–F, Effect of PIM 1 knockdown on cell growth (B), apoptosis (C), activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ) (D), cell invasion (E), and expression of MMP ‐2 and MMP ‐9 (F). * P

    Journal: Cancer Science

    Article Title: Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/ STAT3 signaling in colorectal cancer, et al. Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/STAT3 signaling in colorectal cancer

    doi: 10.1111/cas.13575

    Figure Lengend Snippet: Oncogenic role of PIM 1 in colorectal cancer. A, Knockdown of PIM 1 in HT 29 and SW 480 cells using si RNA . B–F, Effect of PIM 1 knockdown on cell growth (B), apoptosis (C), activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ) (D), cell invasion (E), and expression of MMP ‐2 and MMP ‐9 (F). * P

    Article Snippet: The sections were incubated overnight at 4°C with primary antibodies (human PIM1 [1:100], Ki‐67 [3 μg/mL], cleaved caspase‐3 [1:200] from Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: Activation Assay, Expressing

    Role of reactive oxygen species ( ROS )/ JAK 2/signal transducer and activator of transcription 3 ( STAT 3) signaling in the anticancer effect of hispidulin against colorectal cancer. A–E, Effect of JAK 2/ STAT 3 activator interleukin‐6 ( IL ‐6) and ROS inhibitor N‐acetylcysteine ( NAC ) on hispidulin‐induced growth inhibition (A), apoptosis (B), activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ) (C), suppression of cell invasion (D), and repression of MMP ‐2 and MMP ‐9 expression (E). ** P

    Journal: Cancer Science

    Article Title: Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/ STAT3 signaling in colorectal cancer, et al. Hispidulin suppresses cell growth and metastasis by targeting PIM1 through JAK2/STAT3 signaling in colorectal cancer

    doi: 10.1111/cas.13575

    Figure Lengend Snippet: Role of reactive oxygen species ( ROS )/ JAK 2/signal transducer and activator of transcription 3 ( STAT 3) signaling in the anticancer effect of hispidulin against colorectal cancer. A–E, Effect of JAK 2/ STAT 3 activator interleukin‐6 ( IL ‐6) and ROS inhibitor N‐acetylcysteine ( NAC ) on hispidulin‐induced growth inhibition (A), apoptosis (B), activation of caspase‐3 and poly( ADP ‐ribose) polymerase ( PARP ) (C), suppression of cell invasion (D), and repression of MMP ‐2 and MMP ‐9 expression (E). ** P

    Article Snippet: The sections were incubated overnight at 4°C with primary antibodies (human PIM1 [1:100], Ki‐67 [3 μg/mL], cleaved caspase‐3 [1:200] from Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: Inhibition, Activation Assay, Expressing

    LncRNA PART1 regulated cell growth, apoptosis and ECM-related genes through targeting miR-93-5p. (A) Images of NP cell colonies. The colony formation rates are shown on the right. (B) The apoptosis of NP cells was measured by flow cytometry. The apoptosis rates of NP cells are shown on the right. (C and D) The expression levels of Ki67 and C-caspase-3 in NP cells were measured by western blotting. (E-G) The expression levels of aggrecan, ADAMTS4, collagen II and MMP13 in NP cells were measured by (E and F) western blotting and (G) reverse transcription-quantitative PCR analysis. ** P

    Journal: International Journal of Molecular Medicine

    Article Title: Long non-coding RNA PART1 promotes intervertebral disc degeneration through regulating the miR-93/MMP2 pathway in nucleus pulposus cells

    doi: 10.3892/ijmm.2020.4580

    Figure Lengend Snippet: LncRNA PART1 regulated cell growth, apoptosis and ECM-related genes through targeting miR-93-5p. (A) Images of NP cell colonies. The colony formation rates are shown on the right. (B) The apoptosis of NP cells was measured by flow cytometry. The apoptosis rates of NP cells are shown on the right. (C and D) The expression levels of Ki67 and C-caspase-3 in NP cells were measured by western blotting. (E-G) The expression levels of aggrecan, ADAMTS4, collagen II and MMP13 in NP cells were measured by (E and F) western blotting and (G) reverse transcription-quantitative PCR analysis. ** P

    Article Snippet: The membrane was then blocked by 5% non-fat milk (PA201-01, BioMed) for 10 min at room temperature and then incubated with the primary antibodies: Anti-Ki-67 (1:5,000, ab92742, Abcam), anti-cleaved (C)-caspase-3 (1:500, ab2302, Abcam), anti-aggrecan (1:100, ab3778, Abcam), anti-ADAMTS4 (1:1,000, ab185722, Abcam), anti-collagen II (1:2,000, ab34712, Abcam), anti-MMP13 (1:3,000, ab39012, Abcam) and anti-GAPDH (1:2,000, ab8245, Abcam) at 4°C overnight.

    Techniques: Flow Cytometry, Expressing, Western Blot, Real-time Polymerase Chain Reaction

    Knockout of DFNA5 reduces secondary necrosis in macrophages. ( a ) Immunoblots of S100 lysates from DFNA5 +/+ (WT) and DFNA5 −/− (DFNA5-KO) macrophages stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 (upper), anti-caspase-3 (middle) or anti-β-actin (lower) antibodies. Asterisk indicate non-specific band (NS). ( b , c ) Cytotoxicity of VSV ( b ) ( n =3) and etoposide ( c ) ( n =3) as measured by LDH release in the culture supernatants of DFNA5 +/+ (WT) and DFNA5 −/− (DFNA5-KO) macrophages infected with VSV or treated with etoposide for 8 h. * P

    Journal: Nature Communications

    Article Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

    doi: 10.1038/ncomms14128

    Figure Lengend Snippet: Knockout of DFNA5 reduces secondary necrosis in macrophages. ( a ) Immunoblots of S100 lysates from DFNA5 +/+ (WT) and DFNA5 −/− (DFNA5-KO) macrophages stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 (upper), anti-caspase-3 (middle) or anti-β-actin (lower) antibodies. Asterisk indicate non-specific band (NS). ( b , c ) Cytotoxicity of VSV ( b ) ( n =3) and etoposide ( c ) ( n =3) as measured by LDH release in the culture supernatants of DFNA5 +/+ (WT) and DFNA5 −/− (DFNA5-KO) macrophages infected with VSV or treated with etoposide for 8 h. * P

    Article Snippet: Anti-DFNA5 (Catalogue No. sc-79233), anti-caspase-3 (Catalogue No. sc-7148), anti-GSDMD (Catalogue No. sc-393656) and anti-Bax (Catalogue No. sc-930) were from Santa Cruz.

    Techniques: Knock-Out, Western Blot, Infection

    Signalling pathways leading to activation of DFNA5. Various death stimuli or viral infection can lead to permeabilization of the outer mitochondrial membrane causing the release of cytochrome c, which binds to Apaf-1 leading to assembly of the Apaf-1 apoptosome and activation of caspase-9. Within this complex active caspase-9 cleaves procaspase-3 to generate the active caspase-3 heterodimer. Active caspase-3 in turns cleaves DFNA5 at Asp270 to generate the necrotic DFNA5-N fragment which permeabilizes the plasma membrane by forming large pores causing osmotic lysis of the cell and releasing cellular contents including pro-inflammatory mediators and alamins, into the extracellular space. Caspase-3 can also be activated by the death receptor pathway, which is activated by death receptor ligands at the cell membrane. This pathway can potentially lead to caspase-3-mediated processing of DFNA5 and secondary necrosis.

    Journal: Nature Communications

    Article Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

    doi: 10.1038/ncomms14128

    Figure Lengend Snippet: Signalling pathways leading to activation of DFNA5. Various death stimuli or viral infection can lead to permeabilization of the outer mitochondrial membrane causing the release of cytochrome c, which binds to Apaf-1 leading to assembly of the Apaf-1 apoptosome and activation of caspase-9. Within this complex active caspase-9 cleaves procaspase-3 to generate the active caspase-3 heterodimer. Active caspase-3 in turns cleaves DFNA5 at Asp270 to generate the necrotic DFNA5-N fragment which permeabilizes the plasma membrane by forming large pores causing osmotic lysis of the cell and releasing cellular contents including pro-inflammatory mediators and alamins, into the extracellular space. Caspase-3 can also be activated by the death receptor pathway, which is activated by death receptor ligands at the cell membrane. This pathway can potentially lead to caspase-3-mediated processing of DFNA5 and secondary necrosis.

    Article Snippet: Anti-DFNA5 (Catalogue No. sc-79233), anti-caspase-3 (Catalogue No. sc-7148), anti-GSDMD (Catalogue No. sc-393656) and anti-Bax (Catalogue No. sc-930) were from Santa Cruz.

    Techniques: Activation Assay, Infection, Lysis

    DFNA5 is cleaved by caspase-3 downstream of the Apaf-1 apoptosome. ( a , b ) Immunoblots of S100 lysates from stable 293T-DFNA5-EGFP and 293T-DFNA5-D270E-EGFP cells ( a ), or stable 293T-GSDMD-EGFP cells ( b ) stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 ( a , upper), anti-GSDMD ( b , upper), anti-caspase-3 ( a , b , middle) or anti-β-actin ( a , b , lower) antibodies. ( c ) Immunoblot of endogenous DFNA5 in 293T and HEPG2 total cell lysates. ( c , d ) Immunoblots of S100 lysates from human HEPG2 ( d ) or mouse casp-1/casp-11-double knockout (casp-1/11-dKO) ( e ) macrophages stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 (upper in d , e ), anti-GSDMD (second from top in d ), anti-caspase-3 (third from top in d , middle in e ) or anti-β-actin (fourth from top in d , lower in e ) antibodies. Asterisk indicate non-specific band (NS). Results are representative of at least three independent experiments.

    Journal: Nature Communications

    Article Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

    doi: 10.1038/ncomms14128

    Figure Lengend Snippet: DFNA5 is cleaved by caspase-3 downstream of the Apaf-1 apoptosome. ( a , b ) Immunoblots of S100 lysates from stable 293T-DFNA5-EGFP and 293T-DFNA5-D270E-EGFP cells ( a ), or stable 293T-GSDMD-EGFP cells ( b ) stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 ( a , upper), anti-GSDMD ( b , upper), anti-caspase-3 ( a , b , middle) or anti-β-actin ( a , b , lower) antibodies. ( c ) Immunoblot of endogenous DFNA5 in 293T and HEPG2 total cell lysates. ( c , d ) Immunoblots of S100 lysates from human HEPG2 ( d ) or mouse casp-1/casp-11-double knockout (casp-1/11-dKO) ( e ) macrophages stimulated with cytochrome c for the indicated times at 37 °C. The blots were probed with anti-DFNA5 (upper in d , e ), anti-GSDMD (second from top in d ), anti-caspase-3 (third from top in d , middle in e ) or anti-β-actin (fourth from top in d , lower in e ) antibodies. Asterisk indicate non-specific band (NS). Results are representative of at least three independent experiments.

    Article Snippet: Anti-DFNA5 (Catalogue No. sc-79233), anti-caspase-3 (Catalogue No. sc-7148), anti-GSDMD (Catalogue No. sc-393656) and anti-Bax (Catalogue No. sc-930) were from Santa Cruz.

    Techniques: Western Blot, Double Knockout

    Activation of DFNA5 downstream of the mitochondrial apoptotic pathway. ( a ) Immunoblots of cell lysates from stable 293T-DFNA5-EGFP and 293T-DFNA5-D270E-EGFP cells transfected with vector control (Ctrl) or constructs for Bax, constitutively active T7-tagged caspase-3 (casp-3) or inactive caspase-3 (casp-3-C285A) for 24 h as indicated. The blots were probed with anti-DFNA5 (upper), anti-Bax (middle), or anti-caspase-3 (lower two panels) antibodies. Asterisk indicates endogenous procaspase-3. Double asterisks indicate non-specific band. ( b ) Cytotoxicity of Bax and constitutively active caspase-3 as measured by LDH release in the culture supernatants of the indicated 293T cell lines. ( n =3) * P

    Journal: Nature Communications

    Article Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

    doi: 10.1038/ncomms14128

    Figure Lengend Snippet: Activation of DFNA5 downstream of the mitochondrial apoptotic pathway. ( a ) Immunoblots of cell lysates from stable 293T-DFNA5-EGFP and 293T-DFNA5-D270E-EGFP cells transfected with vector control (Ctrl) or constructs for Bax, constitutively active T7-tagged caspase-3 (casp-3) or inactive caspase-3 (casp-3-C285A) for 24 h as indicated. The blots were probed with anti-DFNA5 (upper), anti-Bax (middle), or anti-caspase-3 (lower two panels) antibodies. Asterisk indicates endogenous procaspase-3. Double asterisks indicate non-specific band. ( b ) Cytotoxicity of Bax and constitutively active caspase-3 as measured by LDH release in the culture supernatants of the indicated 293T cell lines. ( n =3) * P

    Article Snippet: Anti-DFNA5 (Catalogue No. sc-79233), anti-caspase-3 (Catalogue No. sc-7148), anti-GSDMD (Catalogue No. sc-393656) and anti-Bax (Catalogue No. sc-930) were from Santa Cruz.

    Techniques: Activation Assay, Western Blot, Transfection, Plasmid Preparation, Construct

    Activation of DFNA5 downstream of viral infection in macrophages. ( a ) Immunoblots of DFNA5 in cell lysates from uninfected (−) or VSV-infected (1, 5, 10 MOI) WT (left) or casp-1/11 dKO (right) immortalized BMDMs. The lower panels show caspase-3 and β-actin in the same cell lysates. Asterisk indicates non-specific band. ( b , c ) Cytotoxicity of VSV as measured by LDH release in the culture supernatants of WT and casp-1/11 dKO BMDMs infected with VSV for 12 h ( b ) ( n =3) or casp-1/11 dKO BMDMs transfected with control siRNA (siCtrl) or DFNA5 siRNA (siDFNA5) for 48 h and then infected with VSV (1 MOI) for the indicated times ( c ). ( n =3) * P

    Journal: Nature Communications

    Article Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

    doi: 10.1038/ncomms14128

    Figure Lengend Snippet: Activation of DFNA5 downstream of viral infection in macrophages. ( a ) Immunoblots of DFNA5 in cell lysates from uninfected (−) or VSV-infected (1, 5, 10 MOI) WT (left) or casp-1/11 dKO (right) immortalized BMDMs. The lower panels show caspase-3 and β-actin in the same cell lysates. Asterisk indicates non-specific band. ( b , c ) Cytotoxicity of VSV as measured by LDH release in the culture supernatants of WT and casp-1/11 dKO BMDMs infected with VSV for 12 h ( b ) ( n =3) or casp-1/11 dKO BMDMs transfected with control siRNA (siCtrl) or DFNA5 siRNA (siDFNA5) for 48 h and then infected with VSV (1 MOI) for the indicated times ( c ). ( n =3) * P

    Article Snippet: Anti-DFNA5 (Catalogue No. sc-79233), anti-caspase-3 (Catalogue No. sc-7148), anti-GSDMD (Catalogue No. sc-393656) and anti-Bax (Catalogue No. sc-930) were from Santa Cruz.

    Techniques: Activation Assay, Infection, Western Blot, Transfection

    Caspase-3 cleaves DFNA5 after Asp270. ( a ) Immunoblot of purified N-terminal His6-T7-tagged DFNA5 and GSDMD proteins incubated without (−) or with caspase-1 (casp-1) or caspase-3 (casp-3) for 45 min at 37 °C. The blot was probed with anti-T7 antibody. ( b ) Coomassie stained SDS-polyacrylamide gels of TALON-immobilized proteins from uninduced or IPTG-induced BL-21 pET28b-DFNA5 bacteria (left panel), or IPTG-induced BL-21 pET28b-DFNA5 bacteria incubated without (control) or with caspase-3 for 45 min (right panel). The caspase-3-generated N- and C-terminal DFNA5 fragments (DFNA5-N and DFNA5-C, respectively) are indicated. ( c ) Diagrammatic representation of human and mouse DFNA5 proteins showing the caspase-3 recognition motif at aa 267–270. ( d ) Immunoblot of purified N-terminal T7-tagged WT DFNA5 and DFNA5-D270E proteins incubated without (−) or with increasing amounts of caspase-3 for 45 min. The blot was probed with anti-T7 antibody. Results are representative of at least three independent experiments.

    Journal: Nature Communications

    Article Title: Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

    doi: 10.1038/ncomms14128

    Figure Lengend Snippet: Caspase-3 cleaves DFNA5 after Asp270. ( a ) Immunoblot of purified N-terminal His6-T7-tagged DFNA5 and GSDMD proteins incubated without (−) or with caspase-1 (casp-1) or caspase-3 (casp-3) for 45 min at 37 °C. The blot was probed with anti-T7 antibody. ( b ) Coomassie stained SDS-polyacrylamide gels of TALON-immobilized proteins from uninduced or IPTG-induced BL-21 pET28b-DFNA5 bacteria (left panel), or IPTG-induced BL-21 pET28b-DFNA5 bacteria incubated without (control) or with caspase-3 for 45 min (right panel). The caspase-3-generated N- and C-terminal DFNA5 fragments (DFNA5-N and DFNA5-C, respectively) are indicated. ( c ) Diagrammatic representation of human and mouse DFNA5 proteins showing the caspase-3 recognition motif at aa 267–270. ( d ) Immunoblot of purified N-terminal T7-tagged WT DFNA5 and DFNA5-D270E proteins incubated without (−) or with increasing amounts of caspase-3 for 45 min. The blot was probed with anti-T7 antibody. Results are representative of at least three independent experiments.

    Article Snippet: Anti-DFNA5 (Catalogue No. sc-79233), anti-caspase-3 (Catalogue No. sc-7148), anti-GSDMD (Catalogue No. sc-393656) and anti-Bax (Catalogue No. sc-930) were from Santa Cruz.

    Techniques: Purification, Incubation, Staining, Generated

    Changes in the small intestinal epithelium of acute and chronic TNF-mediated injury mouse models. a Schematic of experimental treatment and sampling timeline for acute and chronic TNF-mediated inflammatory injury. b Morphology of duodenal sections illustrating epithelial disruption 1–4 h following a high-dose pulse of TNF (acute model) with concomitant BrdU administration (brown staining), counterstained with Haematoxylin (blue/purple). Arrows indicate the hollow villus tips following stromal retraction induced by TNF and the constriction of the epithelium over the stroma preceding the shedding of the tip, which is re-epithelised at 4 h post-TNF. The epithelium in healthy and chronic inflammation models exhibits standard morphological appearance. Progression of BrdU-labelled cells on the CVEU over time was used to quantify cell dynamics in later analyses. c Images of TUNEL and cleaved-Caspase-3 (CC3) labelled duodenum sections illustrating labelling similarity and differences in cell death intensity along the CVEU of healthy and inflammation mouse models. d Representative images and quantification of cells staining positive for goblet cell mucin (MUC2) in small intestine of control and acute inflammation mouse model at 1, 1.5, and 12 h post-TNF delivery. e Plot symbols show the decrease and recovery of the CVEU length (average number of cells ± standard deviation) in duodenum and ileum over time following the administration of one high-dose pulse of TNF (acute inflammation). Continuous blue and red bands show the average ± standard deviation of the CVEU length in control conditions and the chronic inflammation model, respectively

    Journal: Cell Death & Disease

    Article Title: Elevated apoptosis impairs epithelial cell turnover and shortens villi in TNF-driven intestinal inflammation

    doi: 10.1038/s41419-018-1275-5

    Figure Lengend Snippet: Changes in the small intestinal epithelium of acute and chronic TNF-mediated injury mouse models. a Schematic of experimental treatment and sampling timeline for acute and chronic TNF-mediated inflammatory injury. b Morphology of duodenal sections illustrating epithelial disruption 1–4 h following a high-dose pulse of TNF (acute model) with concomitant BrdU administration (brown staining), counterstained with Haematoxylin (blue/purple). Arrows indicate the hollow villus tips following stromal retraction induced by TNF and the constriction of the epithelium over the stroma preceding the shedding of the tip, which is re-epithelised at 4 h post-TNF. The epithelium in healthy and chronic inflammation models exhibits standard morphological appearance. Progression of BrdU-labelled cells on the CVEU over time was used to quantify cell dynamics in later analyses. c Images of TUNEL and cleaved-Caspase-3 (CC3) labelled duodenum sections illustrating labelling similarity and differences in cell death intensity along the CVEU of healthy and inflammation mouse models. d Representative images and quantification of cells staining positive for goblet cell mucin (MUC2) in small intestine of control and acute inflammation mouse model at 1, 1.5, and 12 h post-TNF delivery. e Plot symbols show the decrease and recovery of the CVEU length (average number of cells ± standard deviation) in duodenum and ileum over time following the administration of one high-dose pulse of TNF (acute inflammation). Continuous blue and red bands show the average ± standard deviation of the CVEU length in control conditions and the chronic inflammation model, respectively

    Article Snippet: Villus cell apoptosis was confirmed histologically by Caspase-3 [rabbit anti-CC3, (R & D Systems, Minneapolis, USA) and goat-anti-rabbit-HRP, (AbCam)], and general cell death by TUNEL assay (Click-iT TUNEL Alexa Fluor 488, Thermo Fisher Scientific) in FFPE duodenal and ileal sections counterstained with H & E or DAPI.

    Techniques: Sampling, Staining, TUNEL Assay, Standard Deviation