rabbit anti-cleaved caspase3 Search Results


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  • 99
    Cell Signaling Technology Inc anti cleaved caspase 3
    Increased progenitor cell proliferation and apoptosis in P2ry13 KO mice (young adults). (A–D) Increase in number and proliferative capacity of type 2a cells and type 3 cells in P2ry13 KO mice. (A) From left to right: Double labeling for Tbr2 (green) and DCX (white), Tbr2 (green) and Ki67 (red), Ki67 (red) and DCX (white) and triple labeling for Tbr2 (green), Ki67 (red) and DCX (white). Double-labeled cells are indicated by yellow arrows and triple-labeled cells by yellow arrowheads. (B–D) Resulting quantitative evaluation of the total number of type 2a cells (B) , the total number of proliferating type 2a cells (C) , and the total number of proliferating DCX + cells (D) (six corresponding sections per animal, n = 7). (E) Immunolabeling for cleaved <t>caspase-3</t> (red) in the GCL. DAPI staining is shown in blue. In both genotypes cleaved caspase-3 + cells were exclusively found in the SGZ and in low numbers. (F) Total number of caspase-3 + cells (14 corresponding sections per animal, n = 7). All graphs represent mean ± SEM. * p
    Anti Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 11265 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cell Signaling Technology Inc rabbit anti cleaved caspase 3
    Hyperglycemia is induced without overt β cell death and ROS-mediated stress is seen in surrounding cells of the islet. (A) After treatment with 0.5, 1 and 2.5 µg/ml doxycycline, there was no subsequent increase in <t>Casp3*</t> expression in these embryos. (B) A hyperglycemic phenotype was observed in embryos treated with 1 µg/ml and 2.5 µg/ml doxycycline. n =3. * P
    Rabbit Anti Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 5795 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc cleaved caspase 3
    Effect of trehalose on apoptosis and ERS in cryopreserved valve cells. (A and B) Western blotting using a cleaved <t>caspase-3</t> antibody on cryopreserved valve cells treated with trehalose (0.1 mol/L) or DMSO for 16 weeks. (C, D and E) Western blotting using GRP78 and CHOP antibodies on cryopreserved valves treated with trehalose (0.1 mol/L) for 16 weeks. Data are expressed as the mean ± SD ( n = 20 per group). ** P
    Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 38178 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cleaved caspase 3/product/Cell Signaling Technology Inc
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    Abcam anti active caspase 3 antibody
    DUSP6 overexpression alleviates HG-induced podocyte apoptosis. (A) Apoptotic cells were detected via flow cytometry. (B) The protein expression levels of Bcl-2, Bax, cleaved <t>caspase-3</t> and caspase-3. ***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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    92
    Cell Signaling Technology Inc rabbit polyclonal anti cleaved caspase 3
    Effects of CLU silencing on viability, proliferation/death and differentiation of cultured OA chondrocytes. ( A ) CLU mRNA and protein expression after 48 and 72 hours, respectively, in scramble (control) and siCLU transfected OA-HACs. ( B ) Cell viability by MTT assay after 24, 48 and 72 hours of scramble and siCLU transfected OA-HACs. ( C ) Representative immunocytochemical images and bar graphs showing Ki67 + and p21 + nuclei in cultured OA-HACs and ( D ) cleaved <t>caspase-3</t> + cytospinned OA-HACs after 72 hours of silencing. ( E ) Gene array shows the modulation of NFkB and Stat-3-related genes in siCLU transfected OA-HACs compared with scramble after 48 hours of silencing. Transcript levels were normalized on GAPDH (internal reference gene). ( F ) mRNA levels by Real-Time PCR of COL2A1, ACAN, MMP13, COL10A1, and ( G ) representative blot and densitometric analysis of MMP13 and COL10A1 in scramble and CLU-silenced OA-HACs. Data are expressed as mean values ± SEM of three independent experiments (each using pooled samples from n=3 OA donors) performed in triplicate. Abbreviations: OA-HACs, OA-Human articular chondrocytes; OD, optical density unit; RLU, relative light unit. Student’s t-test: * P
    Rabbit Polyclonal Anti Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 674 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti cleaved caspase3
    t -AUCB administration attenuated mitochondrial dysfunction, ROS production, and apoptosis in tubules of db/db mice. a Kidney sections stained with JC-1. b Kidney sections stained with Mito SOX. c Western blot analysis of Drp1and Mfn2 expression in kidney tissues. d Quantification of the fluorescence intensity of JC-1 staining in figure a. e Quantification of the fluorescence intensity of Mito SOX staining in figure b. f , g Densitometric analysis of Drp1and Mfn2 expression in the figure c. h Kidney sections stained with Oil Red O staining. i Western blot analysis of PGC-1α and CPT1A expression in kidney tissues. j , k Densitometric analysis of PGC-1α and CPT1A expression in figure i. l Western blot analysis of Bax, Cyt c and <t>cleaved-caspase3</t> expression in kidney tissues. m–o Densitometric analysis of Bax, Cyt c and cleaved-caspase3 expression in the figure l. p Representative images of immunofluorescence double labeling of Tom20 and Bax in different kidney tissues. * P
    Rabbit Anti Cleaved Caspase3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 468 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Cell Signaling Technology Inc rabbit monoclonal anti cleaved caspase 3
    TL induced Akt activation in NSCLC. A549 and NCI-H460 cells were treated for 18–24 h ± 50 nM/100 nM TL. Representative immunoblots ( A ) and quantitation ( B , C ) for CAV-1, pAkt (Ser473), Total Akt, Bcl-2, Bax, Cleaved <t>caspase-3</t> (CC-3) and Cleaved-PARP (C-PARP) protein expression. Protein quantity was normalized to β-Actin. Data are presented as mean ± SD. n = 3–4. * indicates significantly different ( p
    Rabbit Monoclonal Anti Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 363 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit anti cleaved caspase 3
    Deprivation of BCAS2 diminishing Delta-Notch activity is apoptosis-independent. The late third instar larval wing discs of each genotype were isolated and immunostained with <t>anti-Caspase-3</t> antibody (blue; A-D); anti-Cut antibody (red, E-H); the expression of GFP, Cut and Caspase-3 were merged (I-L). Images were taken by confocal microscopy, scale bar, 50 μm. (A, E, I) Control ( en > GFP ). (B, F, J ) The p35 over expression wing disc ( en > GFP , p35 ). (C, G, K) The dBCAS2 -depleted wing disc ( en > GFP , dBCAS2 dsRNA ). (D, H, L) The coexpression of p35 and dBCAS2 dsRNA ( en > GFP , dBCAS2 dsRNA , p35 ).
    Rabbit Anti Cleaved Caspase 3, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 177 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit anti cleaved caspase 3 - by Bioz Stars, 2020-09
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    99
    Cell Signaling Technology Inc rabbit polyclonal anti cleaved caspase 3 antibody
    Deprivation of BCAS2 diminishing Delta-Notch activity is apoptosis-independent. The late third instar larval wing discs of each genotype were isolated and immunostained with <t>anti-Caspase-3</t> antibody (blue; A-D); anti-Cut antibody (red, E-H); the expression of GFP, Cut and Caspase-3 were merged (I-L). Images were taken by confocal microscopy, scale bar, 50 μm. (A, E, I) Control ( en > GFP ). (B, F, J ) The p35 over expression wing disc ( en > GFP , p35 ). (C, G, K) The dBCAS2 -depleted wing disc ( en > GFP , dBCAS2 dsRNA ). (D, H, L) The coexpression of p35 and dBCAS2 dsRNA ( en > GFP , dBCAS2 dsRNA , p35 ).
    Rabbit Polyclonal Anti Cleaved Caspase 3 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 216 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti cleaved caspase 3 antibody/product/Cell Signaling Technology Inc
    Average 99 stars, based on 216 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti cleaved caspase 3 antibody - by Bioz Stars, 2020-09
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    Image Search Results


    Increased progenitor cell proliferation and apoptosis in P2ry13 KO mice (young adults). (A–D) Increase in number and proliferative capacity of type 2a cells and type 3 cells in P2ry13 KO mice. (A) From left to right: Double labeling for Tbr2 (green) and DCX (white), Tbr2 (green) and Ki67 (red), Ki67 (red) and DCX (white) and triple labeling for Tbr2 (green), Ki67 (red) and DCX (white). Double-labeled cells are indicated by yellow arrows and triple-labeled cells by yellow arrowheads. (B–D) Resulting quantitative evaluation of the total number of type 2a cells (B) , the total number of proliferating type 2a cells (C) , and the total number of proliferating DCX + cells (D) (six corresponding sections per animal, n = 7). (E) Immunolabeling for cleaved caspase-3 (red) in the GCL. DAPI staining is shown in blue. In both genotypes cleaved caspase-3 + cells were exclusively found in the SGZ and in low numbers. (F) Total number of caspase-3 + cells (14 corresponding sections per animal, n = 7). All graphs represent mean ± SEM. * p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: Disruption of the Microglial ADP Receptor P2Y13 Enhances Adult Hippocampal Neurogenesis

    doi: 10.3389/fncel.2018.00134

    Figure Lengend Snippet: Increased progenitor cell proliferation and apoptosis in P2ry13 KO mice (young adults). (A–D) Increase in number and proliferative capacity of type 2a cells and type 3 cells in P2ry13 KO mice. (A) From left to right: Double labeling for Tbr2 (green) and DCX (white), Tbr2 (green) and Ki67 (red), Ki67 (red) and DCX (white) and triple labeling for Tbr2 (green), Ki67 (red) and DCX (white). Double-labeled cells are indicated by yellow arrows and triple-labeled cells by yellow arrowheads. (B–D) Resulting quantitative evaluation of the total number of type 2a cells (B) , the total number of proliferating type 2a cells (C) , and the total number of proliferating DCX + cells (D) (six corresponding sections per animal, n = 7). (E) Immunolabeling for cleaved caspase-3 (red) in the GCL. DAPI staining is shown in blue. In both genotypes cleaved caspase-3 + cells were exclusively found in the SGZ and in low numbers. (F) Total number of caspase-3 + cells (14 corresponding sections per animal, n = 7). All graphs represent mean ± SEM. * p

    Article Snippet: The following primary antibodies (in 1% BSA + 0.5% Triton X-100/PBS) were applied overnight at 4°C: anti-Ki-67 (M7249, 1:5, Dako Cytomation), anti-Tbr2 (ab183991, 1:200, Abcam), anti-doublecortin (DCX; sc-8066, 1:200, Santa Cruz Biotechnology), anti-cleaved caspase-3 (Asp175; 9661, 1:500, Cell Signaling Technology), anti-glial fibrillary acidic protein (GFAP; G-3893, 1:500 and G-9269, 1:500, both Sigma-Aldrich), anti-GFP (ab13970, 1:500, Abcam), anti-ionized calcium binding adaptor molecule 1 (Iba1; 019-19741, 1:500, Wako Chemicals).

    Techniques: Mouse Assay, Labeling, Immunolabeling, Staining

    Damaged PGCs are eliminated by apoptosis. a-b,  Quantification of the frequency of PGCs (GOF18-GFP + ) and surrounding somatic cells (GOF18-GFP - ) with ( a )  >  5 53BP1 or ( b )  >  10 γ–H2A.X foci per nucleus at E11.5. ( P  value calculated by unpaired 2-tailed  t  test; data represent mean and s.e.m.; at least 100 PGCs or somatic cells were scored per embryo, each point represents data from one embryo, 53BP1  n  = 4, 3, 3, 5, 3 and 3, γ–H2A.X  n  = 3, 3, 3, 4, 4 and 5, left to right).  c , Representative images of E11.5 gonads stained for phospho-Ser15-p53 (pSer15-p53) and GFP (GOF18-GFP). Quantification of PGCs (GOF18-GFP + ) and somatic cells (GOF18-GFP - ) that stain positively for phospho-Ser15-p53 ( P  value calculated by unpaired 2-tailed  t  test; data represent mean and s.e.m.; at least 100 PGCs or somatic cells were scored per embryo, each point represents data from one embryo,  n  = 6, 3, 2, 8, 4 and 7, left to right).  d , Representative images of E11.5 gonads stained for the marker of apoptosis cleaved-Caspase 3 and GFP (GOF18-GFP) and the quantification of the frequency of PGCs (GOF18-GFP + ) and somatic cells (GOF18-GFP - ) that stain positively for cleaved-Caspase 3 ( P  value calculated by unpaired 2-tailed  t  test; data represent mean and s.e.m., at least 100 PGCs or somatic cells were scored per embryo, each point represents data from one embryo,  n  = 10, 3, 3, 8, 4 and 4, left to right).

    Journal: Nature genetics

    Article Title: DNA crosslink repair safeguards genomic stability during pre-meiotic germ cell development

    doi: 10.1038/s41588-019-0471-2

    Figure Lengend Snippet: Damaged PGCs are eliminated by apoptosis. a-b, Quantification of the frequency of PGCs (GOF18-GFP + ) and surrounding somatic cells (GOF18-GFP - ) with ( a ) > 5 53BP1 or ( b ) > 10 γ–H2A.X foci per nucleus at E11.5. ( P value calculated by unpaired 2-tailed t test; data represent mean and s.e.m.; at least 100 PGCs or somatic cells were scored per embryo, each point represents data from one embryo, 53BP1 n = 4, 3, 3, 5, 3 and 3, γ–H2A.X n = 3, 3, 3, 4, 4 and 5, left to right). c , Representative images of E11.5 gonads stained for phospho-Ser15-p53 (pSer15-p53) and GFP (GOF18-GFP). Quantification of PGCs (GOF18-GFP + ) and somatic cells (GOF18-GFP - ) that stain positively for phospho-Ser15-p53 ( P value calculated by unpaired 2-tailed t test; data represent mean and s.e.m.; at least 100 PGCs or somatic cells were scored per embryo, each point represents data from one embryo, n = 6, 3, 2, 8, 4 and 7, left to right). d , Representative images of E11.5 gonads stained for the marker of apoptosis cleaved-Caspase 3 and GFP (GOF18-GFP) and the quantification of the frequency of PGCs (GOF18-GFP + ) and somatic cells (GOF18-GFP - ) that stain positively for cleaved-Caspase 3 ( P value calculated by unpaired 2-tailed t test; data represent mean and s.e.m., at least 100 PGCs or somatic cells were scored per embryo, each point represents data from one embryo, n = 10, 3, 3, 8, 4 and 4, left to right).

    Article Snippet: Slides were blocked in PBS, 1% w/v BSA, 1% w/v Triton X-100 for 30 minutes at room temperature before being incubated overnight at 4 °C with the following primary antibodies diluted in blocking buffer; anti-GFP 1:500 (Nacalai, GF090R), anti-γ-H2A.X 1:1,000 (Millipore, JBW301), anti-53BP1 1:1,000 (Novus, NB100-304), anti-cleaved Caspase-3 1:400 (Cell Signaling Technology, 9661), anti-phospho-p53 (Ser15) 1:500 (Cell Signaling Technology, D4S1H).

    Techniques: Staining, Marker

    Quantitative analysis of cleaved caspase-3 + cells per high power field (HPF) ( a ) and of BrdU + hepatocytes per HPF ( b ) in liver tissue of sham-treated, of combination (combi)-treated as well as of mono (HPβCD)-treated Npc1 +/+ (sham, n = 7 (BrdU n = 3); combi, n = 9 (BrdU n = 3); mono, n = 15 (BrdU n = 3) and Npc1 −/− mice (sham, n = 10 (BrdU n = 3); combi, n = 10 (BrdU n = 3); mono, n = 11 (BrdU n = 3)) with representative light microscopic images of liver tissue of sham-treated, combi-treated and mono-treated Npc1 −/− mice. Note the significant reduction of apoptosis and proliferation in combi-treated Npc1 −/− mice. Values are given as mean ± SEM; ANOVA; post-hoc pairwise comparison tests: * p

    Journal: International Journal of Molecular Sciences

    Article Title: Evaluation of Two Liver Treatment Strategies in a Mouse Model of Niemann–Pick-Disease Type C1

    doi: 10.3390/ijms19040972

    Figure Lengend Snippet: Quantitative analysis of cleaved caspase-3 + cells per high power field (HPF) ( a ) and of BrdU + hepatocytes per HPF ( b ) in liver tissue of sham-treated, of combination (combi)-treated as well as of mono (HPβCD)-treated Npc1 +/+ (sham, n = 7 (BrdU n = 3); combi, n = 9 (BrdU n = 3); mono, n = 15 (BrdU n = 3) and Npc1 −/− mice (sham, n = 10 (BrdU n = 3); combi, n = 10 (BrdU n = 3); mono, n = 11 (BrdU n = 3)) with representative light microscopic images of liver tissue of sham-treated, combi-treated and mono-treated Npc1 −/− mice. Note the significant reduction of apoptosis and proliferation in combi-treated Npc1 −/− mice. Values are given as mean ± SEM; ANOVA; post-hoc pairwise comparison tests: * p

    Article Snippet: For immunohistochemical analysis of cleaved caspase-3+ cells, F4/80+ von Kupffer cells (resident liver macrophages) and BrdU+ hepatocytes sections were pre-treated with citrate puffer (pH 6.0) in the microwave (700 W for 7 min) and were either exposed to a rabbit anti-cleaved caspase-3 antibody (1:500, Cell Signaling Technology, Frankfurt, Germany), a rat anti-F4/80 (1:10; Serotec, Oxford, UK) or a mouse anti-BrdU antiserum (1:50; DakoCytomation, Dako, Hamburg, Germany).

    Techniques: Mouse Assay

    Compound C abolished melatonin-induced cardioprotective effect on myocardial ischemia/reperfusion injury in type 1 diabetic rats. Myocardial ischemia/reperfusion surgery was performed after 1 month of streptozotocin injection. ( a ) Left ventricular systolic pressure. ( b ) and ( c ) The first derivative of left ventricular pressure (+dP/dt max and −dP/dt max ). Cardiac functional data was continuously monitored during the ischemia (30 min) and reperfusion period (3 hours). ( d ) Myocardial infarct size. ( e ) In situ detection of apoptotic cardiomyocytes by TUNEL staining (200×). ( f ) Myocardial apoptotic index. ( g ) Representative blots. ( h ) caspase-3 expression. ( i ) Bcl-2 expression. ( j ) Bax expression. ( k ) Cleaved caspase-3 expression. The depicted data are the means ± SEM, n = 6/group. ## P

    Journal: Scientific Reports

    Article Title: Melatonin ameliorates myocardial ischemia/reperfusion injury in type 1 diabetic rats by preserving mitochondrial function: role of AMPK-PGC-1α-SIRT3 signaling

    doi: 10.1038/srep41337

    Figure Lengend Snippet: Compound C abolished melatonin-induced cardioprotective effect on myocardial ischemia/reperfusion injury in type 1 diabetic rats. Myocardial ischemia/reperfusion surgery was performed after 1 month of streptozotocin injection. ( a ) Left ventricular systolic pressure. ( b ) and ( c ) The first derivative of left ventricular pressure (+dP/dt max and −dP/dt max ). Cardiac functional data was continuously monitored during the ischemia (30 min) and reperfusion period (3 hours). ( d ) Myocardial infarct size. ( e ) In situ detection of apoptotic cardiomyocytes by TUNEL staining (200×). ( f ) Myocardial apoptotic index. ( g ) Representative blots. ( h ) caspase-3 expression. ( i ) Bcl-2 expression. ( j ) Bax expression. ( k ) Cleaved caspase-3 expression. The depicted data are the means ± SEM, n = 6/group. ## P

    Article Snippet: Then, they were transferred to polyvinylidene difluoride membrane (Millipore, USA) and incubated overnight (4 °C) with p-AMPK, AMPK, PGC-1α, Bcl-2, Bax, caspase-3 and cleaved caspase-3 antibodies (Cell Signaling Technology, MA, USA, 1:1000 dilution), SIRT3, SOD2, NRF1, TFAM, cytochrome c and β-actin antibodies (Santa Cruz, CA, USA, 1:500 dilution) and total OXPHOS antibody cocktail (Abcam biotechnology, Cambridge, UK, 1:1000 dilution).

    Techniques: Injection, Functional Assay, In Situ, TUNEL Assay, Staining, Expressing

    Compound C and SIRT3 siRNA transfection blunted melatonin-induced anti-apoptotic effect against SIR injury in high glucose medium treated H9c2 cells. The H9c2 cells were exposed to high glucose medium (33 mmol/l) for 6 hours before the SIR treatment and during the entire reperfusion period (4 hours). HG-treatment was co-administered with or without melatonin (10 μmol/l) to evaluate its cytoprotective effect. Compound C (3 μmol/l) was administered for 6 hours before the SIR exposure to inhibit the AMPK signaling. ( a ) Cellular viability was presented by dividing the optical density of samples with that of the HG group. ( b ) Representative images of TUNEL staining (200×). ( c ) Percentage of TUNEL positive nuclei. ( d ) Cellular morphology (200×). ( e ) Representative blots. ( f ) Caspase-3 expression. ( g ) Cleaved caspase-3 expression. The depicted data are the means ± SEM, n = 6/group. ρρ P

    Journal: Scientific Reports

    Article Title: Melatonin ameliorates myocardial ischemia/reperfusion injury in type 1 diabetic rats by preserving mitochondrial function: role of AMPK-PGC-1α-SIRT3 signaling

    doi: 10.1038/srep41337

    Figure Lengend Snippet: Compound C and SIRT3 siRNA transfection blunted melatonin-induced anti-apoptotic effect against SIR injury in high glucose medium treated H9c2 cells. The H9c2 cells were exposed to high glucose medium (33 mmol/l) for 6 hours before the SIR treatment and during the entire reperfusion period (4 hours). HG-treatment was co-administered with or without melatonin (10 μmol/l) to evaluate its cytoprotective effect. Compound C (3 μmol/l) was administered for 6 hours before the SIR exposure to inhibit the AMPK signaling. ( a ) Cellular viability was presented by dividing the optical density of samples with that of the HG group. ( b ) Representative images of TUNEL staining (200×). ( c ) Percentage of TUNEL positive nuclei. ( d ) Cellular morphology (200×). ( e ) Representative blots. ( f ) Caspase-3 expression. ( g ) Cleaved caspase-3 expression. The depicted data are the means ± SEM, n = 6/group. ρρ P

    Article Snippet: Then, they were transferred to polyvinylidene difluoride membrane (Millipore, USA) and incubated overnight (4 °C) with p-AMPK, AMPK, PGC-1α, Bcl-2, Bax, caspase-3 and cleaved caspase-3 antibodies (Cell Signaling Technology, MA, USA, 1:1000 dilution), SIRT3, SOD2, NRF1, TFAM, cytochrome c and β-actin antibodies (Santa Cruz, CA, USA, 1:500 dilution) and total OXPHOS antibody cocktail (Abcam biotechnology, Cambridge, UK, 1:1000 dilution).

    Techniques: Transfection, TUNEL Assay, Staining, Expressing

    (A) Representative images of cleaved caspase-3 immunohistochemistry in the hippocampal CA1 region of WT, NOS3 −/− , sGCα1 −/− , and NOS3 −/− CSTg. Size bar indicates 50 μm. (B) Number of TUNEL-positive

    Journal: Critical care medicine

    Article Title: Protective effects of nitric oxide synthase 3 and soluble guanylate cyclase on the outcome of cardiac arrest and cardiopulmonary resuscitation in mice

    doi: 10.1097/CCM.0b013e318192face

    Figure Lengend Snippet: (A) Representative images of cleaved caspase-3 immunohistochemistry in the hippocampal CA1 region of WT, NOS3 −/− , sGCα1 −/− , and NOS3 −/− CSTg. Size bar indicates 50 μm. (B) Number of TUNEL-positive

    Article Snippet: Activation of caspase-3 was assessed by immunohistochemistry in paraffin-embedded brain sections using anti-cleaved caspase-3 antibody (1:80, polyclonal rabbit anti-cleaved caspase-3 antibody, Cell Signaling) according to the protocol recommended by the manufacturer.

    Techniques: Immunohistochemistry, TUNEL Assay

    The knockout of TEM8 inhibits breast and colorectal cancer growth and prolongs survival in vivo ( A ) Average volume of MDA orthotopic tumors over time. Statistical significance was assessed by Unpaired two-tailed t -test. The graph represents two independent experiments of n = 4 and n = 5 tumors per group, p = 0.0002. ( B ) MDA survival curves. Statistical significance was assessed by Log rank test, p ≤ 0.0001. ( C ) Average volume of SW620 subcutaneous tumors over time. Statistical significance was assessed by Unpaired two-tailed t -test, two independent experiments of n = 6 tumors per group, p = 0.0382, ( D ) SW620 survival curves. Statistical significance was assessed by Log rank test, two independent experiments of n = 3 mice per group, p = 0.0108. ( E ) TEM8 expression in TEM8 KO and control tumors was assessed by IHC. ( F ) IHC of cleaved caspase 3 in TEM8 KO and control tumors (left). Quantification of cleaved caspase 3 expression (right). Statistical significance was assessed by Unpaired two-tailed t -test n = 4 tumors, not significant (ns). ( G ) IHC of Ki67 expression in TEM8 KO and control tumors (left). Quantification of Ki67 expression (right). Statistical significance was assessed by Unpaired two-tailed t -test, n = 4 tumors, ns. (A+C) Data represented as mean + SEM. ( F – G ) Data represented as mean ± SEM.

    Journal: Oncotarget

    Article Title: Tumor endothelial marker 8 promotes cancer progression and metastasis

    doi: 10.18632/oncotarget.25734

    Figure Lengend Snippet: The knockout of TEM8 inhibits breast and colorectal cancer growth and prolongs survival in vivo ( A ) Average volume of MDA orthotopic tumors over time. Statistical significance was assessed by Unpaired two-tailed t -test. The graph represents two independent experiments of n = 4 and n = 5 tumors per group, p = 0.0002. ( B ) MDA survival curves. Statistical significance was assessed by Log rank test, p ≤ 0.0001. ( C ) Average volume of SW620 subcutaneous tumors over time. Statistical significance was assessed by Unpaired two-tailed t -test, two independent experiments of n = 6 tumors per group, p = 0.0382, ( D ) SW620 survival curves. Statistical significance was assessed by Log rank test, two independent experiments of n = 3 mice per group, p = 0.0108. ( E ) TEM8 expression in TEM8 KO and control tumors was assessed by IHC. ( F ) IHC of cleaved caspase 3 in TEM8 KO and control tumors (left). Quantification of cleaved caspase 3 expression (right). Statistical significance was assessed by Unpaired two-tailed t -test n = 4 tumors, not significant (ns). ( G ) IHC of Ki67 expression in TEM8 KO and control tumors (left). Quantification of Ki67 expression (right). Statistical significance was assessed by Unpaired two-tailed t -test, n = 4 tumors, ns. (A+C) Data represented as mean + SEM. ( F – G ) Data represented as mean ± SEM.

    Article Snippet: Slides were rinsed in TBS with 0.5% Triton-X 100 (TBS-Tx) and incubated in 100 μl Antibody Diluent with background reducing agents (DAKO, Copenhagen, DK) and primary antibodies (rabbit anti-human TEM8 (ab21270, Abcam) at 1:300 dilution, rabbit anti-human cleaved caspase 3 (D175, Cell Signaling Technology) at 1:500 dilution, rabbit anti-human Ki67 (ab92742, Abcam) at 1:1000 dilution, hamster anti-human CD31/ PECAM-1 (MA3105, Thermo Fisher) at 1:100 dilution, rabbit anti-human PanCytokeratin (PanCK) (ab9377, Abcam) at 1:100 dilution) as appropriate at 4° C overnight.

    Techniques: Knock-Out, In Vivo, Multiple Displacement Amplification, Two Tailed Test, Mouse Assay, Expressing, Immunohistochemistry

    HCV infection activates DR4/DR5-dependent caspase cascade. (A) Western blot analysis of Bax and cleaved caspase-8, caspase-9, and caspase-3 in HCV-infected cells. Huh7.5.1 cells infected with HCVcc in the absence or presence of recombinant TRAIL (100 ng/ml) were used for Western blot analysis with antibodies against the indicated proteins. β-actin was used as an internal loading control. Samples: MC, media control. (B and D) Silencing DR4 and DR5 prevent caspase-9 cleavage and caspase-3/7 activity induced by HCV infection. Huh7.5.1 cells transfected with non-targeting (NT) or gene-specific (ST) siRNA pools targeting DR4 and DR5, respectively, were infected with HCVcc. At 3 days post-infection, the mRNA levels of DR4 and DR5 were analyzed by real-time qRT-PCR (B) (mean±SD; n = 3; *p

    Journal: PLoS ONE

    Article Title: TRAIL Enhances Apoptosis of Human Hepatocellular Carcinoma Cells Sensitized by Hepatitis C Virus Infection: Therapeutic Implications

    doi: 10.1371/journal.pone.0098171

    Figure Lengend Snippet: HCV infection activates DR4/DR5-dependent caspase cascade. (A) Western blot analysis of Bax and cleaved caspase-8, caspase-9, and caspase-3 in HCV-infected cells. Huh7.5.1 cells infected with HCVcc in the absence or presence of recombinant TRAIL (100 ng/ml) were used for Western blot analysis with antibodies against the indicated proteins. β-actin was used as an internal loading control. Samples: MC, media control. (B and D) Silencing DR4 and DR5 prevent caspase-9 cleavage and caspase-3/7 activity induced by HCV infection. Huh7.5.1 cells transfected with non-targeting (NT) or gene-specific (ST) siRNA pools targeting DR4 and DR5, respectively, were infected with HCVcc. At 3 days post-infection, the mRNA levels of DR4 and DR5 were analyzed by real-time qRT-PCR (B) (mean±SD; n = 3; *p

    Article Snippet: Primary antibodies used in this study include the following: rabbit monoclonal anti-cleaved PARP (Cell signaling Technology); mouse monoclonal anti-DR4 (Abcam); rabbit monoclonal anti-DR5 (Cell signaling Technology); rabbit monoclonal anti-cleaved caspase-3 (Cell signaling Technology); rabbit monoclonal anti-cleaved caspase-8 (Cell signaling Technology); rabbit monoclonal anti-cleaved caspase-9 (Cell signaling Technology); rabbit monoclonal anti-cleaved Bid (Invitrogen); mouse monoclonal anti-HCV core (Thermo Fisher Scientific); mouse monoclonal anti-α-tubulin (Sigma); mouse monoclonal anti-β-actin (Sigma).

    Techniques: Infection, Western Blot, Recombinant, Activity Assay, Transfection, Quantitative RT-PCR

    Expression of Nanog and Oct4 in apoptotic cells of hESC treated with nocodazole. hESC cells were treated with nocodazole as described in Figure 3 . Cells were fixed and stained with anti-Nanog (PE), anti-Oct4 (Alexa Fluor 647) and anti-cleaved caspase-3 (detected with anti-rabbit IgG conjugated with Alexa 488) antibodies. (A) Expression of Nanog and (B) Oct4 in cleaved-caspase-3-positive cells. For analysis cellular debris and doublets were excluded. Results are shown as contour plots and are representative of two independent experiments.

    Journal: PLoS ONE

    Article Title: Nocodazole Treatment Decreases Expression of Pluripotency Markers Nanog and Oct4 in Human Embryonic Stem Cells

    doi: 10.1371/journal.pone.0019114

    Figure Lengend Snippet: Expression of Nanog and Oct4 in apoptotic cells of hESC treated with nocodazole. hESC cells were treated with nocodazole as described in Figure 3 . Cells were fixed and stained with anti-Nanog (PE), anti-Oct4 (Alexa Fluor 647) and anti-cleaved caspase-3 (detected with anti-rabbit IgG conjugated with Alexa 488) antibodies. (A) Expression of Nanog and (B) Oct4 in cleaved-caspase-3-positive cells. For analysis cellular debris and doublets were excluded. Results are shown as contour plots and are representative of two independent experiments.

    Article Snippet: Antibodies and reagents Alexa-488-labelled anti-H3 antibodies specific for Ser10 phosphorylation, phospho-Ser28-specific anti-H3 antibodies, Alexa-488-labelled anti-p53 antibodies and anti-cleaved caspase-3 antibodies were obtained from Cell Signaling Technology (Beverly, MA).

    Techniques: Expressing, Staining

    Expression of migration and apoptosis-associated proteins in lung cancer cell lines following treatment with gefitinib with or without Rg3. Protein expression levels of caspase-3, Bax, Bcl-2, E-cadherin, SLUG, SNAIL and GAPDH were determined using western blot analysis in (A) A549 and (B) H1299 cells treated with gefitinib (10 µM) with or without Rg3 (12.5 µg/ml) for 24 h. Rg3, ginsenoside Rg3; H1299 and A549, non-small cell lung cancer cell lines. Bax, Bcl-2-associated X; Bcl-2, B-cell lymphoma 2; SLUG, snail family transcriptional repressor 2; SNAIL, snail family transcriptional repressor 1.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Ginsenoside Rg3 promotes the antitumor activity of gefitinib in lung cancer cell lines

    doi: 10.3892/etm.2018.7001

    Figure Lengend Snippet: Expression of migration and apoptosis-associated proteins in lung cancer cell lines following treatment with gefitinib with or without Rg3. Protein expression levels of caspase-3, Bax, Bcl-2, E-cadherin, SLUG, SNAIL and GAPDH were determined using western blot analysis in (A) A549 and (B) H1299 cells treated with gefitinib (10 µM) with or without Rg3 (12.5 µg/ml) for 24 h. Rg3, ginsenoside Rg3; H1299 and A549, non-small cell lung cancer cell lines. Bax, Bcl-2-associated X; Bcl-2, B-cell lymphoma 2; SLUG, snail family transcriptional repressor 2; SNAIL, snail family transcriptional repressor 1.

    Article Snippet: The membranes were blocked in 5% fat-free milk for 1 h at room temperature and incubated overnight at 4°C with primary antibodies against cleaved-caspase-3 (1:1,000; cat. no. 9661; CST Biological Reagents Co., Ltd., Shanghai, China), snail family transcriptional repressor 1 (SNAIL; 1:500; cat. no. sc-393172), snail family transcriptional repressor 2 (SLUG; 1:500; cat. no. sc-166476), Bcl-2-associated X (Bax; 1:200; cat. no. sc-49; all Santa Cruz Biotechnology, Inc., Dallas, TX, USA), E-cadherin (1:1,000; cat. no. ab15148), B-cell lymphoma 2 (Bcl-2; 1:1,000; cat. no. ab194583), and GAPDH (1:5,000; cat. no. ab181602: All Abcam, Cambridge, UK).

    Techniques: Expressing, Migration, Western Blot

    Effect of TFF3 silencing on the expression of activated caspase-3 and Annexin V. a Active caspase-3 levels were significantly elevated in both siTFF3-treated cells compared with siCtrl-treated cells. * P

    Journal: Experimental & Molecular Medicine

    Article Title: Overexpression of TFF3 is involved in prostate carcinogenesis via blocking mitochondria-mediated apoptosis

    doi: 10.1038/s12276-018-0137-7

    Figure Lengend Snippet: Effect of TFF3 silencing on the expression of activated caspase-3 and Annexin V. a Active caspase-3 levels were significantly elevated in both siTFF3-treated cells compared with siCtrl-treated cells. * P

    Article Snippet: After blocking with 1% BSA in TBS, the cells were incubated overnight at 4 ℃ with primary antibodies, including a rabbit polyclonal anti-TFF3 antibody (Santa Cruz), a rabbit monoclonal anti-cleaved caspase-3 antibody (Cell Signaling Technology), a mouse monoclonal anti-cytochrome c antibody (Santa Cruz) and a goat polyclonal anti-Smac antibody (Santa Cruz).

    Techniques: Expressing

    Schematic summary of the potential TFF3-associated molecular mechanism for prostate carcinogenesis. Overexpressed TFF3 activates the PI3K/AKT pathway, which blocks the mitochondria-induced apoptotic pathway and eventually induces prostate tumorigenesis. TFF3 silencing inhibits the phosphorylation of AKT-1 and the expression of BCL2, which increases the expression and mitochondrial translocation of BAX, and subsequently, the expression of proapoptotic proteins (cytochrome C and Smac/DIABLO) in the mitochondria and their release into the cytosol are elevated. In the cytosol, the elevated proapoptotic proteins activate caspase-9 and caspase-3 and induce apoptotic cell death

    Journal: Experimental & Molecular Medicine

    Article Title: Overexpression of TFF3 is involved in prostate carcinogenesis via blocking mitochondria-mediated apoptosis

    doi: 10.1038/s12276-018-0137-7

    Figure Lengend Snippet: Schematic summary of the potential TFF3-associated molecular mechanism for prostate carcinogenesis. Overexpressed TFF3 activates the PI3K/AKT pathway, which blocks the mitochondria-induced apoptotic pathway and eventually induces prostate tumorigenesis. TFF3 silencing inhibits the phosphorylation of AKT-1 and the expression of BCL2, which increases the expression and mitochondrial translocation of BAX, and subsequently, the expression of proapoptotic proteins (cytochrome C and Smac/DIABLO) in the mitochondria and their release into the cytosol are elevated. In the cytosol, the elevated proapoptotic proteins activate caspase-9 and caspase-3 and induce apoptotic cell death

    Article Snippet: After blocking with 1% BSA in TBS, the cells were incubated overnight at 4 ℃ with primary antibodies, including a rabbit polyclonal anti-TFF3 antibody (Santa Cruz), a rabbit monoclonal anti-cleaved caspase-3 antibody (Cell Signaling Technology), a mouse monoclonal anti-cytochrome c antibody (Santa Cruz) and a goat polyclonal anti-Smac antibody (Santa Cruz).

    Techniques: Expressing, Translocation Assay

    Hyperglycemia is induced without overt β cell death and ROS-mediated stress is seen in surrounding cells of the islet. (A) After treatment with 0.5, 1 and 2.5 µg/ml doxycycline, there was no subsequent increase in Casp3* expression in these embryos. (B) A hyperglycemic phenotype was observed in embryos treated with 1 µg/ml and 2.5 µg/ml doxycycline. n =3. * P

    Journal: Disease Models & Mechanisms

    Article Title: A novel Cre-enabled tetracycline-inducible transgenic system for tissue-specific cytokine expression in the zebrafish: CETI-PIC3

    doi: 10.1242/dmm.042556

    Figure Lengend Snippet: Hyperglycemia is induced without overt β cell death and ROS-mediated stress is seen in surrounding cells of the islet. (A) After treatment with 0.5, 1 and 2.5 µg/ml doxycycline, there was no subsequent increase in Casp3* expression in these embryos. (B) A hyperglycemic phenotype was observed in embryos treated with 1 µg/ml and 2.5 µg/ml doxycycline. n =3. * P

    Article Snippet: The following primary antibodies were used: mouse anti-Tnfa (1:50; Abcam #52B83), guinea pig anti-Insulin (1:200; Invitrogen #180067), rabbit anti-Glucagon (1:50; Sigma-Aldrich #SAB4200685) and rabbit anti-Cleaved caspase 3 (1:100; Cell Signaling Technologies #9661S).

    Techniques: Expressing

    Adeno-associated virus (AAV)-AEG-1 transduction of dopaminergic (DA) neurons in the in vivo SN of healthy mice. a Experimental schematic and the immunostaining for green fluorescent protein (GFP; green) and hemagglutinin (HA; brown) in the SNpc, which is outlined by the dotted elliptical shape, which was conducted following each viral injection. Scale bar, 200 μm. b Representative double immunofluorescent labeling of TH (red) and GFP (green) or TH and HA (green) in the SNpc. Scale bar, 20 μm. c Representative double immunofluorescent labeling for glial fibrillary acidic protein (GFAP)/ionized calcium binding adaptor molecule 1 (Iba1; red), which are markers of astrocytes and microglia, respectively, and GFP/HA (green) in the SNpc of healthy mice. Scale bar, 20 μm. d Immunostaining for TH in the SN and striatum (STR). Scale bars, 200 μm (black) and 50 μm (white) for the SN, and 1000 μm for the STR. e , f The number and optical density of the nigral TH-positive neurons and striatal TH-positive fibers, respectively (one-way ANOVA with Tukey’s post hoc test; n = 4 for each group). CON contralateral side, IPSI ipsilateral side. g Western blot analyses of the levels of cleaved caspase-3 (c-caspase-3) and cleaved poly (ADP-ribose) polymerase 1 (c-PARP-1) following AEG-1 transduction in the SN of healthy brains. * p = 0.005 vs . CON (one-way ANOVA with Tukey’s post hoc test; n = 4 for each group)

    Journal: Cell Death & Disease

    Article Title: Upregulation of neuronal astrocyte elevated gene-1 protects nigral dopaminergic neurons in vivo

    doi: 10.1038/s41419-018-0491-3

    Figure Lengend Snippet: Adeno-associated virus (AAV)-AEG-1 transduction of dopaminergic (DA) neurons in the in vivo SN of healthy mice. a Experimental schematic and the immunostaining for green fluorescent protein (GFP; green) and hemagglutinin (HA; brown) in the SNpc, which is outlined by the dotted elliptical shape, which was conducted following each viral injection. Scale bar, 200 μm. b Representative double immunofluorescent labeling of TH (red) and GFP (green) or TH and HA (green) in the SNpc. Scale bar, 20 μm. c Representative double immunofluorescent labeling for glial fibrillary acidic protein (GFAP)/ionized calcium binding adaptor molecule 1 (Iba1; red), which are markers of astrocytes and microglia, respectively, and GFP/HA (green) in the SNpc of healthy mice. Scale bar, 20 μm. d Immunostaining for TH in the SN and striatum (STR). Scale bars, 200 μm (black) and 50 μm (white) for the SN, and 1000 μm for the STR. e , f The number and optical density of the nigral TH-positive neurons and striatal TH-positive fibers, respectively (one-way ANOVA with Tukey’s post hoc test; n = 4 for each group). CON contralateral side, IPSI ipsilateral side. g Western blot analyses of the levels of cleaved caspase-3 (c-caspase-3) and cleaved poly (ADP-ribose) polymerase 1 (c-PARP-1) following AEG-1 transduction in the SN of healthy brains. * p = 0.005 vs . CON (one-way ANOVA with Tukey’s post hoc test; n = 4 for each group)

    Article Snippet: Materials Materials were purchased from the following companies: 6-OHDA (Sigma, St Louis, MO), desipramine (Sigma), l -ascorbic acid (Sigma), rabbit anti-TH (Pel-Freez, Brown Deer, WI), mouse anti-TH (R & D Systems, Minneapolis, MN), rabbit anti-Iba1 (Wako Pure Chemical Industries, Osaka, Japan), rabbit anti-GFAP (Millipore, Billerica, MA), rabbit anti-AEG-1 (Invitrogen, Camarillo, CA), rabbit anti-GFP (Millipore), mouse anti-HA (Cell Signaling, Beverly, MA), rabbit anti-HA (Cell Signaling), rabbit anti-FLAG (Sigma), rabbit anti-caspase-3 (Cell Signaling), rabbit anti-cleaved caspase-3 (Cell Signaling), rabbit anti-PARP-1 (Cell Signaling), rabbit anti-cleaved PARP-1 (Cell Signaling), rabbit anti-LC3B (Cell Signaling), rabbit anti-4E-BP1 (Cell Signaling), rabbit anti-p-4E-BP1 (Cell Signaling), mouse anti-NeuN (Millipore), rabbit anti-Akt (Cell Signaling), rabbit anti-p-Akt (Cell Signaling), rabbit anti-β-actin (Cell Signaling), rabbit anti-α-tubulin (Cell Signaling), mouse anti-Bcl-2 (Santa Cruz Biotechnology, Santa Cruz, CA), mouse anti-Bax (Santa Cruz Biotechnology), rabbit anti-p62/SQSTM1 (Sigma), biotinylated anti-rabbit IgG (Vector laboratories, Burlingame, CA), Texas Red-conjugated anti-rabbit/mouse IgG (Vector Laboratories), fluorescein (FITC)-conjugated anti-mouse IgG (Vector Laboratories), FITC-conjugated anti-rabbit IgG (Jackson ImmunoResearch Laboratories, Bar Harbor, ME), horseradish peroxidase (HRP)-conjugated anti-rabbit IgG (Enzo Life Sciences, Farmingdale, NY) and HRP-conjugated anti-mouse IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Transduction, In Vivo, Mouse Assay, Immunostaining, Injection, Labeling, Binding Assay, Western Blot

    Anti-apoptotic effects of AEG-1 transduction in DA neurons on 6-OHDA neurotoxicity. a Western blot analyses show a significant increase in the levels of caspase-3, c-caspase-3, and c-PARP1 in the postmortem tissues of patients with PD compared with CON. p = 0.014 for caspase-3, p = 0.019 for c-caspase-3, and p = 0.009 for c-PARP-1, vs . CON ( t -test; n = 4 for each group). b Experimental schematic for Fig. 3c, d. c Representative double immunofluorescence labeling for TH (red) and c-caspase-3 (green) or TH and c-PARP-1 (green) in the mouse SN. AEG-1 upregulation induces reductions in the levels of expression of both c-caspase-3 and c-PARP-1 in TH-positive DA neurons in the SN with 6-OHDA neurotoxicity. Scale bar, 20 μm. d Western blot analyses of the levels of c-caspase-3 and c-PARP-1 in the SN 2 days after 6-OHDA treatment. * p = 0.029, ** p = 0.025, # p = 0.032, and ## p = 0.016 vs . CON; *** p = 0.009 and ### p = 0.002 vs . 6-OHDA alone (one-way ANOVA with Tukey’s post hoc test; n = 4 for each group)

    Journal: Cell Death & Disease

    Article Title: Upregulation of neuronal astrocyte elevated gene-1 protects nigral dopaminergic neurons in vivo

    doi: 10.1038/s41419-018-0491-3

    Figure Lengend Snippet: Anti-apoptotic effects of AEG-1 transduction in DA neurons on 6-OHDA neurotoxicity. a Western blot analyses show a significant increase in the levels of caspase-3, c-caspase-3, and c-PARP1 in the postmortem tissues of patients with PD compared with CON. p = 0.014 for caspase-3, p = 0.019 for c-caspase-3, and p = 0.009 for c-PARP-1, vs . CON ( t -test; n = 4 for each group). b Experimental schematic for Fig. 3c, d. c Representative double immunofluorescence labeling for TH (red) and c-caspase-3 (green) or TH and c-PARP-1 (green) in the mouse SN. AEG-1 upregulation induces reductions in the levels of expression of both c-caspase-3 and c-PARP-1 in TH-positive DA neurons in the SN with 6-OHDA neurotoxicity. Scale bar, 20 μm. d Western blot analyses of the levels of c-caspase-3 and c-PARP-1 in the SN 2 days after 6-OHDA treatment. * p = 0.029, ** p = 0.025, # p = 0.032, and ## p = 0.016 vs . CON; *** p = 0.009 and ### p = 0.002 vs . 6-OHDA alone (one-way ANOVA with Tukey’s post hoc test; n = 4 for each group)

    Article Snippet: Materials Materials were purchased from the following companies: 6-OHDA (Sigma, St Louis, MO), desipramine (Sigma), l -ascorbic acid (Sigma), rabbit anti-TH (Pel-Freez, Brown Deer, WI), mouse anti-TH (R & D Systems, Minneapolis, MN), rabbit anti-Iba1 (Wako Pure Chemical Industries, Osaka, Japan), rabbit anti-GFAP (Millipore, Billerica, MA), rabbit anti-AEG-1 (Invitrogen, Camarillo, CA), rabbit anti-GFP (Millipore), mouse anti-HA (Cell Signaling, Beverly, MA), rabbit anti-HA (Cell Signaling), rabbit anti-FLAG (Sigma), rabbit anti-caspase-3 (Cell Signaling), rabbit anti-cleaved caspase-3 (Cell Signaling), rabbit anti-PARP-1 (Cell Signaling), rabbit anti-cleaved PARP-1 (Cell Signaling), rabbit anti-LC3B (Cell Signaling), rabbit anti-4E-BP1 (Cell Signaling), rabbit anti-p-4E-BP1 (Cell Signaling), mouse anti-NeuN (Millipore), rabbit anti-Akt (Cell Signaling), rabbit anti-p-Akt (Cell Signaling), rabbit anti-β-actin (Cell Signaling), rabbit anti-α-tubulin (Cell Signaling), mouse anti-Bcl-2 (Santa Cruz Biotechnology, Santa Cruz, CA), mouse anti-Bax (Santa Cruz Biotechnology), rabbit anti-p62/SQSTM1 (Sigma), biotinylated anti-rabbit IgG (Vector laboratories, Burlingame, CA), Texas Red-conjugated anti-rabbit/mouse IgG (Vector Laboratories), fluorescein (FITC)-conjugated anti-mouse IgG (Vector Laboratories), FITC-conjugated anti-rabbit IgG (Jackson ImmunoResearch Laboratories, Bar Harbor, ME), horseradish peroxidase (HRP)-conjugated anti-rabbit IgG (Enzo Life Sciences, Farmingdale, NY) and HRP-conjugated anti-mouse IgG (Thermo Fisher Scientific, Rockford, IL).

    Techniques: Transduction, Western Blot, Immunofluorescence, Labeling, Expressing

    Apoptosis of MIN6 cells induced by TM is inhibited by overexpression of DHCR24. (a) A representative fluorescent image of cleaved caspase-3 (green) was obtained by IC analysis 24 h after TM exposure. Scale bar, 50 μ m. (b) The relative fluorescence intensity of cleaved caspase-3 was analyzed with ImageJ software. Mean ± S.D. ( n = 3); ∗ p

    Journal: Journal of Diabetes Research

    Article Title: 3β-Hydroxysteroid-Δ24 Reductase (DHCR24) Protects Pancreatic β Cells from Endoplasmic Reticulum Stress-Induced Apoptosis by Scavenging Excessive Intracellular Reactive Oxygen Species

    doi: 10.1155/2020/3426902

    Figure Lengend Snippet: Apoptosis of MIN6 cells induced by TM is inhibited by overexpression of DHCR24. (a) A representative fluorescent image of cleaved caspase-3 (green) was obtained by IC analysis 24 h after TM exposure. Scale bar, 50 μ m. (b) The relative fluorescence intensity of cleaved caspase-3 was analyzed with ImageJ software. Mean ± S.D. ( n = 3); ∗ p

    Article Snippet: Briefly, cells on coverslips were fixed and blocked, followed by incubation with a mouse anti-myc antibody (Santa Cruz Biotechnology, CA, USA) or rabbit anti-cleaved caspase-3 antibody (Cell Signaling, Beverly, MA) overnight at 4°C.

    Techniques: Over Expression, Fluorescence, Software

    RhoA activity affects cell survival. (A) K562 cells were transfected with MOCK, RhoAN19 or RhoAL63 vectors followed by treatment with 1µM imatinib for the indicated time points in hours. Cell lysates were assessed by western blot for the presence of pro-caspase3 and cleaved active caspase3. Beta actin was used as a loading control. Corresponding densitometric analysis indicates the mean±s.e.m of three independent experiments, (p

    Journal: PLoS ONE

    Article Title: Increased Cytoplasmic Localization of p27kip1 and Its Modulation of RhoA Activity during Progression of Chronic Myeloid Leukemia

    doi: 10.1371/journal.pone.0076527

    Figure Lengend Snippet: RhoA activity affects cell survival. (A) K562 cells were transfected with MOCK, RhoAN19 or RhoAL63 vectors followed by treatment with 1µM imatinib for the indicated time points in hours. Cell lysates were assessed by western blot for the presence of pro-caspase3 and cleaved active caspase3. Beta actin was used as a loading control. Corresponding densitometric analysis indicates the mean±s.e.m of three independent experiments, (p

    Article Snippet: Primary antibodies against phospho p44/42 MAPK, p44/42 MAPK, phospho SAPK/JNK, SAPK/JNK, phospho c-jun and c-jun and cleaved caspase3 were purchased from Cell Signaling Technology (Denvers, USA).

    Techniques: Activity Assay, Transfection, Western Blot

    Effect of trehalose on apoptosis and ERS in cryopreserved valve cells. (A and B) Western blotting using a cleaved caspase-3 antibody on cryopreserved valve cells treated with trehalose (0.1 mol/L) or DMSO for 16 weeks. (C, D and E) Western blotting using GRP78 and CHOP antibodies on cryopreserved valves treated with trehalose (0.1 mol/L) for 16 weeks. Data are expressed as the mean ± SD ( n = 20 per group). ** P

    Journal: PLoS ONE

    Article Title: The cryoprotectant trehalose could inhibit ERS-induced apoptosis by activating autophagy in cryoprotected rat valves

    doi: 10.1371/journal.pone.0194078

    Figure Lengend Snippet: Effect of trehalose on apoptosis and ERS in cryopreserved valve cells. (A and B) Western blotting using a cleaved caspase-3 antibody on cryopreserved valve cells treated with trehalose (0.1 mol/L) or DMSO for 16 weeks. (C, D and E) Western blotting using GRP78 and CHOP antibodies on cryopreserved valves treated with trehalose (0.1 mol/L) for 16 weeks. Data are expressed as the mean ± SD ( n = 20 per group). ** P

    Article Snippet: The following primary antibodies were used in the assays: antibodies for cleaved caspase-3 (no. 9654; Cell Signaling Technology, Danvers, MA, USA), GRP78 (no. 3183; Cell Signaling Technology), CHOP (no. 2895; Cell Signaling Technology), LC3A/B II/I (no. 12741; Cell Signaling Technology), p62 (no. 5114; Cell Signaling Technology), ATG-5 (no. 12994; Cell Signaling Technology), ATG-7 (no. 8558; Cell Signaling Technology), mTOR (no. 2983; Cell Signaling Technology), p-mTOR (Ser2448) (no. 5536; Cell Signaling Technology), p38 MAPK (no. 9212; Cell Signaling Technology), and p-p38 MAPK (no. 4511; Cell Signaling Technology), and β-actin (no. 3700; Cell Signaling Technology) was chosen as loading control.

    Techniques: Western Blot

    DMM suppressed caspase activation in LPS/ d -GalN-challenged mice. The protease activities of (a) caspase-3, (b) caspase-8 and (c) caspase-9 in the liver tissue were detected 6 h after LPS/ d -GalN exposure. Data are presented as the mean ± SD , n = 8. * P

    Journal: Innate Immunity

    Article Title: Succinate dehydrogenase inhibitor dimethyl malonate alleviates LPS/d-galactosamine-induced acute hepatic damage in mice

    doi: 10.1177/1753425919873042

    Figure Lengend Snippet: DMM suppressed caspase activation in LPS/ d -GalN-challenged mice. The protease activities of (a) caspase-3, (b) caspase-8 and (c) caspase-9 in the liver tissue were detected 6 h after LPS/ d -GalN exposure. Data are presented as the mean ± SD , n = 8. * P

    Article Snippet: The rabbit anti-mouse cleaved caspase-3 and GAPDH were provided by Cell Signaling Technology (Danvers, MA).

    Techniques: Activation Assay, Mouse Assay

    DMM decreased the level of cleaved caspase-3 induced by LPS/ d -GalN. (a) The cleaved caspase-3 in liver was measured by Western blot analysis 6 h after LPS/ d -GalN injection. GAPDH was used as the internal control. (b) The blots were scanned and semi-quantified. n = 4. * P

    Journal: Innate Immunity

    Article Title: Succinate dehydrogenase inhibitor dimethyl malonate alleviates LPS/d-galactosamine-induced acute hepatic damage in mice

    doi: 10.1177/1753425919873042

    Figure Lengend Snippet: DMM decreased the level of cleaved caspase-3 induced by LPS/ d -GalN. (a) The cleaved caspase-3 in liver was measured by Western blot analysis 6 h after LPS/ d -GalN injection. GAPDH was used as the internal control. (b) The blots were scanned and semi-quantified. n = 4. * P

    Article Snippet: The rabbit anti-mouse cleaved caspase-3 and GAPDH were provided by Cell Signaling Technology (Danvers, MA).

    Techniques: Western Blot, Injection

    DUSP6 overexpression alleviates HG-induced podocyte apoptosis. (A) Apoptotic cells were detected via flow cytometry. (B) The protein expression levels of Bcl-2, Bax, cleaved caspase-3 and caspase-3. ***P

    Journal: Molecular Medicine Reports

    Article Title: DUSP6 protects murine podocytes from high glucose-induced inflammation and apoptosis

    doi: 10.3892/mmr.2020.11317

    Figure Lengend Snippet: DUSP6 overexpression alleviates HG-induced podocyte apoptosis. (A) Apoptotic cells were detected via flow cytometry. (B) The protein expression levels of Bcl-2, Bax, cleaved caspase-3 and caspase-3. ***P

    Article Snippet: Following blocking with 5% non-fat milk for 2 h at room temperature, the membranes were incubated overnight at 4°C with primary antibodies against: DUSP6 (Abcam; cat. no. ab76310; 1:1,000), nephrin (Abcam; cat. no. ab216341; 1:1,000), Bcl-2 (Abcam; cat. no. ab182858; 1:1,000), Bax (Abcam; cat. no. ab182733; 1:1,000), cleaved caspase-3 (Abcam; cat. no. ab2302; 1:1,000), caspase-3 (Abcam; cat. no. ab44976; 1:1,000), synaptopodin (Santa Cruz Biotechnology, Inc.; cat. no. sc-515842; 1: 500), phosphorylated (p)-ERK1/2 (Cell Signaling Technology, Inc.; cat. no. 9101; 1:1,000), ERK1/2 (Cell Signaling Technology, Inc.; cat. no. 4695; 1:1,000) and GAPDH (Cell Signaling Technology, Inc.; cat. no. 2118; 1:1,000).

    Techniques: Over Expression, Flow Cytometry, Expressing

    CASC2 modulates TRAIL resistance through miR-24/miR-221 a-b  HepG2R and Bel-7402R cells were co-transfected with si-CASC2 and miR-24 inhibitor or miR-221 inhibitor upon TRAIL treatment; the cell viability was determined using MTT assays.  c-d  The protein levels of caspase 8 and cleaved-caspase 8 in si-CASC2 and miR-24 inhibitor co-transfected cells, and the protein levels of caspase 3 and cleaved-caspase 3 in si-CASC2 and miR-221 inhibitor co-transfected cells were determined using Western blot assays.  e-f  The cell apoptosis was determined using flow cytometer assays. The data are presented as mean ± SD of three independent experiments. * P

    Journal: Cell Death & Disease

    Article Title: CASC2/miR-24/miR-221 modulates the TRAIL resistance of hepatocellular carcinoma cell through caspase-8/caspase-3

    doi: 10.1038/s41419-018-0350-2

    Figure Lengend Snippet: CASC2 modulates TRAIL resistance through miR-24/miR-221 a-b HepG2R and Bel-7402R cells were co-transfected with si-CASC2 and miR-24 inhibitor or miR-221 inhibitor upon TRAIL treatment; the cell viability was determined using MTT assays. c-d The protein levels of caspase 8 and cleaved-caspase 8 in si-CASC2 and miR-24 inhibitor co-transfected cells, and the protein levels of caspase 3 and cleaved-caspase 3 in si-CASC2 and miR-221 inhibitor co-transfected cells were determined using Western blot assays. e-f The cell apoptosis was determined using flow cytometer assays. The data are presented as mean ± SD of three independent experiments. * P

    Article Snippet: The blots were probed with the following antibodies: anti-caspase-3 (ab13585, Abcam, MA, USA), anti-cleaved-caspase-3 (ab2302, Abcam), anti-caspase-8 (C4106, Sigma-Aldrich, St. Louis, MO, USA), anti-cleaved-caspase-8 (C4733, Sigma-Aldrich) at 4 °C overnight, the blots were subsequently incubated with HRP-conjugated secondary antibody (1:5000).

    Techniques: Transfection, MTT Assay, Western Blot, Flow Cytometry, Cytometry

    Screening and identification of candidate miRNAs related to TRAIL resistance of hepatocellular carcinoma a  Regular TRAIL-sensitive HepG2S and Bel-7402S cells (S stands for sensitive) and irregular TRAIL-resistant HepG2R and Bel-7402R cells (R stands for resistant) were treated with a series of doses of TRAIL (1, 10, 100, 1000 ng/ml); the cell viability was determined using MTT assays. Data were shown as a percentage normalized to the viability of cells with no TRAIL treatment. The abscissa was the logarithm of TRAIL concentration (log-conc.). IC50 represented the concentration of TRAIL when cell viability was reduced to 50%.  b  The mRNA expression of caspase 3 and caspase 8 were determined using real-time PCR assays.  c  The protein levels of caspase 3 and caspase 8 were determined using Western blot assays.  d  Online tools (Targetscan, RNA22, miRWalk, and Starbase) were used to search for candidate miRNAs that may regulate caspase 3 or caspase 8, respectively. Non-down-regulated miRNAs in TRAIL-resistant tumor cells were selected in conjunction with the chip data of the GEO database; furthermore, the previously reported miRNAs that inhibited hepatocarcinoma proliferation were excluded according to the literature in NCBI.  e – f  Caspase 3 or caspase 8 mRNA expression in response to miRNA overexpression was determined using real-time PCR assays. The data are presented as mean ± SD of three independent experiments. * P

    Journal: Cell Death & Disease

    Article Title: CASC2/miR-24/miR-221 modulates the TRAIL resistance of hepatocellular carcinoma cell through caspase-8/caspase-3

    doi: 10.1038/s41419-018-0350-2

    Figure Lengend Snippet: Screening and identification of candidate miRNAs related to TRAIL resistance of hepatocellular carcinoma a Regular TRAIL-sensitive HepG2S and Bel-7402S cells (S stands for sensitive) and irregular TRAIL-resistant HepG2R and Bel-7402R cells (R stands for resistant) were treated with a series of doses of TRAIL (1, 10, 100, 1000 ng/ml); the cell viability was determined using MTT assays. Data were shown as a percentage normalized to the viability of cells with no TRAIL treatment. The abscissa was the logarithm of TRAIL concentration (log-conc.). IC50 represented the concentration of TRAIL when cell viability was reduced to 50%. b The mRNA expression of caspase 3 and caspase 8 were determined using real-time PCR assays. c The protein levels of caspase 3 and caspase 8 were determined using Western blot assays. d Online tools (Targetscan, RNA22, miRWalk, and Starbase) were used to search for candidate miRNAs that may regulate caspase 3 or caspase 8, respectively. Non-down-regulated miRNAs in TRAIL-resistant tumor cells were selected in conjunction with the chip data of the GEO database; furthermore, the previously reported miRNAs that inhibited hepatocarcinoma proliferation were excluded according to the literature in NCBI. e – f Caspase 3 or caspase 8 mRNA expression in response to miRNA overexpression was determined using real-time PCR assays. The data are presented as mean ± SD of three independent experiments. * P

    Article Snippet: The blots were probed with the following antibodies: anti-caspase-3 (ab13585, Abcam, MA, USA), anti-cleaved-caspase-3 (ab2302, Abcam), anti-caspase-8 (C4106, Sigma-Aldrich, St. Louis, MO, USA), anti-cleaved-caspase-8 (C4733, Sigma-Aldrich) at 4 °C overnight, the blots were subsequently incubated with HRP-conjugated secondary antibody (1:5000).

    Techniques: MTT Assay, Concentration Assay, Expressing, Real-time Polymerase Chain Reaction, Western Blot, Chromatin Immunoprecipitation, Over Expression

    MiR-24/miR-221 negatively regulate Caspase 8/3 through direct targeting a–b  Wild-type (wt-) and mutated-type (mut-) luciferase reporter gene vectors (wt-caspase 3 named wt-CASP3, wt-caspase 8 named wt-CASP8, mut-caspase 3 named mut-CASP3, mut-caspase 8 named mut-CASP8) were constructed. Mut-CASP3 contains a 5 bp mutation in the predicted miR-221 binding site; mut-CASP8 contains a 5 bp mutation in the predicted miR-24 binding site. The above vectors were co-transfected into HEK293 cells with miR-24/miR-221 mimics or inhibitor; the luciferase activity was determined.  c–d  The mimics or inhibitor of miR-24 and miR-221 was transfected into HepG2R and Bel-7402R cells, respectively; the protein levels of caspase 3 or caspase 8 were determined using Western blot assays. The data are presented as mean ± SD of three independent experiments. * P

    Journal: Cell Death & Disease

    Article Title: CASC2/miR-24/miR-221 modulates the TRAIL resistance of hepatocellular carcinoma cell through caspase-8/caspase-3

    doi: 10.1038/s41419-018-0350-2

    Figure Lengend Snippet: MiR-24/miR-221 negatively regulate Caspase 8/3 through direct targeting a–b Wild-type (wt-) and mutated-type (mut-) luciferase reporter gene vectors (wt-caspase 3 named wt-CASP3, wt-caspase 8 named wt-CASP8, mut-caspase 3 named mut-CASP3, mut-caspase 8 named mut-CASP8) were constructed. Mut-CASP3 contains a 5 bp mutation in the predicted miR-221 binding site; mut-CASP8 contains a 5 bp mutation in the predicted miR-24 binding site. The above vectors were co-transfected into HEK293 cells with miR-24/miR-221 mimics or inhibitor; the luciferase activity was determined. c–d The mimics or inhibitor of miR-24 and miR-221 was transfected into HepG2R and Bel-7402R cells, respectively; the protein levels of caspase 3 or caspase 8 were determined using Western blot assays. The data are presented as mean ± SD of three independent experiments. * P

    Article Snippet: The blots were probed with the following antibodies: anti-caspase-3 (ab13585, Abcam, MA, USA), anti-cleaved-caspase-3 (ab2302, Abcam), anti-caspase-8 (C4106, Sigma-Aldrich, St. Louis, MO, USA), anti-cleaved-caspase-8 (C4733, Sigma-Aldrich) at 4 °C overnight, the blots were subsequently incubated with HRP-conjugated secondary antibody (1:5000).

    Techniques: Luciferase, Construct, Mutagenesis, Binding Assay, Transfection, Activity Assay, Western Blot

    Effects of CLU silencing on viability, proliferation/death and differentiation of cultured OA chondrocytes. ( A ) CLU mRNA and protein expression after 48 and 72 hours, respectively, in scramble (control) and siCLU transfected OA-HACs. ( B ) Cell viability by MTT assay after 24, 48 and 72 hours of scramble and siCLU transfected OA-HACs. ( C ) Representative immunocytochemical images and bar graphs showing Ki67 + and p21 + nuclei in cultured OA-HACs and ( D ) cleaved caspase-3 + cytospinned OA-HACs after 72 hours of silencing. ( E ) Gene array shows the modulation of NFkB and Stat-3-related genes in siCLU transfected OA-HACs compared with scramble after 48 hours of silencing. Transcript levels were normalized on GAPDH (internal reference gene). ( F ) mRNA levels by Real-Time PCR of COL2A1, ACAN, MMP13, COL10A1, and ( G ) representative blot and densitometric analysis of MMP13 and COL10A1 in scramble and CLU-silenced OA-HACs. Data are expressed as mean values ± SEM of three independent experiments (each using pooled samples from n=3 OA donors) performed in triplicate. Abbreviations: OA-HACs, OA-Human articular chondrocytes; OD, optical density unit; RLU, relative light unit. Student’s t-test: * P

    Journal: Aging (Albany NY)

    Article Title: Clusterin exerts a cytoprotective and antioxidant effect in human osteoarthritic cartilage

    doi: 10.18632/aging.103310

    Figure Lengend Snippet: Effects of CLU silencing on viability, proliferation/death and differentiation of cultured OA chondrocytes. ( A ) CLU mRNA and protein expression after 48 and 72 hours, respectively, in scramble (control) and siCLU transfected OA-HACs. ( B ) Cell viability by MTT assay after 24, 48 and 72 hours of scramble and siCLU transfected OA-HACs. ( C ) Representative immunocytochemical images and bar graphs showing Ki67 + and p21 + nuclei in cultured OA-HACs and ( D ) cleaved caspase-3 + cytospinned OA-HACs after 72 hours of silencing. ( E ) Gene array shows the modulation of NFkB and Stat-3-related genes in siCLU transfected OA-HACs compared with scramble after 48 hours of silencing. Transcript levels were normalized on GAPDH (internal reference gene). ( F ) mRNA levels by Real-Time PCR of COL2A1, ACAN, MMP13, COL10A1, and ( G ) representative blot and densitometric analysis of MMP13 and COL10A1 in scramble and CLU-silenced OA-HACs. Data are expressed as mean values ± SEM of three independent experiments (each using pooled samples from n=3 OA donors) performed in triplicate. Abbreviations: OA-HACs, OA-Human articular chondrocytes; OD, optical density unit; RLU, relative light unit. Student’s t-test: * P

    Article Snippet: After permeabilization in TBS-0.1% Tween 20 for 5min at RT, slides were incubated with rabbit polyclonal antibody anti-Ki67 (Novus Biologicals, CO, USA, 1:100, 1h at RT), goat polyclonal anti-CLU β (Santa Cruz Biotechnology, 1:50, O/N at +4°C), mouse monoclonal anti-p21 (R & D System Inc., USA, 8μg/ml, 1h at RT), rabbit polyclonal anti-cleaved caspase-3 (Cell Signaling Technology, Inc, MA, USA, 1:500, 1h at RT) and goat polyclonal anti-TNFα (Santa Cruz Biotechnology, 1:100, 2h at RT), with positive and negative controls.

    Techniques: Cell Culture, Expressing, Transfection, MTT Assay, Real-time Polymerase Chain Reaction

    t -AUCB administration attenuated mitochondrial dysfunction, ROS production, and apoptosis in tubules of db/db mice. a Kidney sections stained with JC-1. b Kidney sections stained with Mito SOX. c Western blot analysis of Drp1and Mfn2 expression in kidney tissues. d Quantification of the fluorescence intensity of JC-1 staining in figure a. e Quantification of the fluorescence intensity of Mito SOX staining in figure b. f , g Densitometric analysis of Drp1and Mfn2 expression in the figure c. h Kidney sections stained with Oil Red O staining. i Western blot analysis of PGC-1α and CPT1A expression in kidney tissues. j , k Densitometric analysis of PGC-1α and CPT1A expression in figure i. l Western blot analysis of Bax, Cyt c and cleaved-caspase3 expression in kidney tissues. m–o Densitometric analysis of Bax, Cyt c and cleaved-caspase3 expression in the figure l. p Representative images of immunofluorescence double labeling of Tom20 and Bax in different kidney tissues. * P

    Journal: Cell Death & Disease

    Article Title: Inhibition of soluble epoxide hydrolase attenuates renal tubular mitochondrial dysfunction and ER stress by restoring autophagic flux in diabetic nephropathy

    doi: 10.1038/s41419-020-2594-x

    Figure Lengend Snippet: t -AUCB administration attenuated mitochondrial dysfunction, ROS production, and apoptosis in tubules of db/db mice. a Kidney sections stained with JC-1. b Kidney sections stained with Mito SOX. c Western blot analysis of Drp1and Mfn2 expression in kidney tissues. d Quantification of the fluorescence intensity of JC-1 staining in figure a. e Quantification of the fluorescence intensity of Mito SOX staining in figure b. f , g Densitometric analysis of Drp1and Mfn2 expression in the figure c. h Kidney sections stained with Oil Red O staining. i Western blot analysis of PGC-1α and CPT1A expression in kidney tissues. j , k Densitometric analysis of PGC-1α and CPT1A expression in figure i. l Western blot analysis of Bax, Cyt c and cleaved-caspase3 expression in kidney tissues. m–o Densitometric analysis of Bax, Cyt c and cleaved-caspase3 expression in the figure l. p Representative images of immunofluorescence double labeling of Tom20 and Bax in different kidney tissues. * P

    Article Snippet: The fractionated proteins were transferred onto PVDF membranes (Millipore), which were then blocked with 5% nonfat milk for 3 h. The PVDF membranes were then incubated with the following primary antibodies: mouse anti-sEH (1:1000, Santa Cruz, sc-166961), rabbit anti-Bip (1:1000, Abcam, #21685), rabbit anti-Ire1α (1:1000, CST, #3294), rabbit anti-PERK (1:1000, CST, #3192), rabbit anti-ATF4 (1:1000, CST, #11815), rabbit anti-Caspase12 (1:1000, Abcam, #62484), mouse anti-Chop (1:1000, CST, #2895), rabbit anti-cleaved -caspase3 (1:1000, CST, #9664), rabbit anti-Cytochrome c (1:1000, Santa Cruz, sc-13156), rabbit anti-Bax (1:1000, CST, #2772), rabbit anti-Lamp2 (1:1000, Abcam, #13524), rabbit anti-Atg5 (1:1000, Abcam, # 108327), rabbit anti-LC3 (1:1000, CST, #4108), mouse anti-p62 (1:1000, abcam, #109012), rabbit anti-Parkin (1:1000, Abcam, #77924), mouse anti-PINK1(1:1000, abcam, #186303), rabbit anti-PGC-1α (1:1000, Abcam, #54481), rabbit anti-CPT1A (1:1000, Abcam, #128568) and mouse anti-β-actin (1:5000, Sungene Biotech, # KM9001T).

    Techniques: Mouse Assay, Staining, Western Blot, Expressing, Fluorescence, Pyrolysis Gas Chromatography, Immunofluorescence, Labeling

    TL induced Akt activation in NSCLC. A549 and NCI-H460 cells were treated for 18–24 h ± 50 nM/100 nM TL. Representative immunoblots ( A ) and quantitation ( B , C ) for CAV-1, pAkt (Ser473), Total Akt, Bcl-2, Bax, Cleaved caspase-3 (CC-3) and Cleaved-PARP (C-PARP) protein expression. Protein quantity was normalized to β-Actin. Data are presented as mean ± SD. n = 3–4. * indicates significantly different ( p

    Journal: Oncotarget

    Article Title: Triptolide-induced apoptosis in non-small cell lung cancer via a novel miR204-5p/Caveolin-1/Akt-mediated pathway

    doi: 10.18632/oncotarget.27672

    Figure Lengend Snippet: TL induced Akt activation in NSCLC. A549 and NCI-H460 cells were treated for 18–24 h ± 50 nM/100 nM TL. Representative immunoblots ( A ) and quantitation ( B , C ) for CAV-1, pAkt (Ser473), Total Akt, Bcl-2, Bax, Cleaved caspase-3 (CC-3) and Cleaved-PARP (C-PARP) protein expression. Protein quantity was normalized to β-Actin. Data are presented as mean ± SD. n = 3–4. * indicates significantly different ( p

    Article Snippet: The following primary antibodies were utilized for immunoblotting: rabbit polyclonal anti-caveolin-1 (N-20, 1:1000, Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse monoclonal anti β-actin (C4, 1:10,000, Santa Cruz), rabbit monoclonal anti-SIRT-1 (D1D7, 1:1000, Cell Signaling Technology, Danvers, MA, USA), rabbit monoclonal anti-SIRT-3 (C73E3, 1:1000, Cell Signaling), rabbit polyclonal anti-phospho-Akt [Ser473] (1:1000, Cell Signaling), rabbit monoclonal anti-Akt [pan] (C67E7, 1:1000, Cell Signaling), rabbit monoclonal anti-Bcl-2 (D55G8, 1:1000, Cell Signaling), rabbit polyclonal anti-Bax (2772, 1:1000, Cell Signaling), rabbit monoclonal anti-cleaved caspase-3 [Asp175] (5A1E, 1:1000, Cell Signaling) and rabbit monoclonal anti-cleaved poly (ADP-ribose) polymerase (PARP) [Asp214] (D64E10, 1:1000, Cell Signaling).

    Techniques: Activation Assay, Western Blot, Quantitation Assay, Expressing

    Deprivation of BCAS2 diminishing Delta-Notch activity is apoptosis-independent. The late third instar larval wing discs of each genotype were isolated and immunostained with anti-Caspase-3 antibody (blue; A-D); anti-Cut antibody (red, E-H); the expression of GFP, Cut and Caspase-3 were merged (I-L). Images were taken by confocal microscopy, scale bar, 50 μm. (A, E, I) Control ( en > GFP ). (B, F, J ) The p35 over expression wing disc ( en > GFP , p35 ). (C, G, K) The dBCAS2 -depleted wing disc ( en > GFP , dBCAS2 dsRNA ). (D, H, L) The coexpression of p35 and dBCAS2 dsRNA ( en > GFP , dBCAS2 dsRNA , p35 ).

    Journal: PLoS ONE

    Article Title: BCAS2 Regulates Delta-Notch Signaling Activity through Delta Pre-mRNA Splicing in Drosophila Wing Development

    doi: 10.1371/journal.pone.0130706

    Figure Lengend Snippet: Deprivation of BCAS2 diminishing Delta-Notch activity is apoptosis-independent. The late third instar larval wing discs of each genotype were isolated and immunostained with anti-Caspase-3 antibody (blue; A-D); anti-Cut antibody (red, E-H); the expression of GFP, Cut and Caspase-3 were merged (I-L). Images were taken by confocal microscopy, scale bar, 50 μm. (A, E, I) Control ( en > GFP ). (B, F, J ) The p35 over expression wing disc ( en > GFP , p35 ). (C, G, K) The dBCAS2 -depleted wing disc ( en > GFP , dBCAS2 dsRNA ). (D, H, L) The coexpression of p35 and dBCAS2 dsRNA ( en > GFP , dBCAS2 dsRNA , p35 ).

    Article Snippet: Primary antibodies: mouse anti-Cut (2B10, 1:200, Developmental Studies Hybridoma Bank (DSHB), Iowa City, IA, USA), mouse anti-Delta (C594.B9, 1:200, DSHB), mouse anti-Notch (C17.9C6, 1:100, DSHB), mouse anti-β-gal (1:1000, Sigma-Aldrich, St. Louis, MO, USA), rabbit anti-cleaved caspase-3 (1:200; Abcam).

    Techniques: Activity Assay, Isolation, Expressing, Confocal Microscopy, Over Expression