pro-caspase-3 Search Results


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  • 91
    ATCC procaspase 3
    <t>Procaspase-3</t> levels decreased early after L-78 infection in murine spleen lysates A . Total protein extracts of pooled splenocytes from L-78- and ATCC 43816-infected mice were immunoblotted against procaspase-3. Apoptotic and necrotic HeLa cells were used as controls. β-Actin was used as a loading control. All samples were run on and cut from the same gel. B . Densitometric analysis of procaspase-3. Data are means ± SD from three independent experiments. C, HeLa cells incubated in medium; Ap, apoptotic HeLa cells; N, necrotic HeLa cells. *, p
    Procaspase 3, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore caspase 3
    ANDV nucleocapsid protein inhibits caspase 3-activity. Analysis of possible interactions between ANDV nucleocapsid protein and caspase 3. ( A ) Western blot analyses showing a cleaved fragment of the ANDV nucleocapsid protein (ANDV-N) after incubation with recombinant <t>caspase</t> 3 in the presence or absence of the caspase 3-inhibitor DEVD-CHO. Full-length and cleaved ANDV-N was visualized with the mAb 7B3/F7. One representative experiment out of three is shown. ( B ) ANDV-infected A549 cells were left untreated or treated with staurosporine, in the presence or absence of the caspase-inhibitor Z-VAD-fmk. Lysed cells were then subjected to Western blot analyses to visualize cleavage of the viral ANDV nucleocapsid protein (ANDV-N) after staurosporine-treatment. Full-length and cleaved ANDV-N was visualized with the mAb 7B3/F7. One representative experiment out of three is shown. ( C ) Caspase 3-activity was measured after pre-incubation of recombinant caspase 3 with recombinant ANDV nucleocapsid protein (rANDV-N) or with control protein (rDHFR) for 30 minutes. Level of caspase 3-activity after co-incubation with rDHFRS represent maximal caspase 3 activity. Level of caspase 3-activity after co-incubation of caspase 3 with rANDV-N was compared with caspase 3-activity after co-incubation with rDHFRS. Data shown are mean ± SEM of three independent experiments carried out in duplicate. Two-tailed Student's t test was used for statistical evaluation; * p
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    93
    Epitomics caspase 3
    Effect of GXSTC on apoptosis-associated protein expression in all treated groups. (A) Bands correspond to Bcl-2, Bax, <t>caspase-3</t> and GAPDH. Results of (B) Bax, (C) Bcl-2 and (D) caspase-3 were quantified by densitometry analysis of the bands from (A) and then normalized against GAPDH in the heart tissue. Results were obtained from three independent experiments performed in triplicate. * P
    Caspase 3, supplied by Epitomics, used in various techniques. Bioz Stars score: 93/100, based on 130 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam caspase 3
    From Western blots it was clear that activated cleaved <t>caspase-3</t> was more profound in the co-cultured liver cells than in the corresponding mono-cultured liver cells ( a ). Lanes 1 – 4 are mono-cultured liver cells while lanes 5 – 8 is liver cells co-cultured with head kidney cells. Lanes 1 and 5 are controls, lanes 2 and 6 are cells grown in 20 % H-pro, lanes 3 and 7 are the control cells stressed with 200 µM H 2 O 2 and lanes 4 and 8 are the cells grown in 20 % H-pro stressed with 200 µM H 2 O 2. ( b ) The abundance means of activated cleaved caspase-3 relative to the abundance in the control that are set equal to 100 after the abundance was normalized. Cells grown with H-pro had less active cleaved caspase 3 as compared to controls (p = 0.024, Mann–Whitney U-test n = 5 ± SE)
    Caspase 3, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 4883 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam procaspase 3
    Cleaved caspase-3 expression is reduced in Z-DEVD-FMK injected animals. (A) NM cell bodies, NL cell bodies, NL dendrites and cells in the glial margin express <t>procaspase-3</t> in control embryos and (B) Z-DEVD-FMK injected embryos. (C) In tissue from control animals, cleaved caspase-3 is expressed in NM and in NL dendrites. (D) In tissue from embryos that received injections of Z-DEVD-FMK into the IVth ventricle, cleaved caspase-3 expression was reduced. (E) While background optical density values did not differ, values in NM were significantly lower in treated vs. control embryos (* p
    Procaspase 3, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 103 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology caspase 3
    Effects of caspase inhibitors on ZIKV Env-mediated apoptosis in PC12 cells. (A) Cells were transduced with LV-ZIKV-prM-Env, LV-ZIKV-M-Env, LV-ZIKV-Env or LV-eGFP (100 MOI) for 6 h followed by treatment with either <t>caspase-3</t> inhibitor Ac-DEVD-CMK (100 μmol/L), caspase-8 inhibitor ZIETD-FMK (100 μmol/L), caspase-9 inhibitor ZLEHD-FMK (100 μmol/L) or control solvent (DMSO) for 24 h. Caspase-3, caspase-8 and caspase-9 were detected by western blot. (B) Treated cells were double- stained with Alexa Fluor 647 conjugated annexin V and PI. The annexin V-positive cells as a percent of the total number of cells were measured from flow cytometric analysis. **: P
    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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    93
    Thermo Fisher caspase 3
    Apoptosis and Extracellular ATP Concentration. Proportion of <t>Caspase</t> 3 positive cells post-heat shock, MLO-Y4 osteocytes and B35 neurons combined ( left ). Relative concentration of ATP in cell medium from both sides of the device (heated and unheated)
    Caspase 3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 975 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Abcam anti caspase 3
    <t>Caspase-3</t> expression in the gastric mucosa of rats with acetic acid-induced gastric ulcers treated with oral administration of vehicle, lansoprazole, or hydroalcoholic extract from the leaves of Eugenia punicifolia or 14 d. The data represent relative expression of caspase-3 normalized to the expression of housekeeping genes (actin). The results represent mean ± standard error of the mean for each group ( n = 6). Statistical significance was determined using one-way ANOVA followed by Dunnett's test. No statistically significant differences were found. HEEP: Hydroalcoholic extract from the leaves of Eugenia punicifolia .
    Anti Caspase 3, supplied by Abcam, used in various techniques. Bioz Stars score: 96/100, based on 1167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    R&D Systems caspase 3
    Apoptosis of cortical neurons in traumatic brain injury. ( A ) <t>Caspase-3</t> positive pyramidal cells in the vicinity of a cortical contusion from a patient with traumatic brain injury (cases 18–95). ( B ) Caspase-3 positive neuronal like cells with dendritic processes in the vicinity of the contusion area of another patient with traumatic brain injury. Scale bar = 10 μm.
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    94
    Novus Biologicals caspase 3
    The effect of MPT0E028 on the growth of HCT116 cells  in vivo . All tumors grew to the 1,200-mm 3  endpoint volume. (A) Tumors were measured regularly and growth delay was calculated for treatment groups relative to control tumors (TGD). (B) Kaplan-Meier survival analysis was based on the tumor growth endpoint. (C) Inhibition of tumor growth curves represented a mean±SEM and percentage change in mean tumor volume (percent TGI). (D) Body weights were measured daily during the first week and then 2 times per week. The body weight ratio was calculated relative to the baseline measurement. (E)  In vivo  effect of MPT0E028 on the expression of caspase 3, PARP, acetyl-histone H3 and acetyl-µ-tubulin in HCT116 xenograft tumors as determined by western blotting.
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    91
    Cell Signaling Technology Inc casp3
    Validation of protein and mRNA level dysregulations. (A) Quantitative immunoblots confirmed neuronal loss (marker NeuN), astrogliosis (marker GFAP) and microgliosis (marker IBA1) to occur in Atxn2 -CAG100-KIN spinal cord at the preterminal stage of 14 months age, but not at the early KIN stage of 3 months age and in the Atxn2 -KO at 6 months. Significantly increased levels in KIN at 14 months were also shown for TDP43 and the factor responsible for its cleavage, <t>CASP3.</t> (B) Quantitative RT-PCR analyses showed a significant deficit of NeuN transcript ( Rbfox3 ) already at incipient disease stage in 3-month-old KIN, whereas astrogliosis (marker Gfap ) and microgliosis (marker IBA1 transcript Aif1 ) became significant at late state. Protein abundance (C) and transcript levels (D) were also documented for PGRN (encoded by Grn mRNA) as molecular marker of lysosomal activation and atrophy, as well as RIPK1 as molecular marker of RNA-toxicity and necroptosis. Again, a significant elevation of Grn mRNA at the age of 3 months suggested atrophy and lysosomal breakdown to occur in parallel with first locomotor deficits, predating necroptotic cell death.
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    85
    Santa Cruz Biotechnology pro caspase 3 e8
    Validation of protein and mRNA level dysregulations. (A) Quantitative immunoblots confirmed neuronal loss (marker NeuN), astrogliosis (marker GFAP) and microgliosis (marker IBA1) to occur in Atxn2 -CAG100-KIN spinal cord at the preterminal stage of 14 months age, but not at the early KIN stage of 3 months age and in the Atxn2 -KO at 6 months. Significantly increased levels in KIN at 14 months were also shown for TDP43 and the factor responsible for its cleavage, <t>CASP3.</t> (B) Quantitative RT-PCR analyses showed a significant deficit of NeuN transcript ( Rbfox3 ) already at incipient disease stage in 3-month-old KIN, whereas astrogliosis (marker Gfap ) and microgliosis (marker IBA1 transcript Aif1 ) became significant at late state. Protein abundance (C) and transcript levels (D) were also documented for PGRN (encoded by Grn mRNA) as molecular marker of lysosomal activation and atrophy, as well as RIPK1 as molecular marker of RNA-toxicity and necroptosis. Again, a significant elevation of Grn mRNA at the age of 3 months suggested atrophy and lysosomal breakdown to occur in parallel with first locomotor deficits, predating necroptotic cell death.
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    99
    Millipore caspase 3 levels
    Effects of low concentrations of ethanol, nicotine and salsolinol alone or in combination on <t>caspase-3</t> and β actin protein in human neuroblastoma SH-SY5Y cells. Cells were treated with low concentrations of ethanol (10 mM) or nicotine (20 μM)
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    99
    Millipore anti pro caspase 3
    Deletion of partial CASP-3 genomic DNA in MCF-7 cells. (A) Images of DNA electrophoresis of the polymerase chain reaction (PCR) products for the CASP-3 genomic DNA and cDNA, respectively. Both PCR products from MCF-7 cells are shorter than those from A431 cells, resulting from a 47-base pair deletion within exon 4 of the human CASP-3 genomic DNA. (B) Sequencing results of the PCR products from the two cell lines. The yellow underline indicates the sequence of the deleted fragment. (C) Results of Western blotting analysis show expression of <t>pro-caspase-3</t> protein in A431 cells but not in MCF-7 cells. Tubulin was used as loading control.
    Anti Pro Caspase 3, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti procaspase 3
    LYT (Luoyutong) reduces neuronal apoptosis and decreases the level of <t>caspase-3.</t> (a) Neuronal apoptosis in the ipsilateral cortex was detected by terminal deoxynucleotidyl transferase dUTP nick end labeling and 4′ 6-diamidino-2-phenylindole double staining 14 days after ischemic reperfusion. (b) Expression of activated caspase-3 was detected by Western blot 14 days after ischemic reperfusion. n = 3. ∗ P
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    92
    Santa Cruz Biotechnology anti caspase 3
    Silence ERK pathway partially repeal the antiapoptosis effects of carvacrol. (a) The efficiency and specificity of siRNA directed against ERK. (b)–(d) Ethanol increases hippocampal neurons apoptotic rate and <t>caspase-3</t> activity as well as decreasing cell viability compared with control group. These proapoptotic effects can be reversed by carvacrol. However, when it is silence or block ERK pathway, carvacrol antiapoptotic effects can be partially repealed. The data are expressed as the mean ± SEM ( n = 6 per group). ∗∗ P
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    Abcam active pro caspase 3 ab47131
    Silence ERK pathway partially repeal the antiapoptosis effects of carvacrol. (a) The efficiency and specificity of siRNA directed against ERK. (b)–(d) Ethanol increases hippocampal neurons apoptotic rate and <t>caspase-3</t> activity as well as decreasing cell viability compared with control group. These proapoptotic effects can be reversed by carvacrol. However, when it is silence or block ERK pathway, carvacrol antiapoptotic effects can be partially repealed. The data are expressed as the mean ± SEM ( n = 6 per group). ∗∗ P
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    Image Search Results


    Procaspase-3 levels decreased early after L-78 infection in murine spleen lysates A . Total protein extracts of pooled splenocytes from L-78- and ATCC 43816-infected mice were immunoblotted against procaspase-3. Apoptotic and necrotic HeLa cells were used as controls. β-Actin was used as a loading control. All samples were run on and cut from the same gel. B . Densitometric analysis of procaspase-3. Data are means ± SD from three independent experiments. C, HeLa cells incubated in medium; Ap, apoptotic HeLa cells; N, necrotic HeLa cells. *, p

    Journal: Oncotarget

    Article Title: A fragment of the alarmin prothymosin α as a novel biomarker in murine models of bacteria-induced sepsis

    doi: 10.18632/oncotarget.18149

    Figure Lengend Snippet: Procaspase-3 levels decreased early after L-78 infection in murine spleen lysates A . Total protein extracts of pooled splenocytes from L-78- and ATCC 43816-infected mice were immunoblotted against procaspase-3. Apoptotic and necrotic HeLa cells were used as controls. β-Actin was used as a loading control. All samples were run on and cut from the same gel. B . Densitometric analysis of procaspase-3. Data are means ± SD from three independent experiments. C, HeLa cells incubated in medium; Ap, apoptotic HeLa cells; N, necrotic HeLa cells. *, p

    Article Snippet: Indeed, in L-78 infection, the levels of procaspase-3 were significantly reduced at the early stages pi indicating activation of caspase-3, whereas in the ATCC 43816 model, procaspase-3 levels decreased less.

    Techniques: Infection, Mouse Assay, Incubation

    ANDV nucleocapsid protein inhibits caspase 3-activity. Analysis of possible interactions between ANDV nucleocapsid protein and caspase 3. ( A ) Western blot analyses showing a cleaved fragment of the ANDV nucleocapsid protein (ANDV-N) after incubation with recombinant caspase 3 in the presence or absence of the caspase 3-inhibitor DEVD-CHO. Full-length and cleaved ANDV-N was visualized with the mAb 7B3/F7. One representative experiment out of three is shown. ( B ) ANDV-infected A549 cells were left untreated or treated with staurosporine, in the presence or absence of the caspase-inhibitor Z-VAD-fmk. Lysed cells were then subjected to Western blot analyses to visualize cleavage of the viral ANDV nucleocapsid protein (ANDV-N) after staurosporine-treatment. Full-length and cleaved ANDV-N was visualized with the mAb 7B3/F7. One representative experiment out of three is shown. ( C ) Caspase 3-activity was measured after pre-incubation of recombinant caspase 3 with recombinant ANDV nucleocapsid protein (rANDV-N) or with control protein (rDHFR) for 30 minutes. Level of caspase 3-activity after co-incubation with rDHFRS represent maximal caspase 3 activity. Level of caspase 3-activity after co-incubation of caspase 3 with rANDV-N was compared with caspase 3-activity after co-incubation with rDHFRS. Data shown are mean ± SEM of three independent experiments carried out in duplicate. Two-tailed Student's t test was used for statistical evaluation; * p

    Journal: PLoS Pathogens

    Article Title: Hantavirus-infection Confers Resistance to Cytotoxic Lymphocyte-Mediated Apoptosis

    doi: 10.1371/journal.ppat.1003272

    Figure Lengend Snippet: ANDV nucleocapsid protein inhibits caspase 3-activity. Analysis of possible interactions between ANDV nucleocapsid protein and caspase 3. ( A ) Western blot analyses showing a cleaved fragment of the ANDV nucleocapsid protein (ANDV-N) after incubation with recombinant caspase 3 in the presence or absence of the caspase 3-inhibitor DEVD-CHO. Full-length and cleaved ANDV-N was visualized with the mAb 7B3/F7. One representative experiment out of three is shown. ( B ) ANDV-infected A549 cells were left untreated or treated with staurosporine, in the presence or absence of the caspase-inhibitor Z-VAD-fmk. Lysed cells were then subjected to Western blot analyses to visualize cleavage of the viral ANDV nucleocapsid protein (ANDV-N) after staurosporine-treatment. Full-length and cleaved ANDV-N was visualized with the mAb 7B3/F7. One representative experiment out of three is shown. ( C ) Caspase 3-activity was measured after pre-incubation of recombinant caspase 3 with recombinant ANDV nucleocapsid protein (rANDV-N) or with control protein (rDHFR) for 30 minutes. Level of caspase 3-activity after co-incubation with rDHFRS represent maximal caspase 3 activity. Level of caspase 3-activity after co-incubation of caspase 3 with rANDV-N was compared with caspase 3-activity after co-incubation with rDHFRS. Data shown are mean ± SEM of three independent experiments carried out in duplicate. Two-tailed Student's t test was used for statistical evaluation; * p

    Article Snippet: To analyze nucleocapsid protein-specific inhibition of caspase 3 and granzyme B activity, recombinant human caspase 3 (0.1 µg) or active recombinant granzyme B (0.1 µg) was incubated with 1 µg recombinant ANDV nucleocapsid protein or 1 µg rDHFR as control, for 30 minutes or as stated in the text.

    Techniques: Activity Assay, Western Blot, Incubation, Recombinant, Infection, Two Tailed Test

    Hantavirus-infection inhibits NK cell-mediated activation of caspase 3 in endothelial cells. Prevention of caspase 3 activation in infected cells exposed to IL-2-activated NK cells. ( A ) Representative flow cytometry histogram showing cellular caspase 3-activity in uninfected and HTNV-infected HLA class I blocked endothelial cells with and without co-incubation with IL-2-activated NK cells. Data shown is one representative donor out of six. ( B ) Percentage of caspase 3-positive uninfected and HTNV-infected endothelial cells after co-incubation with IL-2-activated NK cells analyzed by flow cytometry. Data shown represent two independent experiments from six donors. Two-tailed Student's t test was used for statistical evaluation; ** p

    Journal: PLoS Pathogens

    Article Title: Hantavirus-infection Confers Resistance to Cytotoxic Lymphocyte-Mediated Apoptosis

    doi: 10.1371/journal.ppat.1003272

    Figure Lengend Snippet: Hantavirus-infection inhibits NK cell-mediated activation of caspase 3 in endothelial cells. Prevention of caspase 3 activation in infected cells exposed to IL-2-activated NK cells. ( A ) Representative flow cytometry histogram showing cellular caspase 3-activity in uninfected and HTNV-infected HLA class I blocked endothelial cells with and without co-incubation with IL-2-activated NK cells. Data shown is one representative donor out of six. ( B ) Percentage of caspase 3-positive uninfected and HTNV-infected endothelial cells after co-incubation with IL-2-activated NK cells analyzed by flow cytometry. Data shown represent two independent experiments from six donors. Two-tailed Student's t test was used for statistical evaluation; ** p

    Article Snippet: To analyze nucleocapsid protein-specific inhibition of caspase 3 and granzyme B activity, recombinant human caspase 3 (0.1 µg) or active recombinant granzyme B (0.1 µg) was incubated with 1 µg recombinant ANDV nucleocapsid protein or 1 µg rDHFR as control, for 30 minutes or as stated in the text.

    Techniques: Infection, Activation Assay, Flow Cytometry, Cytometry, Activity Assay, Incubation, Two Tailed Test

    Effect of GXSTC on apoptosis-associated protein expression in all treated groups. (A) Bands correspond to Bcl-2, Bax, caspase-3 and GAPDH. Results of (B) Bax, (C) Bcl-2 and (D) caspase-3 were quantified by densitometry analysis of the bands from (A) and then normalized against GAPDH in the heart tissue. Results were obtained from three independent experiments performed in triplicate. * P

    Journal: Experimental and Therapeutic Medicine

    Article Title: Chinese medicinal formula Guanxin Shutong capsule protects the heart against oxidative stress and apoptosis induced by ischemic myocardial injury in rats

    doi: 10.3892/etm.2014.1540

    Figure Lengend Snippet: Effect of GXSTC on apoptosis-associated protein expression in all treated groups. (A) Bands correspond to Bcl-2, Bax, caspase-3 and GAPDH. Results of (B) Bax, (C) Bcl-2 and (D) caspase-3 were quantified by densitometry analysis of the bands from (A) and then normalized against GAPDH in the heart tissue. Results were obtained from three independent experiments performed in triplicate. * P

    Article Snippet: Furthermore, protein expression of proapoptotic Bax and caspase-3 were significantly downregulated, while the antiapoptotic protein, Bcl-2, was upregulated in the GXSTC treated groups when compared with the MI + vehicle group.

    Techniques: Expressing

    From Western blots it was clear that activated cleaved caspase-3 was more profound in the co-cultured liver cells than in the corresponding mono-cultured liver cells ( a ). Lanes 1 – 4 are mono-cultured liver cells while lanes 5 – 8 is liver cells co-cultured with head kidney cells. Lanes 1 and 5 are controls, lanes 2 and 6 are cells grown in 20 % H-pro, lanes 3 and 7 are the control cells stressed with 200 µM H 2 O 2 and lanes 4 and 8 are the cells grown in 20 % H-pro stressed with 200 µM H 2 O 2. ( b ) The abundance means of activated cleaved caspase-3 relative to the abundance in the control that are set equal to 100 after the abundance was normalized. Cells grown with H-pro had less active cleaved caspase 3 as compared to controls (p = 0.024, Mann–Whitney U-test n = 5 ± SE)

    Journal: SpringerPlus

    Article Title: Hydrolyzed fish proteins reduced activation of caspase-3 in H2O2 induced oxidative stressed liver cells isolated from Atlantic salmon (Salmo salar)

    doi: 10.1186/s40064-015-1432-6

    Figure Lengend Snippet: From Western blots it was clear that activated cleaved caspase-3 was more profound in the co-cultured liver cells than in the corresponding mono-cultured liver cells ( a ). Lanes 1 – 4 are mono-cultured liver cells while lanes 5 – 8 is liver cells co-cultured with head kidney cells. Lanes 1 and 5 are controls, lanes 2 and 6 are cells grown in 20 % H-pro, lanes 3 and 7 are the control cells stressed with 200 µM H 2 O 2 and lanes 4 and 8 are the cells grown in 20 % H-pro stressed with 200 µM H 2 O 2. ( b ) The abundance means of activated cleaved caspase-3 relative to the abundance in the control that are set equal to 100 after the abundance was normalized. Cells grown with H-pro had less active cleaved caspase 3 as compared to controls (p = 0.024, Mann–Whitney U-test n = 5 ± SE)

    Article Snippet: This was followed by staining with active caspase-3 (AbCam, cat no #ab77973, 1:50) for 1 h and as a secondary fluorescent antibody goat*rabbit IgG Fluorescin conjugated (AP132F Chemicon, 1:50) giving green fluorescence was used.

    Techniques: Western Blot, Cell Culture, MANN-WHITNEY

    Immunostaining for active cleaved caspase-3 (AbCam, ab77973) verified that cleaved active caspase-3 was higher in the cells cytosol when grown in control media and stressed with 200 µM H 2 O 2 , while the cells grown in media supplemented with H-pro before being stressed with 200 µM H 2 O 2 had almost no active cleaved caspase-3. Providing evidence that the free amino acids and low molecular weight peptides of H-pro had the ability to attenuate activation of caspase-3

    Journal: SpringerPlus

    Article Title: Hydrolyzed fish proteins reduced activation of caspase-3 in H2O2 induced oxidative stressed liver cells isolated from Atlantic salmon (Salmo salar)

    doi: 10.1186/s40064-015-1432-6

    Figure Lengend Snippet: Immunostaining for active cleaved caspase-3 (AbCam, ab77973) verified that cleaved active caspase-3 was higher in the cells cytosol when grown in control media and stressed with 200 µM H 2 O 2 , while the cells grown in media supplemented with H-pro before being stressed with 200 µM H 2 O 2 had almost no active cleaved caspase-3. Providing evidence that the free amino acids and low molecular weight peptides of H-pro had the ability to attenuate activation of caspase-3

    Article Snippet: This was followed by staining with active caspase-3 (AbCam, cat no #ab77973, 1:50) for 1 h and as a secondary fluorescent antibody goat*rabbit IgG Fluorescin conjugated (AP132F Chemicon, 1:50) giving green fluorescence was used.

    Techniques: Immunostaining, Molecular Weight, Activation Assay

    Cleaved caspase-3 expression is reduced in Z-DEVD-FMK injected animals. (A) NM cell bodies, NL cell bodies, NL dendrites and cells in the glial margin express procaspase-3 in control embryos and (B) Z-DEVD-FMK injected embryos. (C) In tissue from control animals, cleaved caspase-3 is expressed in NM and in NL dendrites. (D) In tissue from embryos that received injections of Z-DEVD-FMK into the IVth ventricle, cleaved caspase-3 expression was reduced. (E) While background optical density values did not differ, values in NM were significantly lower in treated vs. control embryos (* p

    Journal: Frontiers in Neural Circuits

    Article Title: Axonal Cleaved Caspase-3 Regulates Axon Targeting and Morphogenesis in the Developing Auditory Brainstem

    doi: 10.3389/fncir.2016.00084

    Figure Lengend Snippet: Cleaved caspase-3 expression is reduced in Z-DEVD-FMK injected animals. (A) NM cell bodies, NL cell bodies, NL dendrites and cells in the glial margin express procaspase-3 in control embryos and (B) Z-DEVD-FMK injected embryos. (C) In tissue from control animals, cleaved caspase-3 is expressed in NM and in NL dendrites. (D) In tissue from embryos that received injections of Z-DEVD-FMK into the IVth ventricle, cleaved caspase-3 expression was reduced. (E) While background optical density values did not differ, values in NM were significantly lower in treated vs. control embryos (* p

    Article Snippet: To label procaspase-3 we used a rabbit polyclonal anti-procaspase-3 primary antibody (Abcam ab90437, Cambridge, MA, USA) diluted 1:500 in blocking solution.

    Techniques: Expressing, Injection

    The effect of NgR silencing on expression of apoptosis-related proteins in NMDA-treated mRGCs ( A ) Western blotting analysis of Bcl-2, activated Bax, total Bax, pro-caspase3 and cleaved caspase3 in the 4 mRGC groups after culturing for 3 days. ( B ) The relative expression of the apoptosis-related proteins (Bcl-2, activated Bax, total Bax, pro-caspase3 and cleaved caspase3) normalized to GAPDH expression is shown. # P

    Journal: Oncotarget

    Article Title: RNAi targeting Nogo Receptor enhanced survival and proliferation of murine retinal ganglion cells during N-methyl-D-aspartate-induced optic nerve crush

    doi: 10.18632/oncotarget.17351

    Figure Lengend Snippet: The effect of NgR silencing on expression of apoptosis-related proteins in NMDA-treated mRGCs ( A ) Western blotting analysis of Bcl-2, activated Bax, total Bax, pro-caspase3 and cleaved caspase3 in the 4 mRGC groups after culturing for 3 days. ( B ) The relative expression of the apoptosis-related proteins (Bcl-2, activated Bax, total Bax, pro-caspase3 and cleaved caspase3) normalized to GAPDH expression is shown. # P

    Article Snippet: After blocking the membrane for 1 h with 5% BSA at room temperature, the membrane was incubated overnight at 4°C with primary antibodies for NgR (1: 1000, ab184556, Abcam, Cambridge, UK), RhoA (1: 5000, ab187027, Abcam, Cambridge, UK), ROCK2 (1: 1000, ab183636, Abcam, Cambridge, UK), Bcl-2 (1: 1000, ab32124, Abcam, Cambridge, UK), total Bax (1: 1000, ab32503, Abcam, USA), activated Bax (1:1000, ALX-804-224-C100, Enzo, Farmingdale, NY, USA), cleaved caspase3 (1:1000, 9661S, CST, San Antonio, TX, USA) and pro-caspase3 (1:1000, ab32150, Abcam, USA).

    Techniques: Expressing, Western Blot

    Procaspase-3 is expressed in brain tumors and its expression is a prognostic factor for survival of glioblastoma patients A. Analysis of CASP3 expression in the NCI REMBRANDT database demonstrates that CASP3 is more highly expressed in brain tumors compared to non-tumor tissues (*, p

    Journal: Oncotarget

    Article Title: Synergistic and targeted therapy with a procaspase-3 activator and temozolomide extends survival in glioma rodent models and is feasible for the treatment of canine malignant glioma patients

    doi: 10.18632/oncotarget.19085

    Figure Lengend Snippet: Procaspase-3 is expressed in brain tumors and its expression is a prognostic factor for survival of glioblastoma patients A. Analysis of CASP3 expression in the NCI REMBRANDT database demonstrates that CASP3 is more highly expressed in brain tumors compared to non-tumor tissues (*, p

    Article Snippet: Slides were incubated with procaspase-3 antibody (Abcam #ab32150) for 39 minutes at a dilution of 1:3000, washed, and then incubated with Rabbit-on-Canine HRP-Polymer (Biocare #RC542) for 30 minutes.

    Techniques: Expressing

    Procaspase-3 immunohistochemical staining of spontaneous canine astrocytomas A portion of the low power image (0.5X) on the far left is enlarged to 200x in the image at right. The blue and red stars show the approximate areas of tumor and normal tissue; some PC-3 positive tumor cells can be observed infiltrating between the tumor mass and normal tissues in images B and C. A. A low grade astrocytoma tumor from a necropsy specimen did not stain positively for procaspase-3. B. Grade III astrocytoma, necropsy specimen. ∼30-40% of cells in the tumor tissue stained with moderate to strong cytoplasmic PC-3 staining intensity; both the cellularity and staining intensity are increased relative to normal brain tissue. C. GBM, necropsy specimen. Over 90% of cells have moderate cytoplasmic PC-3 staining intensity in this tumor; again, both the cellularity and staining intensity are increased relative to normal brain tissue. D. GBM biopsy tissue. > 90% of cells contained moderate to strong cytoplasmic PC-3 staining intensity. This staining intensity is markedly increased as compared to the normal tissues observed in images A, B and C. No normal tissue was available in this sample.

    Journal: Oncotarget

    Article Title: Synergistic and targeted therapy with a procaspase-3 activator and temozolomide extends survival in glioma rodent models and is feasible for the treatment of canine malignant glioma patients

    doi: 10.18632/oncotarget.19085

    Figure Lengend Snippet: Procaspase-3 immunohistochemical staining of spontaneous canine astrocytomas A portion of the low power image (0.5X) on the far left is enlarged to 200x in the image at right. The blue and red stars show the approximate areas of tumor and normal tissue; some PC-3 positive tumor cells can be observed infiltrating between the tumor mass and normal tissues in images B and C. A. A low grade astrocytoma tumor from a necropsy specimen did not stain positively for procaspase-3. B. Grade III astrocytoma, necropsy specimen. ∼30-40% of cells in the tumor tissue stained with moderate to strong cytoplasmic PC-3 staining intensity; both the cellularity and staining intensity are increased relative to normal brain tissue. C. GBM, necropsy specimen. Over 90% of cells have moderate cytoplasmic PC-3 staining intensity in this tumor; again, both the cellularity and staining intensity are increased relative to normal brain tissue. D. GBM biopsy tissue. > 90% of cells contained moderate to strong cytoplasmic PC-3 staining intensity. This staining intensity is markedly increased as compared to the normal tissues observed in images A, B and C. No normal tissue was available in this sample.

    Article Snippet: Slides were incubated with procaspase-3 antibody (Abcam #ab32150) for 39 minutes at a dilution of 1:3000, washed, and then incubated with Rabbit-on-Canine HRP-Polymer (Biocare #RC542) for 30 minutes.

    Techniques: Immunohistochemistry, Staining

    Effects of caspase inhibitors on ZIKV Env-mediated apoptosis in PC12 cells. (A) Cells were transduced with LV-ZIKV-prM-Env, LV-ZIKV-M-Env, LV-ZIKV-Env or LV-eGFP (100 MOI) for 6 h followed by treatment with either caspase-3 inhibitor Ac-DEVD-CMK (100 μmol/L), caspase-8 inhibitor ZIETD-FMK (100 μmol/L), caspase-9 inhibitor ZLEHD-FMK (100 μmol/L) or control solvent (DMSO) for 24 h. Caspase-3, caspase-8 and caspase-9 were detected by western blot. (B) Treated cells were double- stained with Alexa Fluor 647 conjugated annexin V and PI. The annexin V-positive cells as a percent of the total number of cells were measured from flow cytometric analysis. **: P

    Journal: International Journal of Biological Sciences

    Article Title: Zika Virus Envelope Protein induces G2/M Cell Cycle Arrest and Apoptosis via an Intrinsic Cell Death Signaling Pathway in Neuroendocrine PC12 Cells

    doi: 10.7150/ijbs.26400

    Figure Lengend Snippet: Effects of caspase inhibitors on ZIKV Env-mediated apoptosis in PC12 cells. (A) Cells were transduced with LV-ZIKV-prM-Env, LV-ZIKV-M-Env, LV-ZIKV-Env or LV-eGFP (100 MOI) for 6 h followed by treatment with either caspase-3 inhibitor Ac-DEVD-CMK (100 μmol/L), caspase-8 inhibitor ZIETD-FMK (100 μmol/L), caspase-9 inhibitor ZLEHD-FMK (100 μmol/L) or control solvent (DMSO) for 24 h. Caspase-3, caspase-8 and caspase-9 were detected by western blot. (B) Treated cells were double- stained with Alexa Fluor 647 conjugated annexin V and PI. The annexin V-positive cells as a percent of the total number of cells were measured from flow cytometric analysis. **: P

    Article Snippet: These data suggest the involvement of a caspase-9-mediated intrinsic signaling pathway followed by downstream activation of caspase-3 in the apoptosis elicited by overexpression of ZIKV prM-Env, M-Env and Env in PC12 cells.

    Techniques: Transduction, Western Blot, Staining, Flow Cytometry

    Apoptosis and Extracellular ATP Concentration. Proportion of Caspase 3 positive cells post-heat shock, MLO-Y4 osteocytes and B35 neurons combined ( left ). Relative concentration of ATP in cell medium from both sides of the device (heated and unheated)

    Journal: Biomedical microdevices

    Article Title: A multiscale fluidic device for the study of dendrite-mediated cell to cell communication

    doi: 10.1007/s10544-017-0212-1

    Figure Lengend Snippet: Apoptosis and Extracellular ATP Concentration. Proportion of Caspase 3 positive cells post-heat shock, MLO-Y4 osteocytes and B35 neurons combined ( left ). Relative concentration of ATP in cell medium from both sides of the device (heated and unheated)

    Article Snippet: Apoptosis was quantified by caspase 3 dye ( , Thermo Fisher Scientific) on the heated and unheated side of the device at 1, 6, and 12 h post-heat shock.

    Techniques: Concentration Assay

    Caspase-3 expression in the gastric mucosa of rats with acetic acid-induced gastric ulcers treated with oral administration of vehicle, lansoprazole, or hydroalcoholic extract from the leaves of Eugenia punicifolia or 14 d. The data represent relative expression of caspase-3 normalized to the expression of housekeeping genes (actin). The results represent mean ± standard error of the mean for each group ( n = 6). Statistical significance was determined using one-way ANOVA followed by Dunnett's test. No statistically significant differences were found. HEEP: Hydroalcoholic extract from the leaves of Eugenia punicifolia .

    Journal: World Journal of Gastroenterology

    Article Title: Sex-specific effects of Eugenia punicifolia extract on gastric ulcer healing in rats

    doi: 10.3748/wjg.v24.i38.4369

    Figure Lengend Snippet: Caspase-3 expression in the gastric mucosa of rats with acetic acid-induced gastric ulcers treated with oral administration of vehicle, lansoprazole, or hydroalcoholic extract from the leaves of Eugenia punicifolia or 14 d. The data represent relative expression of caspase-3 normalized to the expression of housekeeping genes (actin). The results represent mean ± standard error of the mean for each group ( n = 6). Statistical significance was determined using one-way ANOVA followed by Dunnett's test. No statistically significant differences were found. HEEP: Hydroalcoholic extract from the leaves of Eugenia punicifolia .

    Article Snippet: In the next step, the proteins were electrophoretically transferred onto a nitrocellulose membrane or PVDF membrane (for epidermal growth factor (EGF)), blocked with 5% non-fat milk diluted in PBS, and incubated with the following primary antibodies: anti-cyclooxygenase (COX)-1 (1:10.000, ab133319); anti-COX-2 (1:1000, ab52237); anti-vascular endothelial growth factor (VEGF) (1:1.000, ab46154); anti-EGF (1:800, ab77851), anti-Bcl-2 (1:800, ab59348), anti-caspase-3 (1:10.000, ab32499), anti-caspase-8 (1:2.000, ab25901), and anti-caspase-9 (1:5.000, ab32539) (all from Abcam, Cambridge, MA, United States).

    Techniques: Expressing

    GRP78, caspase-12, and caspase-3 protein expression in mouse colon tissue (immunohistochemical staining, 400×). A, blank control group; B, model group; C, low-dose BBR group; D, medium-dose BBR group; E, high-dose BBR group.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Effect of Berberine from Coptis chinensis on Apoptosis of Intestinal Epithelial Cells in a Mouse Model of Ulcerative Colitis: Role of Endoplasmic Reticulum Stress

    doi: 10.1155/2020/3784671

    Figure Lengend Snippet: GRP78, caspase-12, and caspase-3 protein expression in mouse colon tissue (immunohistochemical staining, 400×). A, blank control group; B, model group; C, low-dose BBR group; D, medium-dose BBR group; E, high-dose BBR group.

    Article Snippet: Drugs and Reagents The chemicals utilized in this study were as follows: dextran sulfate sodium (DSS; MP Biomedicals, LLC, Solon, OH, USA; lot number: BJ14745, molecular weight: 5000); berberine hydrochloride (BBR; Shanghai Yuanye Bio-technology Co., Ltd., Shanghai, China; lot number: Y18D8C50814, molecular weight: 371.81); glucose-regulated protein 78 (GRP78), caspase-12, and caspase-3 primary antibodies (Abcam, Cambridge, UK; lot numbers: GR309483-1, ab62484, and ab13847, respectively); anti-rabbit and anti-mouse secondary antibody (Beijing ZSGB-BIO, Beijing, China; lot numbers: K167722B and K175212C, respectively); proteinase K (Beijing Tiangen, Beijing, China; lot number: M2011); DAB chromogenic reagent kit (Beijing ZSGB-BIO, lot number: K167722A); TUNEL in situ apoptosis detection kit (Roche, Basel, Switzerland; lot number: 11906800); high-purity total RNA rapid extraction kit (Shanghai Generay, Shanghai, China; lot number: 1703G01); HiScript-II Q RT SuperMix for qPCR reverse transcription kit (Nanjing Vazyme, Nanjing, China; lot number: 7E092G6); and ChamQ SYBR Color qPCR Master Mix (Nanjing Vazyme Co.; lot number: 7E092H6).

    Techniques: Expressing, Immunohistochemistry, Staining

    Apoptosis of cortical neurons in traumatic brain injury. ( A ) Caspase-3 positive pyramidal cells in the vicinity of a cortical contusion from a patient with traumatic brain injury (cases 18–95). ( B ) Caspase-3 positive neuronal like cells with dendritic processes in the vicinity of the contusion area of another patient with traumatic brain injury. Scale bar = 10 μm.

    Journal: Brain

    Article Title: In vivo monitoring of neuronal loss in traumatic brain injury: a microdialysis study

    doi: 10.1093/brain/awq360

    Figure Lengend Snippet: Apoptosis of cortical neurons in traumatic brain injury. ( A ) Caspase-3 positive pyramidal cells in the vicinity of a cortical contusion from a patient with traumatic brain injury (cases 18–95). ( B ) Caspase-3 positive neuronal like cells with dendritic processes in the vicinity of the contusion area of another patient with traumatic brain injury. Scale bar = 10 μm.

    Article Snippet: Neuronal apoptosis was assessed by staining for caspase-3 (1:500, Clone 269518, Code MAB 835, R & D System, Minneapolis, USA) as described ( ; ; ).

    Techniques:

    The effect of MPT0E028 on the growth of HCT116 cells  in vivo . All tumors grew to the 1,200-mm 3  endpoint volume. (A) Tumors were measured regularly and growth delay was calculated for treatment groups relative to control tumors (TGD). (B) Kaplan-Meier survival analysis was based on the tumor growth endpoint. (C) Inhibition of tumor growth curves represented a mean±SEM and percentage change in mean tumor volume (percent TGI). (D) Body weights were measured daily during the first week and then 2 times per week. The body weight ratio was calculated relative to the baseline measurement. (E)  In vivo  effect of MPT0E028 on the expression of caspase 3, PARP, acetyl-histone H3 and acetyl-µ-tubulin in HCT116 xenograft tumors as determined by western blotting.

    Journal: PLoS ONE

    Article Title: Anticancer Activity of MPT0E028, a Novel Potent Histone Deacetylase Inhibitor, in Human Colorectal Cancer HCT116 Cells In Vitro and In Vivo

    doi: 10.1371/journal.pone.0043645

    Figure Lengend Snippet: The effect of MPT0E028 on the growth of HCT116 cells in vivo . All tumors grew to the 1,200-mm 3 endpoint volume. (A) Tumors were measured regularly and growth delay was calculated for treatment groups relative to control tumors (TGD). (B) Kaplan-Meier survival analysis was based on the tumor growth endpoint. (C) Inhibition of tumor growth curves represented a mean±SEM and percentage change in mean tumor volume (percent TGI). (D) Body weights were measured daily during the first week and then 2 times per week. The body weight ratio was calculated relative to the baseline measurement. (E) In vivo effect of MPT0E028 on the expression of caspase 3, PARP, acetyl-histone H3 and acetyl-µ-tubulin in HCT116 xenograft tumors as determined by western blotting.

    Article Snippet: As shown in , caspase 3, PARP and acetyl-histone H3 were substantially induced in MPT0E028-treated group while acetyl-µ-tubulin were found more profoundly in SAHA-treated group, which is consistent with our finding in vitro .

    Techniques: In Vivo, Inhibition, Expressing, Western Blot

    The effects of MPT0E028 on cell growth and cell cycle progression in human HCT116 cells. (A) Concentration-dependent effect of MPT0E028 and SAHA on cell growth. HCT116 cells were incubated without or with the indicated concentrations of MPT0E028 or SAHA for 48 h. Cell growth was evaluated by SRB assay. Data were expressed as mean±S.E.M. of at least 3 independent experiments. (B) Concentration-dependent effects of MPT0E028 and SAHA on cell cycle progression. HCT116 cells were treated without or with the indicated concentrations of MPT0E028 or SAHA for 24 h and were analyzed by flow cytometry for cell cycle distribution. (C, D) Data shown are the means of at least 3 independent experiments. (E) Time-dependent effects of MPT0E028 and SAHA on subG1 population. HCT116 cells were treated without or with 1 µM MPT0E028 or SAHA for the indicated time interval and were analyzed by flow cytometry for subG1 population. (F) MPT0E028 induced-caspase 3 and PARP activation. HCT116 cells were treated without or with the indicated concentration of MPT0E028 or SAHA for 24 h subject to western blot for caspase 3 and PARP analysis. (G) MPT0E028 induced casepase-dependent cell apoptosis. HCT116 cells were treated without or with 3 µM MPTE028, SAHA or 20 µM z-VAD-fmk for 24 h and subjected to western blot for caspase 3 and PARP analysis.

    Journal: PLoS ONE

    Article Title: Anticancer Activity of MPT0E028, a Novel Potent Histone Deacetylase Inhibitor, in Human Colorectal Cancer HCT116 Cells In Vitro and In Vivo

    doi: 10.1371/journal.pone.0043645

    Figure Lengend Snippet: The effects of MPT0E028 on cell growth and cell cycle progression in human HCT116 cells. (A) Concentration-dependent effect of MPT0E028 and SAHA on cell growth. HCT116 cells were incubated without or with the indicated concentrations of MPT0E028 or SAHA for 48 h. Cell growth was evaluated by SRB assay. Data were expressed as mean±S.E.M. of at least 3 independent experiments. (B) Concentration-dependent effects of MPT0E028 and SAHA on cell cycle progression. HCT116 cells were treated without or with the indicated concentrations of MPT0E028 or SAHA for 24 h and were analyzed by flow cytometry for cell cycle distribution. (C, D) Data shown are the means of at least 3 independent experiments. (E) Time-dependent effects of MPT0E028 and SAHA on subG1 population. HCT116 cells were treated without or with 1 µM MPT0E028 or SAHA for the indicated time interval and were analyzed by flow cytometry for subG1 population. (F) MPT0E028 induced-caspase 3 and PARP activation. HCT116 cells were treated without or with the indicated concentration of MPT0E028 or SAHA for 24 h subject to western blot for caspase 3 and PARP analysis. (G) MPT0E028 induced casepase-dependent cell apoptosis. HCT116 cells were treated without or with 3 µM MPTE028, SAHA or 20 µM z-VAD-fmk for 24 h and subjected to western blot for caspase 3 and PARP analysis.

    Article Snippet: As shown in , caspase 3, PARP and acetyl-histone H3 were substantially induced in MPT0E028-treated group while acetyl-µ-tubulin were found more profoundly in SAHA-treated group, which is consistent with our finding in vitro .

    Techniques: Concentration Assay, Incubation, Sulforhodamine B Assay, Flow Cytometry, Cytometry, Activation Assay, Western Blot

    Validation of protein and mRNA level dysregulations. (A) Quantitative immunoblots confirmed neuronal loss (marker NeuN), astrogliosis (marker GFAP) and microgliosis (marker IBA1) to occur in Atxn2 -CAG100-KIN spinal cord at the preterminal stage of 14 months age, but not at the early KIN stage of 3 months age and in the Atxn2 -KO at 6 months. Significantly increased levels in KIN at 14 months were also shown for TDP43 and the factor responsible for its cleavage, CASP3. (B) Quantitative RT-PCR analyses showed a significant deficit of NeuN transcript ( Rbfox3 ) already at incipient disease stage in 3-month-old KIN, whereas astrogliosis (marker Gfap ) and microgliosis (marker IBA1 transcript Aif1 ) became significant at late state. Protein abundance (C) and transcript levels (D) were also documented for PGRN (encoded by Grn mRNA) as molecular marker of lysosomal activation and atrophy, as well as RIPK1 as molecular marker of RNA-toxicity and necroptosis. Again, a significant elevation of Grn mRNA at the age of 3 months suggested atrophy and lysosomal breakdown to occur in parallel with first locomotor deficits, predating necroptotic cell death.

    Journal: bioRxiv

    Article Title: Atxn2-CAG100-KnockIn mouse spinal cord shows progressive TDP43 pathology associated with cholesterol biosynthesis suppression

    doi: 10.1101/838177

    Figure Lengend Snippet: Validation of protein and mRNA level dysregulations. (A) Quantitative immunoblots confirmed neuronal loss (marker NeuN), astrogliosis (marker GFAP) and microgliosis (marker IBA1) to occur in Atxn2 -CAG100-KIN spinal cord at the preterminal stage of 14 months age, but not at the early KIN stage of 3 months age and in the Atxn2 -KO at 6 months. Significantly increased levels in KIN at 14 months were also shown for TDP43 and the factor responsible for its cleavage, CASP3. (B) Quantitative RT-PCR analyses showed a significant deficit of NeuN transcript ( Rbfox3 ) already at incipient disease stage in 3-month-old KIN, whereas astrogliosis (marker Gfap ) and microgliosis (marker IBA1 transcript Aif1 ) became significant at late state. Protein abundance (C) and transcript levels (D) were also documented for PGRN (encoded by Grn mRNA) as molecular marker of lysosomal activation and atrophy, as well as RIPK1 as molecular marker of RNA-toxicity and necroptosis. Again, a significant elevation of Grn mRNA at the age of 3 months suggested atrophy and lysosomal breakdown to occur in parallel with first locomotor deficits, predating necroptotic cell death.

    Article Snippet: The following antibodies were used: ACTB (Sigma A5441, 1:10000), ATXN2 (Proteintech 21776-1-AP, 1:500), CASP3 (Cell Signaling 9665, 1:1000), GFAP (Dako ZO334, 1:2000), GPNMB (Biotechne AF 2330, 1:500), IBA1 (Wako 019-19741, 1:2000), NeuN (Millipore ABN78, 1:1000), PGRN (Biotechne AF 2557, 1:250), PQBP1 (Biomol A302-802A-M, 1:500), RIPK1 (Cell Signaling 3493S, 1:500), TDP43 (Abcam ab41881, 1:1000).

    Techniques: Western Blot, Marker, Quantitative RT-PCR, Activation Assay

    Effects of low concentrations of ethanol, nicotine and salsolinol alone or in combination on caspase-3 and β actin protein in human neuroblastoma SH-SY5Y cells. Cells were treated with low concentrations of ethanol (10 mM) or nicotine (20 μM)

    Journal: Neurotoxicity research

    Article Title: Toxic Effects of Low Alcohol and Nicotine Combinations in SH-SY5Y Cells are Apoptotically Mediated

    doi: 10.1007/s12640-011-9239-x

    Figure Lengend Snippet: Effects of low concentrations of ethanol, nicotine and salsolinol alone or in combination on caspase-3 and β actin protein in human neuroblastoma SH-SY5Y cells. Cells were treated with low concentrations of ethanol (10 mM) or nicotine (20 μM)

    Article Snippet: To quantify caspase-3 levels, following the 24 h incubation cells were removed and were incubated in cell lysis buffer (10 mM Tris-buffer, 5 mM EDTA, 150 mM NaCl, 0.5% Triton X-100 (v/v) with protease inhibitors (Sigma-Aldrich, St. Louis, MO).

    Techniques:

    Deletion of partial CASP-3 genomic DNA in MCF-7 cells. (A) Images of DNA electrophoresis of the polymerase chain reaction (PCR) products for the CASP-3 genomic DNA and cDNA, respectively. Both PCR products from MCF-7 cells are shorter than those from A431 cells, resulting from a 47-base pair deletion within exon 4 of the human CASP-3 genomic DNA. (B) Sequencing results of the PCR products from the two cell lines. The yellow underline indicates the sequence of the deleted fragment. (C) Results of Western blotting analysis show expression of pro-caspase-3 protein in A431 cells but not in MCF-7 cells. Tubulin was used as loading control.

    Journal: Journal of Breast Cancer

    Article Title: Cell-in-Cell Death Is Not Restricted by Caspase-3 Deficiency in MCF-7 Cells

    doi: 10.4048/jbc.2016.19.3.231

    Figure Lengend Snippet: Deletion of partial CASP-3 genomic DNA in MCF-7 cells. (A) Images of DNA electrophoresis of the polymerase chain reaction (PCR) products for the CASP-3 genomic DNA and cDNA, respectively. Both PCR products from MCF-7 cells are shorter than those from A431 cells, resulting from a 47-base pair deletion within exon 4 of the human CASP-3 genomic DNA. (B) Sequencing results of the PCR products from the two cell lines. The yellow underline indicates the sequence of the deleted fragment. (C) Results of Western blotting analysis show expression of pro-caspase-3 protein in A431 cells but not in MCF-7 cells. Tubulin was used as loading control.

    Article Snippet: Membranes were probed separately with anti-pro-caspase-3 (Millipore, Billerica, USA) and anti-activated caspase-3 (Millipore) antibodies to detect the expression of caspase-3.

    Techniques: Nucleic Acid Electrophoresis, Polymerase Chain Reaction, Sequencing, Western Blot, Expressing

    Lysosome-dependent cell-in-cell death of A431 and MCF-7 cell lines. (A) Kinetic quantification of internalized terminal-deoxynucleotidyl transferase mediated nick end labeling (TUNEL) positive cells, internalized cells containing cleaved caspase-3 and internalized cells demonstrating lysosome activation in cell-in-cell structures of A431 cells and MCF-7 cells. One representative experiment of three independent experiments is shown. Data are presented as means±SD. (B) Confocal images show TUNEL positive (green) and DNA fragmentation (blue) of internalized A431 cells (red) and MCF-7 cells (red) at 48 hours. Both internalized A431 and MCF-7 showed inconspicuous changes in cell size and gradual nuclei degradation after entosis. Nuclei were labeled with 4',6-diamidino-2-phenylindole (DAPI). The scale bars are 10 µm. (C) As early as 6 hours after cell engulfment, the release of active cathepsin B (red) from the lysosomes into the plasma of the internalized cells was detected and was also seen in the surrounding cytoplasm of outer cells. Cells were stained with CellTracker™ Green and cell nuclei were labeled with DAPI. The scale bars are 10 µm. (D) A431 cells (green) and MCF-7 (green) cells are stained for lysosomes using LysoTracker™ Red (red), which binds to acidified compartments after 30 hours of culture. Confocal images show positive staining for cathepsin B in the cytoplasm of internalized cells. Scale bars are 10 µm.

    Journal: Journal of Breast Cancer

    Article Title: Cell-in-Cell Death Is Not Restricted by Caspase-3 Deficiency in MCF-7 Cells

    doi: 10.4048/jbc.2016.19.3.231

    Figure Lengend Snippet: Lysosome-dependent cell-in-cell death of A431 and MCF-7 cell lines. (A) Kinetic quantification of internalized terminal-deoxynucleotidyl transferase mediated nick end labeling (TUNEL) positive cells, internalized cells containing cleaved caspase-3 and internalized cells demonstrating lysosome activation in cell-in-cell structures of A431 cells and MCF-7 cells. One representative experiment of three independent experiments is shown. Data are presented as means±SD. (B) Confocal images show TUNEL positive (green) and DNA fragmentation (blue) of internalized A431 cells (red) and MCF-7 cells (red) at 48 hours. Both internalized A431 and MCF-7 showed inconspicuous changes in cell size and gradual nuclei degradation after entosis. Nuclei were labeled with 4',6-diamidino-2-phenylindole (DAPI). The scale bars are 10 µm. (C) As early as 6 hours after cell engulfment, the release of active cathepsin B (red) from the lysosomes into the plasma of the internalized cells was detected and was also seen in the surrounding cytoplasm of outer cells. Cells were stained with CellTracker™ Green and cell nuclei were labeled with DAPI. The scale bars are 10 µm. (D) A431 cells (green) and MCF-7 (green) cells are stained for lysosomes using LysoTracker™ Red (red), which binds to acidified compartments after 30 hours of culture. Confocal images show positive staining for cathepsin B in the cytoplasm of internalized cells. Scale bars are 10 µm.

    Article Snippet: Membranes were probed separately with anti-pro-caspase-3 (Millipore, Billerica, USA) and anti-activated caspase-3 (Millipore) antibodies to detect the expression of caspase-3.

    Techniques: End Labeling, TUNEL Assay, Activation Assay, Labeling, Staining

    Absence of caspase-3 protein in MCF-7 cells leading to an atypical apoptosis. (A) Expression of cleaved caspase-3 protein in A431 cells but not in MCF-7 cells. Both tumor cell lines were treated with (+) or without (–) staurosporine (staurosp.) for 16 hours and the cell lysates were analyzed by Western blotting. β-Actin was used as loading control. (B) Cytotoxicity assays of A431 and MCF-7 cells using the LDH method after treatment with staurosporine for 16 hours. Cells treated with the solvent dimethyl sulphoxide (DMSO) were used as negative controls. (C) Terminal-deoxynucleoitidyl transferase mediated nick end labeling (TUNEL) assay showed similar mortalities of the two cell lines following treatment with staurosporine for 16 hours. (D) Confocal images show positive TUNEL staining in both A431 and MCF-7 cells after treatment with staurosporine. Nuclear pyknosis was obvious in dying A431 cells but not in dying MCF-7 cells. Cells were labeled with CellTracker™ Red, and cell nuclei were stained with 4',6-diamidino-2-phenylindole (DAPI). The scale bars are 10 µm. (E) Cell cycle analysis of A431 and MCF-7 cells treated with or without staurosporine for 8 hours. The sub-G1 apoptotic peak demonstrating nuclear pyknosis in apoptotic cells is seen before the G0/G1 peak in A431 cells but not in MCF-7 cells after apoptosis induction. (F) DNA was prepared from cells untreated or treated for 8 hours or 16 hours with staurosporine and analyzed using a 1.6% agarose gel. There was obvious DNA ladder formation in A431 but not in MCF-7 cells after apoptosis induction. Lane M: DNA ladder.

    Journal: Journal of Breast Cancer

    Article Title: Cell-in-Cell Death Is Not Restricted by Caspase-3 Deficiency in MCF-7 Cells

    doi: 10.4048/jbc.2016.19.3.231

    Figure Lengend Snippet: Absence of caspase-3 protein in MCF-7 cells leading to an atypical apoptosis. (A) Expression of cleaved caspase-3 protein in A431 cells but not in MCF-7 cells. Both tumor cell lines were treated with (+) or without (–) staurosporine (staurosp.) for 16 hours and the cell lysates were analyzed by Western blotting. β-Actin was used as loading control. (B) Cytotoxicity assays of A431 and MCF-7 cells using the LDH method after treatment with staurosporine for 16 hours. Cells treated with the solvent dimethyl sulphoxide (DMSO) were used as negative controls. (C) Terminal-deoxynucleoitidyl transferase mediated nick end labeling (TUNEL) assay showed similar mortalities of the two cell lines following treatment with staurosporine for 16 hours. (D) Confocal images show positive TUNEL staining in both A431 and MCF-7 cells after treatment with staurosporine. Nuclear pyknosis was obvious in dying A431 cells but not in dying MCF-7 cells. Cells were labeled with CellTracker™ Red, and cell nuclei were stained with 4',6-diamidino-2-phenylindole (DAPI). The scale bars are 10 µm. (E) Cell cycle analysis of A431 and MCF-7 cells treated with or without staurosporine for 8 hours. The sub-G1 apoptotic peak demonstrating nuclear pyknosis in apoptotic cells is seen before the G0/G1 peak in A431 cells but not in MCF-7 cells after apoptosis induction. (F) DNA was prepared from cells untreated or treated for 8 hours or 16 hours with staurosporine and analyzed using a 1.6% agarose gel. There was obvious DNA ladder formation in A431 but not in MCF-7 cells after apoptosis induction. Lane M: DNA ladder.

    Article Snippet: Membranes were probed separately with anti-pro-caspase-3 (Millipore, Billerica, USA) and anti-activated caspase-3 (Millipore) antibodies to detect the expression of caspase-3.

    Techniques: Expressing, Western Blot, End Labeling, TUNEL Assay, Staining, Labeling, Cell Cycle Assay, Agarose Gel Electrophoresis

    Entosis converting to apoptosis in the presence of caspase-3. (A) Immunofluorescence of cleaved caspase-3 activity in A431 cells, caspase-3 expressing MCF-7 cells and MCF-7 cells with or without concanamycin A (con A) treatment. The three kinds of cells showed typical lysosomal cell-in-cell death before treatment. After treatment we could see clear caspase-3 activation, nuclear shrinkage, nuclear pyknosis and other apoptotic forms in A431 and caspase-3 expressing MCF-7 cells. In contrast, no caspase-3 activity or other apoptosis characteristics was detected in MCF-7 cells after the same treatment. These pictures were taken after 24 hours of cell incubation. The scale bars are 10 µm. Arrows point to entosis cells. (B) Result of Western blot showed fusion protein caspase-3-green fluorescent protein (GFP) (arrows marked) expressed in caspase-3 expressing MCF-7 cells which was about 69 kDa. (C) Result of Western blotting showed caspase-3-GFP (69 kDa) and cleaved caspase-3 (17 kDa, arrow marked) were detected in caspase-3 expressing MCF-7 cells but not in MCF-7 cells. Both of the cells were treated with staurosporine for 16 hours. (D) Statistical analysis of cell-in-cell death of A431 cells, caspase-3 expressing MCF-7 cells and MCF-7 cells with or without Concanamycin A treatment for 48 hours determined by terminal-deoxynucleotidyl transferase mediated nick end labeling (TUNEL) assay. Data are presented as means±SD.

    Journal: Journal of Breast Cancer

    Article Title: Cell-in-Cell Death Is Not Restricted by Caspase-3 Deficiency in MCF-7 Cells

    doi: 10.4048/jbc.2016.19.3.231

    Figure Lengend Snippet: Entosis converting to apoptosis in the presence of caspase-3. (A) Immunofluorescence of cleaved caspase-3 activity in A431 cells, caspase-3 expressing MCF-7 cells and MCF-7 cells with or without concanamycin A (con A) treatment. The three kinds of cells showed typical lysosomal cell-in-cell death before treatment. After treatment we could see clear caspase-3 activation, nuclear shrinkage, nuclear pyknosis and other apoptotic forms in A431 and caspase-3 expressing MCF-7 cells. In contrast, no caspase-3 activity or other apoptosis characteristics was detected in MCF-7 cells after the same treatment. These pictures were taken after 24 hours of cell incubation. The scale bars are 10 µm. Arrows point to entosis cells. (B) Result of Western blot showed fusion protein caspase-3-green fluorescent protein (GFP) (arrows marked) expressed in caspase-3 expressing MCF-7 cells which was about 69 kDa. (C) Result of Western blotting showed caspase-3-GFP (69 kDa) and cleaved caspase-3 (17 kDa, arrow marked) were detected in caspase-3 expressing MCF-7 cells but not in MCF-7 cells. Both of the cells were treated with staurosporine for 16 hours. (D) Statistical analysis of cell-in-cell death of A431 cells, caspase-3 expressing MCF-7 cells and MCF-7 cells with or without Concanamycin A treatment for 48 hours determined by terminal-deoxynucleotidyl transferase mediated nick end labeling (TUNEL) assay. Data are presented as means±SD.

    Article Snippet: Membranes were probed separately with anti-pro-caspase-3 (Millipore, Billerica, USA) and anti-activated caspase-3 (Millipore) antibodies to detect the expression of caspase-3.

    Techniques: Immunofluorescence, Activity Assay, Expressing, Activation Assay, Incubation, Western Blot, End Labeling, TUNEL Assay

    LYT (Luoyutong) reduces neuronal apoptosis and decreases the level of caspase-3. (a) Neuronal apoptosis in the ipsilateral cortex was detected by terminal deoxynucleotidyl transferase dUTP nick end labeling and 4′ 6-diamidino-2-phenylindole double staining 14 days after ischemic reperfusion. (b) Expression of activated caspase-3 was detected by Western blot 14 days after ischemic reperfusion. n = 3. ∗ P

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Luoyutong Treatment Promotes Functional Recovery and Neuronal Plasticity after Cerebral Ischemia-Reperfusion Injury in Rats

    doi: 10.1155/2015/369021

    Figure Lengend Snippet: LYT (Luoyutong) reduces neuronal apoptosis and decreases the level of caspase-3. (a) Neuronal apoptosis in the ipsilateral cortex was detected by terminal deoxynucleotidyl transferase dUTP nick end labeling and 4′ 6-diamidino-2-phenylindole double staining 14 days after ischemic reperfusion. (b) Expression of activated caspase-3 was detected by Western blot 14 days after ischemic reperfusion. n = 3. ∗ P

    Article Snippet: Membranes were incubated overnight at 4°C in a 1 : 1000 dilution of primary antibodies against caspase-3 (Abcam, Cambridge, UK), synaptophysin (Abcam), MAP-2 (Cell Signaling Technology, Boston, MA, USA), MBP (Abcam), brain derived neurotrophic factor (BDNF) (Abcam), or basic fibroblast growth factor (b-FGF) (Abcam).

    Techniques: TUNEL Assay, Double Staining, Expressing, Western Blot

    Silence ERK pathway partially repeal the antiapoptosis effects of carvacrol. (a) The efficiency and specificity of siRNA directed against ERK. (b)–(d) Ethanol increases hippocampal neurons apoptotic rate and caspase-3 activity as well as decreasing cell viability compared with control group. These proapoptotic effects can be reversed by carvacrol. However, when it is silence or block ERK pathway, carvacrol antiapoptotic effects can be partially repealed. The data are expressed as the mean ± SEM ( n = 6 per group). ∗∗ P

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: The Neuroprotective Effects of Carvacrol on Ethanol-Induced Hippocampal Neurons Impairment via the Antioxidative and Antiapoptotic Pathways

    doi: 10.1155/2017/4079425

    Figure Lengend Snippet: Silence ERK pathway partially repeal the antiapoptosis effects of carvacrol. (a) The efficiency and specificity of siRNA directed against ERK. (b)–(d) Ethanol increases hippocampal neurons apoptotic rate and caspase-3 activity as well as decreasing cell viability compared with control group. These proapoptotic effects can be reversed by carvacrol. However, when it is silence or block ERK pathway, carvacrol antiapoptotic effects can be partially repealed. The data are expressed as the mean ± SEM ( n = 6 per group). ∗∗ P

    Article Snippet: The membranes were then blocked using 5% fat-free milk in Tris-buffered saline with 1% Tween-20 (TBS-T) for 1 h and then were incubated with the following incubation with primary antibodies overnight at 4°C: anti-caspase-3 (1 : 300, Santa Cruz), anti-Bcl-2 (1 : 200, Santa Cruz), anti-Bax (1 : 200, Santa Cruz), anti-phospho-ERK (1 : 1000, Cell Signaling), anti-ERK (1 : 1000, Cell Signaling), anti-phospho-JNK (1 : 200, Santa Cruz), anti-JNK (1 : 200, Santa Cruz), anti-phospho-p38 (1 : 200, Santa Cruz), anti-p38 (1 : 200, Santa Cruz), and anti-β -actin (1 : 2000, Santa Cruz), respectively.

    Techniques: Activity Assay, Blocking Assay

    Carvacrol altered the protein expression of caspase-3, Bcl-2, and Bax of the hippocampus in ethanol-treated C57BL/6 mice and hippocampal neurons. (a), (b), and (c) show the quantitative analysis of the protein levels of caspase-3, Bcl-2, and Bax in mouse hippocampi and hippocampal neurons, respectively. The data were normalized to the loading control GAPDH. The data are expressed as the mean ± SEM ( n = 6 per group). ∗∗ P

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: The Neuroprotective Effects of Carvacrol on Ethanol-Induced Hippocampal Neurons Impairment via the Antioxidative and Antiapoptotic Pathways

    doi: 10.1155/2017/4079425

    Figure Lengend Snippet: Carvacrol altered the protein expression of caspase-3, Bcl-2, and Bax of the hippocampus in ethanol-treated C57BL/6 mice and hippocampal neurons. (a), (b), and (c) show the quantitative analysis of the protein levels of caspase-3, Bcl-2, and Bax in mouse hippocampi and hippocampal neurons, respectively. The data were normalized to the loading control GAPDH. The data are expressed as the mean ± SEM ( n = 6 per group). ∗∗ P

    Article Snippet: The membranes were then blocked using 5% fat-free milk in Tris-buffered saline with 1% Tween-20 (TBS-T) for 1 h and then were incubated with the following incubation with primary antibodies overnight at 4°C: anti-caspase-3 (1 : 300, Santa Cruz), anti-Bcl-2 (1 : 200, Santa Cruz), anti-Bax (1 : 200, Santa Cruz), anti-phospho-ERK (1 : 1000, Cell Signaling), anti-ERK (1 : 1000, Cell Signaling), anti-phospho-JNK (1 : 200, Santa Cruz), anti-JNK (1 : 200, Santa Cruz), anti-phospho-p38 (1 : 200, Santa Cruz), anti-p38 (1 : 200, Santa Cruz), and anti-β -actin (1 : 2000, Santa Cruz), respectively.

    Techniques: Expressing, Mouse Assay