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irreversible caspase-3 inhibitor zdevd.fmk  (Becton Dickinson)

 
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    Becton Dickinson irreversible caspase-3 inhibitor zdevd.fmk
    Wild-type (WT) and Fas deficient (lpr) mice were treated with one intratracheal instillation of recombinant human soluble FasL (rh-sFasL, 25 ng/g body wt), or PBS (as control). At 16 h post-instillation, we measured (A) the number of nuclei containing DNA strand breaks (TUNEL-positive signal) in lung tissue sections, and <t>(B)</t> <t>caspase-3</t> activity in the lung homogenates. Merged images of representative lung tissue sections from PBS or FasL-treated WT mice (C), showed that occludin and ZO1 protein signals (red) were diminished in the alveolar walls only in areas with TUNEL positive cells (green). Original image magnification X400. n of 5 mice per group for the immunofluorescence analyses. In the graphs, each dot represents an individual mouse (n= 10 mice per group). Horizontal bars represent means. *P < 0.05 vs WT-PBS group
    Irreversible Caspase 3 Inhibitor Zdevd.Fmk, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/zdevd+fmk/irreversible+caspase+3+inhibitor+zdevd+fmk/pmc06339809-189-1-16
    Average 90 stars, based on 1 article reviews
    irreversible caspase-3 inhibitor zdevd.fmk - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Fas activation alters tight junction proteins in acute lung injury."

    Article Title: Fas activation alters tight junction proteins in acute lung injury.

    Journal: Thorax

    doi: 10.1136/thoraxjnl-2018-211535

    Wild-type (WT) and Fas deficient (lpr) mice were treated with one intratracheal instillation of recombinant human soluble FasL (rh-sFasL, 25 ng/g body wt), or PBS (as control). At 16 h post-instillation, we measured (A) the number of nuclei containing DNA strand breaks (TUNEL-positive signal) in lung tissue sections, and (B) caspase-3 activity in the lung homogenates. Merged images of representative lung tissue sections from PBS or FasL-treated WT mice (C), showed that occludin and ZO1 protein signals (red) were diminished in the alveolar walls only in areas with TUNEL positive cells (green). Original image magnification X400. n of 5 mice per group for the immunofluorescence analyses. In the graphs, each dot represents an individual mouse (n= 10 mice per group). Horizontal bars represent means. *P < 0.05 vs WT-PBS group
    Figure Legend Snippet: Wild-type (WT) and Fas deficient (lpr) mice were treated with one intratracheal instillation of recombinant human soluble FasL (rh-sFasL, 25 ng/g body wt), or PBS (as control). At 16 h post-instillation, we measured (A) the number of nuclei containing DNA strand breaks (TUNEL-positive signal) in lung tissue sections, and (B) caspase-3 activity in the lung homogenates. Merged images of representative lung tissue sections from PBS or FasL-treated WT mice (C), showed that occludin and ZO1 protein signals (red) were diminished in the alveolar walls only in areas with TUNEL positive cells (green). Original image magnification X400. n of 5 mice per group for the immunofluorescence analyses. In the graphs, each dot represents an individual mouse (n= 10 mice per group). Horizontal bars represent means. *P < 0.05 vs WT-PBS group

    Techniques Used: Recombinant, TUNEL Assay, Activity Assay, Immunofluorescence

    HPAEpiC monolayers were pre-incubated with caspase-3 inhibitor zDEVD.fmk (or zFA.fmk or vehicle as controls) and exposed for 2 h to rh-sFasL (100 ng/mL or 300 ng/mL) or medium only (MO) (A-C). After treatment, we measured (A) caspase 3-activity, (B) percentage of cell death and (C) FITC-albumin permeability in these cell monolayers. HPAEpiC monolayers were also pre-incubated with the tyrosine-kinase specific inhibitor genistein (or vehicle as control) (D-H) and exposed for 2 h to rh-sFasL (100 ng/mL or 300 ng/mL) or medium only (MO). After treatment, we measured IL-8 concentration in cell supernatant by ELISA (D), percentage of cell death by PrestoBlue (E), permeability to FITC-albumin (F), IL-6 concentration in cell supernatant by ELISA (G), and tyrosine kinase activity in the cell monolayers (H). Cell monolayers treated with medium only were used to determine 100% survival. Results from 4 separate experiments performed in duplicate. Each dot of the graphs represents a single data point. Horizontal bars represent means. *P<0.05 vs all conditions with MO; # P< 0.05.
    Figure Legend Snippet: HPAEpiC monolayers were pre-incubated with caspase-3 inhibitor zDEVD.fmk (or zFA.fmk or vehicle as controls) and exposed for 2 h to rh-sFasL (100 ng/mL or 300 ng/mL) or medium only (MO) (A-C). After treatment, we measured (A) caspase 3-activity, (B) percentage of cell death and (C) FITC-albumin permeability in these cell monolayers. HPAEpiC monolayers were also pre-incubated with the tyrosine-kinase specific inhibitor genistein (or vehicle as control) (D-H) and exposed for 2 h to rh-sFasL (100 ng/mL or 300 ng/mL) or medium only (MO). After treatment, we measured IL-8 concentration in cell supernatant by ELISA (D), percentage of cell death by PrestoBlue (E), permeability to FITC-albumin (F), IL-6 concentration in cell supernatant by ELISA (G), and tyrosine kinase activity in the cell monolayers (H). Cell monolayers treated with medium only were used to determine 100% survival. Results from 4 separate experiments performed in duplicate. Each dot of the graphs represents a single data point. Horizontal bars represent means. *P<0.05 vs all conditions with MO; # P< 0.05.

    Techniques Used: Incubation, Activity Assay, Permeability, Concentration Assay, Enzyme-linked Immunosorbent Assay

    After 2 h exposure of rh-sFasL (+FasL) at the dose of 100 ng/mL or medium only (-FasL), the concentrations of occludin and ZO1 proteins were measured by ELISA in HAECpiC monolayers pre-incubated with the caspase-3 inhibitor zDEVD.fmk, its inactive analog (zFA.fmk), or the tyrosine kinase inhibitor genistein or vehicle (DMSO). Compared to control cells, rh-sFasL decreased the concentrations of occludin and ZO1 in cell protein extracts (A and B, respectively). Representative immunofluorescence images (original image magnification X400) (C) show the expression of occludin and ZO1 proteins (red signals) localized along the cytoplasmic membrane of control cells in HAECpiC monolayers (−rhFasL/+vehicle). Exposure to rh-sFasL resulted in a global decrease of occludin and ZO1 fluorescence signals that was particularly profound in the cytoplasmic extensions, while some signal remained close to the cell nuclei (DAPI staining, blue signal). Only pre-incubation with the caspase-3 inhibitor zDEVD.fmk prevented the sFasL-induced decrease of occludin and ZO1 proteins evaluated both by ELISA (A and B) and by immunocytochemistry (C). Representative immunofluorescence images at larger magnification (x1000) show the decreased expression of occludin and ZO1 proteins (red signals) in HAECpiC monolayers treated with rh-sFasL (+rh-sFasL/+vehicle) compared with control cells (−rh-sFasL/+vehicle) (D) Results from 4 separate experiments performed in duplicate. Each dot of the graphs represents a single data point. Horizontal bars represent means. *P<0.05 vs their corresponding-rh-sFasL conditions.
    Figure Legend Snippet: After 2 h exposure of rh-sFasL (+FasL) at the dose of 100 ng/mL or medium only (-FasL), the concentrations of occludin and ZO1 proteins were measured by ELISA in HAECpiC monolayers pre-incubated with the caspase-3 inhibitor zDEVD.fmk, its inactive analog (zFA.fmk), or the tyrosine kinase inhibitor genistein or vehicle (DMSO). Compared to control cells, rh-sFasL decreased the concentrations of occludin and ZO1 in cell protein extracts (A and B, respectively). Representative immunofluorescence images (original image magnification X400) (C) show the expression of occludin and ZO1 proteins (red signals) localized along the cytoplasmic membrane of control cells in HAECpiC monolayers (−rhFasL/+vehicle). Exposure to rh-sFasL resulted in a global decrease of occludin and ZO1 fluorescence signals that was particularly profound in the cytoplasmic extensions, while some signal remained close to the cell nuclei (DAPI staining, blue signal). Only pre-incubation with the caspase-3 inhibitor zDEVD.fmk prevented the sFasL-induced decrease of occludin and ZO1 proteins evaluated both by ELISA (A and B) and by immunocytochemistry (C). Representative immunofluorescence images at larger magnification (x1000) show the decreased expression of occludin and ZO1 proteins (red signals) in HAECpiC monolayers treated with rh-sFasL (+rh-sFasL/+vehicle) compared with control cells (−rh-sFasL/+vehicle) (D) Results from 4 separate experiments performed in duplicate. Each dot of the graphs represents a single data point. Horizontal bars represent means. *P<0.05 vs their corresponding-rh-sFasL conditions.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Incubation, Immunofluorescence, Expressing, Fluorescence, Staining, Immunocytochemistry



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    Detection of apoptosis-related factors in NHEK cell lysates following sorafenib and antifungal drug treatment. Detection of (A) cIAP-1 (70 kDa) and (C) cleaved caspase-3 (19 kDa) in the cell lysate was performed using western blotting. (B) Bands were semi-quantified using ImageJ, and data were expressed as the relative ratio of cIAP-1/β-actin. Statistical analysis was conducted using one-way ANOVA followed by Tukey’s test; ns indicates not significant. Sora or S: sorafenib, Keto: ketoconazole, Itra: itraconazole. All results are presented as the mean ± SD of triplicate experiments. (D) Various concentrations of sorafenib, with or without 50 μmM ZVAD or ZDEVD, were added to cultured NHEK cells. DMSO was used as the solvent for both sorafenib and the inhibitors. After overnight incubation, cell viability was assessed using the cell-counting kit-8 assay. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s test; ** p < 0.01 and * p < 0.05 (vs DMSO (-)).

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    doi: 10.2340/actadv.v105.40697

    Figure Lengend Snippet: Detection of apoptosis-related factors in NHEK cell lysates following sorafenib and antifungal drug treatment. Detection of (A) cIAP-1 (70 kDa) and (C) cleaved caspase-3 (19 kDa) in the cell lysate was performed using western blotting. (B) Bands were semi-quantified using ImageJ, and data were expressed as the relative ratio of cIAP-1/β-actin. Statistical analysis was conducted using one-way ANOVA followed by Tukey’s test; ns indicates not significant. Sora or S: sorafenib, Keto: ketoconazole, Itra: itraconazole. All results are presented as the mean ± SD of triplicate experiments. (D) Various concentrations of sorafenib, with or without 50 μmM ZVAD or ZDEVD, were added to cultured NHEK cells. DMSO was used as the solvent for both sorafenib and the inhibitors. After overnight incubation, cell viability was assessed using the cell-counting kit-8 assay. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s test; ** p < 0.01 and * p < 0.05 (vs DMSO (-)).

    Article Snippet: Z-DEVD-FMK (ZDEVD) and Z-VAD-FMK (ZVAD) were from Selleck Chemicals (Houston, TX, USA).

    Techniques: Western Blot, Cell Culture, Solvent, Incubation, Cell Counting

    The primary human colon cancer cells, pCan1, underwent treatment with IMT1 (1 μM). Subsequently, they were cultivated for the designated duration, and the assessments including the Caspase-3 activity ( A ) and the Caspase-9 activity ( B ), expression of apoptosis-related proteins ( C ), and cytosol cytochrome C contents (ELISA assays, D ) were performed. Cell apoptosis was tested through nuclear TUNEL staining assays ( E ). Preceding IMT1 (1 μM) treatment for the specified period, pCan1 cells underwent pretreatment with zDEVD-fmk (50 μM) or zVAD-fmk (50 μM) for 1 h. Subsequent assessments included the evaluation of apoptosis via nuclear TUNEL staining assays ( F ) and the determination of cell death through Trypan blue staining ( G ). Other primary colon cancer cells (“pCan-2/pCan-3”) or immortalized colon cancer cells (HCT116) were exposed to IMT1 (1 μM) for a designated duration and assessments included the Caspase-3 activity ( H ) and nuclear TUNEL staining ( I ). “Veh” represents the vehicle control (0.1% DMSO). The data were presented as mean ± standard deviation (SD, n = 5), with *indicating P < 0.05 compared to the “Veh” treatment ( A – I ) and # indicating P < 0.05 compared to the IMT1 only treatment ( F , G ). The experiments were repeated five times, yielding consistent results. The scale bar is set at 100 μm.

    Journal: Cell Death & Disease

    Article Title: Targeting POLRMT by IMT1 inhibits colorectal cancer cell growth

    doi: 10.1038/s41419-024-07023-8

    Figure Lengend Snippet: The primary human colon cancer cells, pCan1, underwent treatment with IMT1 (1 μM). Subsequently, they were cultivated for the designated duration, and the assessments including the Caspase-3 activity ( A ) and the Caspase-9 activity ( B ), expression of apoptosis-related proteins ( C ), and cytosol cytochrome C contents (ELISA assays, D ) were performed. Cell apoptosis was tested through nuclear TUNEL staining assays ( E ). Preceding IMT1 (1 μM) treatment for the specified period, pCan1 cells underwent pretreatment with zDEVD-fmk (50 μM) or zVAD-fmk (50 μM) for 1 h. Subsequent assessments included the evaluation of apoptosis via nuclear TUNEL staining assays ( F ) and the determination of cell death through Trypan blue staining ( G ). Other primary colon cancer cells (“pCan-2/pCan-3”) or immortalized colon cancer cells (HCT116) were exposed to IMT1 (1 μM) for a designated duration and assessments included the Caspase-3 activity ( H ) and nuclear TUNEL staining ( I ). “Veh” represents the vehicle control (0.1% DMSO). The data were presented as mean ± standard deviation (SD, n = 5), with *indicating P < 0.05 compared to the “Veh” treatment ( A – I ) and # indicating P < 0.05 compared to the IMT1 only treatment ( F , G ). The experiments were repeated five times, yielding consistent results. The scale bar is set at 100 μm.

    Article Snippet: The pan-caspase inhibitor (zVAD-fmk) and the specific caspase-9 inhibitor zDEVD-fmk were procured from Calbiochem (Darmstadt, Germany).

    Techniques: Activity Assay, Expressing, Enzyme-linked Immunosorbent Assay, TUNEL Assay, Staining, Control, Standard Deviation