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146 results for “Caspase”
Data for: Caspase-Based Fusion Protein Technology: Substrate Cleavability Described by Computational Modeling and Simulation
<p>This dataset contains all files necessary to set up the simulations conducted in this work. It further contains the scripts that were used to do the stitching and combining of the CASPON-tag and the N-termini of the POIs. The manuscript was just submitted and accepted: <a href="https://doi.org/10.1021/acs.jcim.4c00316">10.1021/acs.jcim.4c00316</a></p>
Figure 6. Caspase 3 in Physical characterization and wound healing properties of Zamzam water
Figure 6. Caspase 3 levels of treatment groups. ***Extremely high significant at p <0.001 when compared to Group 1; **Highly significant lesser at p <0.01 on comparing with Group 2; ns: nonsignificant when compared to group 3 at p <0.05. Group 1: Normal control; Group 2: Disease control (wound without treatment); Group 3: Standard control (treatment with povidoneiodine cream); Group 4: Zamzam water treatment group.
Figure 5. Caspase 9 in Physical characterization and wound healing properties of Zamzam water
Figure 5. Caspase 9 levels of treatment groups. ***Extremely high significant at p <0.001 when compared to Group 1; **Significantly lesser at p <0.01 on comparing with Group 2; ns: nonsignificant on comparing with group 3 at p <0.05. Group 1: Normal control; Group 2: Disease control (wound without treatment); Group 3: Standard control (treatment with povidone-iodine cream); Group 4: Zamzam water treatment group.
Quantitative phase microscopy timelapse dataset of PNT1A, DU-145 and LNCaP cells with annotated caspase 3,7-dependent and independent cell death
<p>Time-lapse dataset of prostatic cell lines (DU-145, PNT1A, LNCaP) exposed to cell death-inducing compounds (staurosporine, doxorubicin) and black phosphorus. The time-lapse dataset is annotated as follows: (1) cell masks and cell numbers, (2) by cell death type and timepoint of death in the attached xlsx file. This dataset is supplementary to the article:</p> <p>Vicar, T., Raudenska, M., Gumulec, J. <em>et al.</em> The Quantitative-Phase Dynamics of Apoptosis and Lytic Cell Death. <em>Sci Rep</em> <strong>10, </strong>1566 (2020). <a href="https://doi.org/10.1038/s41598-020-58474-w">https://doi.org/10.1038/s41598-020-58474-w</a></p> <p>Correlative fluorescence microscopy is in a separate dataset <a href="https://doi.org/10.5281/zenodo.4531900">10.5281/zenodo.4531900</a></p> <p>Code is available at <a href="https://github.com/tomasvicar/CellDeathDetect">https://github.com/tomasvicar/CellDeathDetect</a></p> <p><strong>Methods</strong></p> <p><em>Cell culture and cultured cell conditions</em><br> LNCaP cell line was established from a lymph node metastase of the hormone-refractory patient and contains a mutation in the AR gene. This mutation creates a promiscuous AR that can bind to different types of steroids. LNCaP cells are AR-positive, PSA-positive, PTEN-negative and harbor wild-type p53 {Skjoth, 2006 #150; Mitchell, 2000 #149}. PNT1A is immortalized non-tumorigenic epithelial cell line. PNT1A cells harbour wild-type p53. However, SV40 induced T-antigen expression inhibits the activity of p53. This cell line had lost the expression of androgen receptor (AR) and prostate-specific antigen (PSA) (Raudenska, 2019). DU-145 cell line is derived from the metastatic site in the brain and contains P223L and V274F mutations in p53. This cell line is PSA and AR-negative and androgen independent (Chappell, 2012). All cell lines used in this study were purchased from HPA Culture Collections (Salisbury, UK). and were cultured in RPMI-1640 medium with 10 % FBS. The medium was supplemented with antibiotics (penicillin 100 U/ml and streptomycin 0.1 mg/ml). Cells were maintained at 37°C in a humidified (60%) incubator with 5% CO2 (Sanyo, Japan).</p> <p><em>Correlative time-lapse quantitative phase-fluorescence imaging</em></p> <p>QPI and fluorescence imaging were performed by using multimodal holographic microscope Q-PHASE (TESCAN, Brno, Czech Republic). To determine the amount of caspase-3/7 product accumulation, cells were loaded with 2 µM CellEventTM Caspase-3/7 Green Detection Reagent (Life Technologies, Carlsbad, CA, USA) according to the manufacturer’s protocol and visualized using FITC 488 nm filter. To detect the cells with a loss of plasma membrane integrity, cells were stained with 1 ug/ml propidium iodide (Sigma Aldrich Co., St. Louis, MO, USA) and visualized using TRITC 542 nm filter. Nuclear morphology and chromatin condensation were analyzed using Hoechst 33342 nuclear staining (ENZO, Lausen, Switzerland) and visualized using DAPI 461 nm filter. Cells were cultivated in Flow chambers μ-Slide I Lauer Family (Ibidi, Martinsried, Germany). To maintain standard cultivation conditions (37°C, humidified air (60%) with 5% CO2) during time-lapse experiments, cells were placed in the gas chamber H201 - for Mad City Labs Z100/Z500 piezo Z-stages (Okolab, Ottaviano NA, Italy). To image enough cells in one field of view, lens Nikon Plan 10/0.30 were chosen. For each cell line and each treatment, seven fields of view were observed with the frame rate 3 mins/frame for 24 or 48 h respectively. Holograms were captured by CCD camera (XIMEA MR4021 MC-VELETA), fluorescence images were captured using ANDOR Zyla 5.5 sCMOS camera. Complete quantitative phase image reconstruction and image processing were performed in Q-PHASE control software. Cell dry mass values were derived according to {Prescher, 2005 #177} and {Park, 2018 #178} from the phase (eq. (1)), where m is cell dry mass density (in pg/μm2), φ is detected phase (in rad), λ is wavelength in μm (0.65 μm in Q-PHASE), and α is specific refraction increment (≈0.18 μm3/pg). All values in the formula except the Phi are constant. Phi (Phase) is the value measured directly by the microscope. Integrated phase shift through a cell is proportional to its dry mass, which enables studying changes in cell mass distribution (Park et al., 2018).</p> <p><strong>File description</strong></p> <p>There are three archives included for particular cell lines:</p> <ul> <li>QPI_annotated_timelapse_DU145.zip for DU-145 cells</li> <li>QPI_annotated_timelapse_PNT1A.zip for PNT1A cells</li> <li>QPI_annotated_timelapse_LNCaP.zip for LNCaP cells</li> </ul> <p>The archive includes of following files:</p> <ul> <li><strong>Tiff with time-lapse</strong> quantitative phase image (32-bit files 600x600px with values in pg/um2 with framerate 1 frame/3minutes with 1.59 px/um), named <em>QPI_cellline_treatment_FOV.tiff</em></li> <li><strong>Tiff file with segmentation</strong> mask for particular cells named <em>mask_cellline_treatment_FOV.tiff</em></li> <li><strong>xlsx table</strong> with cell death type (1 for apoptosis, 2 for necrosis, 3 for ambiguous/surviving) and time of death for representative cell number from mask, named <em>labels_cellline_treatment_FOV.xlsx</em></li> </ul> <p>file naming has following conventions:</p> <ul> <li>cell names: DU145, PNT1A, LNCaP for particular cell line</li> <li>treatments: st, bp, do for staurosporine, black phosphorus and doxorubicin</li> <li>fields of view: 1 to 7</li> </ul> <p>e.g. QPI_DU145_st_4.tif, mask_DU145_st_4.tif, labels_DU145_st_4.xlsx</p> <p>Note that correlative fluorescence images are available at <a href="https://doi.org/10.5281/zenodo.4531900">10.5281/zenodo.4531900</a></p>
Figure 3. Negative Caspase-3 in Investigation of protective effects of lithium borate on spermatogenesis and testes histopathology against cadmium-induced acute toxicity in rats
Figure 3. Negative Caspase-3 expressions in testes tissues of control and LTB groups (A and C), severe Caspase-3 expression in spermatocytes of Cd group (arrowheads) (B), mild Caspase- 3 expression in spermatocytes (arrowheads) of LTB + Cd group (D), IHC - P, Bar: 20 µm.
Catalysis of Ac-DEVD-AMC by caspase-3 (dataset formatted for analysis by interferENZY)
<p><strong>Main description</strong></p> <p>This dataset depicts the catalysis of the fluorogenic substrate Ac-DEVD-AMC to the fluorescent substrate AMC by recombinant purified caspase-3, for fixed concentration of enzyme and variation of concentration of initial substrate. It was originally documented in <em>Biophysical Chemistry 252 (2019) 106193</em> (<a href="https://doi.org/10.1016/j.bpc.2019.106193">https://doi.org/10.1016/j.bpc.2019.106193</a>), and then used as a study case for the webserver interferENZY (a web-based tool for enzymatic assay validation and standardized kinetic analysis; visit <a href="https://interferenzy.i3s.up.pt">https://interferenzy.i3s.up.pt</a> for more information). To this end, it was converted to the format here presented: tab-separated *.txt input required for interferENZY analysis.</p> <p> </p> <p><strong>Dataset organization</strong></p> <p>Line 1: Tab-separated initial concentrations of substrate Ac-DEVD-AMC in micromolar (µM) concentration</p> <p>Line 2: Concentration of enzyme (1 U)</p> <p>Line 3: Units of time</p> <p>Line 4: Units of concentration for substrate values and measurements</p> <p>Line 5: Dataset name</p> <p>Line 6 and downwards: Tab-separated column-pairs of the progress curves (time,Product) corresponding to the indicated values of initial concentrations of substrate in line 1</p> <p> </p> <p><strong>Contact information:</strong></p> <p>Maria Filipa Pinto (mfpinto@i3s.up.pt)<br> Pedro M. Martins (pmartins@ibmc.up.pt)</p> <p>i3S – Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. Telephone number: +351 226 074 900</p>
Exprimental Data:Caspase-11 non-canonical inflammasome mediates the expression of proinflammatory cytokines in murine macrophages infected with leptospira interrogans.
<p>This is the exprimental data of manuscripts submitted in ALL LIFE magazine. The title is Caspase-11 non-canonical inflammasome mediates the expression of proinflammatory cytokines in murine macrophages infected with leptospira interrogans.)</p>
Molecular dynamics simulations data of Caspase-3 enzyme with pentapeptide ligand DEVDG and its chiral mutant DEVdG having D-Asp at fourth position
<p>Amino acids in proteins are maintained in one specific L chiral form in the body. D-amino acids are not normally incorporated into proteins and their accumulation has been associated with several conditions including schizophrenia, amyotrophic lateral sclerosis, and other age-related disorders. However, the mechanisms by which the accumulation of D-amino-acids in proteins may lead to pathophysiological consequences remain poorly understood. In this work, we studied a model protease system, caspase-3 that specifically hydrolyses the 4’–5’ peptide bond of the pentapeptide substrate DEVDG. Through extensive molecular dynamics simulations, free energy calculations and distance maps, we reveal that caspase-3 naturally rejects the pentapeptide containing D-Asp substrate, DEVdG and prevents catalytic activity by caspase. The importance of this chiral discriminating capacity is evident from chiral-selective in vivo experimental assays to detect caspase-bound D-Asp in Drosophila where altering the chiral balance created impaired caspase activity and impaired apoptosis, increased tumour formation, and premature death. The modelling data reveals the molecular level charge balancing that enforces the chiral recognition necessary to maintain homeostasis across the cell, tissue, and organ level.</p>
Raw Data for the article: Cigarette smoke promotes inflammasome-independent activation of caspase-1 and -4 leading to gasdermin D cleavage in human macrophages
<p>Mechanisms and consequences of gasdermin D (GSDMD) activation in cigarette smoke (CS)-associated inflammation and lung disease are unknown. GSDMD is a downstream effector of caspase-1, -8, and -4. Upon cleavage, GSDMD generates pores into cell membranes. Different degrees of GSDMD activation are associated with a range of physiological outputs ranging from cell hyperactivation to pyroptosis. We have previously reported that in human monocyte-derived macrophages CS extract (CSE) inhibits the NLRP3 inflammasome and shifts the response to lipopolysaccharide (LPS) towards the TLR4-TRIF axis leading to activation of caspase-8, which, in turn, activates caspase-1. In the present work, we investigated whether other ASC-dependent inflammasomes could be involved in caspase activation by CSE and whether caspase activation led to GSDMD cleavage and other downstream effects. Presented results demonstrate that CSE promoted ASC-independent activation of caspase-1 leading to GSDMD cleavage and increased cell permeability, in the absence of cell death. GSDMD cleavage was strongly enhanced upon stimulation with LPS+CSE, suggesting a synergistic effect between the two stimuli. Noteworthy, CSE promoted LPS internalization leading to caspase-4 activation, thus contributing to increased GSDMD cleavage. Caspase-dependent GSDMD cleavage was associated with mitochondrial superoxide generation. Increased cleaved GSDMD was found in lung macrophages of smokers compared to ex-smokers and non-smoking controls. Our findings revealed that ASC-independent activation of caspase-1, -4, and -8 and GSDMD cleavage upon exposure to CS may contribute to macrophage dysfunction and feed the chronic inflammation observed in the smokers' lung.</p>
Data for: ASC oligomer favors caspase-1 CARD domain recruitment after intracellular potassium efflux
<p class="MsoNormal"><span>Signaling through the inflammasome is important for the inflammatory response. Low concentrations of intracellular K<sup>+</sup>are associated with the specific oligomerization and activation of the NLRP3 inflammasome, a type of inflammasome involved in sterile inflammation. After NLRP3 oligomerization, ASC protein binds and forms oligomeric filaments that culminate in large protein complexes named ASC specks. ASC specks are also initiated from different inflammasome scaffolds, such as AIM2, NLRC4 or Pyrin. ASC oligomers recruit caspase-1 and then induce its activation through interactions between their respective caspase activation and recruitment domains (CARD). So far ASC oligomerization and caspase-1 activation are K<sup>+</sup>-independent processes. Here we found that, when there is low intracellular K<sup>+</sup>, ASC oligomers change their structure independently of NLRP3 and make the ASC<sup>CARD</sup> domain more accessible for the recruitment of the pro-caspase-1<sup>CARD</sup> domain. Therefore, conditions that decrease intracellular K<sup>+</sup> not only drive NLRP3 responses but also enhance the recruitment of pro-caspase-1 CARD domain into the ASC specks.</span></p>
Emricasan, an Oral Caspase Inhibitor, in Subjects With NASH Cirrhosis and Severe Portal Hypertension
ClinicalTrials.gov study NCT02960204. IPD Sharing: NO. Countries: 3. Publications: 1.
Data for: ASC oligomer favors caspase-1 CARD domain recruitment after intracellular potassium efflux
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Data from: Reduced internalization of TNF-ɑ/TNFR1 down-regulates caspase dependent phagocytosis induced cell death (PICD) in neonatal monocytes
Phagocytosis-induced cell death (PICD) is diminished in cord blood monocytes (CBMO) as compared to cells from adults (PBMO) due to differences in the CD95-pathway. This may support a prolonged pro-inflammatory response with sequels of sustained inflammation as seen in neonatal sepsis. Here we hypothesized that TNF-α mediated induction of apoptosis is impaired in CBMO due to differences in the TNFR1-dependent internalization. Monocytes were infected with Escherichia coli-GFP (E. coli-GFP). Monocyte phenotype, phagocytic activity, induction of apoptosis, and TNF-α/TNF-receptor (TNFR) -expression were analysed. In the course of infection TNF-α-secretion of CBMO was reduced to 40% as compared to PBMO (p<0.05). Neutralization of TNF-α by an αTNF-α antibody reduced apoptotic PICD in PBMO four-fold (p < 0.05 vs. infection with E. coli). PICD in CBMO was reduced 5-fold compared to PBMO and showed less responsiveness to αTNF-α antibody. CBMO expressed less pro-apoptotic TNFR1, which, after administration of TNF-α or infection with E. coli was internalized to a lesser extent. With similar phagocytic capacity, reduced TNFR1 internalization in CBMO was accompanied by lower activation of caspase-8 (p < 0.05 vs. PBMO). Stronger caspase-8 activation in PBMO caused more activation of effector caspase-3 and apoptosis (all p < 0.05 vs. PBMO). Our results demonstrate that TNFR1 internalization is critical in mediating PICD in monocytes after infection with E.coli and is reduced in CBMO.
Role of Tyrosine Kinase Lyn and Cleaved Form by Caspases in Psoriasis
ClinicalTrials.gov study NCT01538342. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Serum Caspase 3, Annexin a2 and Soluble Fas Levels and Endometriosis
ClinicalTrials.gov study NCT03020108. IPD Sharing: NO. Countries: 1. Publications: 1.
Evaluation of Mucoadhesive Tacrolimus Patch on Caspase-3 Inducing Apoptosis in Oral Lichen Planus
ClinicalTrials.gov study NCT05139667. IPD Sharing: UNDECIDED. Countries: 1. Publications: 1.
Administration of Donor T Cells With the Caspase-9 Suicide Gene
ClinicalTrials.gov study NCT01494103. IPD Sharing: NO. Countries: 1. Publications: 1.
CASPALLO: Allodepleted T Cells Transduced With Inducible Caspase 9 Suicide Gene
ClinicalTrials.gov study NCT00710892. IPD Sharing: NO. Countries: 1. Publications: 4.
Emricasan, a Caspase Inhibitor, for Evaluation in Subjects With Non-Alcoholic Steatohepatitis (NASH) Fibrosis
ClinicalTrials.gov study NCT02686762. IPD Sharing: NO. Countries: 3. Publications: 1.
A Dose-Finding Study of the Second Mitochondrial Activator of Caspases (SMAC) Mimetic Debio 1143 When Given in Combination With Avelumab to Participants With Advanced Solid Malignancies and to Partici
ClinicalTrials.gov study NCT03270176. IPD Sharing: NO. Countries: 3. Publications: 1.
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
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