Search results for "CASP"

showing 10 items of 470 documents

Deglycosylated bleomycin induces apoptosis in lymphoma cell via c-jun NH2-terminal kinase but not reactive oxygen species

2007

Bleomycin (BLM) has demonstrated potent activity in treating malignant lymphomas but its therapeutic efficacy is hampered by induction of lung fibrosis. This side effect is related to the ability of the drug to generate reactive oxygen species in lung cells. In the present study, we evaluated the consequences of deglycosylation of BLM in term of cytotoxic activity and generation of reactive oxygen species. When tested on U937 human lymphoma cells, both compounds generated a typical apoptotic phenotype. Cell death induction was associated with Bax oligomerization, dissipation of the mitochondrial membrane potential, release of cytochrome c, caspase activation, chromatin condensation and inte…

Programmed cell deathFas Ligand ProteinLymphomaCellApoptosisDNA FragmentationBiologymedicine.disease_causeBiochemistryTNF-Related Apoptosis-Inducing LigandBleomycinmedicineHumansDeath domainPharmacologychemistry.chemical_classificationReactive oxygen speciesAntibiotics AntineoplasticU937 cellCytochrome cJNK Mitogen-Activated Protein KinasesU937 CellsMolecular biologymedicine.anatomical_structurechemistryBiochemistryApoptosisCaspasesbiology.proteinReactive Oxygen SpeciesOxidative stressBiochemical Pharmacology
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Knockout of myeloid cell leukemia-1 induces liver damage and increases apoptosis susceptibility of murine hepatocytes

2008

Apoptosis, or programmed cell death, regulates tissue development and homeostasis in multi-cellular organisms. Extrinsic or intrinsic death signals activate pro-apoptotic pathways, resulting in the activation of caspases and finally in cell death. An important event during apoptosis process is the permeabilization of the outer mitochondrial membrane (OMM). Integrity of the OMM is regulated by the Bcl-2 protein family, which is divided into three groups: anti-apoptotic members Bcl-2, Bcl-xL and myeloid cell leukemia-1 (Mcl-1), pro-apoptotic multidomain members Bax and Bak, and pro-apoptotic BH3-only proteins. Mitochondrial activation is regulated by selective interactions of Bcl-2 proteins v…

Programmed cell deathGenotypeCellular differentiation610 Medicine & healthApoptosisBiologyPolymerase Chain ReactionArticleMiceimmune system diseases10049 Institute of Pathology and Molecular Pathologyhemic and lymphatic diseasesmedicineAnimalsAspartate AminotransferasesneoplasmsDNA PrimersHepatologyCaspase 3Alanine TransaminaseCell DifferentiationDNAFas receptorCell biologyMyeloid Cell Leukemia Sequence 1 ProteinHaematopoiesisGene Expression RegulationLiverProto-Oncogene Proteins c-bcl-2ApoptosisHepatocytesMyeloid Cell Leukemia Sequence 1 ProteinRNA2721 HepatologyHepatocyte growth factorStem cellmedicine.drugHepatology
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Caspase-dependent apoptosis during infection with Cryptosporidium parvum

1999

The protozoan parasite Cryptosporidium parvum causes persistent diarrhea and malnutrition in children and the diarrhea-wasting syndrome in AIDS. No therapy exists for eliminating the parasite in the absence of a healthy immune response. Although it had been reported that infection of intestinal cell lines with C. parvum leads to host cell death, the mechanisms of cytolysis have not been characterized. We show here that infection with C. parvum leads to typical apoptotic nuclear condensation and DNA fragmentation in host cells. Both nuclear condensation and DNA fragmentation are inhibited by a caspase inhibitor, showing that caspases are involved in this type of apoptosis. Finally, blocking …

Programmed cell deathImmunologyCryptosporidiosisApoptosisDNA FragmentationCysteine Proteinase InhibitorsMicrobiologyCaspase-Dependent ApoptosisAmino Acid Chloromethyl KetonesCell LineImmune systemparasitic diseasesAnimalsHumansComputingMilieux_MISCELLANEOUSCaspaseCryptosporidium parvumbiologybiology.organism_classificationCaspase InhibitorsVirologyCytolysisPOUVOIR PATHOGENE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyInfectious DiseasesCryptosporidium parvumMicroscopy FluorescenceApoptosisCaspasesbiology.proteinDNA fragmentationHeLa CellsMicrobes and Infection
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Role of caspase-8 in hepatocyte response to infection and injury in mice.

2007

Caspase-8 has been implicated in signaling for apoptotic cell death and for certain nonapoptotic functions. However, knowledge of actual physiological or pathophysiological processes to which this enzyme contributes is lacking. Using a mouse model and employing the conditional knockout approach to delete the caspase-8 gene specifically in the liver, we found that caspase-8 deficiency in hepatocytes facilitates infection of the liver by Listeria monocytogenes, attenuates the hepatocyte proliferation wave during the first 48 hours after partial hepatectomy and, depending on the genetic background of the mice, prompts a chronic inflammatory response to the hepatectomy, as a result of which the…

Programmed cell deathInflammationCaspase 8MiceConditional gene knockoutmedicineAnimalsListeriosisCaspaseCell ProliferationInflammationMice KnockoutCaspase 8HepatologybiologyCell DeathCell growthLiver Regenerationmedicine.anatomical_structureHepatocyteImmunologyCancer researchChronic inflammatory responsebiology.proteinHepatocytesmedicine.symptomHepatology (Baltimore, Md.)
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Parthenolide induces caspase-independent and AIF-mediated cell death in human osteosarcoma and melanoma cells

2013

The mechanism of the cytotoxic effect exerted by parthenolide on tumor cells is not clearly defined today. This article shows that parthenolide stimulates in human osteosarcoma MG63 and melanoma SK-MEL-28 cells a mechanism of cell death, which is not prevented by z-VAD-fmk and other caspase inhibitors. In particular treatment with parthenolide rapidly stimulated (1-2 h) reactive oxygen species (ROS) generation by inducing activation of extracellular signal-regulated kinase 1/2 (ERK 1/2) and NADPH oxidase. This event caused depletion of thiol groups and glutathione, NF-κB inhibition, c-Jun N-terminal kinase (JNK) activation, cell detachment from the matrix, and cellular shrinkage. The increa…

Programmed cell deathMAP Kinase Signaling SystemPhysiologyClinical BiochemistryAmino Acid Chloromethyl Ketoneschemistry.chemical_compoundCell Line TumorSettore BIO/10 - BiochimicaHumansParthenolidePropidium iodideFragmentation (cell biology)MelanomaCaspaseOsteosarcomaCell DeathbiologyNF-kappa BApoptosis Inducing FactorNADPH OxidasesCell BiologyCaspase InhibitorsCell biologyGene Expression Regulation NeoplasticchemistryApoptosisCell cultureCaspasesbiology.proteinApoptosis-inducing factorReactive Oxygen SpeciesSesquiterpenesParthenolide caspase-independent cell death ROS AIFJournal of Cellular Physiology
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Targeting the mitochondrial pathway to induce apoptosis/necrosis through ROS by a newly developed Schiff’s base to overcome MDR in cancer

2011

Abstract Multidrug resistance (MDR) in cancer, a major obstacle to successful application of cancer chemotherapy, is often characterized by over-expression of multidrug resistance-related proteins such as MRP1, P-gp or elevated glutathione (GSH) level. Efflux of drugs by functional P-gp, MRP1 and elevated GSH level can confer resistance to apoptosis induced by a range of different stimuli. Therefore, it is necessary to develop new cell death inducers with relatively lower toxicity toward non-malignant cells that can overcome MDR by induction of apoptotic or non-apoptotic cell death pathways. Herein we report the synthesis and spectroscopic characterization of a GSH depleting, redox active S…

Programmed cell deathMagnetic Resonance SpectroscopyNecrosisApoptosisMitochondrionBiologymedicine.disease_causeBiochemistryEhrlich ascites carcinomaMiceNecrosisCell Line TumorNeoplasmsSpectroscopy Fourier Transform InfraredmedicineAnimalsCytotoxic T cellCytotoxicitySchiff BasesCalpainCaspase 3General MedicineFlow CytometryGlutathioneMitochondriaBiochemistryDrug Resistance NeoplasmApoptosisCancer researchCalciumSpectrophotometry Ultravioletmedicine.symptomReactive Oxygen SpeciesOxidative stressBiochimie
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Differential Roles of JNK in ConA/GalN and ConA-Induced Liver Injury in Mice

2008

Tumor necrosis factor-alpha-mediated liver injury can be induced by several different means; however, the signaling events and mechanisms of cell death are likely different. We investigated the mechanism of both apoptotic and necrotic hepatocyte cell death as well as the role of c-Jun NH2-terminal kinase (JNK) in the ConA and ConA/D-galactosamine (GalN) models of murine liver injury. ConA alone induced primarily necrotic cell death with no caspase activation, whereas ConA/GalN induced apoptosis in addition to necrotic cell death. The bi-modal death pattern in the ConA/GalN model was confirmed by the use of transgenic mice expressing a dominant-negative form of Fas-associated death domain in…

Programmed cell deathNecrosisFas-Associated Death Domain ProteinApoptosisGalactosamineMitochondria Liverchemical and pharmacologic phenomenaCaspase 8Pathology and Forensic MedicineMiceNecrosisConcanavalin AmedicineAnimalsPhosphorylationDeath domainLiver injuryCaspase 8biologyLiver DiseasesJNK Mitogen-Activated Protein Kinasesmedicine.diseaseMolecular biologyEnzyme ActivationMice Inbred C57BLDisease Models Animalmedicine.anatomical_structureConcanavalin AApoptosisHepatocytebiology.proteinMutant ProteinsChemical and Drug Induced Liver Injurymedicine.symptomGene DeletionRegular ArticlesBH3 Interacting Domain Death Agonist ProteinThe American Journal of Pathology
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Caspase-8 regulates TNF-alpha induced epithelial necroptosis and terminal ileitis

2011

Two groups identify the regulation of death-receptor-induced necroptosis as an epithelial intrinsic mechanism that is important for the maintenance of immune homeostasis and the prevention of intestinal inflammation in mice. Welz et al. describe an unexpected physiological function for FADD (Fas-associated protein with death domain), an adaptor protein required for death-receptor-induced apoptosis. Mice with intestinal epithelial specific knockout of FADD develop severe colon inflammation due to increased death of FADD-deficient colonic epithelial cells. Gunther et al. report a novel and unexpected function of caspase-8 in maintaining immune homeostasis in the gut. Caspase-8 expression by g…

Programmed cell deathPaneth CellsNecroptosisInflammationApoptosisBiologyIn Vitro Techniquesdigestive systemArticle03 medical and health sciencesMiceNecrosis0302 clinical medicineCrohn DiseasemedicineAnimalsHumansFADD030304 developmental biology0303 health sciencesCaspase 8MultidisciplinaryInnate immune systemTumor Necrosis Factor-alphaColitisIntestinal epithelium3. Good healthmedicine.anatomical_structure030220 oncology & carcinogenesisReceptor-Interacting Protein Serine-Threonine KinasesPaneth cellImmunologybiology.proteinCancer researchTumor necrosis factor alphaGoblet Cellsmedicine.symptomGene DeletionNature
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8,8-bis-(Dihydroconiferyl)-diferulate displayed impressive cytotoxicity towards a panel of human and animal cancer cells

2020

Abstract Background Recalcitrant cancers appear as a major obstacle to chemotherapy, prompting scientists to intensify the search for novel drugs to tackle the cell lines expressing multi-drug resistant (MDR) phenotypes. Purpose The purpose of this study was to evaluate the antiproliferative potential of a ferrulic acid derivative, 8,8-bis-(dihydroconiferyl)-diferulate (DHCF2) on a panel of 18 cancer cell lines, including various sensitive and drug-resistant phenotypes, belonging to human and animals. The mode of induction of cell death by this compound was further studied. Methods The antiproliferative activity, autophagy, ferroptotic and necroptotic cell death were evaluated by the resazu…

Programmed cell deathPharmaceutical ScienceApoptosisMice03 medical and health sciences0302 clinical medicineCell Line TumorDrug DiscoverymedicineAnimalsHumansCytotoxic T cellCytotoxicityCaspase030304 developmental biologyPharmacology0303 health sciencesLeukemiabiologyPlant ExtractsChemistrymedicine.diseaseAntineoplastic Agents PhytogenicDrug Resistance MultipleLeukemiaComplementary and alternative medicineDoxorubicinDrug Resistance NeoplasmCell cultureApoptosis030220 oncology & carcinogenesisCancer cellbiology.proteinCancer researchMolecular MedicinePhytomedicine
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A new technique for real-time analysis of caspase-3 dependent neuronal cell death

2007

Several markers are available to identify cells undergoing programmed cell death, but so far they are only applicable on fixed material. Therefore, no information on the kinetics of apoptosis can be obtained, although apoptosis is a dynamic cell process. Here, we describe a new technique that allows the real-time observation of the onset of apoptosis in primary neurons. Neurons are transfected with a plasmid that codes for a fluorescent protein localized in the soma. Upon activation of caspase-3, which represents the point-of-no-return in the apoptosis process, the fusion protein is cleaved and as a consequence translocates into the nucleus. The onset of apoptosis is thus visualized by tran…

Programmed cell deathRecombinant Fusion ProteinsCellApoptosisCaspase 3BiologyMiceComputer SystemsmedicineAnimalsCells CulturedNeuronsMice Inbred BALB CTUNEL assayStaining and LabelingCaspase 3General NeuroscienceImage EnhancementFusion proteinCell biologymedicine.anatomical_structureAnimals NewbornMicroscopy FluorescenceApoptosisSomaNucleusJournal of Neuroscience Methods
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