Search results for "caspases"

showing 10 items of 157 documents

Differentiation capacity of epithelial cells in the sponge Suberites domuncula.

2004

Sponges (phylum Porifera) represent the oldest metazoans. Their characteristic metazoan adhesion molecules and transcription factors enable them to establish a complex "Bauplan" ; three major differentiated cell types (epithelial cells, skeletal cells/sclerocytes, and contractile cells) can be distinguished. Since no molecular markers are as yet available to distinguish these somatic cells or the corresponding embryonic cells from which they originate, we have selected the following three genes for their characterization: noggin (a signaling molecule in development), a caspase that encodes an apoptotic molecule, and silicatein. Silicatein is an enzyme that is involved in the synthesis of si…

HistologySuberites domuncula; sponges; cell differentiationCellular differentiationMolecular Sequence DataPinacodermBiologyPathology and Forensic MedicineEvolution MolecularDemospongeMesohylAnimalsAmino Acid SequenceNogginCloning MolecularPhylogenySclerocyteCell AggregationSequence Homology Amino AcidSilicatesProteinsCell DifferentiationCell BiologyAnatomybiology.organism_classificationCell biologySuberites domunculaSpongeCaspasesCarrier ProteinsSuberitesCell and tissue research
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Sponge Bcl-2 homologous protein (BHP2-GC) confers distinct stress resistance to human HEK-293 cells

2001

It is established that sponges, the phylogenetically oldest still extant phylum of Metazoa, possess key molecules of the apoptotic pathways, that is members from the Bcl-2 family and a pro-apoptotic molecule with death domains. Here we report on transfection studies of human cells with a sponge gene, GCBHP2. Sponge tissue was exposed to heat shock and tributyltin, which caused an upregulation of gene expression of GCBHP2. The cDNA GCBHP2 was introduced into human HEK-293 cells and mouse NIH-3T3 cells; the stable transfection was confirmed by the identification of the transcripts, by Western blotting as well as by immunofluorescence using antibodies raised against the recombinant polypeptide…

Hot Temperatureanimal structuresCell SurvivalvirusesMolecular Sequence DataDrug ResistanceApoptosisAntibodiesCell LineMiceComplementary DNAGene expressionAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCaspase 3ChemistryfungiHEK 293 cellsCell BiologyTransfectionbiology.organism_classificationMolecular biologyPoriferaProtein Structure TertiaryUp-RegulationEnzyme ActivationBlotSpongeProto-Oncogene Proteins c-bcl-2Cell cultureCaspasesembryonic structuresbiology.proteinTrialkyltin CompoundsAntibodySequence AlignmentHeat-Shock ResponseCell Death & Differentiation
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Cigarette smoke promotes inflammasome‐independent activation of caspase‐1 and ‐4 leading to gasdermin D cleavage in human macrophages

2022

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 investig…

InflammationLipopolysaccharidesPore Forming Cytotoxic Proteinsalveolar macrophages caspasecigarette smoke inflammasome lung Caspase 1 Caspases Caspases Initiator Humans Inflammation Intracellular Signaling Peptides and Proteins Lipopolysaccharides Lipopolysaccharides NLR Family Pyrin Domain-Containing 3 Protein Phosphate-Binding Proteins Pore Forming Cytotoxic Proteins Tobacco Cigarette Smoking Inflammasomes.InflammasomesSettore BIO/16 - Anatomia UmanaMacrophagesCaspase 1Intracellular Signaling Peptides and ProteinsPhosphate-Binding ProteinsBiochemistryCaspases InitiatorCigarette SmokingCaspasesNLR Family Pyrin Domain-Containing 3 ProteinTobaccoGeneticsHumansMolecular BiologyBiotechnologyThe FASEB Journal
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Dinitrosyl-iron triggers apoptosis in Jurkat cells despite overexpression of Bcl-2

2004

Cells expressing the cytokine-inducible NO synthase are known to trigger apoptosis in neighboring cells. Paramagnetic dinitrosyl nonheme iron complexes (DNIC) were found in tumor tissue about 40 years ago; however, the role of these NO(+)-bearing species is not completely understood. In the human Jurkat leukemia cell line, the application of the model complex DNIC-thiosulfate (50-200 microM) induced apoptosis (defined by phosphatidylserine externalization) in a concentration- and time-dependent manner. In Jurkat cells, the pan-caspase inhibitor, zVADfmk (50 microM), and/or stable transfection of antiapoptotic protein, Bcl-2, was unable to afford protection against DNIC-induced apoptosis. Th…

IronNitrosationCellApoptosisBiochemistryJurkat cellsMetal ChelatorNitric oxideJurkat Cellschemistry.chemical_compoundPhysiology (medical)medicineExtracellularPiHumansElectron Spin Resonance SpectroscopyGlutathioneCaspase InhibitorsCell biologymedicine.anatomical_structureGene Expression RegulationProto-Oncogene Proteins c-bcl-2chemistryApoptosisCaspasesNitrogen OxidesFree Radical Biology and Medicine
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cFLIPL Inhibits Tumor Necrosis Factor-related Apoptosis-inducing Ligand-mediated NF-κB Activation at the Death-inducing Signaling Complex in Human Ke…

2004

Human keratinocytes undergo apoptosis following treatment with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via surface-expressed TRAIL receptors 1 and 2. In addition, TRAIL triggers nonapoptotic signaling pathways including activation of the transcription factor NF-kappaB, in particular when TRAIL-induced apoptosis is blocked. The intracellular protein cFLIP(L) interferes with TRAIL-induced apoptosis at the death-inducing signaling complex (DISC) in many cell types. To study the role of cFLIP(L) in TRAIL signaling, we established stable HaCaT keratinocyte cell lines expressing varying levels of cFLIP(L). Functional analysis revealed that relative cFLIP(L) levels correlat…

KeratinocytesCytoplasmReceptor complexCell SurvivalCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisCell SeparationBiologyCaspase 8Sensitivity and SpecificityBiochemistryProinflammatory cytokineTNF-Related Apoptosis-Inducing LigandRibonucleasesCell Line TumorHumansEnzyme InhibitorsMolecular BiologyTranscription factorSkinInflammationCaspase 8Membrane GlycoproteinsTumor Necrosis Factor-alphaIntracellular Signaling Peptides and ProteinsNF-kappa BCell BiologyFlow CytometryRecombinant ProteinsCell biologyRetroviridaeApoptosisCaspasesDeath-inducing signaling complexRNATumor necrosis factor alphaSignal transductionApoptosis Regulatory ProteinsPropidiumProtein BindingSignal TransductionJournal of Biological Chemistry
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Ablation of c-FLIP in hepatocytes enhances death-receptor mediated apoptosis and toxic liver injury in vivo

2010

Background & Aims Apoptosis is crucially involved in acute and chronic liver injury, including viral, cholestatic, toxic, and metabolic liver disease. Additionally, dysregulation of apoptosis signaling pathways has been implicated in hepatocarcinogenesis. The most prominent members of the apoptosis-mediating tumor necrosis factor receptor superfamily are the TNF-R1 (CD120a) and the CD95 (Apo-1/Fas) receptor. Although extensively studied, the intracellular signaling events in hepatocytes are only incompletely understood. Methods To examine the role of the caspase-8 homolog cellular FLICE-inhibitory protein (c-FLIP) in liver injury, we generated mice with hepatocyte specific deletion of c-FLI…

LipopolysaccharidesProgrammed cell deathMAP Kinase Signaling SystemCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisGalactosamineBiologyCaspase 8MiceLiver diseaseConcanavalin AmedicineAnimalsfas ReceptorAnthracenesMice KnockoutLiver injuryHepatologyReceptors Death DomainFas receptormedicine.diseasemedicine.anatomical_structureApoptosisCaspasesHepatocyteDeath-inducing signaling complexHepatocytesCancer researchFemaleChemical and Drug Induced Liver InjuryJournal of Hepatology
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Dominant negative MORT1/FADD rescues mice from CD95 and TNF-induced liver failure

2002

Derangement of the apoptotic program is considered an important cause of liver disease. It became clear that receptor-mediated apoptosis is of specific interest in this context, and CD95 and CD120a, both members of the tumor necrosis factor (TNF) receptor superfamily, are the most prominent cell death receptors involved. The death signal is induced upon ligand binding by recruitment of caspases via the adapter molecule MORT1/FADD to the receptor and their subsequent activation. To investigate the role of MORT1/FADD in hepatocyte apoptosis, we generated transgenic mice expressing liver-specific dominant negative mutant. Mice looked grossly normal; breeding and liver development were not diff…

Lipopolysaccharidesmedicine.medical_specialtyProgrammed cell deathFas-Associated Death Domain ProteinOligonucleotidesMice TransgenicAntibodiesReceptors Tumor Necrosis FactorMiceLiver diseaseAntigens CDAlbuminsInternal medicinemedicineAnimalsfas ReceptorFADDPromoter Regions GeneticAdaptor Proteins Signal TransducingLiver injuryHepatitisMice Inbred BALB CHepatologybiologyTumor Necrosis Factor-alphamedicine.diseaseFas receptorMice Inbred C57BLEndocrinologyReceptors Tumor Necrosis Factor Type IApoptosisCaspasesbiology.proteinTumor necrosis factor alphaCarrier ProteinsLiver FailureHepatology
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pp32/PHAPI determines the apoptosis response of non-small-cell lung cancer

2007

During malignant transformation, cancer cells have to evade cell-intrinsic tumor suppressor mechanisms including apoptosis, thus acquiring a phenotype that is relatively resistant to clinically applied anticancer therapies. Molecular characterization of apoptotic signal transduction defects may help to identify prognostic markers and to develop novel therapeutic strategies. To this end we have undertaken functional analyses of drug-induced apoptosis in human non-small cell-lung cancer (NSCLC) cells. We found that primary drug resistance correlated with defects in apoptosome-dependent caspase activation in vitro. While cytochrome c-induced apoptosome formation was maintained, the subsequent …

Lung NeoplasmsTransplantation HeterologousAntineoplastic AgentsApoptosisMice SCIDBiologyMalignant transformationMiceProstate cancerIn vivoCarcinoma Non-Small-Cell LungmedicineAnimalsHumansLung cancerMolecular BiologyIntracellular Signaling Peptides and ProteinsNuclear ProteinsRNA-Binding ProteinsCancerCell Biologymedicine.diseaseCell biologyEnzyme ActivationApoptosisCaspasesCancer cellCancer researchSignal transductionNeoplasm TransplantationCell Death & Differentiation
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Potentiation of the antitumor effects of both selective cyclooxygenase-1 and cyclooxygenase-2 inhibitors in human hepatic cancer cells by inhibition …

2007

The molecular mechanisms behind the anti-neoplastic effects of non-steroidal anti-inflammatory drugs (NSAIDs) are not completely understood and cannot be explained by the inhibition of the cyclooxygenase (COX) enzymes COX-1 and COX-2 alone. We previously reported that both the selective COX-1 inhibitor SC-560 and the selective COX-2 inhibitor CAY10404 exhibit anti-tumor effects in human hepatoma cells. NSAID inhibitors have many COX-independent actions and, among others, the mitogen-activated protein kinase (MAPK) pathways are targets for NSAIDs. Here, we examined the role of MEK/ERK1/2 signaling in the anti-neoplastic effects of both selective COX-1 and COX-2 inhibitors in two human hepato…

MAPK/ERK pathwayCancer ResearchCarcinoma HepatocellularTime FactorsBlotting WesternApoptosisPharmacologyCOX-1 COX-2 NSAIDs MEK1/2 ERK1/2NitrilesButadienesTumor Cells CulturedHumansCyclooxygenase InhibitorsSulfonesEnzyme InhibitorsPhosphorylationProtein kinase ACell ProliferationPharmacologychemistry.chemical_classificationMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein Kinase 3biologyDose-Response Relationship DrugLiver NeoplasmsCytochromes cLong-term potentiationDrug SynergismIsoxazolesFlow CytometryEnzymeOncologychemistryCyclooxygenase 2CaspasesCancer cellbiology.proteinCyclooxygenase 1Molecular MedicineMEK-ERK PathwayPyrazolesDrug Therapy CombinationCyclooxygenaseHepatoma cellCancer biologytherapy
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Differential inhibition of TRAIL-mediated DR5-DISC formation by decoy receptors 1 and 2.

2006

International audience; Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a member of the TNF family that induces cancer cell death by apoptosis with some selectivity. TRAIL-induced apoptosis is mediated by the transmembrane receptors death receptor 4 (DR4) (also known as TRAIL-R1) and DR5 (TRAIL-R2). TRAIL can also bind decoy receptor 1 (DcR1) (TRAIL-R3) and DcR2 (TRAIL-R4) that fail to induce apoptosis since they lack and have a truncated cytoplasmic death domain, respectively. In addition, DcR1 and DcR2 inhibit DR4- and DR5-mediated, TRAIL-induced apoptosis and we demonstrate here that this occurs through distinct mechanisms. While DcR1 prevents the assembly of the…

MESH : Hela CellsMESH: Membrane GlycoproteinsMESH: Membrane MicrodomainsDecoy Receptor 1ApoptosisMESH : Membrane GlycoproteinsReceptors Tumor Necrosis FactorTNF-Related Apoptosis-Inducing LigandMESH : TNF-Related Apoptosis-Inducing LigandJurkat Cells0302 clinical medicineMESH : Tumor Necrosis Factor Decoy ReceptorsMESH: Jurkat CellsDecoy receptorsReceptorCells CulturedMESH : Jurkat CellsMESH : Tumor Necrosis Factor-alpha0303 health sciencesMembrane GlycoproteinsMESH : Protein BindingArticlesMESH : Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor Receptor-Associated Peptides and ProteinsCell biology030220 oncology & carcinogenesisCaspasesDeath-inducing signaling complexApoptosis/drug effects; Apoptosis Regulatory Proteins/antagonists & inhibitors; Apoptosis Regulatory Proteins/pharmacology; Caspases/metabolism; Cells Cultured; Death Domain Receptor Signaling Adaptor Proteins; Enzyme Activation/drug effects; GPI-Linked Proteins; HeLa Cells; Humans; Jurkat Cells; Membrane Glycoproteins/antagonists & inhibitors; Membrane Glycoproteins/pharmacology; Membrane Microdomains/drug effects; Protein Binding/drug effects; Receptors TNF-Related Apoptosis-Inducing Ligand; Receptors Tumor Necrosis Factor/metabolism; TNF-Related Apoptosis-Inducing Ligand; Tumor Necrosis Factor Decoy Receptors; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/metabolism; Tumor Necrosis Factor-alpha/antagonists & inhibitors; Tumor Necrosis Factor-alpha/pharmacologyMESH : Apoptosis Regulatory ProteinsMESH: TNF-Related Apoptosis-Inducing LigandProtein BindingMESH: Cells CulturedDeath Domain Receptor Signaling Adaptor ProteinsMESH: Enzyme ActivationBiologyMESH: Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsGPI-Linked Proteins03 medical and health sciencesMembrane MicrodomainsCell surface receptorMESH : Cells Cultured[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptors Tumor Necrosis Factor Member 10cHumansMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Receptors TNF-Related Apoptosis-Inducing LigandMESH : Receptors TNF-Related Apoptosis-Inducing LigandMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyDeath domainMESH: CaspasesMESH: HumansTumor Necrosis Factor-alphaMESH: Apoptosis Regulatory ProteinsMESH: ApoptosisMESH : HumansCell BiologyMESH: Receptors Tumor Necrosis FactorMESH: Tumor Necrosis Factor Decoy ReceptorsMESH : Receptors Tumor Necrosis FactorEnzyme ActivationMESH: Hela CellsReceptors TNF-Related Apoptosis-Inducing LigandTumor Necrosis Factor Decoy ReceptorsApoptosisMESH: Tumor Necrosis Factor-alphaMESH : Membrane MicrodomainsMESH : CaspasesApoptosis Regulatory ProteinsMESH : Enzyme ActivationMESH : ApoptosisMESH : Death Domain Receptor Signaling Adaptor ProteinsTumor Necrosis Factor Decoy ReceptorsHeLa CellsMESH: Death Domain Receptor Signaling Adaptor Proteins
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