Search results for "CASP"

showing 10 items of 470 documents

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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Caspase-2 is an initiator caspase responsible for pore-forming toxin-mediated apoptosis

2012

Bacterial pathogens modulate host cell apoptosis to establish a successful infection. Pore-forming toxins (PFTs) secreted by pathogenic bacteria are major virulence factors and have been shown to induce various forms of cell death in infected cells. Here we demonstrate that the highly conserved caspase-2 is required for PFT-mediated apoptosis. Despite being the second mammalian caspase to be identified, the role of caspase-2 during apoptosis remains enigmatic. We show that caspase-2 functions as an initiator caspase during Staphylococcus aureus alpha-toxin- and Aeromonas aerolysin-mediated apoptosis in epithelial cells. Downregulation of caspase-2 leads to a strong inhibition of PFT-mediate…

Inhibitor of apoptosis domain0303 health sciencesProgrammed cell deathPore-forming toxinGeneral Immunology and MicrobiologybiologyNLRP1General Neuroscience030302 biochemistry & molecular biologyCaspase 2Molecular biologyGeneral Biochemistry Genetics and Molecular Biology3. Good healthCell biology03 medical and health sciencesDownregulation and upregulationApoptosisbiology.proteinMolecular BiologyCaspase030304 developmental biologyThe EMBO Journal
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Potassium regulates IL-1 beta processing via calcium-independent phospholipase A2.

2000

Abstract We report that potassium leakage from cells leads to activation of the Ca2+-independent phospholipase A2 (iPLA2), and the latter plays a pivotal role in regulating the cleavage of pro-IL-1β by the IL-converting enzyme caspase-1 in human monocytes. K+ efflux led to increases of cellular levels of glycerophosphocholine, an unambiguous indicator of phospholipase A2 activation. Both maturation of IL-1β and formation of glycerophosphocholine were blocked by bromoenol lactone, the specific iPLA2 inhibitor. Bromoenol lactone-dependent inhibition of IL-1β processing was not due to perturbation of the export machinery for pro-IL-1β and IL-1β or to caspase-1 suppression. Conspicuously, activ…

Intracellular FluidPotassiumImmunologychemistry.chemical_elementNaphthalenesCleavage (embryo)MonocytesPhospholipases APhospholipase A2Calcium-Independent Phospholipase A2Immunology and AllergyHumansCells Culturedchemistry.chemical_classificationCalcium metabolismbiologyTumor Necrosis Factor-alphaCaspase 1Biological TransportCaspase InhibitorsCell biologyEnzyme ActivationPhospholipases A2EnzymechemistryPyronesbiology.proteinPotassiumCalciumEffluxBromoenol lactoneProtein Processing Post-TranslationalImmunosuppressive AgentsInterleukin-1Journal of immunology (Baltimore, Md. : 1950)
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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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Regulation of X Chromosome-Linked Inhibitor of Apoptosis Protein (XIAP) in Kainic Acid Induced Neuronal Cell Death in the Rat Hippocampus

2001

INTRODUCTION. Inhibitor of apoptosis protein (IAP) family consists of several antiapoptotic proteins conserved among species. The IAPs have a well-conserved motif of approximately 65 residues, called the baculovirus inhibitory repeat (BIR) (1). Baculovirus and drosophila IAPs have two, but most IAPs contain three BIR domains. Most of the IAPs also have a C-terminal RING domain which consists of conserved amino acids with zinc binding capacity. XIAP is one of the five known human IAPs and it binds directly and inhibits the activity of caspases (2). The BIR2 domain in XIAP is sufficient to mediate this inhibition (3). However little is known about the presence and function of XIAP in the nerv…

Kainic acidProgrammed cell deathbiologylcsh:Tlcsh:RShort Reportlcsh:MedicineColocalizationNuclease protection assayGeneral MedicineHippocampal formationInhibitor of apoptosislcsh:TechnologyGeneral Biochemistry Genetics and Molecular BiologyXIAPCell biologychemistry.chemical_compoundnervous systemchemistrybiology.proteinlcsh:Qlcsh:ScienceCaspaseGeneral Environmental ScienceThe Scientific World Journal
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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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Does the orthodontic treatment induces dental pulp cellular death? Caspase-3 and-9, HSP60 and TUNEL expression

2011

Objective: To evaluate the hypothesis of human dental pulp cell death during orthodontic treatement (O.T) and the degree of apoptosis through the expression level of the proteins Caspase-3,-9, TUNEL and HSP60. Materials and methods: Human dental Pulp were coming from both male and female patients (N=20; age 10-14years). The technique used was the Straight Wire, which involves Nickel-Titanium or Steel archwires. The increase of pressure applied on teeth was gradual. Some patients were subjected to a premolar extraction after 3 months treatment, and others after 6 months. Samples were Bouin-fixed, paraffin-embedded and afterwards processed for immunohistochemistry using anti-caspase-3,-9 anti…

Key Words: Caspase-9 orthodontic treatment Dental Pulp
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Liver X Receptor ligand cytotoxicity in colon cancer cells and not in normal colon epithelial cells depends on LXRβ subcellular localization

2015

Increasing evidence indicates that Liver X Receptors (LXRs) have some anticancer properties. We recently demonstrated that LXR ligands induce colon cancer cell pyroptosis through an LXRβ-dependent pathway. In the present study, we showed that human colon cancer cell lines presented differential cytoplasmic localizations of LXRβ. This localization correlated with caspase-1 activation and cell death induction under treatment with LXR ligand. The association of LXRβ with the truncated form of RXRα (t-RXRα) was responsible for the sequestration of LXRβ in the cytoplasm in colon cancer cells. Moreover t-RXRα was not expressed in normal colon epithelial cells. These cells presented a predominantl…

LXRβCytoplasmmedicine.medical_specialtyHydrocarbons FluorinatedColonColorectal cancerCaspase 1BiologyLigandsCell Line03 medical and health sciences0302 clinical medicineCell Line TumorInternal medicineRXRαsubcellular localizationmedicineHumansIntestinal MucosaLiver X receptorCytotoxicityLiver X Receptors030304 developmental biologySulfonamides0303 health sciencesRetinoid X Receptor alphaRetinoid X receptor alphaCaspase 1PyroptosisEpithelial CellsHCT116 CellsOrphan Nuclear ReceptorsSubcellular localizationmedicine.disease3. Good healthEnzyme ActivationGene Expression Regulation NeoplasticEndocrinologycolon cancerOncologyCell culture030220 oncology & carcinogenesisColonic NeoplasmsCancer researchPriority Research PaperOncotarget
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Immunohistochemical expression and distribution of orexin, orphanin and leptin in the major salivary glands of some mammals

2012

Abstract: The aim of the study was to assess the involvement of apoptotic factors, cytokeratins and metalloproteinase- 9 in the histogenesis of both Epithelialized Gingival Lesions (EGL) and Periapical Lesions (PAL). 55 consecutive patients, 30 with PAL and 25 with EGL, were selected for the study after clinical and radiological examinations. The PAL patients had severe periapical lesions and tooth decay with exposure of the pulp chamber. All PAL and EGL biopsies were surgically extracted, fixed in 10% buffered formalin, and processed for routine light microscopy. Ten biopsies of each category were processed for immunohistochemistry (IHC). Serial paraffin sections were stained by IHC with a…

LeptinKey words: cytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosis IHC PCNA TUNELSettore BIO/17 - Istologiamedicine.medical_specialtyHistologySubmandibular Glandcytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosis IHC PCNA TUNEL [Key words]major salivary glands orphanin FQ nociception orexin leptin IHC rat sheep cowBiologySalivary GlandsPathology and Forensic MedicineOrexin-ASublingual Glandstomatognathic systemInternal medicineMajor Salivary GlandOrexigenicmedicineEndocrine systemAnimalsParotid GlandMammalsOrexinsSheepSalivary glandNeuropeptidesConnective tissue stromaIntracellular Signaling Peptides and ProteinsGeneral MedicineImmunohistochemistryEpitheliumOrexinRatsmedicine.anatomical_structureEndocrinologyOpioid PeptidesCattlemedicine.drug
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New insight into the inhibition of the inflammatory response to experimental delayed-type hypersensitivity reactions in mice by scropolioside A.

2006

Scropolioside A, an iridoid isolated from Scrophularia auriculata ssp. pseudoauriculata, showed anti-inflammatory properties against different experimental models of delayed-type hypersensitivity. This iridoid reduced the oedema induced by oxazolone by 79% (72 h) at 0.5 mg/ear while reducing that induced by sheep red blood cells by 47% (18 h), 45% (24 h) and 36% (48 h) at 10 mg/kg. In vivo it reduced both oedema formation and cell infiltration whereas in vitro it reduced the proliferation of activated T-lymphocytes (IC50 of 67.74 microM). Treatment with scropolioside A (100 microM) 18 and 24 h after phytohemagglutinin stimulation increased the number of cells arrested in the subG(0) phase w…

LipopolysaccharidesNecrosisErythrocytesLeukotriene B4NeutrophilsT-LymphocytesAnti-Inflammatory AgentsStimulationInflammationApoptosisLymphocyte proliferationPharmacologyBiologyLeukotriene B4DinoprostoneNitric oxideCell LineOxazolonechemistry.chemical_compoundMiceGlucosidesmedicineAnimalsEdemaHumansHypersensitivity DelayedPyransPharmacologySheepPancreatic ElastaseCaspase 3MacrophagesOxazoloneEarAllergenschemistryDelayed hypersensitivityImmunologyCytokinesFemalemedicine.symptomEuropean journal of pharmacology
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