Search results for "Caspase-3"

showing 10 items of 15 documents

Autophagy is required for sea urchin oogenesis and early development.

2016

SummaryAutophagy is a major intracellular pathway for the degradation and recycling of cytosolic components. Emerging evidence has demonstrated its crucial role during the embryo development of invertebrates and vertebrates. We recently demonstrated a massive activation of autophagy in Paracentrotus lividus embryos under cadmium stress conditions, and the existence of a temporal relationship between induced autophagy and apoptosis. Although there have been numerous studies on the role of autophagy in the development of different organisms, information on the autophagic process during oogenesis or at the start of development in marine invertebrates is very limited. Here we report our recent …

0301 basic medicineEmbryo NonmammalianFluorescent Antibody TechniqueCaspase 3ApoptosisFertilization in VitroBiologyParacentrotus lividus03 medical and health sciencesbiology.animalOrganelleBotanyAutophagyAnimalsSettore BIO/06 - Anatomia Comparata E CitologiaSea urchinLC3 Caspase-3 Embryos Oocytes Paracentrotus lividusAutophagyEmbryoCell BiologyMarine invertebratesbiology.organism_classificationCell biology030104 developmental biologyOocytesParacentrotusMacrolidesMicrotubule-Associated ProteinsIntracellularDevelopmental BiologyZygote (Cambridge, England)
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Coexpresión de NG2/GFAP tras la diferenciación en células transfectadas con las mutaciones de GFAP y en células procedentes de gliomas indiferenciados

2020

Resumen: Introducción: La enfermedad de Alexander es una enfermedad rara causada por mutaciones en el gen que codifica la proteína glial ácida fibrilar (GFAP). En un estudio previo hemos observado que la diferenciación de neuroesferas transfectadas con estas mutaciones genera un tipo celular que comparte la expresión de GFAP y NG2. Objetivos: Determinar el efecto de las mutaciones en marcadores moleculares en comparación con células de glioma diferenciados que expresan simultáneamente GFAP y NG2. Métodos: Se utilizaron muestras de glioblastoma humana (GLM) y neuroesferas procedentes de rata transfectadas con mutaciones de GFAP para el análisis de la expresión tras diferenciación de GFAP y N…

0301 basic medicineGFAPmacromolecular substancesGliomalcsh:RC346-42903 medical and health sciences030104 developmental biology0302 clinical medicinenervous systemCaspase-3Alexander diseaseNG2Neurology (clinical)030217 neurology & neurosurgerylcsh:Neurology. Diseases of the nervous systemNeurología
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Transcriptomic study of the toxic mechanism triggered by beauvericin in Jurkat cells

2018

Beauvericin (BEA), an ionophoric cyclic hexadepsipeptide mycotoxin, is able to increase oxidative stress by altering membrane ion permeability and uncoupling oxidative phosphorylation. A toxicogenomic study was performed to investigate gene expression changes triggered by BEA exposure (1.5, 3 and 5 mu M; 24 h) in Jurkat cells through RNA-sequencing and differential gene expression analysis. Perturbed gene expression was observed in a concentration dependent manner, with 43 differentially expressed genes (DEGs) overlapped in the three studied concentrations. Gene ontology (GO) analysis showed several biological processes related to electron transport chain, oxidative phosphorylation, and cel…

0301 basic medicineProgrammed cell deathCYTOCHROME-C RELEASEBCL-2 FAMILYCell Membrane PermeabilityRespiratory chainCell Culture TechniquesCASPASE-3 ACTIVATIONApoptosisOxidative phosphorylationCHO-K1 CELLSToxicologyJurkat cellsOxidative PhosphorylationElectron Transport03 medical and health sciencesJurkat CellsFUSARIUM MYCOTOXINSImmunotoxicologyDepsipeptidesHumansREAL-TIME PCROXIDATIVE STRESSTranscriptomicsCaspaseINDUCED APOPTOSISLEUKEMIA-CELLS030102 biochemistry & molecular biologybiologyDose-Response Relationship DrugChemistryJurkatGene Expression ProfilingBcl-2 familyDEATHGeneral MedicineBeauvericinToxicogenomicsCell biologyGene expression profiling030104 developmental biologyMitochondrial respiratory chainGene Ontologybiology.proteinRNA-seqTranscriptomeToxicology Letters
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The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex (CubipyOXA) leads to cell death in NCI-H292 cancer cells

2017

Abstract Cell survival and proliferation are central to carcinogenesis, involving various mechanisms among which those that impede apoptosis are important. In this, the role of the molecular chaperone Hsp60 is unclear since it has been reported that it can be both, pro- or anti-apoptotic. A solution to this riddle is crucial to the development of anti-cancer therapies targeting Hsp60. We addressed this question using a tumor cell line, NCI-H292, and [Cu(3,5-bis(2′-pyridyl)-1,2,4-oxadiazole) 2 (H 2 O) 2 ](ClO 4 ) 2 , CubipyOXA , a copper-containing compound with cytotoxic properties. We treated cells with various doses of the compound and measured cell viability; apoptosis indicators; and le…

0301 basic medicineProgrammed cell deathanimal structuresApoptosischemical and pharmacologic phenomenaCaspase 3medicine.disease_causecomplex mixturesBiochemistryMitochondrial ProteinsHsp60/pC3 complexInorganic Chemistry03 medical and health sciences0302 clinical medicineCoordination ComplexesCell Line TumorNeoplasmsCubipyOXAmedicineHumansCytotoxic T cellViability assayCancerOxadiazolesCaspase 3ChemistryfungiApoptosiChaperonin 60Hsp60Neoplasm ProteinsCell biology030104 developmental biologyApoptosisPro-caspase-3 (pC3)Multiprotein Complexes030220 oncology & carcinogenesisCancer cellHSP60Apoptosis; Cancer; CubipyOXA; Hsp60; Hsp60/pC3 complex; Pro-caspase-3 (pC3); Biochemistry; Inorganic ChemistryCarcinogenesisCopper
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Alexander Disease Mutations Produce Cells with Coexpression of Glial Fibrillary Acidic Protein and NG2 in Neurosphere Cultures and Inhibit Differenti…

2017

Background Alexander disease (AxD) is a rare disease caused by mutations in the gene encoding glial fibrillary acidic protein (GFAP). The disease is characterized by presence of GFAP aggregates in the cytoplasm of astrocytes and loss of myelin. Objectives Determine the effect of AxD-related mutations on adult neurogenesis. Methods We transfected different types of mutant GFAP into neurospheres using the nucleofection technique. Results We find that mutations may cause coexpression of GFAP and NG2 in neurosphere cultures, which would inhibit the differentiation of precursors into oligodendrocytes and thus explain the myelin loss occurring in the disease. Transfection produces cells that diff…

0301 basic medicinecaspase-3Cathepsin Dmacromolecular substancesHSP27lcsh:RC346-429oligodendrocyte precursors03 medical and health sciencesMyelin0302 clinical medicineAlexander diseaseNG2Neurosphereneurospheresmedicinecathepsinlcsh:Neurology. Diseases of the nervous systemOriginal ResearchGlial fibrillary acidic proteinbiologyNeurogenesisNestinGFAP stainmedicine.diseaseMolecular biologyAlexander disease030104 developmental biologymedicine.anatomical_structurenervous systemNeurologyglial fibrillary acidic proteinbiology.proteinNeurology (clinical)030217 neurology & neurosurgeryNeuroscienceFrontiers in Neurology
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Involvement of caspase-3 and GD3 ganglioside in ceramide-induced apoptosis in Farber disease.

2000

Farber's disease (FD) is a rare genetic disorder caused by ceramidase deficiency, which results in ceramide accumulation in lung, liver, colon, skeletal muscle, cartilage, and bone. Although this disease has been symptomatically characterized, little is known about its molecular pathogenetic process. Because recent studies reported that ceramide accumulation induces GD3 ganglioside formation and apoptosis, we investigated, in tissue obtained via colonoscopy from seriously involved patients, the possible involvement of ceramide in FD colonocyte destruction. Histochemical and TUNEL analyses of paraffin-embedded sections revealed that 45 ± 4.3% of FD colonocytes showed morphological signs of …

AdultCeramidePathologymedicine.medical_specialtyHistologyColonCaspase 3ApoptosisCeramideschemistry.chemical_compoundGangliosidesmedicineGD3 gangliosideHumansIntestinal MucosaCaspaseFarber diseaseFarber diseaseTUNEL assaybiologyCaspase 3ApoptosiCell Biologymedicine.diseaseCeramidaseCaspaseK18EpitheliumActive caspase-3Lysosomal Storage Diseasesmedicine.anatomical_structurechemistryApoptosisCaspasesCancer researchbiology.proteinAnatomyActive caspase-3; Apoptosis; Caspases; Farber disease; GD3 ganglioside; K18; Anatomy; Cell BiologyThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
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Immunohistochemical expression of apoptotic factors, cytokeratins, and metalloproteinase-9 in periapical and epithelialized gingival lesions

2012

Bellmann K, 2010, CELL STRESS CHAPERON, V15, P101, DOI 10.1007-s12192-009-0126-9; Cappello Francesco, 2011, Front Biosci (Schol Ed), V3, P341, DOI 10.2741-s155; Cappello F, 2006, CANCER, V107, P2417, DOI 10.1002-cncr.22265; Cappello F, 2002, EUR J HISTOCHEM, V46, P199; Carneiro E, 2009, ORAL SURG ORAL MED O, V107, P127, DOI 10.1016-j.tripleo.2008.07.030; Chandra D, 2007, J BIOL CHEM, V282, P31289, DOI 10.1074-jbc.M702777200; Fujita Y, 2011, ODONTOLOGY, V100, P215; Garcia Celia Carrillo, 2007, Med Oral Patol Oral Cir Bucal, V12, pE585; Garcia CC, 2009, ORAL SURG ORAL MED O, V107, pE43, DOI 10.1016-j.tripleo.2008.12.002; Gregory CD, 2011, J PATHOL, V223, P177, DOI 10.1002-path.2792; Gupta S, …

Histologybusiness.industryCaspase 3GingivaApoptosisGeneral MedicineMolecular biologyImmunohistochemistryCaspase 9EpitheliumPathology and Forensic MedicineCell stressMatrix Metalloproteinase 9cytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosisIHC PCNA TUNELProliferating Cell Nuclear AntigenMedicineHumansKeratinsbusinessApoptosis Regulatory ProteinsPeriapical Granuloma
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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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Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells.

2008

Hsp60, a mitochondrial chaperonin highly conserved during evolution, has been found elevated in the cytosol of cancer cells, both in vivo and in vitro, but its role in determining apoptosis during oxidative stress (OS) has not yet been fully elucidated. The aim of the present work was to study the effects of OS on Hsp60 levels and its interactions with procaspase- 3 (p-C3) and p53 in tumor cells. NCI-H292 (mucoepidermoid carcinoma) cells were exposed to various concentrations of hydrogen peroxide (H2O2) for 24 hours. Cell viability was determined by Trypan blue and MTT assays. DNA damage was assessed by the Comet assay, and apoptosis was measured by the AnnexinV cytofluorimetric test. Expos…

Lung Neoplasmsanimal structuresHistologyCell SurvivalDNA damageBlotting WesternBiophysicsHsp60;procaspase-3;mucoepidermoid carcinomaGene ExpressionTetrazolium SaltsApoptosisBiologymedicine.disease_causechemistry.chemical_compoundCell Line TumormedicineHumansChaperonin Hsp60 Cpn60 procaspase-3 caspase- 3 DNA damage p53 apoptosis.Viability assaylcsh:QH301-705.5FormazansCaspase 3Settore BIO/16 - Anatomia UmanaChaperonin 60DNAHydrogen PeroxideTrypan BlueCell BiologyImmunohistochemistryMolecular biologyComet assayOxidative Stresslcsh:Biology (General)chemistryApoptosisCancer cellCarcinoma MucoepidermoidHSP60Trypan blueComet AssayTumor Suppressor Protein p53Oxidative stressDNA Damage
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Bruce/apollon promotes hippocampal neuron survival and is downregulated by kainic acid

2005

Prolonged or excess stimulation of excitatory amino acid receptors leads to seizures and the induction of excitotoxic nerve cell injury. Kainic acid acting on glutamate receptors produces degeneration of vulnerable neurons in parts of the hippocampus and amygdala, but the exact mechanisms are not fully understood. We have here investigated whether the anti-apoptotic protein Bruce is involved in kainic acid-induced neurodegeneration. In the rat hippocampus and cortex, Bruce was exclusively expressed by neurons. The levels of Bruce were rapidly downregulated by kainic acid in hippocampal neurons as shown both in vivo and in cell culture. Caspase-3 was activated in neurons exhibiting low level…

MaleKainic acidCell SurvivalBiophysicsExcitotoxicityBruce/apollon Hippocampus Kainic acid Excitotoxicity Neuronal death Caspase-3 Cytochrome cDown-RegulationHippocampusStimulationBiologyHippocampal formationmedicine.disease_causeHippocampusBiochemistrychemistry.chemical_compoundDownregulation and upregulationmedicineAnimalsRats WistarMolecular BiologyCells CulturedNeuronsKainic AcidDose-Response Relationship DrugNeurodegenerationGlutamate receptorCell Biologymedicine.diseaseRatsCell biologynervous systemchemistryBiochemistryUbiquitin-Conjugating Enzymeshuman activitiescirculatory and respiratory physiology
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