Search results for "HEAT-SHOCK PROTEINS"

showing 10 items of 310 documents

Cadmium induces the expression of specific stress proteins in sea urchin embryos.

2004

Abstract Marine organisms are highly sensitive to many environmental stresses, and consequently, the analysis of their bio-molecular responses to different stress agents is very important for the understanding of putative repair mechanisms. Sea urchin embryos represent a simple though significant model system to test how specific stress can simultaneously affect development and protein expression. Here, we used Paracentrotus lividus sea urchin embryos to study the effects of time-dependent continuous exposure to subacute/sublethal cadmium concentrations. We found that, between 15 and 24 h of exposure, the synthesis of a specific set of stress proteins (90, 72–70, 56, 28, and 25 kDa) was ind…

Embryo NonmammalianBiophysicschemistry.chemical_elementWestern blotBiologyEmbryo developmentBiochemistryGel electrophoresiParacentrotus lividusStress proteins; Embryo development; Gel electrophoresis; Western blotWestern blotCadmium ChloridemedicineMorphogenesisStress ProteinsAnimalsElectrophoresis Gel Two-DimensionalSettore BIO/06 - Anatomia Comparata E CitologiaMolecular BiologyCells CulturedHeat-Shock ProteinsGel electrophoresisCadmiummedicine.diagnostic_testStress proteinEmbryogenesisCell BiologyGastrulaSea urchin embryoBlastulabiology.organism_classificationMolecular biologyCell biologyHighly sensitiveKineticschemistryFertilizationSea UrchinsFemaleBiochemical and biophysical research communications
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Studies on heat shock proteins in sea urchin development

1999

Work on stress proteins in sea urchin embryos carried out over the last 20 years is reviewed and the following major results are described. Entire sea urchin embryos, if subjected to a rise in temperature at any postblastular stage undergo a wave of heat shock protein (hsp) synthesis and survive. If subjected to the same rise between fertilization and blastula formation, they are not yet able to synthesize hsp and die. Four clones coding for the major hsp, hsp70, have been isolated and sequenced; evidence for the existence of a heat shock factor has been provided, and a mechanism for the developmental regulation of hsp synthesis discussed. Intra- embryonic and intracellular hsp location has…

Embryo NonmammalianGene Expression Regulation DevelopmentalApoptosisEmbryoCell BiologyBiologyBlastulaMolecular biologyEmbryonic stem cellHsp70Cell biologyHeat shock factorSea UrchinsHeat shock proteinbiology.animalCarcinogensAnimalsTetradecanoylphorbol AcetateHSP70 Heat-Shock ProteinsSea urchinIntracellularDevelopmental BiologyDevelopment, Growth and Differentiation
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Sea urchin embryos as an in vivo model for the assessment of manganese toxicity: developmental and stress response effects.

2009

In the marine environment increasing concentrations of bio-available compounds often result from anthropogenic activities. Among metal ions, manganese represents a new emergent factor in environmental contamination. Here, we studied the effects of manganese on Paracentrotus lividus sea urchin embryos using biological and biochemical approaches for the analysis of impact on development, tissue accumulation and stress markers. Embryos were continuously exposed from fertilization to manganese at concentrations ranging from 1.0 to 61.6 mg l(-1), monitored for developmental abnormalities at 48 h after fertilization, and used for atomic spectrometric analysis at various times from 6 to 72 h. We f…

Embryo NonmammalianHealth Toxicology and Mutagenesischemistry.chemical_elementApoptosisManganeseManagement Monitoring Policy and LawToxicologyParacentrotus lividusToxicologyHuman fertilizationStress PhysiologicalIn vivoToxicity TestsAnimalsManganeseTUNEL assaybiologyHSC70 Heat-Shock ProteinsEmbryoChaperonin 60General MedicineEmbryo-toxicity Marine environment Metal accumulation Stress proteins Apoptosis ROSbiology.organism_classificationCell biologychemistryModels AnimalToxicityParacentrotusBiomarkersWater Pollutants ChemicalIntracellular
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Sea urchin HSF activity in vitro and in transgenic embryos.

1997

Evidence is provided for the presence at the physiological temperature of 20 degrees C of a heat shock transcriptor factor, HSF, in the nuclei of P.lividus embryos. This HSF is able to specifically bind in vitro the heat shock element, HSE, of the promoter of the hsp70 gene i.v., as suggested by DNA-protein binding reactions and DNAse I protection assays. Upon heat-shock, at the temperature of 31 degrees C, its ability to bind the HSE units becomes much higher. The HSF activated by heat-shock drives in vivo the transcription of the beta-galactosidase reporter gene in transgenic sea urchin gastrulae. An ATF-like transcription factor, widely described in other organisms but not at all in sea …

Embryo NonmammalianHot TemperatureSea UrchinTranscription FactorTransgeneRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsTransfectionBiochemistryAnimals Genetically ModifiedTranscription (biology)Genes Reporterbiology.animalHeat shock proteinAnimalsHSP70 Heat-Shock ProteinsCell NucleuPromoter Regions GeneticMolecular BiologySea urchinTranscription factorHeat-Shock ProteinsCell NucleusHSP70 Heat-Shock ProteinReporter genebiologyBase SequenceAnimalTemperatureHeat-Shock ProteinPromoterCell BiologyGastrulabeta-GalactosidaseMolecular biologyCell biologyHsp70BiophysicSea UrchinsRecombinant Fusion ProteinTranscription FactorsBiochemical and biophysical research communications
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Mitochondrial localization and temporal expression of the Drosophila melanogaster DnaJ homologous tumor suppressor Tid50

1998

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (tid) was identified as a homolog of all dnaJ-like genes known to date which have been well preserved in evolution. Homozygous D. melanogaster l(2)tid mutants l(2)tid1, l(2)tid2 and l(2)tid3 are characterized by neoplastic transformation of the adult integumental primordia, the imaginal discs, and the death at the time of puparium formation. The first part of this study is concerned with the identification and subcellular localization of the l(2)tid-encoded protein, Tid50. The second part examines its tissue specific expression during wild-type development and in tumorous imaginal discs. To specify the functi…

Embryo NonmammalianTumor suppressor geneMutantGenes InsectCell FractionationBiochemistryCell LineMitochondrial ProteinsMelanogasterAnimalsDrosophila ProteinsGenes Tumor SuppressorNeoplastic transformationRNA MessengerGeneHeat-Shock ProteinsbiologyPupaGene Expression Regulation DevelopmentalRNANeoplasms ExperimentalSequence Analysis DNAOriginal ArticlesCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyMitochondriaGene Expression Regulation NeoplasticImaginal discDrosophila melanogasterOrgan SpecificityLarvaRabbitsDrosophila melanogasterCell Stress & Chaperones
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EGTA treatment causes the synthesis of heat shock proteins in sea urchin embryos.

2000

Paracentrotus lividus embryos, at post-blastular stage, when subjected to a rise in temperature from physiologic (20 degrees C) to 31 degrees C, synthesize a large group of heat shock proteins (hsps), and show a severe inhibition of bulk protein synthesis. We show, by mono- and two-dimensional electrophoresis, that also EGTA (ethylene glycol-bis[beta-aminoethyl ether] tetraacetic acid) treatment induces in sea urchin embryos both marked inhibition of bulk protein synthesis and the synthesis of the entire set of hsps. Furthermore, EGTA-treated sea urchin embryos are able to survive at a temperature otherwise lethal (35 degrees C) becoming thermotolerant. Because incubation with a different c…

Embryo NonmammalianbiologyEthylenediaminetetraacetic acidbiology.organism_classificationParacentrotus lividuschemistry.chemical_compoundEGTAchemistryBiochemistrybiology.animalHeat shock proteinSea UrchinsProtein biosynthesisBiophysicsAnimalsChelationElectrophoresis Gel Two-DimensionalMolecular BiologySea urchinIncubationEgtazic AcidEdetic AcidHeat-Shock ProteinsChelating AgentsMolecular cell biology research communications : MCBRC
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High levels of the molecular chaperone Mdg1/ERdj4 reflect the activation state of endothelial cells

2003

Mdg1/ERdj4, a mammalian chaperone that belongs to the HSP40 protein family, has been reported to be located in the endoplasmic reticulum (ER), is induced by ER stress, and protects ER stressed cells from apoptosis. Here we show that under normal physiological conditions, Mdg1/ERdj4 is expressed at various levels in the vasculature due to different activation states of the endothelium. To elucidate the stimuli that induce ER stress and thus upregulate Mdg1/ERdj4, we investigated the effect of several endothelium specific stressors on its expression. Mdg1/ERdj4 mRNA is induced by activated macrophages, by nitric oxide (NO) and heat shock, and during terminal cell differentiation, whereas shea…

EndotheliumCell SurvivalCellular differentiationApoptosisCell CommunicationEndoplasmic ReticulumNitric OxideMiceStress PhysiologicalmedicineAnimalsHumansRNA MessengerHeat shockEndoplasmic Reticulum Chaperone BiPbiologyMacrophagesEndoplasmic reticulumMembrane ProteinsProteinsCell BiologyHSP40 Heat-Shock ProteinsCoculture TechniquesUp-RegulationHsp70Cell biologyProtein Transportmedicine.anatomical_structureApoptosisChaperone (protein)biology.proteinUnfolded protein responseEndothelium VascularStress MechanicalCarrier ProteinsCell NucleolusHeat-Shock ResponseHeLa CellsMolecular ChaperonesExperimental Cell Research
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A field methodology to study effects of UV radiation on fish larvae.

2003

There is a considerable lack of in situ specific information about the effects of UV-B radiation on limnic animals studied in the field. We exposed larval pike (Esox lucius L.) in two types of cuvettes (glass and quartz) placed at different depths (5 or 15 cm) to natural solar UV or to artificially enhanced UV-B (lamps on 3 h per day), simulating the scenarios for coming decades. Dose realism and comparability with earlier laboratory experiments was the main purpose, and therefore UV-B irradiances to the surface as well as underwater irradiances were directly measured. Result showed that UV-B dose rates in natural waters are low even though DOC concentration was low (4.8 mg/l) in our study …

Environmental EngineeringUltraviolet RaysPopulation DynamicsRadiationFish larvaemedicine.disease_causeRisk AssessmentAnimal sciencemedicineAnimalsHSP70 Heat-Shock ProteinsWaste Management and DisposalEsoxWater Science and TechnologyCivil and Structural EngineeringPikecomputer.programming_languagebiologyBehavior AnimalEcologySuperoxide DismutaseEcological ModelingEnvironmental factorbiology.organism_classificationPollutionRadiation effectCuvetteLarvaEsocidaeEnvironmental scienceDose ratecomputerBiomarkersEnvironmental MonitoringWater research
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Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity?

2012

Abstract The cytoskeleton is a highly complex network of three major intracellular filaments, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs). This network plays a key role in the control of cell shape, division, functions and interactions in animal organs and tissues. Dysregulation of the network can contribute to numerous human diseases. Although small HSPs (sHSPs) and in particular HSP27 (HSPB1) or αB-crystallin (HSPB5) display a wide range of cellular properties, they are mostly known for their ability to protect cells under stress conditions. Mutations in some sHSPs have been found to affect their ability to interact with cytoskeleton proteins, leading to IF a…

Epithelial-Mesenchymal TransitionIntermediate FilamentsVimentinmacromolecular substancesMicrofilamentBiochemistry03 medical and health sciences0302 clinical medicineHsp27MicrotubuleStress PhysiologicalHeat shock proteinNeoplasmsAnimalsHumansCytoskeletonIntermediate filament030304 developmental biology0303 health sciencesbiologyGenetic Diseases InbornCell BiologyFibrosisCell biologyHeat-Shock Proteins SmallMutationbiology.proteinDesmin030217 neurology & neurosurgeryThe international journal of biochemistrycell biology
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Extracellular Hsp70 Enhances Mesoangioblast Migration via an Autocrine Signaling Pathway

2016

Mouse mesoangioblasts are vessel-associated progenitor stem cells endowed with the ability of multipotent mesoderm differentiation. Therefore, they represent a promising tool in the regeneration of injured tissues. Several studies have demonstrated that homing of mesoangioblasts into blood and injured tissues are mainly controlled by cytokines/chemokines and other inflammatory factors. However, little is known about the molecular mechanisms regulating their ability to traverse the extracellular matrix (ECM). Here, we demonstrate that membrane vesicles released by mesoangioblasts contain Hsp70, and that the released Hsp70 is able to interact by an autocrine mechanism with Toll-like receptor …

Extracellular VesicleNF-kappa BEndothelial CellsModels BiologicalHsp70Toll-Like Receptor 4Autocrine CommunicationMicePhosphatidylinositol 3-KinasesMembrane MicrodomainsMatrix Metalloproteinase 9NF-KappaB Inhibitor alphaCell MovementMesoangioblast Stem CellAnimalsMatrix Metalloproteinase 2HSP70 Heat-Shock ProteinsExtracellular SpaceMatrix MetalloproteinaseProto-Oncogene Proteins c-aktLow Density Lipoprotein Receptor-Related Protein-1MigrationProtein BindingSignal Transduction
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