Search results for "heat shock"

showing 10 items of 303 documents

Cloning of sponge heat shock proteins: evolutionary relationships between the major kingdoms

2009

In the present study we have cloned from sponges (Porifera) those molecules which are involved in the protection of organisms against physiological and stress conditions; the inducible heat shock protein Mr 70,000, hsp70, from the marine sponge Geodia cydonium, its interacting hsp40, a DnaJ-like protein (from G. cydonium) and the constitutively expressed counterpart the glucose-regulated protein Mr 78,000, GRP78 from Suberites domuncula. Alignments of the sequences revealed that the deduced aa sequences of all sponge hsp's share high homology to other metazoan sequences, and are separated from related sequences from plants and fungi (hsp70, GRP78, DnaJ) as well as Bacteria (DnaK, the hsp70 …

CloningGeneticsPhylogenetic treeBiologybiology.organism_classificationMicrobiologySuberites domunculaPhylogeneticsHeat shock proteinGenBankGeneticsAnimal Science and ZoologyMolecular BiologyGeneEcology Evolution Behavior and SystematicsArchaeaJournal of Zoological Systematics and Evolutionary Research
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Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 an…

2003

Nuclear domains called ND10 or PML bodies might function as nuclear depots by recruiting or releasing certain proteins. Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences. Exposure to sublethal environmental stress revealed a sequential release of ND10-associated proteins. Upon heat shock Daxx and Sp100 were released but PML remained, whereas exposure to subtoxic concentrations of CdCl2 induced the release of ND10-associated proteins, including PML, with Sp100 remaining in a few sites. In both cases,recovery times were simil…

Co-Repressor ProteinsMAP Kinase Signaling SystemMacromolecular SubstancesSUMO-1 ProteinPromyelocytic Leukemia ProteinMicePromyelocytic leukemia proteinDeath-associated protein 6Stress PhysiologicalHeat shock proteinEndopeptidasesAnimalsHSP70 Heat-Shock ProteinsEnzyme InhibitorsHeat shockTranscription factorCells CulturedHeat-Shock ProteinsbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsCell BiologyCell Nucleus StructuresNeoplasm ProteinsCell biologyHsp70Cysteine EndopeptidasesEukaryotic CellsGene Expression RegulationImmunologybiology.proteinSignal transductionCarrier ProteinsCo-Repressor ProteinsHeat-Shock ResponseCadmiumMolecular ChaperonesTranscription FactorsJournal of Cell Science
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Identifying conserved genes involved in crop tolerance to cold stress

2022

Low temperature is a limiting factor for crop productivity in tropical and subtropical climates. Cold stress response in plants involves perceiving and relaying the signal through a transcriptional cascade composed of different transduction components, resulting in altered gene activity. We performed a meta-analysis of four previously published datasets of cold-tolerant and cold-sensitive crops to better understand the gene regulatory networks and identify key genes involved in cold stress tolerance conserved across phylogenetically distant species. Re-analysing the raw data with the same bioinformatics pipeline, we identified common cold tolerance-related genes. We found 236 and 242 common…

Cold-Shock Responseheat shock proteinPlant Sciencedifferentially expressed genemeta-analysiDroughtsabiotic streCold TemperatureSettore AGR/03 - Arboricoltura Generale E Coltivazioni ArboreePlant BreedingtranscriptomicsGene Expression Regulation Plantchilling and freezing stresseSettore AGR/07 - Genetica AgrariacropRNA-seqAgronomy and Crop Science
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Hsp60 Inhibitors and Modulators

2019

In this chapter, we focus on the 60 KDa Heat Shock Protein (Hsp60) and discuss some of its biological, molecular and pathological features. The structural and mechanistic aspect of the Hsp60 folding cycle will be also presented. We further illustrate how Hsp60 may be involved in many diseases and therefore considered as an effective therapeutic or theranostic target. Finally, the state-of-the-art on the development of Hsp60 and bacterial GroEL inhibitors and modulators of their expression will be illustrated. This is discussed in the light of a negative chaperonotherapy, and the consequent development of inhibitors, as well as positive chaperonotherapy, in the event its excessive activity i…

Cpn60Excessive activityHsp60 inhibitoranimal structuresHeat shock proteinChemistryPyrazolopyrimidinefungiAvrainvillamidechemical and pharmacologic phenomenaComputational biologyMizoribineSettore CHIM/06 - Chimica OrganicaCarboranylphenoxyacetanilideHsp60complex mixturesGroELGroELHspD1Heat shock proteinHSP60AvrainvillamideEpolactaene
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Deciliation: A stressful event for Paracentrotus lividus embryos.

1998

In this report, by using mono- and two-dimensional electrophoretic analysis, we demonstrate that deciliation on sea urchin embryos induces a stress response. Deciliation indeed causes not only the activation of ciliary subroutine, but also a transient decrease of bulk protein synthesis. This decrease is in agreement with our previous results on heat shock response in sea urchin, although deciliation does not induce the expression of the same main hsp set. We were able to characterize one main deciliation-stress protein of 40 kDa whose expression is transiently induced by deciliation and whose localisation is likely to be nuclear.

CytoplasmEmbryo NonmammalianBiophysicsBiochemistryParacentrotus lividusFight-or-flight responseMethionineStress Physiologicalbiology.animalProtein biosynthesisAnimalsRegenerationElectrophoresis Gel Two-DimensionalCiliaHeat shockMolecular BiologySea urchinCell NucleusSaline Solution HypertonicbiologyProteinsEmbryoCell BiologyGastrulaSea urchin embryobiology.organism_classificationMolecular biologyCell biologyProtein BiosynthesisSea UrchinsElectrophoresis Polyacrylamide GelBiochemical and biophysical research communications
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(DIS)Assembly and Structural Stability of mtHsp60 and its Precursor NaÏve Form

2015

Heat shock protein 60kDa is a molecular chaperone (GroEL human homolog) that assists protein folding in mitochondria (mtHsp60). It is synthesized in the cell cytoplasm as a higher molecular weight precursor form (p-mtHsp60) containing a N-terminal targeting sequence, that is cleaved after import into the mitochondrial matrix [1, 2].It has been established, and demonstrated by various techniques, Hsp60 can accumulate in the cytosol, in various pathological conditions (i.e., cancer and chronic inflammatory diseases). The cytosolical Hsp60 accumulation mechanism may occur with or without mitochondrial release concomitantly, so that in the cytosol the two types of 60 kDa chaperonin proteins, (m…

CytosolBiochemistryCytoplasmHeat shock proteinBiophysicsHSP60Protein foldingIsothermal titration calorimetryBiologyGroELProtein secondary structureBiophysical Journal
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Heat shock protein-antigen fusions lose their enhanced immunostimulatory capacity after endotoxin depletion.

2008

Heat shock proteins (HSPs) induce cross-presentation of antigens by dendritic cells (DC) as well as DC maturation. These properties make HSP antigen complexes good candidates to prime CD8 T cell responses against tumor-associated antigens. In this study, we analyzed four different members of the HSP70 family fused to a fragment of ovalbumin (OVA) as a model tumor antigen. E. coli-derived recombinant HSP70-OVA fusion proteins efficiently primed antigen-specific cytotoxic T cells in short-term in vivo immunization assays. Because of concerns that the adjuvant effect of HSPs may be due to endotoxin contamination, we studied this issue in detail. Induction of OVA-specific cytotoxicity was signi…

Cytotoxicity ImmunologicCpG OligodeoxynucleotideOvalbuminRecombinant Fusion ProteinsImmunologyReceptors Antigen T-CellMice TransgenicBiologyCD8-Positive T-LymphocytesLymphocyte ActivationMiceImmune systemCross-PrimingAntigenAdjuvants ImmunologicHeat shock proteinNeoplasmsCytotoxic T cellAnimalsHSP70 Heat-Shock ProteinsAntigensMolecular BiologyTLR9Dendritic CellsMolecular biologyFusion proteinTumor antigenEndotoxinsMice Inbred C57BLOligodeoxyribonucleotidesT-Lymphocytes CytotoxicMolecular immunology
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Correlation between the level of the potential biomarker, heat-shock protein, and the occurrence of DNA damage in the dab, Limanda limanda: a field s…

2000

In the present study, heat-shock protein of M-r 70 kDa (HSP70), a marker of cellular stress response, was validated as a potential biomarker under field conditions. The dab, Limanda limanda (female, size greater than or equal to 25 cm, spawning maturity stage 2) was used as the indicator organism. The data on HSP level were correlated with the occurrence of DNA damage, measured in the same specimens of L. limanda, to prove the usefulness of the method. The area under investigation was the North Sea. Four locations were selected: station N01, close to Heligoland, in the North Sea; station N04 at the Dogger Bank; station N06 at the Firth of Forth; and station G08 in the English Channel. Ten a…

DNA damageZoologyEnvironmental pollutionMarine BiologyFlounderAquatic ScienceBiologyOceanographymedicine.disease_causeHeat shock proteinGermanymedicineAnimalsLimandaHSP70 Heat-Shock ProteinsNorth seaEnvironmental factordab;Limanda limanda;biomarker;heat-shock protein;DNA damage;North seaGeneral Medicinebiology.organism_classificationPollutionEnglandLiverPotential biomarkersFemaleBioindicatorBiomarkersDNA DamageEnvironmental MonitoringMarine environmental research
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Developmental control of the heat-shock stress regulon in Streptomyces coelicolor

1995

In the differentiating eubacterium Streptomyces coelicolor, nutritional imbalances activate a developmental programme which involves the heat-shock stress regulon. In liquid batch cultures, the growth curve could be separated into four components: rapid growth 1 (RG1), transition (T), rapid growth 2 (RG2) and stationary (S). Patterns of gene expression in cultures subjected to heat shock in various phases were recorded on two-dimensional gels and analysed using advanced statistical methods. The responses of all heat-shock proteins (HSPs) were highly dependent upon the growth phase, thus demonstrating that the four phases of growth were physiologically distinct. For many HSPs, the levels of …

DNA BacterialGrowth phaseBlotting WesternRegulonMicrobiologyMicrobiologyBacterial ProteinsHeat shock stressGene expressionElectrophoresis Gel Two-DimensionalEubacteriumIsoelectric PointMolecular BiologyGenebiologyStreptomyces coelicolorCell DifferentiationGene Expression Regulation BacterialGrowth curve (biology)Reference Standardsbiology.organism_classificationStreptomycesCell biologyMolecular WeightRegulonHeat-Shock ResponseMolecular Microbiology
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The Chaperone Activity of Clusterin is Dependent on Glycosylation and Redox Environment

2014

Background/Aims: Clusterin (CLU), also known as Apolipoprotein J (ApoJ) is a highly glycosylated extracellular chaperone. In humans it is expressed from a broad spectrum of tissues and related to a plethora of physiological and pathophysiological processes, such as Alzheimer's disease, atherosclerosis and cancer. In its dominant form it is expressed as a secretory protein (secreted CLU, sCLU). During its maturation, the sCLU-precursor is N-glycosylated and cleaved into an α- and a β-chain, which are connected by five symmetrical disulfide bonds. Recently, it has been demonstrated that besides the predominant sCLU, rare intracellular CLU forms are expressed in stressed cells. Since these for…

DNA ComplementaryGlycosylationGlycosylationPhysiologyMutantCarbohydrateslcsh:Physiologylcsh:Biochemistrychemistry.chemical_compoundChaperonesHumanslcsh:QD415-436Redox biologySecretory pathwaylcsh:QP1-981ClusterinbiologyRetro-translocationProprotein convertaseProteostasis networkOxidative StressClusterinSecretory proteinHeat shockchemistryBiochemistryApolipoprotein JChaperone (protein)Proteolysisbiology.proteinOxidation-ReductionIntracellularMolecular ChaperonesFurin-like proprotein convertasesCellular Physiology and Biochemistry
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