Search results for " heat-shock proteins"

showing 10 items of 186 documents

Principal component analysis on molecular descriptors as an alternative point of view in the search of new Hsp90 inhibitors

2009

Inhibiting a protein that regulates multiple signal transduction pathways in cancer cells is an attractive goal for cancer therapy. Heat shock protein 90 (Hsp90) is one of the most promising molecular targets for such an approach. In fact, Hsp90 is a ubiquitous molecular chaperone protein that is involved in folding, activating and assembling of many key mediators of signal transduction, cellular growth, differentiation, stress-response and apoptothic pathways. With the aim to analyze which molecular descriptors have the higher importance in the binding interactions of these classes, we first performed molecular docking experiments on the 187 Hsp90 inhibitors included in the BindingDB, a pu…

Databases FactualProtein ConformationDrug Evaluation PreclinicalCancer therapyPrincipal component analysiNaphtholsBiochemistryBinding databaseMolecular descriptorsStructure-Activity RelationshipStructural BiologyMolecular descriptorHeat shock proteinComputer SimulationHSP90 Heat-Shock ProteinsPrincipal Component AnalysisBinding SitesbiologyHeat shock proteinOrganic ChemistryComputational BiologyIsoxazolesHsp90Settore CHIM/08 - Chimica FarmaceuticaComputational MathematicsBiochemistryPurinesDocking (molecular)Principal component analysisMolecular dockingbiology.proteinPyrazolesBindingDBSignal transduction
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Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis

2013

In this work we analysed, by immunohistochemistry, a series of brain tumors to detect the levels and cellular distribution of Hsp60 and Hsp70. We found that Hsp60 levels were significantly higher than those of Hsp70 in neuroepithelial tumors, while levels of both molecules were not significantly different from each other in meningeal neoplasms. In particular, Hsp60 immunopositivity was present mainly at the cytoplasmic level, while Hsp70 immunopositivity was found both in the cytoplasm and in the nucleus of tumor cells. The levels of these molecules in healthy control cells were always very low. Finally, Hsp60 and Hsp70 levels did not correlate with the different types (WHO grade) of neopla…

AdultMalePathologymedicine.medical_specialtyanimal structuresHistologyAdolescentNeuroepithelial CellsBiophysicschemical and pharmacologic phenomenaBiologymedulloblastomamedicine.disease_causemeningiomacomplex mixturesHsp60 Hsp70 astrocytoma glioblastoma multiformae medulloblastoma meningiomaHsp70Meningeal NeoplasmsmedicineHumansHSP70 Heat-Shock ProteinsMeningeal NeoplasmChildastrocytomalcsh:QH301-705.5AgedAged 80 and overMedulloblastomaHsp60 Hsp70 astrocytoma glioblastoma multiformae medulloblastoma meningioma.Brain NeoplasmsBrief ReportfungiAstrocytomaChaperonin 60Cell BiologyMiddle AgedHsp60medicine.diseaseImmunohistochemistryNeoplasms NeuroepithelialNeuroepithelial cellglioblastoma multiformaelcsh:Biology (General)Tumor progressionChild PreschoolCancer cellImmunohistochemistryFemaleCarcinogenesisEuropean Journal of Histochemistry
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HSP90 and eNOS partially co-localize and change cellular localization in relation to different ECM components in 2D and 3D cultures of adult rat card…

2007

Background information. Cultivation techniques promoting three-dimensional organization of mammalian cells are of increasing interest, since they confer key functionalities of the native ECM (extracellular matrix) with a power for regenerative medicine applications. Since ECM compliance influences a number of cell functions, Matrigel-based gels have become attractive tools, because of the ease with which their mechanical properties can be controlled. In the present study, we took advantage of the chemical and mechanical tunability of commonly used cell culture substrates, and co-cultures to evaluate, on both two- and three-dimensional cultivated adult rat cardiomyocytes, the impact of ECM c…

Nitric Oxide Synthase Type IIICell Culture TechniquesFluorescent Antibody TechniqueBiocompatible Materialslaw.inventionExtracellular matrixMicroscopy Electron TransmissionLamininConfocal microscopylawEnosAnimalsMyocytes CardiacHSP90 Heat-Shock ProteinsCellular localizationCells CulturedMatrigelMicroscopy ConfocalbiologyCell BiologyGeneral MedicineFibroblastsbiology.organism_classificationCoculture TechniquesCell biologyExtracellular MatrixFibronectinsRatsFibronectinDrug CombinationsProtein TransportCell culturebiology.proteinhsp90 ENOSProteoglycansCollagenLamininBiology of the cell
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Targeting heat shock proteins in cancer

2010

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are powerful chaperones. Their expression is induced in response to a wide variety of physiological and environmental insults including anti-cancer chemotherapy, thus allowing the cell to survive to lethal conditions. Different functions of HSPs have been described to account for their cytoprotective function, including their role as molecular chaperones as they play a central role in the correct folding of misfolded proteins, but also their anti-apoptotic properties. HSPs are often overexpressed in cancer cells and this constitutive expression is necessary for cancer cells' survival. HSPs may have oncogene-like functions and likewise mediat…

Protein Foldingendocrine systemCancer ResearchCell SurvivalProtein ConformationCellAntineoplastic AgentsApoptosisBreast NeoplasmsHsp27NeoplasmsHeat shock proteinmedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHeat-Shock ProteinsCell ProliferationbiologyCell growthCancermedicine.diseaseHsp90Hsp70Cell biologymedicine.anatomical_structureOncologyDrug Resistance NeoplasmCancer cellbiology.proteinMolecular ChaperonesCancer Letters
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Cloning and sequencing of the dnaK region of Streptomyces coelicolor A3(2)

1993

Abstract The dnaK homologue of Streptomyces coelicolor A3(2) strain M145 has been cloned and sequenced. Nucleotide sequence analysis of a 2.5-kb region revealed an open reading frame (ORF) encoding a predicted DnaK protein of 618 amino acids (Mr = 66 274). The dnaK coding sequence displays extreme codon bias and shows a strong preference for CGY and GGY, for Arg and Gly codons, respectively. The predicted DnaK sequence has a high Lys:Arg ratio which is not typical of streptomycete proteins. The region immediately downstream from dnaK contains an ORF for a GrpE-like protein; the predicted start codon of grpE overlaps the last two codons of dnaK, indicating that the two genes are translationa…

DNA BacterialMolecular Sequence Datagenetic processesBacterial ProteinsStart codonGeneticsCoding regionHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularCodonGeneHeat-Shock Proteinschemistry.chemical_classificationGeneticsBase SequencebiologyEscherichia coli ProteinsStreptomyces coelicolorNucleic acid sequenceStreptococcusGeneral Medicinebiology.organism_classificationAmino acidOpen reading framechemistryGenes BacterialProtein BiosynthesisCodon usage biasbiological sciencesbacteriaSequence AlignmentGene
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Induction of Hsp70 by the Herbicide Oxyfluorfen (Goal) in the Egyptian Nile Fish, Oreochromis niloticus

1999

This paper deals with the expression of the biomarker hsp70 in the liver and kidney of the freshwater fish Oreochromis niloticus following exposure to the herbicide oxyfluorfen (Goal). Fishes were exposed to three concentrations, the 96-h LC50 (3 mg/L), the 96-h (1/2)LC50 (1.5 mg/L), and the 96-h (1/4)LC50 (0.75 mg/L) of oxyfluorfen for 6, 15, and 24 days, respectively, and samples were taken at three different time periods for each concentration. The livers responded to the herbicide by an induction of the expression of both the constitutive (hsp75; Mr 75 kDa) and the inducible (hsp73; Mr 73 kDa) hsp70 proteins. In kidney, the herbicide induced a time-dependent increase in the expression o…

food.ingredientHealth Toxicology and MutagenesisBiologyKidneyToxicologyAnimal sciencefoodHalogenated Diphenyl EthersAnimalsEcotoxicologyHSP70 Heat-Shock ProteinsIncubationEcologyPhenyl EthersTilapiaGeneral MedicinePesticidebiology.organism_classificationPollutionHsp70OreochromisLiverToxicityFreshwater fishEgyptElectrophoresis Polyacrylamide GelTilapiaArchives of Environmental Contamination and Toxicology
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Assessment of Targeted Next-Generation Sequencing as a Tool for the Diagnosis of Charcot-Marie-Tooth Disease and Hereditary Motor Neuropathy

2016

Charcot-Marie-Tooth disease is characterized by broad genetic heterogeneity with >50 known disease-associated genes. Mutations in some of these genes can cause a pure motor form of hereditary motor neuropathy, the genetics of which are poorly characterized. We designed a panel comprising 56 genes associated with Charcot-Marie-Tooth disease/hereditary motor neuropathy. We validated this diagnostic tool by first testing 11 patients with pathological mutations. A cohort of 33 affected subjects was selected for this study. The DNAJB2 c.352+1G>A mutation was detected in two cases; novel changes and/or variants with low frequency (50 known disease-associated genes. Mutations in some of these gene…

0301 basic medicineMaleDiseaseBioinformaticsDNA sequencingPathology and Forensic Medicine03 medical and health sciences0302 clinical medicineCharcot-Marie-Tooth DiseaseMedicineHumansGeneGeneticsbusiness.industryGenetic heterogeneityHaplotypeCase-control studyHigh-Throughput Nucleotide SequencingReproducibility of ResultsHSP40 Heat-Shock Proteins030104 developmental biologyHaplotypesCase-Control StudiesMutation (genetic algorithm)MutationMolecular MedicineFemalebusinessHereditary Sensory and Motor Neuropathy030217 neurology & neurosurgeryFounder effectMolecular Chaperones
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Correction: Oncogenic extracellular HSP70 disrupts the gap-junctional coupling between capillary cells

2021

High levels of circulating heat shock protein 70 (HSP70) are detected in many cancers. In order to explore the effects of extracellular HSP70 on human microvascular endothelial cells (HMEC), we initially used gap-FRAP technique. Extracellular human HSP70 (rhHSP70), but not rhHSP27, blocks the gap-junction intercellular communication (GJIC) between HMEC, disrupts the structural integrity of HMEC junction plaques, and decreases connexin43 (Cx43) expression, which correlates with the phosphorylation of Cx43 serine residues. Further exploration of these effects identified a rapid transactivation of the Epidermal Growth Factor Receptor in a Toll-Like Receptor 4-dependent manner, preceding its in…

Junctional couplingChemistryCapillary actionCorrectionEndothelial CellsGap JunctionsCell CommunicationRecombinant ProteinsHsp70OncologyConnexin 43BiophysicsExtracellularHumansHSP70 Heat-Shock ProteinsPhosphorylationOncotarget
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In vitro effect of cadmium and copper on separated blood leukocytes of Dicentrarchus labrax.

2013

The immunotoxic effects of heavy metals on blood leukocytes of sea bass (Dicentrarchus labrax) were examined. The cells, separated by a discontinuous Percoll-gradients, were exposed in vitro to various sublethal concentrations of cadmium and copper (10(-7) M, 10(-5) M, and 10(-3) M) and their immunotoxic effect was then evaluated by measuring neutral red uptake, MU assay, DNA fragmentation and Hsp70 gene expression. First of all, we demonstrated that the cells treated in vitro could incorporate Cd and Cu. A relationship between heavy metal exposure and dose-time-dependent alterations in responses of leukocytes from blood was found for both metals, but copper was more immunotoxic than cadmiu…

MTTNeutral redMembrane permeabilityHealth Toxicology and MutagenesisSettore BIO/05 - Zoologiachemistry.chemical_elementNRchemistry.chemical_compoundReal-time-PCRLeukocytesAnimalsMTT assayHSP70 Heat-Shock ProteinsCytotoxicityCadmiumHeavy metal; Leukocytes; NR; MTT; Hsp70 gene; Real-time-PCRbiologyPublic Health Environmental and Occupational HealthGeneral MedicineLeukocytebiology.organism_classificationPollutionMolecular biologyIn vitroHeavy metalchemistryGene Expression RegulationNeutral RedImmunologyHsp70 geneDNA fragmentationDicentrarchusBassCopperWater Pollutants ChemicalCadmium
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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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