Search results for "Heat-Shock Protein"

showing 10 items of 310 documents

Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5.

1995

Abstract In this study, we report the molecular cloning of a novel Drosophila melanogaster small heat-shock (HS)-homologous gene, l(2)efl, identified on the right arm of the second chromosome at locus 59F4,5. We describe the temporal expression of l(2)efl in the wild-type and present its structure. The deduced amino-acid sequence of the Efl protein shows significant homology to all known small HS proteins identified in Drosophila and vertebrates, and to mammalian α-crystallin.

Signal peptideTranscription GeneticMolecular Sequence DataRestriction MappingLocus (genetics)Genes InsectMolecular cloningHomology (biology)biology.animalSequence Homology Nucleic AcidGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerRelated geneCloning MolecularGeneHeat-Shock ProteinsIn Situ HybridizationGeneticsbiologyBase SequenceSequence Homology Amino AcidVertebrateGeneral MedicineSequence Analysis DNAbiology.organism_classificationDrosophila melanogasterInsect HormonesGenes LethalDrosophila melanogasterGene
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4,5,6,7-Tetrahydro-isoxazolo-[4,5-c]-pyridines as a new class of cytotoxic Hsp90 inhibitors.

2014

Hsp90 is considered an interesting therapeutic target for anticancer drug development. Here we describe a new class of 4,5,6,7-tetrahydro-isoxazolo-[4,5-c]-pyridine compounds. A small library of derivatives has been synthesized and investigated. Some reported compounds show interesting properties combining both notable binding to Hsp90 and potent cell growth inhibitory activity. N-5 substitution with a 2,4 resorcinol carboxamide appears crucial for activity. Moreover, a derivative bearing a hydroxamic acid residue bound to C-3 amide portion was found to inhibit both Hsp90 and HDAC6.

Spectrometry Mass Electrospray IonizationMagnetic Resonance Spectroscopymedicine.drug_classStereochemistryPyridinesCarboxamideApoptosisResorcinolAnti-cancer drugschemistry.chemical_compoundResidue (chemistry)AmideDrug DiscoveryHeat shock protein 90 Anti-cancer drugs 4567-Tetrahydro-isoxazolo-[45-c]- pyridinesmedicineCytotoxic T cellHumansHeat shock protein 90HSP90 Heat-Shock ProteinsPharmacologyHydroxamic acidChemistryCell growthOrganic ChemistryGeneral MedicineNuclear magnetic resonance spectroscopy4 5 6 7-Tetrahydro-isoxazolo-[4 5-c]-pyridinesFlow CytometrySettore CHIM/08 - Chimica Farmaceuticahsp90Settore BIO/14 - Farmacologia4 5 6 7-Tetrahydro-isoxazolo-[4 5-c]-pyridines; Anti-cancer drugs; Heat shock protein 90;K562 CellsCell DivisionEuropean journal of medicinal chemistry
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Phytochemical Profile and Apoptotic Activity of Onopordum cynarocephalum.

2012

A phytochemical investigation of acetone and chloroform extracts of the aerial parts of Onopordum cynarocephalum Boiss. et Blanche was carried out. It led to the isolation of two new sesquiterpenes, the elemane aldehyde (2) and the eudesmane (11), together with 15 known compounds: two lignans (1 and 15) and 13 sesquiterpenes (3–10, 12–14, 16, 17). The structures were elucidated by spectroscopic analyses, especially 1D and 2D NMR spectra. The anti-growth effect against three human melanoma cell lines, M14, A375, and A2058, of the different extracts and compounds of O. cynarocephalum was also investigated. Among them, the chloroform extract exhibited the strongest biological activity, while t…

StereochemistryPharmaceutical ScienceApoptosisDNA FragmentationLignansAnalytical Chemistrychemistry.chemical_compoundInhibitory Concentration 50cytotoxic activity Onopordum cynarocephalum Boiss. et BlancheCell Line TumorDrug DiscoveryHumansSesquiterpenes EudesmaneHSP70 Heat-Shock ProteinsFuransArctigeninCell ProliferationPharmacologyLignanChloroformPlants MedicinalbiologyDose-Response Relationship DrugMolecular StructureCaspase 3Plant ExtractsOrganic ChemistryOnopordumPTEN PhosphohydrolaseBiological activityPlant Components AerialAntineoplastic Agents PhytogenicEnzyme assayMonocyclic SesquiterpenesComplementary and alternative medicinePhytochemicalchemistryApoptosisbiology.proteinMolecular MedicineDNA fragmentationSesquiterpenes
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Intratumoral Heterogeneity for hsp90β mRNA Levels in a Breast Cancer Cell Line

1997

BC-3A and BC-61 are two breast cancer cell lines that have been cloned from parental 8701-BC cells and exhibit different biosynthetic, proliferative, and invasive properties in vitro. In the attempt to search whether alterations in the profiles of gene expression could be detected, we have submitted both cytotypes to identification of differentially expressed cDNAs. In addition, steroid hormone receptor mRNA arrays and in vivo tumorigenesis of the two lines have been checked. The technique used allowed identification of changes in the expression of the 90-kD heat shock protein-beta (hsp90beta) which is prominently down-regulated in BC-61 cells. Because we have also found that these cells, w…

Steroid hormone receptorMice NudeEstrogen receptorBreast NeoplasmsBiologymedicine.disease_causeMiceBreast cancerIn vivoHeat shock proteinGene expressionTumor Cells CulturedGeneticsmedicineAnimalsHumansHSP90 Heat-Shock ProteinsRNA MessengerRNA NeoplasmMolecular BiologyDNA NeoplasmCell BiologyGeneral Medicinemedicine.diseaseMolecular biologyIn vitroGene Expression Regulation NeoplasticReceptors EstrogenReceptors ProgesteroneCarcinogenesisDNA and Cell Biology
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Different Efficiency of Heat Shock Proteins (HSP) to Activate Human Monocytes and Dendritic Cells: Superiority of HSP60

2002

Abstract One essential immunoregulatory function of heat shock protein (HSP) is activation of the innate immune system. We investigated the activation of human monocytes and monocyte-derived dendritic cells (DC) by recombinant human HSP60, human inducible HSP72, and preparations of human gp96 and HSP70 under stringent conditions, in the absence of serum and with highly purified monocytes. HSP60 induced human DC maturation and activated human DC to secrete proinflammatory cytokines. HSP72 induced DC maturation to a lesser extent, but activated human monocytes and immature DC as efficiently as HSP60 to release proinflammatory cytokines. The independence of the effects of HSP60 and HSP72 from …

T-Lymphocytesmedicine.medical_treatmentImmunologyHSP72 Heat-Shock ProteinsPeptide bindingBiologyLymphocyte ActivationMonocytesProinflammatory cytokineAntigens NeoplasmHeat shock proteinmedicineHumansImmunology and AllergyHSP70 Heat-Shock ProteinsSecretionHeat-Shock ProteinsInnate immune systemCell DifferentiationChaperonin 60Dendritic CellsMolecular biologyCoculture TechniquesRecombinant ProteinsHsp70CytokineCytokinesHSP60Inflammation MediatorsSignal TransductionThe Journal of Immunology
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Discovery and validation of small-molecule heat-shock protein 90 inhibitors through multimodality molecular imaging in living subjects.

2012

Up-regulation of the folding machinery of the heat-shock protein 90 (Hsp90) chaperone protein is crucial for cancer progression. The two Hsp90 isoforms (α and β) play different roles in response to chemotherapy. To identify isoform-selective inhibitors of Hsp90(α/β)/cochaperone p23 interactions, we developed a dual-luciferase (Renilla and Firefly) reporter system for high-throughput screening (HTS) and monitoring the efficacy of Hsp90 inhibitors in cell culture and live mice. HTS of a 30,176 small-molecule chemical library in cell culture identified a compound, N -(5-methylisoxazol-3-yl)-2-[4-(thiophen-2-yl)-6-(trifluoromethyl)pyrimidin-2-ylthio]acetamide (CP9), that binds to Hsp90(α/β) an…

Thymidine kinase activityProtein FoldingImmunoprecipitationLactams MacrocyclicBlotting WesternMice NudeThiophenesBiologyThioacetamideTritiumSmall Molecule LibrariesMiceco-chaperone p23Luciferases FireflyHeat shock proteinCell Line TumorNeoplasmsAcetamidesDrug DiscoveryBenzoquinonesAnimalsHumansImmunoprecipitationProtein IsoformsLuciferaseHSP90 Heat-Shock ProteinsLuciferases RenillaProstaglandin-E SynthasesMultidisciplinaryCell growthImidazolesbioluminescence imagingHsp90Small moleculeMolecular biologydrug developmentHigh-Throughput Screening Assayssmall-molecule inhibitorsIntramolecular OxidoreductasesLeadPNAS PlusCell culturePositron-Emission TomographyPyrazinesbiology.proteinPET/computed tomography imagingTomography X-Ray ComputedProceedings of the National Academy of Sciences of the United States of America
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Constitutive hsp70 is essential to mitosis during early cleavage of Paracentrotus lividus embryos: The blockage of constitutive hsp70 impairs mitosis

1999

Localization of constitutive hsp70 in eggs and early embryos of sea urchin Paracentrotus lividus is shown by means of in situ immunostaining. An accumulation of this protein is shown in the mitotic structures (asters, spindles and centrosomes). Microinjection of anti-hsp70 antibodies into eggs causes impairment of formation of mitotic structures and of cell division. This impairment goes from a complete mitotic block, to irregular mitotic apparatus formation with irregular cleavage, depending upon the antibody concentration. The localization of hsp70 after antibody microinjection is also described. Blockage of mitotic apparatus formation by nocodazole also blocks the concentration of hsp70 …

Time FactorsGrowth InhibitorMicroinjectionsCell divisionTime FactorSea UrchinCleavage Stage OvumBiophysicsMitosisCleavage (embryo)BiochemistryParacentrotus lividuschemistry.chemical_compoundbiology.animalAnimalsHSP70 Heat-Shock ProteinsSea urchin embryoMitosisMicroinjectionSea urchinMolecular BiologyConstitutive hsp70HSP70 Heat-Shock ProteinbiologyDose-Response Relationship DrugAnimalNocodazoleCell Biologybiology.organism_classificationMitosiGrowth InhibitorsMicroinjectionCell biologyNocodazolechemistryBiophysicCentrosomeSea UrchinsFertilizationembryonic structures
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Coelomocytes and post-traumatic response in the common sea star Asterias rubens.

2008

Coelomocytes are recognized as the main cellular component of the echinoderm immune system. They are the first line of defense and their number and type can vary dramatically during infections or following injury. Sea stars have been used as a model system to study the regeneration process after autotomy or predation. In the present study we examined the cellular and biochemical responses of coelomocytes from the European sea star Asterias rubens to traumatic stress using immunochemical and biochemical approaches. In terms of trauma and post-traumatic stress period, here we consider the experimental arm amputation and the repair phase involved in the first 24 hours post-amputation, which mi…

Time FactorsImmunocytochemistryPopulationCell CountBiochemistryAndrologymedicineAnimalsHSP70 Heat-Shock ProteinsPseudopodiaeducationGlycoproteinseducation.field_of_studyPhagocytesbiologyAsteriasAntibodies MonoclonalCell BiologyOriginal Articlesbiology.organism_classificationStrongylocentrotus purpuratusCoelomic epitheliummedicine.anatomical_structureEchinodermAsteriasImmunologyCoelomAutotomyCell stresschaperones
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Adaptive response of osteoblasts grown on a titanium surface: morphology, cell proliferation and stress protein synthesis.

2005

Titanium is one of the most widely used biomaterials in orthopaedic, dental and trauma surgery. Superficial adhesion and cell proliferation represent the first steps of cell-biomaterial interactions. The efficacy of this early phase influences the subsequent ability to differentiate, and hence the knowledge of these cell activities is important for studying and improving the biocompatibility of biomaterials. The aim of this study was to test the adaptive ability of osteoblastic cells grown on titanium surfaces, including morphologic, proliferative and adaptative aspects.

Titaniumcell proliferation HSP70 morphology SaoS-2 titaniummedicine.medical_specialtyOsteoblastsGeneral VeterinaryAnimal healthbusiness.industryCell SurvivalCell CountGeneral MedicineCell Growth ProcessesCell biologyCell LineFamily medicineHuman anatomymedicineMicroscopy Electron ScanningAnimalsHSP70 Heat-Shock ProteinsbusinessA titaniumVeterinary research communications
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The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon

1995

Transcriptional studies have demonstrated that the dnaK gene of Streptomyces coelicolor A3(2) is contained within a 4.3 kb operon. The operon is transcribed from a single (transiently) heat-inducible promoter, dnaKp, that resembles the typical vegetative (sigma 70-recognized) eubacterial consensus promoter sequence. dnaK transcription was found to be heat-inducible at all stages of development in surface-grown cultures. In addition, at the normal growth temperature of 30 degrees C, dnaK transcript levels were shown to vary at different stages of development, being more abundant in young germinating cultures and in mycelium undergoing sporogenesis. The nucleotide sequence of the dnaK operon …

Transcription GeneticOperonMolecular Sequence Datalac operonRepressorMicrobiologytrp operonOpen Reading FramesOperonEscherichia coligal operonHSP70 Heat-Shock ProteinsAmino Acid SequencePromoter Regions GeneticMolecular BiologyHeat-Shock ProteinsGeneticsBinding SitesBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsStreptomyces coelicolorCell DifferentiationPromoterGene Expression Regulation BacterialBlotting Northernbiology.organism_classificationMolecular biologyRecombinant ProteinsStreptomycesGenes BacterialbacteriaL-arabinose operonHeat-Shock ResponseProtein BindingMolecular Microbiology
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