Search results for " heat-shock proteins"

showing 10 items of 186 documents

Heat shock protein-27 protects human bronchial epithelial cells against oxidative stress-mediated apoptosis: possible implication in asthma.

2002

Inflammation of the human bronchial epithelium, as observed in asthmatics, is characterized by the selective death of the columnar epithelial cells, which desquamate from the basal cells. Tissue repair initiates from basal cells that resist inflammation. Here, we have evaluated the extent of apoptosis as well as the Hsp27 level of expression in epithelial cells from bronchial biopsy samples taken from normal and asthmatic subjects. Hsp27 is a chaperone whose expression protects against oxidative stress. We report that in asthmatic subjects the basal epithelium cells express a high level of Hsp27 but no apoptotic morphology. In contrast, apoptotic columnar cells are devoid of Hsp27 expressio…

Adultendocrine systemanimal structuresHSP27 Heat-Shock ProteinsInflammationApoptosisBronchiColumnar CellRespiratory MucosaBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicHsp27Heat shock proteinmedicineBronchial BiopsyHumansHeat-Shock ProteinsEpithelial CellsCell BiologyHydrogen PeroxideOriginal ArticlesMiddle AgedOxidantsEpitheliumAsthmaCell biologyNeoplasm ProteinsOxidative Stressmedicine.anatomical_structureApoptosisImmunologybiology.proteinmedicine.symptomOxidative stressMolecular ChaperonesCell stresschaperones
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Aldehyde dehydrogenase and HSP90 co-localize in human glioblastoma biopsy cells.

2013

The concept of a stem cell subpopulation as understood from normal epithelial tissue or bone marrow function has been extended to our understanding of cancer tissue and is now the target of treatment efforts specifically directed to this subpopulation. In glioblastoma, as well as in other cancers, increased expression of aldehyde dehydrogenase (ALDH) has been found localized within a minority sub-population of tumor cells which demonstrate stem cell properties. A separate body of research associated increased expression of heat-shock protein-90 (HSP90) with stem cell attributes. We present here results from our initial immunohistochemistry study of human glioblastoma biopsy tissue where bot…

Aldehyde dehydrogenasePharmacologyBiochemistryAldehyde dehydrogenase; Disulfiram; Glioblastoma; HSP90; Ritonavir; Stem cell; TemozolomideCancer stem cellBiopsyDisulfirammedicineTemozolomideHSP90HumansHSP90 Heat-Shock ProteinsTemozolomideRitonavirStem cellmedicine.diagnostic_testbiologyCancerGeneral MedicineAldehyde Dehydrogenasemedicine.diseaseGene Expression Regulation NeoplasticProtein Transportmedicine.anatomical_structurebiology.proteinCancer researchImmunohistochemistryBone marrowStem cellGlioblastomamedicine.drugBiochimie
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Stabilization of hsp70 mRNA on prolonged cell exposure to hypertonicity

2002

AbstractProlonged exposure of 3T3 cells to 0.5 osM hypertonic medium induced the accumulation of hsp70 mRNAs. This increase in mRNA levels required active protein synthesis. A weak and transient activation of heat shock factor 1 (HSF1) was noted, but it was temporally uncoupled to the accumulation of the hsp70 mRNAs. Nuclear run-on assay and transfection experiments showed that hsp70 gene transcription was not affected by hypertonicity. ActD chase experiments showed that during hypertonic treatment, degradation of hsp70 mRNAs was markedly reduced. This effect did not appear to be a general phenomenon since the increase in mRNA level of another gene induced by hypertonicity (ATA2 transporter…

Amino Acid Transport System ATranscription GeneticBiologyTransfectionMiceHeat Shock Transcription FactorsTranscription (biology)Heat shock proteinATA2 mRNAAnimalsHSP70 Heat-Shock ProteinsRNA MessengerHSF1HypertonicityMolecular BiologySaline Solution HypertonicMessenger RNAHeat shock proteinMRNA stabilizationTransfection3T3 CellsCell Biologyhsp70 mRNAMolecular biologyHsp70DNA-Binding ProteinsProtein BiosynthesisRNA stabilizationmRNA stabilizationTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Synthesis and biological activities of a new class of heat shock protein 90 inhibitors, designed by energy-based pharmacophore virtual screening

2013

The design through energy-based pharmacophore virtual screening has led to aminocyanopyridine derivatives as efficacious new inhibitors of Hsp90. The synthesized compounds showed a good affinity for the Hsp90 ATP binding site in the competitive binding assay. Moreover, they showed an excellent antiproliferative activity against a large number of human tumor cell lines. Further biological studies on the derivative with the higher EC50 confirmed its specific influence on the cellular pathways involving Hsp90.

AminopyridinesInhibitory Concentration 50Structure-Activity RelationshipUser-Computer InterfaceHeat shock proteinCell Line TumorSettore BIO/10 - BiochimicaDrug DiscoveryHumansHSP90 Heat-Shock ProteinsBinding siteVirtual screeningheat shock protein 90 inhibitors energy-based pharmacophore virtual screening cell cycle antiproliferative activitybiologyChemistryHsp90Combinatorial chemistrySettore CHIM/08 - Chimica FarmaceuticaHuman tumorMolecular Docking SimulationCell cultureDrug DesignEnergy basedbiology.proteinMolecular MedicinePharmacophoreDrug Screening Assays Antitumor
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Physiological and agonistic behavioural response of Procambarus clarkii to an acoustic stimulus

2012

Summary This study examined the effects of an acoustic stimulus on the haemolymph and agonistic behaviour of the red swamp crayfish Procambarus clarkii. The experiment was conducted in a tank equipped with a video recording system using 6 groups (3 control and 3 test groups) of five adult crayfish (30 specimens in total). After one hour of habituation, the behaviour of the crayfish was monitored for two hours. During the second hour, the animals in the test groups were exposed to a linear sweep (frequency range 0.1-25 kHz; peak amplitude 148 dBrms re 1 µPa at 12 kHz) acoustic stimulus for 30 minutes. Exposure to the noise produced significant variations in haemato-immunological parameters a…

Blood GlucoseFish ProteinsMaleHemocytesSound SpectrographyPhysiologyVideo RecordingCell CountAstacoideaAquatic ScienceStimulus (physiology)Animal scienceHemolymphAgonistic behaviourAnimalsHSP70 Heat-Shock ProteinsHabituationMolecular BiologyEcology Evolution Behavior and SystematicsVideo recordingProcambarus clarkiibiologyHemagglutinationOsmolar ConcentrationAnatomyacoustic stress agonistic behaviour physiological response red swamp crayfish.biology.organism_classificationCrayfishAcoustic StimulationInsect ScienceFemaleAnimal Science and ZoologyRabbitsAgonistic BehaviorJournal of Experimental Biology
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Profiling the physiological and molecular response to sulfonamidic drag in Procambarus clarkii

2014

Sulfamethoxazole (SMZ) is one of the most widely employed sulfonamides. Because of the widespread use of SMZ, a considerable amount is indeed expected to be introduced into the environment. The cytotoxicity of SMZ relies mainly on arylhydroxylamine metabolites (S-NOH) of SMZ and it is associated with the production of reactive oxygen species (ROS). There is limited information about the toxic potential of SMZ at the cellular and molecular levels, especially in aquatic and/or non-target organisms. In the present study, the red swamp crayfish (Procambarus clarkii), being tolerant to extreme environmental conditions and resistant to disease, was used as a model organism to profile the molecula…

Blood GlucoseGillsHemocytesAntioxidantSulfamethoxazolePhysiologyHealth Toxicology and Mutagenesismedicine.medical_treatmentHepatopancreasHaemolymphatic parametersAquacultureAstacoideaToxicologyBiochemistryArthropod ProteinsAnti-Infective AgentsRed swamp crayfishStress PhysiologicalGene expressionmedicineAnimalsMetallothioneinHSP70 Heat-Shock ProteinsTissue DistributionAntiossidanti enzymesharmony patio parameters proinflammatory genes red swap crac fish sulfametoxazoleProcambarus clarkiichemistry.chemical_classificationReactive oxygen speciesbiologyGene Expression Regulation DevelopmentalProinflammatory genesCell BiologyGeneral Medicinebiology.organism_classificationBlood Cell CountHsp70FerritinBiochemistrychemistryMolecular ResponseFerritinsbiology.proteinMetallothioneinAntioxidant enzymesOxidoreductasesBiomarkersWater Pollutants Chemical
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Inhibition of HSP70: a challenging anti-cancer strategy.

2012

HSP70 is a chaperone that accumulates in the cells after many different stresses promoting cell survival in response to the adverse conditions. In contrast to normal cells, most cancer cells abundantly express HSP70 at the basal level to resist to various insults at different stages of tumorigenesis and during anti-cancer treatment. This cancer cells addiction for HSP70 is the rational for its targeting in cancer therapy. Much effort has been dedicated in the last years for the active search of HSP70 inhibitors. Additionally, the recent clinical trials on highly promising inhibitors of another stress protein, HSP90, showed compensatory increase in HSP70 levels and raised the question of nec…

Cancer ResearchAntineoplastic AgentsApoptosismedicine.disease_cause03 medical and health sciences0302 clinical medicineImmune systemStress PhysiologicalHeat shock proteinNeoplasmsmedicineAutophagyAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular Targeted Therapy030304 developmental biology0303 health sciencesbiologyHsp903. Good healthNeoplasm ProteinsProtein Structure TertiaryClinical trialOncologyApoptosisDrug Resistance Neoplasm030220 oncology & carcinogenesisChaperone (protein)Drug DesignCancer cellImmunologybiology.proteinCancer researchDrug Screening Assays AntitumorCarcinogenesisMolecular ChaperonesCancer letters
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Nanofitins targeting heat shock protein 110: an innovative immunotherapeutic modality in cancer.

2021

The presence of an inactivating heat shock protein 110 (HSP110) mutation in colorectal cancers has been correlated with an excellent prognosis and with the ability of HSP110 to favor the formation of tolerogenic (M2-like) macrophages. These clinical and experimental results suggest a potentially powerful new strategy against colorectal cancer: the inhibition of HSP110. In this work, as an alternative to neutralizing antibodies, Nanofitins (scaffold ~7 kDa proteins) targeting HSP110 were isolated from the screening of a synthetic Nanofitin library, and their capacity to bind (immunoprecipitation, biolayer interferometry) and to inhibit HSP110 was analyzed in vitro and in vivo. Three Nanofiti…

Cancer ResearchMice03 medical and health sciencesLymphocytes Tumor-Infiltrating0302 clinical medicineImmune systemPeptide LibraryIn vivoCell Line TumorHeat shock proteinTumor MicroenvironmentmedicineAnimalsHumansCytotoxic T cellHSP110 Heat-Shock Proteinssmall peptide moleculesTumor microenvironmentanticancer targeted therapybiologyChemistryMacrophagesCancer[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciencesmedicine.diseaseXenograft Model Antitumor AssaysPeptide FragmentsIn vitro3. Good healthNanofitinsOncologyPositron-Emission Tomography030220 oncology & carcinogenesisbiology.proteinCancer researchFemaleAntibodyColorectal NeoplasmsHSP110
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Hsp72 controls bortezomib-induced HepG2 cell death via interaction with pro-apoptotic factors.

2007

The proteasome inhibitor bortezomib is an efficacious inducer of apoptosis in the hepatoma HepG2 cell line. This study shows that bortezomib increased in these cells the level of the survival factor Hsp72 in a time- and dose-dependent manner. In a first phase of treatment, Hsp72 rapidly increased so that at 24 h of incubation with 50 nM bortezomib its level was approximately five-fold higher than the control. In this phase Hsp72 seemed to play a role in preventing HepG2 cell death, since it interacted with and sequestered the pro-apoptotic factors p53, AIF, Bax and Apaf-1. During a second day of treatment, although the nuclear levels of Hsp72, p53 and AIF increased, the interaction of Hsp72…

Cancer ResearchProgrammed cell deathCarcinoma HepatocellularTime FactorsCellBlotting WesternApoptosisHSP72 Heat-Shock ProteinsAmino Acid Chloromethyl KetonesBortezomibCell Line TumormedicineHumansImmunoprecipitationProtease Inhibitorscardiovascular diseasesCaspasebcl-2-Associated X ProteinOncogenebiologyBortezomibReverse Transcriptase Polymerase Chain ReactionLiver NeoplasmsApoptosis Inducing Factorproteasome inhibitor hepatocarcinoma apoptosisGeneral MedicineCell cycleBoronic Acidsmedicine.anatomical_structureApoptotic Protease-Activating Factor 1OncologyApoptosisPyrazinesProteasome inhibitorCancer researchbiology.proteinTumor Suppressor Protein p53Apoptosis Regulatory Proteinsmedicine.drugProtein Binding
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Oligodendroglioma cells shed microvesicles which contain TRAIL as well as molecular chaperones and induce cell death in astrocytes.

2011

Microvesicles (MVs) shed from G26/24 oligodendroglioma cells were previously reported to cause a reproducible, dose-dependent, inhibitory effect on neurite outgrowth, and eventually neuronal apoptosis, when added to primary cultures of rat cortical neurons. These effects were reduced but not abolished by functional monoclonal antibodies against Fas-L. In order to investigate whether MVs contain other factors able to induce cell death, we tested them for TRAIL and found clear evidence of its presence in the vesicles. This finding suggests the possibility that Fas-L and TRAIL cooperate in inducing brain cell death. Aimed at understanding the route through which the vesicles deliver their mess…

Cancer ResearchProgrammed cell deathNeuritemedicine.drug_classOligodendrogliomaCellCell CommunicationBiologyMonoclonal antibodyTNF-Related Apoptosis-Inducing LigandCell-Derived MicroparticlesmedicineAnimalsHSP70 Heat-Shock ProteinsRats WistarCells CulturedCell DeathVesicleHSC70 Heat-Shock ProteinsCell cycleMicrovesiclesRatsCell biologymedicine.anatomical_structureOncologyApoptosisAstrocytesCulture Media Conditionedmicrovesicles oligodendroglioma astrocytes TRAIL Hsp70Molecular Chaperones
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