Search results for "heat shock"

showing 10 items of 303 documents

Protective role of heat shock proteins in Parkinson's disease.

2010

Parkinson’s disease (PD) is the second most common neurodegenerative disease after Alzheimer’s disease. Despite a large amount of research, the pathogenetic mechanism of these diseases has not yet been clarified. Abnormal protein folding, oxidative stress, mitochondrial dysfunction, and apoptotic mechanisms have all been reported as causes of neurodegenerative diseases in association with neuroinflammatory mechanisms which, by generating deleterious molecules, could promote the cascade of events leading to neurodegeneration. Heat shock proteins (HSPs) play a central role in preventing protein misfolding and inhibiting apoptotic activity, and represent a class of proteins potentially involve…

Heat shock proteins Parkinson disease neuroprotective roleParkinson's diseasebiologyNeurodegenerationParkinson DiseaseDiseasemedicine.diseasemedicine.disease_causeHsp90Hsp70PathogenesisNeurologyHeat shock proteinImmunologymedicinebiology.proteinAnimalsHumansHSP70 Heat-Shock ProteinsNeurology (clinical)HSP90 Heat-Shock ProteinsNeuroscienceOxidative stressHeat-Shock ProteinsNeuro-degenerative diseases
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Role of heme oxygenase-1 (HSP32) and HSP90 in glioblastoma

2017

Glioblastoma (GBM) is the most common and malignant primary brain tumor in adults. The current treatment regimes for glioblastoma demonstrated a low efficiency and offer a poor prognosis. Advancements in conventional treatment strategies have only yielded modest improvements in overall survival. The heat shockproteins, heme oxygenase-1 (HO-1) and Hsp90, serve these pivotal roles in tumor cells and have been identified as effective targets for developing therapeutics. This topic review summarizes the current preclinical and clinical evidences and rationale to define the potential of HO-1 and Hsp90 in GBM progression and chemoresistance.

Heme oxygenaseMolecular chaperonesHeat shock proteinHsp90GlioblastomaCancer
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Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein…

1997

AbstractThe large L envelope protein of the hepatitis B virus has the peculiar capacity to adopt two transmembrane topologies. The N-terminal preS domain of L initially remains in the cytosol while the S domain is cotranslationally inserted into the endoplasmic reticulum membrane. The preS region of about half of the L molecules is posttranslationally translocated to the lumenal space. We now demonstrate that the repression of cotranslational translocation of preS is conferred by a preS1-specific sequence. By analysis of L deletion mutants, the cytosolic anchorage determinant was mapped to amino acid sequence 70 to 94 of L. The intrinsic potential of this determinant to suppress cotranslati…

Hepatitis B virusHSC70 Heat-Shock ProteinsRecombinant Fusion ProteinsPlasma protein bindingBiologyGenes envCytosolViral Envelope ProteinsHeat shock proteinVirologyHumansHSP70 Heat-Shock ProteinsBinding sitePromoter Regions GeneticPeptide sequenceBinding SitesBase SequenceCell-Free SystemEndoplasmic reticulumHSC70 Heat-Shock ProteinsOligonucleotides AntisenseMolecular biologyTransmembrane proteinChaperone (protein)Protein Biosynthesisbiology.proteinMutagenesis Site-DirectedMetallothioneinCarrier ProteinsProtein BindingVirology
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Expression of the 60 kDa heat shock protein in normal and inflamed liver.

1993

The 60 kDa heat shock proteins (HSP 60) have been well conserved throughout evolution and are highly immunogenic. Cross-reactivity between bacterial and mammalian HSP 60 is considered a likely mechanism in the pathogenesis of autoimmune diseases. T cell and B cell reactivity to HSP 60 is found in patients with rheumatoid or juvenile arthritis, and the expression of HSP 60 in the inflamed joint is found to be increased. In this study the presence of HSP 60 was demonstrated in normal and inflamed lives. HSP 60 was found to be predominantly expressed in hepatocytes and Kupffer cells, and mainly localized in mitochondria. Heat stress in the form of a 1 h incubation at 42 degrees C increased HSP…

HepatitisHepatologyT cellKupffer cellInflammationAutoimmune hepatitisChaperonin 60Biologymedicine.diseaseMolecular biologyHepatitisPathogenesismedicine.anatomical_structureLiverReference ValuesHeat shock proteinImmunologyChronic DiseasemedicineHumansmedicine.symptomB cellHeat-Shock ProteinsJournal of hepatology
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HSP10,HSP70 AND HSP90 IMMUNOHISTOCHEMICAL LEVELS CHANGE IN ULCERATIVE COLITIS AFTER THERAPY

2011

Ulcerative colitis (UC) is a form of inflammatory bowel disease (IBD) characterized by damage of large bowel mucosa and frequent extra-intestinal autoimmune comorbidities. The role played in IBD pathogenesis by molecular chaperones known to interact with components of the immune system involved in inflammation is unclear. We previously demonstrated that mucosal Hsp60 decreases in UC patients treated with conventional therapies (mesalazine, probiotics), suggesting that this chaperonin could be a reliable biomarker useful for monitoring response to treatment, and that it might play a role in pathogenesis. In the present work we investigated three other heat shock protein/molecular chaperones:…

HistologyBiophysicsDown-RegulationInflammationcomorbidity.Inflammatory bowel diseaseulcerative colitis heat shock proteins Hsp molecular chaperones inflammation comorbidity.Pathogenesischemistry.chemical_compoundMesalazineulcerative colitis heat shock proteins Hsp molecular chaperones inflammation comorbidityHeat shock proteinChaperonin 10MedicineHspHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsColitisMesalaminelcsh:QH301-705.5ulcerative colitisbusiness.industryBrief Reportmolecular chaperonesAnti-Inflammatory Agents Non-SteroidalCell Biologymedicine.diseaseUlcerative colitisImmunohistochemistrydigestive system diseaseschemistrylcsh:Biology (General)inflammationImmunologyheat shock proteinsBiomarker (medicine)Colitis Ulcerativemedicine.symptombusiness
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Cellular responses and HSP70 expression during wound healing in Holothuria tubulosa (Gmelin, 1788).

2014

Wound repair is a key event in the regeneration mechanisms of echinoderms. We studied, at the behavioural, cellular and molecular levels, the wound healing processes in Holothuria tubulosa after injuries to the body wall. The experiments were performed for periods of up to 72 h, and various coelomocyte counts, as well as the expression of heat shock proteins (HS27, HSP70 and HSP90), were recorded. Dermal wound healing was nearly complete within 72 h. In the early stages, we observed the injured animals twisting their bodies to keep their injuries on the surface of the water for the extrusion of the buccal pedicles. At the cellular level, we found time-dependent variations in the circulating…

HolothurianStreImmunoblottingSettore BIO/05 - ZoologiaHSP27 Heat-Shock ProteinsAquatic ScienceAndrologyWestern blotHeat shock proteinmedicineHSPEnvironmental ChemistryAnimalsHolothuriaHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsSettore BIO/06 - Anatomia Comparata E CitologiaCoelomocyteWound Healingmedicine.diagnostic_testbiologyRegeneration (biology)Holothuria tubulosaGeneral Medicinebiology.organism_classificationHsp70Organ SpecificityImmunologyCoelomocyteWound healingHolothuriaFishshellfish immunology
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Mild Heat Stress Enhances Angiogenesis in a Co-culture System Consisting of Primary Human Osteoblasts and Outgrowth Endothelial Cells

2013

The repair and regeneration of large bone defects, including the formation of functional vasculature, represents a highly challenging task for tissue engineering and regenerative medicine. Recent studies have shown that vascularization and ossification can be stimulated by mild heat stress (MHS), which would offer the option to enhance the bone regeneration process by relatively simple means. However, the mechanisms of MHS-enhanced angiogenesis and osteogenesis, as well as potential risks for the treated cells are unclear. We have investigated the direct effect of MHS on angiogenesis and osteogenesis in a co-culture system of human outgrowth endothelial cells (OECs) and primary osteoblasts …

Hot TemperatureCell SurvivalAngiogenesisCellular differentiationBiomedical EngineeringNeovascularization PhysiologicMedicine (miscellaneous)ApoptosisBioengineeringBiologyRegenerative medicineArticleTissue engineeringOsteogenesisHeat shock proteinHumansRNA MessengerHeat shockBone regenerationCells CulturedCaspase 7OsteoblastsCaspase 3Regeneration (biology)Endothelial CellsCell DifferentiationCoculture TechniquesCapillariesUp-RegulationCell biologyImmunologyHeat-Shock ResponseTissue Engineering Part C: Methods
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Transcriptional and translational study of the Drosophila subobscura hsp83 gene in normal and heat-shock conditions

1993

In this paper we report a transcriptional and translational study of the hsp83 gene of Drosophila subobscura. This gene is located at the 18C region of the J chromosome. A monoclonal antibody raised against hsp83 was used for the immunological detection of this protein by Western blotting throughout the development of D. subobscura in control and heat-shock conditions. Our results indicate that puff 18C is not only heat-shock inducible but is also expressed during normal development and its level of expression increases at the end of the prepupa period. We detected hsp83 at normal temperatures, in particular developmental stages with the exception of the larval and the beginning of prepupa…

Hot TemperaturePolytene chromosomeTranscription GeneticGene ExpressionGenes InsectGeneral MedicineBiologybiology.organism_classificationMolecular biologyDrosophila subobscuraGene productTranscription (biology)Protein BiosynthesisHeat shock proteinDrosophilidaeGene expressionGeneticsAnimalsDrosophilaMolecular BiologyGeneHeat-Shock ProteinsBiotechnologyGenome
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Transcription of heat shock gene loci versus non-heat shock loci in Chironomus polytene chromosomes: evidence for heat-induced formation of novel put…

1995

The heat shock response of Chironomus polytene chromosomes was reexamined. The in vivo effects of heat shock on chromosomal [3H]uridine labeling, RNA polymerase II distribution and ribonucleoprotein (RNP) formation were investigated. One primary result is a clarification of the number and location of chromosomal sites strongly induced by treatment at 37 degrees C for 60 min. In total, seven major heat shock loci were identified by transcription autoradiography in Chironomus tentans: I-20A, II-16B, II-10C, II-4B, II-1C, III-12B, and IV-5C. Secondly, combining immunofluorescence with transcription autoradiography, I find RNA polymerase II occurring after heat shock at multiple chromosomal sit…

Hot TemperatureTranscription GeneticGenes InsectRNA polymerase IIBiologyChironomidaeChromosomesTranscription (biology)GeneticsTranscriptional regulationAnimalsHeat shockUridineHeat-Shock ProteinsGenetics (clinical)RibonucleoproteinHSPA14RNAMolecular biologyCell biologyHeat shock factorMicroscopy ElectronGene Expression RegulationRibonucleoproteinsbiology.proteinAutoradiographyRNA Polymerase IIChromosoma
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MOLECULAR CHAPERONES IN HUMAN SALIVARY GLANDS: HSP90 A BIOMARKER IN HEALTH AND DISEASE

2022

Hsp90 biomarkerchaperone systemdifferential diagnosisheat shock proteinnegative chaperonotherapyGanetespibsalivary gland tumor
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