Search results for "HSp70"

showing 10 items of 206 documents

The effects of treated effluents on the intensity of papillomatosis and HSP70 expression in roach.

2008

Epidermal papillomatosis in fish has been proposed as an indicator of environmental stress but experimental evidence of connection between contaminants and papillomatosis in fish is scarce. We studied changes in the intensity of epidermal papillomatosis and the expression of heat shock protein 70 (HSP70) in roach, Rutilus rutilus, exposed to treated pulp mill and municipal effluents. In male roach, the increase in papillomatosis intensity was higher in fish exposed to 15% than in fish exposed to 1.5% concentration of municipal effluent. No differences were observed in papillomatosis development in females, or in HSP70 expression. In all the experiments conducted, the increasing effect of ef…

GillsMalePaperVeterinary medicineympäristöpulp mill effluentssex differenceHealth Toxicology and Mutagenesisheat shock proteinCyprinidaeIndustrial WastePapillomatosisEnvironmental stressWaste Disposal FluidmedicineihokasvaintautiAnimalsmunicipal effluentsHSP70 Heat-Shock ProteinsWater Pollutantspapilloma diseasesärkipapillomatoosiEffluentHSP70Hsp70 expressionbiologyPapillomaEcologydigestive oral and skin physiologyEnvironmental stressorPublic Health Environmental and Occupational HealthstressiGeneral Medicinebiology.organism_classificationPollutionenvironmental stressaltistuminenFish <Actinopterygii>Femalemedicine.symptomRutilusjätevedetWaste disposalEcotoxicology and environmental safety
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Concomitant cellular expression of heat shock regulated genes of hepatitis B virus surface antigen and of human growth hormone by a NIH-3T3 cell line.

1993

A plasmid carrying a DNA fragment of hepatitis B virus, coding for the pre-S2 and the entire S region of the surface antigen (HBsAg), placed under the control of the promoter of the human 70 kDa heat shock protein gene (hsp70), was introduced into Line 6, a recombinant cell line that was selected from NIH-3T3 cells previously transfected with a similar construct coding for the human growth hormone cDNA gene (chGH) and with the plasmid pEJ carrying the Ha-rasEJ activated cellular oncogene. The resulting cell line, EMS8, expressed: (1) hsp70/HBsAg and hsp70/hGH hybrid genes, (2) the human Ha-rasEJ oncogene, and (3) the neomycin resistance gene, the two last plasmid markers being used for cell…

HBsAgHepatitis B Surface AntigensHealth Toxicology and MutagenesisCell BiologyTransfection3T3 CellsBiologyToxicologyMolecular biologyRecombinant ProteinsHsp70Cell LineMicePlasmidCell cultureHeat shock proteinGrowth HormoneGene expressionAnimalsHumansHybridization GeneticRNA MessengerPeptide Chain Initiation TranslationalGeneHeat-Shock ProteinsCell biology and toxicology
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Modulazione In vivo dell’Hsp70 negli emociti di Rhynchophorus ferrugineus dopo trattamento con Bacillus thuringiensis

2011

Diversi tipi di stress ambientali possono indurre l’espressione delle Hsps vengono rapidamente sintetizzate all'interno delle cellule dopo esposizione ad uno stressor. Le HSPs sono raggruppate in diverse famiglie in base alle dimensioni delle proteine. Nella maggior parte degli organismi ci sono diversi geni che codificano i membri di questa famiglia HSP. In studi precedenti è stata valutata l'interazione tra Bacillus thuringiensis e gli emociti circolanti di Rhynchophorus ferrugineus il punteruolo rosso delle palme. Questo coleottero è grande, da due a cinque centimetri di lunghezza, ed è di colore rosso ruggine, le sue larve scavano buche fino a un metro lungo il tronco delle palme, e può…

HSP70 Rhynchophorus ferrugineusSettore BIO/05 - Zoologia
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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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Manganese effects on haematopoietic cells and circulating coelomocytes of Asterias rubens (Linnaeus)

2008

Abstract Manganese (Mn) is a naturally abundant metal in marine sediments where it mainly occurs as MnO 2 . During hypoxic conditions it is converted into a bioavailable state, Mn 2+ , and can reach levels that previously have shown effects on immune competent cells of the crustacean, Nephrops norvegicus . Here we investigated if Mn also affects circulating coelomocytes and their renewal in the common sea star, Asterias rubens , when exposed to concentrations of Mn that can be found in nature. When the sea stars were exposed to Mn it accumulated in the coelomic fluid and the number of circulating coelomocytes, in contrast to what was recorded in Nephrops , increased significantly. By using …

HemocytesMitotic indexCell divisionCell SurvivalHealth Toxicology and MutagenesisBlotting WesternCell CountAquatic ScienceBiologyPhagocytosisNephrops norvegicusMitotic IndexmedicineAnimalsHSP70 Heat-Shock ProteinsCell ProliferationManganeseAsteriasAnatomybiology.organism_classificationMolecular biologyCoelomic epitheliumHsp70Haematopoiesismedicine.anatomical_structureAsteriasCoelomWater Pollutants ChemicalAquatic Toxicology
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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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Chaperones Involved in Hepatitis B Virus Morphogenesis

1999

Little is known about host cell factors necessary for hepatitis B virus (HBV) assembly which involves envelopment of cytosolic nucleocapsids by the S, M and L transmembrane viral envelope proteins and subsequent budding into intraluminal cisternae. Central to virogenesis is the L protein that mediates hepatocyte receptor binding and envelopment of capsids. To serve these topologically conflicting roles, L protein exhibits an unusual dual membrane topology, disposing its N-terminal preS domain inside and outside of the virion lipid envelope. The mixed topology is achieved by posttranslational preS translocation of about half of the L protein molecules across a post-endoplasmic reticulum memb…

Hepatitis B virusProtein FoldingCalnexinHSC70 Heat-Shock ProteinsClinical BiochemistryBiochemistryViral Matrix ProteinsCytosolViral Envelope ProteinsViral envelopeCalnexinMorphogenesisAnimalsHumansHSP70 Heat-Shock ProteinsProtein PrecursorsMolecular BiologyHepatitis B Surface AntigensViral matrix proteinbiologyChemistryCalcium-Binding ProteinsHSC70 Heat-Shock ProteinsBiological TransportVirologyTransmembrane proteinCell biologyProtein BiosynthesisMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein foldingCarrier ProteinsMolecular ChaperonesBiological Chemistry
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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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Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

2008

Mouse A6 mesoangioblasts express Hsp70 even in the absence of cellular stress. Its expression and its intracellular localization were investigated under normal growth conditions and under hyperthermic stress. Immunofluorescence assays indicated that without any stress a fraction of Hsp70 co-localized with actin microfilaments, in the cell cortex and in the contractile ring of dividing cells, while the Hsc70 chaperone did not. Hsp70 immunoprecipitation assays confirmed that a portion of Hsp70 binds actin. Immunoblot assays showed that both proteins were present in the nucleus. After heat treatment Hsp70 and actin continued to co-localize in the leading edge of A6 cells but not on microfilame…

Hot TemperatureHistologyPhysiologyImmunoprecipitationHsp70 Hsc70 Mesoangioblastmacromolecular substancesMicrofilamentCell LineMiceStress PhysiologicalCell cortexAnimalsHumansHSP70 Heat-Shock ProteinsActinbiologyStem CellsHSC70 Heat-Shock ProteinsCell BiologyGeneral MedicineActinsGlomerular MesangiumHsp70Cell biologyCell cultureChaperone (protein)biology.proteinCell DivisionCytokinesisMolecular ChaperonesJournal of Molecular Histology
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