Search results for "Hsp"

showing 10 items of 557 documents

Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.

2008

AbstractThe hepatitis B virus L protein forms a dual topology in the endoplasmic reticulum (ER) via a process involving cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain. Here, we show that preS posttranslocation depends on the action of the ER chaperone BiP. To modulate the in vivo BiP activity, we designed an approach based on overexpressing its positive and negative regulators, ER-localized DnaJ-domain containing protein 4 (ERdj4) and BiP-associated protein (BAP), respectively. The feasibility of this approach was confirmed by demonstrating that BAP, but not ERdj4, destabilizes the L/BiP complex. Overexpressing BAP or ERdj4 inhibits…

Hepatitis B virusgenetic structuresBiPBiophysicsHemagglutinin (influenza)Chromosomal translocationmacromolecular substancesmedicine.disease_causeEndoplasmic ReticulumBiochemistryCell LineAdenosine TriphosphateViral Envelope ProteinsStructural BiologyIn vivoCalnexinHBVGeneticsmedicineHumansMolecular BiologyEndoplasmic Reticulum Chaperone BiPTranslocational regulationHeat-Shock ProteinsHepatitis B virusbiologyEndoplasmic reticulumMembrane ProteinsCell BiologyHSP40 Heat-Shock ProteinsMolecular biologyProtein Structure TertiaryProtein TransportDual topologyMembrane topologyProtein BiosynthesisMembrane topologybiology.proteinPosttranslational translocationMolecular ChaperonesFEBS letters
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Trattamento laparoscopico del megacolon agangliare

2007

Recent trends in surgery for Hirschsprung's disease have been toward early repair and fewer surgical stages. Laparoscopy can be used for colon pull-through even in neonates adding the advantages of a minimally invasive approach to those of the traditional technique. the personal experience in the use of laparoscopically assisted endorectal pull-through in the treatment of Hirschsprung's disease in reported. the advantages it offers are outlined, including excellent visualization of the operative field, accurate dissection of the bowel from pelvic structures, and minimally invasive abdominal wounds. Preliminary results show that laparoscopically assisted endorectal pull-through is one of the…

Hirschsprung's disease laparoscopy endorectal pull-through
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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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The chaperone system in cancer therapies: Hsp90

2023

AbstractThe chaperone system (CS) of an organism is composed of molecular chaperones, chaperone co-factors, co-chaperones, and chaperone receptors and interactors. It is present throughout the body but with distinctive features for each cell and tissue type. Previous studies pertaining to the CS of the salivary glands have determined the quantitative and distribution patterns for several members, the chaperones, in normal and diseased glands, focusing on tumors. Chaperones are cytoprotective, but can also be etiopathogenic agents causing diseases, the chaperonopathies. Some chaperones such as Hsp90 potentiate tumor growth, proliferation, and metastasization. Quantitative data available on t…

HistologyPhysiologyAktChaperonopathieMolecular chaperoneChaperone systemHsp90Cell BiologyGeneral MedicineNF-kBNegative chaperonotherapy
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Post-translational modifications of hsp60 and its extracellular release via exosomes are induced by the histone deacetylase inhibitor (HDACi) SAHA in…

2015

The chaperonin Hsp60 has multiple functions, among which that of supporting the growth of some type of tumours (1). HDACi (histone-deacetylase inhibitors) are drugs that regulate gene expression via modulation of epigenetic mechanisms, and induce tumor-cell death (2). Here, we show that in the tumor cells H292 the HDACi SAHA decreases the intracellular level of Hps60 and promotes its extracellular trafficking by exosomal vesicles. SAHA caused a time- and dose-dependent decrease in cell viability with a G/2M cell-cycle arrest at 24 h and cell death at 48 h. These effects were accompanied by production of reactive oxygen species and mitochondrial membrane-potential dissipation. The marked dec…

Histone deacetylase inhibitorHistone deacetylase inhibitor; Hsp60; nitration; exosomesexosomesHsp60nitration
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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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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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HSP60 IS THE MOST PREDICTIVE HEAT SHOCK PROTEIN DURING LARGE BOWEL CARCINOGENESIS

2014

Hsp 60 Large Bowel Exosomes.
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Expression of Heat Shock Proteins Hsp10, Hsp27, Hsp60, Hsp70 and Hsp90 in urothelial carcinoma of urinary bladder

2006

Hsp urothelial carcinoma
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