Search results for "Shock proteins"

showing 10 items of 347 documents

Comparative analysis of Hsp10 and Hsp90 expression in healthy mucosa and adenocarcinoma of the large bowel.

2014

Heat shock proteins (Hsps) assist other proteins in their folding and drive the degradation of defective proteins. During evolution, these proteins have also acquired other roles. Hsp10 is involved in immunomodulation and tumor progression. Hsp90 stabilizes a range of "client" proteins involved in cell signaling. The present study evaluated the expression levels of Hsp10 and Hsp90 in normal mucosa and adenocarcinoma samples of human large bowel.Samples of normal mucosa and adenocarcinoma were collected and Reverse transcriptase-polymerase chain reaction RT-PCR, western blotting (WB) analyses, as well as immunohistochemistry were performed to evaluate the expression levels of Hsp10 and Hsp90…

Hsp10Reverse Transcriptase Polymerase Chain Reactionlarge bowel adenocarcinomaBlotting WesternColonic NeoplasmsRT-PCRChaperonin 10HumansHsp90HSP90 Heat-Shock ProteinsAdenocarcinomaIntestinal MucosaImmunohistochemistryAnticancer research
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Intensified oxidative and nitrosative stress following combined ALA-based photodynamic therapy and local hyperthermia in rat tumors.

2003

Oxidative stress-related changes in tumors upon localized hyperthermia (HT), 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) and their combination (ALA+HT) were examined after the observation that the antitumor effects of ALA-PDT could be significantly enhanced upon simultaneous application of HT. Rats bearing s.c. DS-sarcomas (0.6–1.0 ml) on the hind foot dorsum were anesthetized and underwent one of the following treatments: (i) ALA-PDT (375 mg/kg 5-ALA i.v.); (ii) localized HT, 43°C for 60 min; (iii) combined ALA-PDT and HT [=ALA+HT]. Appropriate control experiments were also performed. After treatment, tumors were excised and rapidly frozen for later analysis of nitrosative s…

HyperthermiaMaleCancer ResearchLightNitrosationApoptosisPharmacologymedicine.disease_causeRats Sprague-Dawleychemistry.chemical_compoundIn vivoHeat shock proteinmedicineAnimalsHSP70 Heat-Shock ProteinsHeat-Shock Proteinschemistry.chemical_classificationGlutathione PeroxidasePhotosensitizing AgentsGlutathione peroxidaseSarcomaGlutathioneAminolevulinic Acidmedicine.diseaseGlutathioneHsp70RatsGene Expression Regulation NeoplasticOncologyBiochemistrychemistryPhotochemotherapyApoptosisHeme Oxygenase (Decyclizing)OxygenasesOxidative stressCell DivisionHeme Oxygenase-1International journal of cancer
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Expression Profile of Stress Proteins, Intermediate Filaments, and Adhesion Molecules in Experimentally Denervated and Reinnervated Rat Facial Muscle

1997

The immunohistochemical profiles of ubiquitin, heat shock protein 70, alpha-B-crystallin, desmin, vimentin, neural cell adhesion molecule (N-CAM), and tenascin in rat facial muscle were studied after permanent denervation by transection of the facial plexus on one side and compared with findings after immediate reinnervation by hypoglossal-facial nerve anastomosis subsequent to transection on the contralateral side. Levator labii muscle samples were collected sequentially at 2, 6, 7, 10, 20, and 24 weeks after surgery. Normal levator labii muscle fibers showed physiological expression of desmin and alpha-B-crystallin. Denervated rat facial muscle displayed distinct up-regulation of ubiquiti…

Hypoglossal NervePathologymedicine.medical_specialtyTime Factorsanimal structuresMuscle Fibers SkeletalFacial MusclesTenascinDesminIntermediate Filament ProteinsDevelopmental NeurosciencemedicineAnimalsVimentinHSP70 Heat-Shock ProteinsRats WistarIntermediate filamentNeural Cell Adhesion MoleculesUbiquitinsHeat-Shock ProteinsConnective Tissue CellsDenervationMuscle DenervationbiologyAnastomosis SurgicalTenascinmusculoskeletal systemCrystallinsImmunohistochemistryMuscle DenervationRatsSarcoplasmic ReticulumFacial musclesmedicine.anatomical_structureNeurologyConnective Tissuebiology.proteinFemaleNeural cell adhesion moleculeDesminAtrophyReinnervationExperimental Neurology
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HEAT SHOCK PROTEINS AND AUTOIMMUNE SYSTEM ACTIVATION IN IBD: ARTICULAR MANIFESTATIONS AND THE EPIDEMIOLOGICAL FREQUENCY IN ORTHPEDICS

2013

clinical evidence suggest that arthritis is one of the complications of inflammatori bowel disease (IBD) of which the etiological causes are still not completely understood. Among the possible explanations the most probable theory is poor regulation of the intestinal immune system, which causes a cross-like immune reactivity against the resident micro flora. Arthritis is these subjects involves different joints and is asymmetric, with greater involvement of the large joints of the lower limbs. Joints may also be involved with the spinal forms of sacroileitis and ankilosing spondylitis. This clinical evidence explains the existence of Lesnioski-Crohn's disease, a variant of IBD in which pati…

IBD Intestinal Bowel Disease Microbiota Arthritis Heat Shock Proteins HSPSettore MED/18 - Chirurgia GeneraleSettore MED/09 - Medicina InternaSettore MED/33 - Malattie Apparato Locomotore
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HSP90 and HSP70: Implication in Inflammation Processes and Therapeutic Approaches for Myeloproliferative Neoplasms.

2015

Myeloproliferative neoplasms (MPN) are clonal stem cell disorders that lead to the excessive production of one or more blood cell lineages. It has been reported that, in most MPN, inflammatory cytokines are frequently increased, indicating that inflammation plays a crucial role in these disorders. Heat shock proteins (HSP) are induced in response to many stressful conditions from heat shock to hypoxia and inflammation. Besides their chaperone and cytoprotective functions, HSPs are key players during inflammation, hence the term “chaperokine.” Through their chaperone activity, HSP90, a stabilizer of many oncogenes (e.g., JAK2), and HSP70, a powerful antiapoptotic chaperone, tightly regulate …

ImmunologyInflammationReview ArticleBiologyModels BiologicalProinflammatory cytokineMyeloproliferative DisordersHeat shock proteinlcsh:PathologymedicineHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular Targeted TherapyMyeloproliferative DisordersCell BiologyHsp90Chaperone (protein)ImmunologyCancer researchbiology.proteinmedicine.symptomSignal transductionStem cellInflammation Mediatorslcsh:RB1-214Signal TransductionMediators of inflammation
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Serological identification of HSP105 as a novel non-Hodgkin lymphoma therapeutic target.

2011

Abstract We reported that the clinical efficacy of dendritic cell–based vaccination is strongly associated with immunologic responses in relapsed B-cell non-Hodgkin lymphoma (B-NHL) patients. We have now investigated whether postvaccination antibodies from responders recognize novel shared NHL-restricted antigens. Immunohistochemistry and flow cytometry showed that they cross-react with allogeneic B-NHLs at significantly higher levels than their matched prevaccination samples or nonresponders' antibodies. Western blot analysis of DOHH-2 lymphoma proteome revealed a sharp band migrating at approximately 100 to 110 kDa only with postvaccine repertoires from responders. Mass spectrometry ident…

ImmunologyMice SCIDBiochemistryAntibodiesFlow cytometryAntigen-Antibody ReactionsCohort StudiesHSP105MiceAntigenhemic and lymphatic diseasesCell Line TumormedicineAnimalsHumansSerologic TestsHSP110 Heat-Shock Proteinsmedicine.diagnostic_testbiologybusiness.industryLymphoma Non-HodgkinHSP105; non-Hodgkin lymphoma.Cell BiologyHematologyCell cyclemedicine.diseaseImmunohistochemistryLymphomaGranzyme BGene Expression Regulation Neoplasticnon-Hodgkin lymphoma.Spectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinImmunohistochemistryAntibodybusinessDiffuse large B-cell lymphoma
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Geldanamycin and its derivatives as Hsp90 inhibitors

2012

The Hsp90 molecule, one of the most abundant heat shock proteins in mammalian cells, maintains homeostasis and prevents stress-induced cellular damage. Hsp90 is expressed under normal conditions at a level of about 1-2 Percent of total proteins, while its expression increases 2-10 fold in cancer cells. The two main constitutively expressed isoforms of Hsp90 are known as Hsp90-alpha and Hsp90-beta, and their upregulation is associated with tumor progression, invasion and formation of metastases, as well as development of drug resistance. The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and…

IndolesLactams MacrocyclicCyclin-Dependent KinaseAntineoplastic AgentsTanespimycinBenzoquinoneModels BiologicalAntineoplastic Agentchemistry.chemical_compoundDownregulation and upregulationTransforming Growth Factor betaCyclin-dependent kinaseHeat shock proteinBenzoquinonespolycyclic compoundsAnimalsHumansHSP90 Heat-Shock ProteinsbiologyAnimalTriazolesGeldanamycinHsp90Cyclin-Dependent KinasesProto-Oncogene Proteins c-rafHSP90 Heat-Shock Proteinsrc-Family KinaseschemistryTumor progressionMutationCancer cellbiology.proteinCancer researchMacrolidesMacrolideTriazoleTumor Suppressor Protein p53Animals; Antineoplastic Agents; Benzoquinones; Cyclin-Dependent Kinases; HSP90 Heat-Shock Proteins; Humans; Lactams Macrocyclic; Macrolides; Models Biological; Mutation; Novobiocin; Proto-Oncogene Proteins c-raf; Transforming Growth Factor beta; Triazoles; Tumor Suppressor Protein p53; src-Family KinasesNovobiocinHumanFrontiers in Bioscience
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HSP70 sequestration by free α-globin promotes ineffective erythropoiesis in β-thalassaemia

2014

International audience; β-Thalassaemia major (β-TM) is an inherited haemoglobinopathy caused by a quantitative defect in the synthesis of β-globin chains of haemoglobin, leading to the accumulation of free α-globin chains that form toxic aggregates. Despite extensive knowledge of the molecular defects causing β-TM, little is known of the mechanisms responsible for the ineffective erythropoiesis observed in the condition, which is characterized by accelerated erythroid differentiation, maturation arrest and apoptosis at the polychromatophilic stage. We have previously demonstrated that normal human erythroid maturation requires a transient activation of caspase-3 at the later stages of matur…

Ineffective erythropoiesisCytoplasmErythroblastsCell SurvivalMutantApoptosis[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyalpha-globin[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Biologymedicine.disease_causeProtein Refolding03 medical and health sciences0302 clinical medicinealpha-GlobinsBone Marrowhemic and lymphatic diseasesmedicineHumans[ SDV.MHEP.HEM ] Life Sciences [q-bio]/Human health and pathology/HematologyErythropoiesisGATA1 Transcription FactorHSP70 Heat-Shock ProteinsMolecular Targeted TherapyCells CulturedHSP70030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesMultidisciplinaryCaspase 3beta-Thalassemia[ SDV.BC.BC ] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]GATA1[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/Hematology[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMolecular biologyHsp70Enzyme ActivationKineticsGene Expression RegulationCytoplasm030220 oncology & carcinogenesisChaperone (protein)biology.proteinErythropoiesisbeta-ThalassaemiaProtein Binding
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Heat Shock Proteins Alterations in Rheumatoid Arthritis

2022

Rheumatoid arthritis (RA) is a chronic inflammatory and autoimmune disease characterized by the attack of the immune system on the body’s healthy joint lining and degeneration of articular structures. This disease involves an increased release of inflammatory mediators in the affected joint that sensitize sensory neurons and create a positive feedback loop to further enhance their release. Among these mediators, the cytokines and neuropeptides are responsible for the crippling pain and the persistent neurogenic inflammation associated with RA. More importantly, specific proteins released either centrally or peripherally have been shown to play opposing roles in the pathogenesis of this dise…

InflammationHeat shock proteins Hsp therapy Inflammation Neurogenic inflammation Rheumatoid arthritis VaccineOrganic ChemistryGeneral MedicineChaperonin 60CatalysisComputer Science ApplicationsInorganic ChemistryArthritis RheumatoidHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologySpectroscopyHeat-Shock Proteins
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Correction: Oncogenic extracellular HSP70 disrupts the gap-junctional coupling between capillary cells

2021

High levels of circulating heat shock protein 70 (HSP70) are detected in many cancers. In order to explore the effects of extracellular HSP70 on human microvascular endothelial cells (HMEC), we initially used gap-FRAP technique. Extracellular human HSP70 (rhHSP70), but not rhHSP27, blocks the gap-junction intercellular communication (GJIC) between HMEC, disrupts the structural integrity of HMEC junction plaques, and decreases connexin43 (Cx43) expression, which correlates with the phosphorylation of Cx43 serine residues. Further exploration of these effects identified a rapid transactivation of the Epidermal Growth Factor Receptor in a Toll-Like Receptor 4-dependent manner, preceding its in…

Junctional couplingChemistryCapillary actionCorrectionEndothelial CellsGap JunctionsCell CommunicationRecombinant ProteinsHsp70OncologyConnexin 43BiophysicsExtracellularHumansHSP70 Heat-Shock ProteinsPhosphorylationOncotarget
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