Search results for "Heat-shock proteins"

showing 10 items of 310 documents

Do not stress, just differentiate: role of stress proteins in hematopoiesis

2015

Hematopoiesis permits the constant regeneration of the blood system and is a permanent example of cell differentiation. Defects in its tight regulation can lead to either cell death or abnormal proliferation and may translate into multiple types of blood disorders, including leukemia. Heat shock proteins (HSPs), the expression of which is controlled by heat shock factors (HSFs, currently four known members),1 are a set of highly conserved proteins induced in response to a wide variety of physiological and environmental stress. HSP/HSF overexpression or mislocalization has been described in many cancers, particularly in hematology, and other diseases. Therefore, the involvement of HSFs/HSPs …

Cancer Researchmedicine.medical_specialtyCellular differentiationImmunologyBiologyMiceCellular and Molecular NeuroscienceHeat Shock Transcription FactorsInternal medicineHeat shock proteinmedicineAnimalsProtein IsoformsRNA MessengerHeat shockTranscription factorHeat-Shock ProteinsHematologyCell DifferentiationNews and CommentaryCell BiologyHematopoiesisCell biologyDNA-Binding ProteinsHeat shock factorHaematopoiesisCaspasesHSP60Heat-Shock ResponseTranscription FactorsCell Death & Disease
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Heat Shock Protein Vaccines Against Cancer

1993

Vaccination of mice with heat shock proteins (HSPs) derived from a tumor makes the mice resistant to the tumor from which the HSP was obtained. This phenomenon has been demonstrated with three HSPs--gp96, hsp90, and hsp70. Vaccination with HSPs also elicits antigen-specific cytotoxic T lymphocytes (CTLs). The specific immunogenicity of HSPs derives apparently, not from the HSPs per se, but from the peptides bound to them. These observations provide the basis for a new generation of vaccines against cancer. The HSP-based cancer vaccines circumvent two of the most intractable hurdles to cancer immunotherapy. One of them is the possibility that human cancers, like cancers of experimental anima…

Cancer Researchmedicine.medical_treatmentImmunologychemical and pharmacologic phenomenaBiologyInfectionsEpitopeMiceImmune systemAntigenCancer immunotherapyHeat shock proteinmedicineAnimalsImmunology and AllergyCytotoxic T cellHeat-Shock ProteinsPharmacologyMice Inbred BALB CMice Inbred C3HHistocompatibility Antigens Class IVaccinationCancerhemic and immune systemsImmunotherapymedicine.diseaseImmunologySarcoma ExperimentalT-Lymphocytes CytotoxicJournal of Immunotherapy
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Targeting cancer with peptide aptamers

2011

Renaud Seigneuric 1,2 , Jessica Gobbo 1,2 , Pierre Colas 3 , Carmen Garrido 1,2 1 Heat Shock Proteins and Cancer, INSERM, UMR 866 IFR 100, Faculty of Medicine, 7 Boulevard Jeanne D'Arc, 21000 Dijon, France 2 Universite de Bourgogne, Dijon, France 3 CNRS USR 3151, P2I2 Group, Station Biologique, Roscoff, Bretagne, France Received: June 22, 2011; Accepted: June 24, 2011; Published: June 24, 2011; Correspondence: Renaud Seigneuric, email: // // Abstract A major endeavour in cancer chemotherapy is to develop agents that specifically target a biomolecule of interest. There are two main classes of targeting agents: small molecules and biologics. Among biologics (e.g.: antibodies), DNA, RNA but al…

Cancer chemotherapyAptamermedicine.medical_treatmentRecombinant Fusion ProteinsPeptide Aptamersheat shock proteinAntineoplastic AgentsComputational biologyPharmacologyBiologyTargeted therapy03 medical and health sciences0302 clinical medicineNeoplasmsmedicineHumansNanotechnologyMolecular Targeted TherapyHeat-Shock Proteins030304 developmental biologyCancer0303 health sciencesClinical Trials as TopicCanceraptamerAntineoplastic Protocolsmedicine.diseasetargeted therapypeptide3. Good healthOncology030220 oncology & carcinogenesisResearch PerspectivesAptamers PeptideOncotarget
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1267 HSP70-2 polymorphism as a risk factor for carotid plaque rupture and cerebral ischaemia in old type 2 diabetes-atherosclerotic patients.

2005

Patients with type 2 diabetes mellitus (NIDDM) are at risk for macrovascular disease complications, such as myocardial infarction (MI) or stroke from plaque rupture. Cytokines play a key role in plaque vulnerability. IFN-gamma inhibits collagen synthesis thereby affecting plaque stability. High IL-6, TNF-alpha, and dyslipidemia are risk factors for thrombosis. Abnormal increments of HSP70 in atherosclerotic plaques might lead to plaque instability and rupture caused by chronic inflammation, which up-regulates the expression of pro-inflammatory cytokines (IL-6 and TNF-alpha) in human monocytes. Studies of a polymorphic PstI site lying in the coding region at position 1267 of the HSP70-2 gene…

Carotid Artery DiseasesMaleAgingmedicine.medical_specialtyGenotypeArteriosclerosisType 2 diabetesGastroenterologyBrain IschemiaInterferon-gammaGene FrequencyRisk FactorsInternal medicinemedicineHumansCarotid StenosisHSP70 Heat-Shock ProteinsMyocardial infarctionRNA MessengerAllelesTriglyceridesMacrovascular diseaseAgedGlycated HemoglobinRupturePolymorphism Geneticbusiness.industryInterleukin-6Tumor Necrosis Factor-alphaType 2 Diabetes MellitusOdds ratioCholesterol LDLMiddle Agedmedicine.diseaseThrombosisEndocrinologyCarotid ArteriesDiabetes Mellitus Type 2Relative riskFemalebusinessDyslipidemiaDevelopmental BiologyMechanisms of ageing and development
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Inhibition of stearoyl-CoA desaturase 1 expression induces CHOP-dependent cell death in human cancer cells.

2010

Background Cancer cells present a sustained de novo fatty acid synthesis with an increase of saturated and monounsaturated fatty acid (MUFA) production. This change in fatty acid metabolism is associated with overexpression of stearoyl-CoA desaturase 1 (Scd1), which catalyses the transformation of saturated fatty acids into monounsaturated fatty acids (e.g., oleic acid). Several reports demonstrated that inhibition of Scd1 led to the blocking of proliferation and induction of apoptosis in cancer cells. Nevertheless, mechanisms of cell death activation remain to be better understood. Principal Findings In this study, we demonstrated that Scd1 extinction by siRNA triggered abolition of de nov…

Cell SurvivalEukaryotic Initiation Factor-2lcsh:MedicineApoptosisCHOPBiologyCell Biology/Cell SignalingCell Linechemistry.chemical_compoundCell Line TumorNeoplasmsHumansRNA Small Interferinglcsh:ScienceEndoplasmic Reticulum Chaperone BiPFatty acid synthesisHeat-Shock ProteinsCell ProliferationTranscription Factor CHOPMultidisciplinaryFatty acid metabolismCell DeathCell growthFatty Acidslcsh:RCell Biology/Cellular Death and Stress ResponsesMolecular biologyCell biologychemistryOncologyApoptosisCancer celllipids (amino acids peptides and proteins)lcsh:QStearoyl-CoA desaturase-1Stearoyl-CoA DesaturaseTranscription Factor CHOPResearch ArticleOleic AcidPLoS ONE
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PTHrP [67-86] regulates the expression of stress proteins in breast cancer cells inducing modifications in urokinase-plasminogen activator and MMP-1 …

2003

It was previously reported that a midregion domain of parathyroid hormone-related protein (PTHrP), that is, [67-86]-amide, is able to restrain growth and promote matrigel penetration by the 8701-BC cell line, derived from a biopsy fragment of a primary ductal infiltrating carcinoma of the human breast, and that cell invasion in vitro is drastically impaired by inactivation of urokinase-plasminogen activator (uPa). In this study we started a more detailed investigation of the possible effects on gene expression arising from the interaction between PTHrP [67-86]-amide and 8701-BC breast cancer cells by a combination of conventional-, differential display-and semi-quantitative multiplex-polyme…

CellBreast NeoplasmsBiologyHeat Shock Transcription FactorsDownregulation and upregulationCell Line TumorHeat shock proteinmedicineHumansNeoplasm InvasivenessHSP90 Heat-Shock ProteinsEnzyme InhibitorsHSF1Heat-Shock ProteinsMatrigelActivator (genetics)CarcinomaParathyroid Hormone-Related ProteinCell BiologyOligonucleotides AntisenseUrokinase-Type Plasminogen ActivatorMolecular biologyPeptide FragmentsProtein Structure TertiaryUp-RegulationDNA-Binding ProteinsGene Expression Regulation NeoplasticHeat shock factormedicine.anatomical_structureCell cultureCancer researchFemaleQuercetinMatrix Metalloproteinase 1Transcription FactorsJournal of Cell Science
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HSP60 expression during carcinogenesis: a molecular “Proteus” of carcinogenesis?

2005

Sir, I read with much interest the comprehensive review by Ciocca and Calderwood (2005) in which they analyze the diagnostic, prognostic, predictive, and treatment values of a number of Hsps in oncology. Concerning the implications of Hsps in cancer diagnosis in particular, they report that since “Hsps are overexpressed in a wide range of malignant cells and tissues … Hsp detection is not useful in diagnostic immunopathology.” Nevertheless, “Hsp expression levels can help indicate the presence of abnormal changes during the process of carcinogenesis.” The authors support this remark by reference to several papers by our group (Cappello et al 2002–2003, 2003a, 2003b, 2003c) in which we demon…

Cellular differentiationBiologymedicine.disease_causeBioinformaticsBiochemistryAdjuvants ImmunologicNeoplasmsGene expressionmedicineAnimalsHumansNeoplasmHeat-Shock ProteinsCancerCell BiologyHsp60Prognosismedicine.diseaseSquamous metaplasiaImmune SystemLetter from the EditorCancer researchBiomarker (medicine)HSP60CarcinogenesisCell Stress & Chaperones
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The Role of the Heme Oxygenase System in the Metabolic Syndrome

2014

Molecular chaperones and the heat shock response play a major role in the maintenance of cellular homeostasis under various pathological conditions. In particular, their role is to regulate protein conformation, protect proteins from misfolding and aggregation, and maintain signalling and organellarnetworks. Among variousheat shock proteins, Hsp32 also known as heme oxygenase-1 (HO-1), has demonstrated an important role in metabolic syndrome. In particular, the HO system seems to play a major role in the complex pathophysiological cascade involved in insulin resistance mechanisms, and adipocyte functions as measured by the release of important adipokynes. The aim of the present review is to…

Cellular homeostasisBiologychemistry.chemical_compoundProtein structureInsulin resistanceDrug DiscoverymedicineHumansMetabolic syndrome heme oxygenase insulin sensitivity adiponectin heat shock proteins.Heat shockHemeHeat-Shock ProteinsMetabolic SyndromePharmacologySettore BIO/16 - Anatomia Umanamedicine.diseaseCell biologyHeme oxygenasechemistryBiochemistryShock (circulatory)Insulin Resistancemedicine.symptomMetabolic syndromeHeme Oxygenase-1Molecular Chaperones
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Melanoma-Reactive Class I-Restricted Cytotoxic T Cell Clones Are Stimulated by Dendritic Cells Loaded with Synthetic Peptides, but Fail to Respond to…

2003

Abstract Immunization with heat shock proteins (hsp) isolated from cancer cells has been shown to induce a protective antitumor response. The mechanism of hsp-dependent cellular immunity has been attributed to a variety of immunological activities mediated by hsp. Hsp have been shown to bind antigenic peptides, trim the bound peptides by intrinsic enzymatic activity, improve endocytosis of the chaperoned peptides by APCs, and enhance the ability of APCs to stimulate peptide-specific T cells. We have investigated the potential capacity of hsp70 and gp96 to function as a mediator for Ag-specific CTL stimulation in an in vitro model for human melanoma. Repetitive stimulation of PBLs by autolog…

Cellular immunityT cellImmunologyAntigen-Presenting CellsEpitopes T-LymphocyteBiologyLymphocyte ActivationEpitopeInterferon-gammaMART-1 AntigenAntigenAntigens NeoplasmCell Line TumorHLA-A2 AntigenmedicineHumansImmunology and AllergyCytotoxic T cellHSP70 Heat-Shock ProteinsLymphocyte CountAntigen-presenting cellMelanomaHeat-Shock ProteinsCell Line TransformedAntigen PresentationMonophenol MonooxygenaseDendritic CellsMolecular biologyCoculture TechniquesClone CellsNeoplasm ProteinsUp-RegulationCTL*medicine.anatomical_structureCancer cellK562 CellsPeptidesT-Lymphocytes CytotoxicThe Journal of Immunology
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Stimulation of synovial fluid mononuclear cells with the human 65-kD heat shock protein or with live enterobacteria leads to preferential expansion o…

1992

SUMMARY T lymphocyte responses to heterologous or self 65-kD heat shock protein (hsp) have been implicated in the pathogenesis of various forms of arthritis. To delineate the relationship of 65-kD hsp to different synovial fluid (SF) T cell subsets, we stimulated synovial fluid (SFMC) and peripheral blood mononuclear cells (PBMC) from patients with different inflammatory rheumatic diseases and from healthy controls with human or mycobacterial 65-kD hsp, tetanus toxoid (TT), heat-killed or live Yersinia enterocotitica. Phenotyping of the resulting T cell lines revealed an increase of up to 97% TCR-γδ+ lymphocytes in the 65-kD hsp-stimulatcd SF-derived lines. This expansion of TCR-γδ+ cells w…

Cellular immunityT cellReceptors Antigen T-Cell alpha-betaT-LymphocytesImmunologyBiologyYersiniaLymphocyte ActivationPeripheral blood mononuclear cellMonocytesCell LineAntigenEnterobacteriaceaeHeat shock proteinSynovial FluidmedicineImmunology and AllergySynovial fluidHumansHeat-Shock ProteinsReceptors Antigen T-Cell gamma-deltaT lymphocytebiology.organism_classificationClone Cellsmedicine.anatomical_structurePhenotypeImmunologyResearch Article
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