Search results for "HEAT-SHOCK PROTEINS"

showing 10 items of 310 documents

Proliferative response of synovial fluid and peripheral blood mononuclear cells to arthritogenic and non-arthritogenic microbial antigens and to the …

1990

Cellular immune responses to microbial antigens have been implicated in the pathogenesis of some forms of arthritis including reactive arthritis, Reiter's syndrome, ankylosing spondylitis and rheumatoid arthritis. We investigated the proliferative T cell responses of paired peripheral blood (PB) and synovial fluid (SF) mononuclear cells (MC) to so-called arthritogenic bacteria (Yersinia enterocolitica and Salmonella typhimurium), to control antigens, such as Candida albicans, mumps virus and purified protein derivative, to the recombinant mycobacterial 65-kDa heat-shock protein (hsp 65) and the mitogen phytohemagglutinin (PHA) in 16 patients with different inflammatory rheumatic diseases. T…

Salmonella typhimuriumMicrobiology (medical)Antigens FungalT cellImmunologyArthritisInflammationBiologyLymphocyte ActivationPeripheral blood mononuclear cellEpitopeImmune systemEnterobacteriaceaeAntigenCandida albicansSynovial FluidmedicineHumansImmunology and AllergySynovial fluidPhytohemagglutininsHeat-Shock ProteinsYersinia enterocoliticaAntigens BacterialArthritisGeneral Medicinemedicine.diseasemedicine.anatomical_structureImmunologyLeukocytes Mononuclearmedicine.symptomMedical Microbiology and Immunology
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Localization of HSP70, Cdc2, and cyclin B in sea urchin oocytes in non-stressed conditions.

2003

In Paracentrotus lividus embryos, a Mediterranean sea urchin species, HSP70 is present in all the cells. During cell division it localizes under normal growth conditions on the centrosomes and on the whole isolated mitotic apparatus. Now, in situ hybridization, Western blot analyses, and immunohistochemistry show that the HSP70 mRNA is present in both small and large P. lividus oocytes, that all four isoforms of HSP70 can be found also in the oocytes, and that a certain amount of HSP70 localizes on asters and spindles during polar body formation. Moreover, two representative cell-cycle related proteins, cyclin B, and Cdc2, are present both in small and large oocytes, concentrating in the ge…

Sea urchinCell divisionBlotting WesternBiophysicsCyclin BCdc2In situ hybridizationCyclin BBiochemistryParacentrotus lividusPolar bodybiology.animalCDC2 Protein KinaseAnimalsProtein IsoformsHSP70 Heat-Shock ProteinsRNA MessengerSea urchinMolecular BiologyHSP70In Situ HybridizationCyclin-dependent kinase 1biologyOvaryCell Biologybiology.organism_classificationMolecular biologyImmunohistochemistryCell biologyOogenesiBiophysicCytoplasmSea Urchinsbiology.proteinOocytesElectrophoresis Polyacrylamide GelFemaleCell DivisionBiochemical and biophysical research communications
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The dual role of p53: DNA protection and antioxidant.

2011

The classical functions of p53 protein are those related to its role on DNA damage, cell growth arrest, senescence and apoptosis. For this reason it is called 'the guardian of the genome' and is considered one of the most important players in the development of cancer. However, more recently it has been show that p53 is not only involved in cancer, but also in ageing. p53 is stimulated by stress, which in turn results in the activation of a wide range of transcriptional targets. Low-intensity stress will activate p53 in a manner which results in antioxidant response, thus protecting against ageing because of its antioxidant function. On the contrary, high-intensity activation of p53 will re…

SenescenceGenome instabilityDNA protectionAgingDNA damageBiologymedicine.disease_causeBiochemistryAntioxidantsGenomic InstabilityNeoplasmsmedicineAnimalsHumansCellular SenescenceHeat-Shock ProteinsCell growthCell CycleGeneral MedicineCell cycleCell biologyBiochemistryAgeingTumor Suppressor Protein p53Reactive Oxygen SpeciesOxidative stressFree radical research
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Improved acid tolerance of a recombinant strain of Escherichia coli expressing genes from the acidophilic bacterium Oenococcus oeni.

2001

Aims:Oenococcus oeni is a lactic acid bacterium used in wine fermentation. Two open reading frames (orfB and orfC) were identified in the upstream region of the hsp18 gene, encoding the small heat-shock protein Lo18. Expression of these genes in conditions of acid stress was studied in Escherichia coli. Methods and Results: Sequence analysis showed that orfB encodes a putative transcriptional regulator of the LysR family. The protein encoded by orfC shares homologies with multi-drug resistance systems. Heterologous expression of orfB, orfC and hsp18 genes in Escherichia coli significantly enhanced the viability of the host strain under acidic conditions. Conclusions: It was demonstrated tha…

Sequence analysisMolecular Sequence DataRestriction MappingDNA RecombinantGene Expressionmedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyOpen Reading FramesBacterial ProteinsmedicineEscherichia coliAmino Acid SequenceEscherichia coliGeneHeat-Shock ProteinsOenococcus oeniGeneticsbiologyBase Sequencebiology.organism_classificationEnterobacteriaceaeAdaptation PhysiologicalGram-Positive CocciOpen reading frameGenes BacterialHeterologous expressionGenetic EngineeringAcidsOenococcusCell DivisionLeuconostocPlasmidsLetters in applied microbiology
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Effect of sodium dodecyl sulfate (SDS) on stress response in the Mediterranean mussel (Mytilus Galloprovincialis): Regulatory volumedecrease (Rvd) an…

2014

In this study the effects of an anionic surfactant, sodium dodecyl sulfate (SDS), are assessed on the Mediterranean mussel (. Mytilus galloprovincialis), exposed for 18 days at a concentration ranging from 0.1. mg/l to 1. mg/l. The effects are monitored using biomarkers related to stress response, such as regulatory volume decrease (RVD), and to oxidative stress, such as reactive oxygen species (ROS), endogenous antioxidant systems and Hsp70 levels. The results demonstrate that cells from the digestive gland of M. galloprovincialis, exposed to SDS were not able to perform the RVD owing to osmotic stress. Further, SDS causes oxidative stress in treated organisms, as demonstrated by the incre…

Settore BIO/07 - EcologiaAntioxidantOsmotic shockHealth Toxicology and Mutagenesismedicine.medical_treatmentEndogenous antioxidantsMytilus galloprovincialiSDS; Regulatory volume decrease; oxidative stressAquatic Sciencemedicine.disease_causeAntioxidantsSuperoxide dismutasechemistry.chemical_compoundOsmoregulationSettore BIO/10 - BiochimicamedicineAnimalsHSP70 Heat-Shock ProteinsSodium dodecyl sulfateSDS (sodium dodecyl sulfate)Settore BIO/06 - Anatomia Comparata E Citologiachemistry.chemical_classificationMytilusReactive oxygen speciesbiologySodium Dodecyl SulfateMolecular biologyOxidative StresschemistryBiochemistryCatalasebiomarkers of oxidative strebiology.proteinOsmoregulationCell volume regulationReactive Oxygen SpeciesOxidative stressBiomarkersWater Pollutants Chemical
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The Chaperone System in Breast Cancer: Roles and Therapeutic Prospects of the Molecular Chaperones Hsp27, Hsp60, Hsp70, and Hsp90

2022

Breast cancer (BC) is a major public health problem, with key pieces of information needed for developing preventive and curative measures still missing. For example, the participation of the chaperone system (CS) in carcinogenesis and anti-cancer responses is poorly understood, although it can be predicted to be a crucial factor in these mechanisms. The chief components of the CS are the molecular chaperones, and here we discuss four of them, Hsp27, Hsp60, Hsp70, and Hsp90, focusing on their pro-carcinogenic roles in BC and potential for developing anti-BC therapies. These chaperones can be targets of negative chaperonotherapy, namely the elimination/blocking/inhibition of the chaperone(s)…

Settore BIO/16 - Anatomia UmanaCarcinogenesisOrganic ChemistryHSP27 Heat-Shock ProteinsBreast NeoplasmsChaperonin 60General MedicineCatalysisComputer Science ApplicationsInorganic ChemistryHumansbreast cancer chaperone system Hsp inhibitors Hsp27Hsp60Hsp70Hsp90 molecular chaperones immunotherapy negative chaperonotherapyCarcinogenesisFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologySpectroscopyInternational Journal of Molecular Sciences
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The Chaperone System in Salivary Glands: Hsp90 Prospects for Differential Diagnosis and Treatment of Malignant Tumors

2022

Salivary gland tumors represent a serious medical problem and new tools for differential diagnosis and patient monitoring are needed. Here, we present data and discuss the potential of molecular chaperones as biomarkers and therapeutic targets, focusing on Hsp10 and Hsp90. The salivary glands are key physiological elements but, unfortunately, the information and the means available for the management of their pathologies, including cancer, are scarce. Progress in the study of carcinogenesis has occurred on various fronts lately, one of which has been the identification of the chaperone system (CS) as a physiological system with presence in all cells and tissues (including the salivary gland…

Settore BIO/16 - Anatomia UmanaOrganic ChemistryAntineoplastic AgentsGeneral MedicineSettore MED/08 - Anatomia PatologicaSalivary Gland NeoplasmsSalivary GlandsCatalysisComputer Science ApplicationsDiagnosis DifferentialInorganic ChemistryHumanschaperone system differential diagnosis Ganetespib Hsp90 Hsp90 biomarker Hsp90 pathogenic negative chaperonotherapysalivary gland tumors Diagnosis Differential Humans Molecular Chaperones Salivary Glands Antineoplastic Agents Salivary Gland NeoplasmsHSP90 Heat-Shock ProteinsPhysical and Theoretical Chemistrysalivary gland tumors; chaperone system; Hsp90; Hsp90 pathogenic; negative chaperonotherapy; Ganetespib; Hsp90 biomarker; differential diagnosisMolecular BiologySpectroscopyMolecular Chaperones
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Hsp27 and Hsp60 in human submandibular salivary gland: Quantitative patterns in healthy and cancerous tissues with potential implications for differe…

2021

Tumors of the submandibular salivary gland (SMG) are uncommon but sufficiently frequent for the physician to consider them in routine examinations and for the pathologist to be prepared to differentiate them from other tissue abnormalities. However, scarcity of specimens makes training difficult, a situation compounded by the lack of accepted universal diagnostic guidelines. Furthermore, there is little information on the chaperone system (CS) of the gland, despite the increasing evidence of its participation in carcinogenesis as a biomarker for diagnosis and patient follow up, and in the mechanisms by which the tumor cells thrive. We are investigating this aspect of various tumors, and her…

Settore BIO/17 - IstologiaMalePathologymedicine.medical_specialtyHistologyCarcinogenesisAdenoid cystic carcinomaSubmandibular GlandHsp27 Hsp60 Pleomorphic adenoma Submandibular salivary glandAdenoid cystic carcinomamedicine.disease_causeDiagnosis DifferentialMitochondrial ProteinsPleomorphic adenomaHsp27Biomarkers TumormedicineHumansHeat-Shock ProteinsSalivary glandbiologySettore BIO/16 - Anatomia Umanabusiness.industryChaperonin 60Cell BiologyGeneral Medicinemedicine.diseaseNeoplasm ProteinsSubmandibular Gland Neoplasmsmedicine.anatomical_structurebiology.proteinBiomarker (medicine)ImmunohistochemistryChaperone systemFemaleDifferential diagnosisbusinessCarcinogenesisMolecular ChaperonesActa Histochemica
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Tumor protein 53-induced nuclear protein 1 expression is repressed by miR-155, and its restoration inhibits pancreatic tumor development.

2007

Pancreatic cancer is a disease with an extremely poor prognosis. Tumor protein 53-induced nuclear protein 1 ( TP53INP1 ) is a proapoptotic stress-induced p53 target gene. In this article, we show by immunohistochemical analysis that TP53INP1 expression is dramatically reduced in pancreatic ductal adenocarcinoma (PDAC) and this decrease occurs early during pancreatic cancer development. TP53INP1 reexpression in the pancreatic cancer-derived cell line MiaPaCa2 strongly reduced its capacity to form s.c., i.p., and intrapancreatic tumors in nude mice. This anti-tumoral capacity is, at least in part, due to the induction of caspase 3-mediated apoptosis. In addition, TP53INP1 −/− mouse embryonic…

Settore MED/06 - Oncologia MedicaTransplantation HeterologousGene ExpressionMice NudeMicePancreatic tumorPancreatic cancerCell Line TumormicroRNAGene expressionmedicineAnimalsHumansRNA NeoplasmNuclear proteinCaspaseHeat-Shock ProteinsMice KnockoutMultidisciplinarybiologyBase Sequenceapoptosis pancreatic cancer ponasterone A tumor suppressor micro RNANuclear ProteinsBiological Sciencesmedicine.diseaseTransplantationPancreatic NeoplasmsMicroRNAsCell Transformation NeoplasticApoptosisCancer researchbiology.proteinTumor Suppressor Protein p53Carrier ProteinsNeoplasm TransplantationCarcinoma Pancreatic DuctalProceedings of the National Academy of Sciences of the United States of America
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HSP-MOLECULAR CHAPERONES IN CANCER BIOGENESIS AND TUMOR THERAPY: AN OVERVIEW

2012

Molecular chaperones, many of which are heat-shock proteins (HSPs), are an important class of molecules with various functions. Pathological conditions in which chaperones become etiological and/or pathogenic factors are called chaperonopathies, and are classified into by defect, by excess, and by "mistake". In the latter case, the chaperone is structurally and functionally normal but paqrtecipates in pathwais that favor diseases, aòlthough in some cases the chaperone may have post-translational modifications that may lead it to change its location and function and, thus, to become pathogenic. For example, HSP-chaperones are involved in acrcinogenesis in various ways, so that some forms of …

Settore MED/18 - Chirurgia GeneraleCell Transformation NeoplasticSettore MED/09 - Medicina InternaSettore BIO/16 - Anatomia UmanaNeoplasmsmolecular chaperones chapoeronig system chaperonology chaperonopathy by mistake cancer HSP60 chaperonin chaperonopathy.AnimalsHumansMolecular Targeted TherapyCancer VaccinesHeat-Shock Proteins
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