Search results for "HSP60"

showing 10 items of 160 documents

L'hsp60 e l'hsp10 sono iperespresse durante la cancerogenesi prostatica

2003

Prostata hsp60 hsp10
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Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.

2020

The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial−mesenchymal transition and, alteration of protein homeostasis. In the tumors of the brain, proteotoxic stress represents one of the main triggering agents for cell transformation. Curcumin is a natural compound with anti-inflammatory and anti-cancer properties with promising potential for the development of therapeutic drugs for the treatment of cancer as well as neurodegenerative diseases. Among the mediators of cancer development, HSP60 is a key factor for the maintenance of…

Protein FoldingCurcuminCell SurvivalCellCatalysisMalignant transformationCell Linelcsh:ChemistryInorganic ChemistryMitochondrial Proteinschemistry.chemical_compoundNeuroblastomaDownregulation and upregulationHeat shock proteinmedicinepost-translational modificationsHumansSecretionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCell ProliferationHeat shock proteinDose-Response Relationship DrugCommunicationOrganic Chemistrymolecular chaperonesUbiquitinationGeneral MedicineChaperonin 60Computer Science ApplicationsCell biologyUp-RegulationBrain tumorGene Expression Regulation Neoplasticmedicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999chemistryApoptosisheat shock proteinsMolecular chaperoneCurcuminbrain tumorsHSP60Post-translational modificationHSP60extracellular HSP60International journal of molecular sciences
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Molecular Chaperones and Thyroid Cancer

2021

Thyroid cancers are the most common of the endocrine system malignancies and progress must be made in the areas of differential diagnosis and treatment to improve patient management. Advances in the understanding of carcinogenic mechanisms have occurred in various fronts, including studies of the chaperone system (CS). Components of the CS are found to be quantitatively increased or decreased, and some correlations have been established between the quantitative changes and tumor type, prognosis, and response to treatment. These correlations provide the basis for identifying distinctive patterns useful in differential diagnosis and for planning experiments aiming at elucidating the role of t…

QH301-705.5thyroid tumorsHsp90Reviewmedicine.disease_causeCatalysisChaperoninHsp70Inorganic ChemistryHsp27chaperone systemdifferential diagnosismedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsThyroid NeoplasmsBiology (General)Physical and Theoretical ChemistryHsp27QD1-999Molecular BiologyThyroid cancerSpectroscopychaperonotherapybiologychaperonopathies by mistakeOrganic ChemistryThyroidmolecular chaperonesChaperonin 60General Medicinemedicine.diseaseHsp60Hsp90Computer Science ApplicationsChemistrymedicine.anatomical_structureChaperone (protein)biology.proteinCancer researchHSP60CarcinogenesisInternational Journal of Molecular Sciences
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A novel copper compound, CuNV110, induces apoptosis in tumor cells by dissociation of the Hsp60- pro-caspase 3 complex

2015

The biological activity of CuNV1110, a novel copper chemical compound, has been recently studied on cancer cells and it has been showed that it reduces the cell viability, in a dose and time dependent manner, and induces cell apoptosis. In this study we evaluated the possible mechanisms by which CuNV1110 induces cell apoptosis. In particular we looked at its effects on Hsp60 levels and caspase 3 activation. We used an in vitro model of a pulmonary mucoepidermoid carcinoma (NCI-H292 cells). We found that CuNV1110 reduces the cell viability and induces cell apoptosis in a dose/time dependent manner. Then, we found that Hsp60 levels decrease with the increasing concentrations of CuNV110; by co…

Respiratory cells; pulmonary cancer; Hsp60; caspase 3; apoptosis.Respiratory cells pulmonary cancer Hsp60 caspase 3 apoptosis
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Heat Shock Protein-60 and Risk for Cardiovascular Disease

2011

Cardiovascular disease (CVD) is a leading cause of morbidity and mortality worldwide. There is growing evidence that molecularchaperones, many of which are heat shock proteins HSPs, are involved in CVD pathogenesis. In this review we focus on HSP60,the human mitochondrial chaperone that also displays extramitochondrial and extracellular functions. HSP60 is typically cytoprotectivebut a number of stress conditions determine its conversion to a potentially toxic molecule for cells and tissues. We present illustrative examplesof specific subtypes of CVD where HSP60 is implicated in the initiation and/or progression of disease. The data not only indicatea pathogenic role for HSP60 but also its …

Riskanimal structuresChaperonin Heat shock protein-60 cardiomyocytes heart failure cardiovascular diseases atherosclerosisChaperonin heat shock protein 60 cardiomyocytes heart failure cardiovascular disease atherosclerosis apoptosis microRNAs (miRs) diabetes Atrial fibrillationApoptosischemical and pharmacologic phenomenaDiseaseBioinformaticsAutoimmune DiseasesPathogenesisHeat shock proteinAtrial FibrillationDrug DiscoveryExtracellularAnimalsHumansMyocytes CardiacHeart FailurePharmacologybiologyfungiChaperonin 60AtherosclerosisResponse to treatmentCardiovascular DiseasesReperfusion InjuryChaperone (protein)HypertensionImmunologybiology.proteinHSP60Stress conditionsBiomarkersCurrent Pharmaceutical Design
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Hsp60 and human aging: Les liaisons dangereuses 

2013

Stressors can cause abnormal intracellular accumulation of Hsp60 and its localization in extramitochondrial sites, secretion, and circulation, with immune system activation. Dysfunction of chaperones associated with their quantitative and qualitative decline with aging (chaperonopathies of aging) characterizes senescence and is a potential causal factor in the physiological deterioration that occurs with it. The role of Hsp60 in aging is not easy to elucidate, because aging is accompanied by pathologies (e.g., cardiovascular and neurodegenerative disorders, osteoporosis, diabetes, cancer, etc.) in which Hsp60 has been implicated but, although those disorders are more frequent in the elderly…

SenescenceAginganimal structuresOsteoporosischemical and pharmacologic phenomenaInflammationDiseaseBiologycomplex mixturesMitochondrial ProteinsPathogenesisImmune systemDiabetes mellitusmedicineHumansCellular SenescenceAutoantibodiesHeart FailurefungiHSP 60 AGING CHAPERONES.Neurodegenerative DiseasesChaperonin 60Atherosclerosismedicine.diseaseMitochondriaImmune SystemImmunologyHSP60Arthropathy Neurogenicmedicine.symptomFrontiers in Bioscience
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Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

SenescencebiologyGeneral NeuroscienceGeneral Biochemistry Genetics and Molecular BiologyCell biologyCo-chaperoneImmune systemHistory and Philosophy of ScienceChaperone (protein)biology.proteinProtein foldingHSP60Functional declineReceptorAnnals of the New York Academy of Sciences
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Is chlamydial heat shock protein 60 a risk factor for oncogenesis?

2004

Heat shock protein 60 (HSP60) plays an important role in the protein folding of prokaryotic and eukaryotic cells. Most of the papers published on chlamydial HSP60 concern its role in immune response during infection. In the last decade, exposure to Chlamydia trachomatis has been consistently associated with the development of cervical and ovarian cancer. Moreover, it has been suggested that chlamydial HSP60 may have an anti- apoptotic effect during persistent infection. We hypothesize that the accumulation of exogenous chlamydial HSP60 in the cytoplasm of actively replicating eukaryotic cells may interfere with the regulation of the apoptotic pathway. The concomitant expression of viral onc…

Senescencechlamydia hsp60Genital Neoplasms Femalechemical and pharmacologic phenomenaApoptosisChlamydia trachomatisBiologymedicine.disease_causeCellular and Molecular NeuroscienceImmune systemBacterial ProteinsRisk FactorsHeat shock proteinmedicineHumansNeoplastic transformationMolecular BiologyPharmacologyCell BiologyChaperonin 60Chlamydia InfectionsCell biologyCell Transformation NeoplasticApoptosisImmunologyMolecular MedicineHSP60FemaleCarcinogenesisChlamydia trachomatis
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A comparative analysis of the products of GROEL-1 gene fromChlamydia trachomatisserovar D and the HSP60 var1 transcript fromHomo sapienssuggests a po…

2009

Summary Chlamydia trachomatis serovar D produces large quantities of HSP60-1 during infections, which accumulate inside the host cell inducing autoimmunity. We compare the aminoacid sequences of the human HSP60 with the bacterial counterpart to better elucidate how CTHSP60 may simulate HSP60 from human origin during infection and may induce an autoimmune response. As a result of the comparison we suggest several possible epitopes of the CTHSP60, which may induce autoimmunity.

Serotypeanimal structuresTranscription GeneticMolecular Sequence DataImmunologyAutoimmunityChlamydia trachomatischemical and pharmacologic phenomenaBiologymedicine.disease_causecomplex mixturesEpitopeAutoimmunityGeneticsmedicineHumansAmino Acid SequenceMolecular BiologyGeneGenetics (clinical)GeneticsBase SequencefungiChaperonin 60General MedicineChlamydia InfectionsHsp60 Chlamydia trachomatisGroELHomo sapiensHSP60Chlamydia trachomatisSequence AlignmentInternational Journal of Immunogenetics
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THE ROLE OF HSP60 IN AMYLOID BETA PATHWAY: RELEVANCE TO ALZHEIMER’S DISEASE

Alzheimer’s disease (AD) is a devastating neurodegenerative disorder affecting more than 40 million individuals worldwide. The high number of factors triggering the onset of AD justifies the current absence of disease-modifying therapies. The involved pathological mechanisms are still elusive and, therefore, the finding of effective therapies requires further elucidation of biomolecular mechanisms controlling AD pathogenesis. Particularly, the aberrant amyloidogenic cleavage of amyloid precursor protein (APP), amyloid beta (Aβ) peptide misfolding and oligomerization, and the impairment of the protein quality control machinery are key hallmarks characterizing the onset of the disease. Furthe…

Settore BIO/16 - Anatomia UmanaAmyloid beta peptideaggregationchaperoneAlzheimer's diseaseHsp60misfolding7PA2
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