Search results for " chaperonotherapy"

showing 10 items of 12 documents

Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy.

2008

Hsp60 in eukaryotes is considered typically a mitochondrial chaperone (also called Cpn60) but in the last few years it has become clear that it also occurs in the cytosol, the cell surface, the extracellular space, and in the peripheral blood. Studies with prokaryotic models have shown that Hsp60 plays a role in assisting nascent polypeptides to reach a native conformation, and that it interacts with Hsp10 (which also resides in the mitochondria and is also named Cpn10). In addition to its role in polypeptide folding in association with Hsp10, other functions and interacting molecules have been identified for Hsp60 in the last several years. Some of these newly identified functions are asso…

MalechaperoninCancer ResearchProtein Foldinganimal structuresChaperoninsCell SurvivalCelldifferential diagnosiGene ExpressionAntineoplastic AgentsApoptosisBiologyMitochondrionmedicine.disease_causeBioinformaticsDiagnosis Differentialtumor-cell survivalCell Line TumorNeoplasmstumor diagnosiExtracellularmedicineHumansHsp60 (Cpn60)chaperonotherapyPharmacologyClinical Oncologymonitoring response to treatmentanti-tumor immune responsefungiHsp60 (Cpn60); tumor-cell survival; apoptosis; tumor diagnosis; differential diagnosis; assessing prognosis; monitoring response to treatment; chaperonotherapy; anti-tumor immune response; chaperonin; protein foldingassessing prognosiChaperonin 60PrognosisapoptosiCell biologyCytosolmedicine.anatomical_structureOncologyChaperone (protein)biology.proteinMolecular MedicineHSP60FemaleCarcinogenesisSignal TransductionCancer biologytherapy
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Chaperonology: A novel research field for experimental medicine in the XXI century.

2007

Settore BIO/16 - Anatomia Umanachaperones chaperonins hsp60 hsp10 chaperonopathies chaperonotherapy
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Alzheimer's Disease and Molecular Chaperones: Current Knowledge and the Future of Chaperonotherapy

2016

Background: Alzheimer’s disease (AD) is a dementia, a neurodegenerative condition, and a protein-misfolding disease or proteinopathy, characterized by protein deposits, extracellular plaques and intracellular neurofibrillary tangles, which contain the AD’s typical pathological proteins, abnormal [1]-amyloid and hyperphosphorylated tau, respectively, and are located predominantly in the cortex of the frontal, parietal, and temporal brain lobes. What is the role of molecular chaperones in AD? Data indicate that molecular chaperones, also known as Hsp, are involved in AD, probably displaying protective roles and/or acting as pathogenic factors as it occurs in chaperonopathies in which case AD …

0301 basic medicineChaperonotherapyDisease03 medical and health sciencesAlzheimer DiseaseDrug DiscoveryProtein-misfolding diseasemedicineExtracellularAnimalsHumansDementiaAlzheimer’s disease; Chaperonopathies; Chaperonotherapy; Molecular chaperones; Protein-misfolding diseases; Tau; β-amyloid; Pharmacology; Drug Discovery3003 Pharmaceutical ScienceGenePharmacologybiologyβ-amyloidDrug Discovery3003 Pharmaceutical Sciencemedicine.diseaseHsp90030104 developmental biologyChaperone (protein)ImmunologyChaperonopathieMolecular chaperonebiology.proteinHSP60TauAlzheimer’s diseaseNeuroscienceIntracellularMolecular ChaperonesCurrent Pharmaceutical Design
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MOLECULAR CHAPERONES IN HUMAN SALIVARY GLANDS: HSP90 A BIOMARKER IN HEALTH AND DISEASE

2022

Hsp90 biomarkerchaperone systemdifferential diagnosisheat shock proteinnegative chaperonotherapyGanetespibsalivary gland tumor
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Hsp60 chaperonopathies and chaperonotherapy: targets and agents

2014

Hsp60 (Cpn60) assembles into a tetradecamer that interacts with the co-chaperonin Hsp10 (Cpn10) to assist client polypeptides to fold, but it also has other roles, including participation in pathogenic mechanisms.Hsp60 chaperonopathies are pathological conditions, inherited or acquired, in which the chaperone plays a determinant etiologic-pathogenic role. These diseases justify selection of Hsp60 as a target for developing agents that interfere with its pathogenic effects. We provide information on how to proceed.The information available encourages the development of ways to improve Hsp60 activity (positive chaperonotherapy) when deficient or to block it (negative chaperonotherapy) when pa…

InflammationPharmacologyanimal structuresChaperonin 60biologyProtein ConformationfungiClinical BiochemistryChaperonin 60BioinformaticsAutoimmune Diseasesautoimmunity cancer carboranylphenoxyacetanilide chaperonopathies chaperonotherapy chemical compounds Cpn60 electrophilic compounds epolactaene functional domain GroEL Hsp60 inflammation mizoribine structural domainNeoplasmsChaperone (protein)Expert opinionDrug DiscoveryImmunologybiology.proteinAnimalsHumansMolecular MedicineHSP60Cytokine formationA determinantExpert Opinion on Therapeutic Targets
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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 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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Chaperonology: The Third Eye on Brain Gliomas

2018

The European Organization for Research and Treatment of Cancer/National Cancer Institute of Canada Phase III trial has validated as a current regimen for high-grade gliomas (HGG) a maximal safe surgical resection followed by radiotherapy with concurrent temozolamide. However, it is essential to balance maximal tumor resection with preservation of the patient&rsquo

Oncologymedicine.medical_specialtymedicine.medical_treatmentArticlelcsh:RC321-571Third eye03 medical and health sciences0302 clinical medicineHigh-grade gliomaInternal medicinemedicineSurvival ratelcsh:Neurosciences. Biological psychiatry. NeuropsychiatrychaperonotherapychaperonologyNeuroscience (all)neuroimagingHeat shock proteinbusiness.industrySettore BIO/16 - Anatomia UmanaSettore MED/27 - NeurochirurgiaGeneral NeuroscienceChaperonology; Chaperonotherapy; Heat shock proteins; High-grade gliomas; Molecular chaperones; Neuroimaging; Neuromonitoring; Neuroscience (all)molecular chaperonesCancermedicine.diseaseBrain gliomas3. Good healthBrain diseaseNatural historyRadiation therapyRegimen030220 oncology & carcinogenesisheat shock proteinsMolecular chaperonebusinesshigh-grade gliomas030217 neurology & neurosurgeryneuromonitoringBrain 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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Chaperonin Hsp60 and Cancer Therapies

2020

The heat shock protein 60 (Hsp60) is a chaperonin belonging to the chaperoning (chaperone) system that typically contributes to protein homeostasis inside mitochondria, but also plays various non-canonical roles unrelated to protein quality control beyond the organelle. Chaperonopathies are disorders in which chaperones play an etiologic-pathogenic role and contribute to the onset/progression of disease. Hsp60 chaperonopathies by mistake are diseases in which the chaperonin is apparently normal (as far as it can be determined with current methodologies) but it actively contributes to pathology, for example in certain types of cancer, and autoimmune and chronic inflammatory disorders. In cer…

Settore BIO/17 - Istologiabiologybusiness.industryfungiDiseaseTumor initiationMitochondrionMicrovesiclesChaperoninAnticancer chaperonotherapy Biomarker Cancer Chaperonin Chaperoning (chaperone) system Chaperonopathies Exosomes Heat shock proteins Hsp60 Immune response Therapy Tumor VaccineChaperone (protein)Heat shock proteinbiology.proteinCancer researchMedicineHSP60business
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