Search results for "chaperonopathies"

showing 9 items of 29 documents

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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Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated…

2023

Mutations in genes encoding molecular chaperones, for instance the genes encoding the subunits of the chaperonin CCT (chaperonin containing TCP-1, also known as TRiC), are associated with rare neurodegenerative disorders. Using a classical molecular dynamics approach, we investigated the occurrence of conformational changes and differences in physicochemical properties of the CCT5 mutations His147Arg and Leu224Val associated with a sensory and a motor distal neuropathy, respectively. The apical domain of both variants was substantially but differently affected by the mutations, although these were in other domains. The distribution of hydrogen bonds and electrostatic potentials on the surfa…

Settore BIO/16 - Anatomia UmanaOrganic ChemistryCCT5 mutationsGeneral Medicineprotein bindingCatalysisComputer Science ApplicationsInorganic Chemistryelectrostatic potentialCCT5 chaperonopathieschaperone systemhydrogen bondsPhysical and Theoretical ChemistryCCT5Molecular BiologySpectroscopyapical domainSettore CHIM/02 - Chimica Fisica
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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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Muscle Histopathological Abnormalities in a Patient With a CCT5 Mutation Predicted to Affect the Apical Domain of the Chaperonin Subunit.

2022

Recognition of diseases associated with mutations of the chaperone system genes, e.g., chaperonopathies, is on the rise. Hereditary and clinical aspects are established, but the impact of the mutation on the chaperone molecule and the mechanisms underpinning the tissue abnormalities are not. Here, histological features of skeletal muscle from a patient with a severe, early onset, distal motor neuropathy, carrying a mutation on the CCT5 subunit (MUT) were examined in comparison with normal muscle (CTR). The MUT muscle was considerably modified; atrophy of fibers and disruption of the tissue architecture were prominent, with many fibers in apoptosis. CCT5 was diversely present in the sarcolem…

Settore BIO/17 - IstologiaCCT5 neurochaperonopathies chaperonin neurodegenerative diseases neuropathies chaperone system muscle histopathology CCT5 apical domainSettore MED/38 - Pediatria Generale E SpecialisticaSettore BIO/16 - Anatomia UmanaSettore MED/30 - Malattie Apparato VisivoBiochemistry Genetics and Molecular Biology (miscellaneous)Molecular BiologyBiochemistrySettore CHIM/02 - Chimica FisicaFrontiers in molecular biosciences
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GENETIC NEUROCHAPERONOPATHIES ASSOCIATED WITH CCT5 AND HSP60 VARIANTS: ANALYSIS OF THEIR MOLECULAR ANATOMY AND POSSIBLE PATHOGENIC IMPLICATIONS

2022

Settore BIO/17 - IstologiaMISSENSE MUTATIONMITOCHONDRIAPROTEOSTASISMOLECULAR DYNAMICSCHAPERONE SYSTEMCCT5HSP60GENETIC NEUROCHAPERONOPATHIESBIOINFORMATICS ANALYSIS
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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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Role of CD1A and HSP60 in the antitumoral response of oesophageal cancer

2011

Oesophageal cancer (OC) is one of the most common and severe forms of tumor. A wider knowledge of molecular mechanisms which lead to a normal epithelium becoming a neoplasm may reveal new strategies to improve treatment and outcome of this disease. In this review, we report recent findings concerning molecular events which take place during carcinogenesis of the oesophagus. In particular, we focus on the role of two molecules, CD1a and Hsp60, which are overexpressed in oesophageal and many other types of tumor. Both molecules may present tumor antigens and promote in situ the stimulation of an antitumoral immune activity. We suggest there is a synergistic action between these molecules. Fur…

Settore BIO/17 - Istologialcsh:Internal medicineCancer ResearchDiseasemedicine.disease_causeImmune systemAntigenmedicineNeoplasmlcsh:RC31-1245Settore BIO/16 - Anatomia Umanabusiness.industryCancerImmune response - Dendritic cells - Chaperonopathies - Chaperonotherapylcsh:Other systems of medicinemedicine.diseaselcsh:RZ201-999EpitheliumChaperonopathies Chaperonotherapy Dendritic cells Immune responsemedicine.anatomical_structureOncologyImmunologyCancer researchCarcinogenesisbusinessIntracellularOncology Reviews
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Chaperonopathies and chaperonotherapy. Hsp60 as therapeutic target in cancer: potential benefits and risks.

2013

In this minireview we focus on Hsp60 as a target for anticancer therapy. We discuss the new concepts of chaperonopathies and chaperonotherapy and present information on Hsp60 localization in the cell membrane of human tumor cells. We describe novel mechanisms for Hsp60 reaching the extracellular environment that involve membrane-associated stages, as well as data on anti-Hsp60 antibodies found in human sera, both in normal subjects and patients affected by autoimmune diseases. Finally, we discuss possible therapeutic applications of anti-Hsp60 antibodies in cancer treatment, evaluating also side effects on non-tumor cells. In conclusion, the way for investigating Hsp60-targeted anti-tumor t…

animal structuresCellchemical and pharmacologic phenomenaAntineoplastic AgentsBiologycomplex mixturesRisk AssessmentCell membraneDrug Delivery SystemsRisk FactorsNeoplasmsDrug DiscoverymedicineExtracellularAnimalsHumansSecretionPharmacologyMechanism (biology)fungiCancerChaperonin 60medicine.diseasemedicine.anatomical_structureImmunologybiology.proteinCancer researchHsp60 Cpn60 HSPD1 plasma membrane antibodies autoantibodies antitumor immunotherapy anticancer therapy chaperonopathies human sera.HSP60AntibodyCurrent pharmaceutical design
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Editorial: Physiology and Pathophysiology of Heat Shock Protein 60

2020

business.industrypost translational modificationshepatocellular carcinomaacquired chaperonopathieBioinformaticsHsp60Biochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryPathophysiologypost translational modificationlcsh:Biology (General)cardiovascular diseasegenetic chaperonopathieHeat shock proteinPosttranslational modificationMedicineHSP60acquired chaperonopathiesbusinessgenetic chaperonopathieslcsh:QH301-705.5Molecular Biologychaperonotherapy
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