Search results for "chaperoning system"

showing 8 items of 8 documents

Molecular chaperones in tumors of salivary glands.

2020

The salivary glands are key components of the mouth and play a central role in its physiology. Their importance may be appreciated considering their number, occurrence in pairs, and distribution in the mouth: two parotids, two submandibular, two sublingual, and many other small ones scattered throughout the mouth. They produce saliva, without which ingestion of non-liquid nutrients and speech would be practically impossible. Nevertheless, the physiology and pathology of salivary glands are poorly understood. For instance, tumors of salivary glands occur, and their incidence is on the rise, but their etiology and pathogenesis are virtually unknown, although some risk factors have been identi…

0301 basic medicineSalivaHistologyPhysiologyDifferential diagnosiBiologyBioinformaticsmedicine.disease_causePathogenesis03 medical and health sciencesstomatognathic systemmedicineHSPAnimalsHumansEndoplasmic Reticulum Chaperone BiPTumorsSalivary glandTumorigenesiChaperoning system030102 biochemistry & molecular biologySalivary glandCell BiologyGeneral MedicineSalivary Gland Neoplasms030104 developmental biologymedicine.anatomical_structureCell Transformation NeoplasticChaperone (protein)Etiologybiology.proteinMolecular chaperoneBiomarker (medicine)Disease SusceptibilityDifferential diagnosisCarcinogenesisMolecular ChaperonesJournal of molecular histology
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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…

AgingProtein Foldingchaperonopathies by mistakeSettore BIO/16 - Anatomia Umanachaperoning systemImmune Systemchaperoning system interactionchaperonopathieCarrier Proteinschaperonotherapy Hsp60Molecular ChaperonesAnnals of the New York Academy of Sciences
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Depleted uranium induces human carcinogenesis involving the immune and chaperoning systems: Realities and working hypotheses

2019

Abstract Cancer is caused by a combination of factors, genetic, epigenetics and environmental. Among the latter, environmental pollutants absorbed by contact, inhalation, or ingestion are major proven or suspected culprits. Depleted uranium (DU) is one of them directly pertinent to the military and civilians working in militarized areas. It is considered a weak carcinogen but its implication in cancer development in exposed individuals is supported by various data. Since not all subjects exposed to DU develop cancer, it is likely that DU-dependent carcinogenesis requires cofactors, such as genetic predisposition and deficiencies of the chaperoning and immune systems. It is of the essence to…

0301 basic medicineNeoplasms Radiation-InducedCarcinogenesisNatural killer cellPreventive measureWorking hypothesisBioinformaticsmedicine.disease_causeRisk AssessmentEpigenesis Genetic03 medical and health sciences0302 clinical medicineImmune systemOccupational ExposureGenetic predispositionmedicineHumansBone marrowDepleted uraniumSkinAir PollutantsChaperoning systemCarcinogenic cofactorbusiness.industryGenetic predispositionMicrobiotaMedicine (all)CancerEnvironmental ExposureGeneral MedicineArmed ConflictsModels Theoreticalmedicine.diseaseEnvironmental pollutantMilitary PersonnelImmune system030104 developmental biologyCarcinogensMolecular chaperoneUraniumEnvironmental PollutantsCancer developmentCarcinogenesisbusiness030217 neurology & neurosurgeryMolecular ChaperonesMedical Hypotheses
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Missense Mutations of Human Hsp60: A Computational Analysis to Unveil Their Pathological Significance

2020

Two chaperonopathies have been linked to mutations in the human hsp60 (hHsp60; HSPD1) gene, but other existing variants might cause diseases, even if there is no comprehensive information about this possibility. To fill this vacuum, which might be at the basis of misdiagnoses or simply ignorance of chaperonopathies in patients who would benefit by proper identification of their ailments, we searched the sequenced human genomes available in public databases to determine the range of missense mutations in the single hsp60 gene. A total of 224 missense mutations were identified, including those already characterized. Detailed examination of these mutations was carried out to assess their possi…

0301 basic medicineHsp60 gene variantlcsh:QH426-470chaperoning systemMutantunderdiagnosed chaperonopathiesDiseaseBiology03 medical and health sciences0302 clinical medicinehuman genomeGeneticsMissense mutationGeneGenetics (clinical)Hsp60 genetic chaperonopathieOriginal ResearchGeneticschemistry.chemical_classificationHsp60 genetic chaperonopathieshuman genomesHsp60 gene variantsAmino acidlcsh:Genetics030104 developmental biologychemistry030220 oncology & carcinogenesisMolecular MedicineHSP60Human genomeIdentification (biology)Frontiers in Genetics
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A Novel CCT5 Missense Variant Associated with Early Onset Motor Neuropathy

2020

Diseases associated with acquired or genetic defects in members of the chaperoning system (CS) are increasingly found and have been collectively termed chaperonopathies. Illustrative instances of genetic chaperonopathies involve the genes for chaperonins of Groups I (e.g., Heat shock protein 60, Hsp60) and II (e.g., Chaperonin Containing T-Complex polypeptide 1, CCT). Examples of the former are hypomyelinating leukodystrophy 4 (HLD4 or MitCHAP60) and hereditary spastic paraplegia (SPG13). A distal sensory mutilating neuropathy has been linked to a mutation [p.(His147Arg)] in subunit 5 of the CCT5 gene. Here, we describe a new possibly pathogenic variant [p.(Leu224Val)] of the same subunit b…

Mutation.Hereditary spastic paraplegiaProtein subunitchaperoning systemMutation MissenseBiologyMolecular Dynamics Simulationmedicine.disease_causeCatalysisArticleChaperoninInorganic Chemistrylcsh:ChemistryHeat shock proteinmedicineMissense mutationHumansPhysical and Theoretical Chemistrymotor neuropathyAge of OnsetGenetic variantMolecular BiologyGenelcsh:QH301-705.5SpectroscopyExome sequencingMyelin SheathGenetic chaperonopathieGeneticsMutationgenetic variantsOrganic ChemistryInfant NewbornGeneral Medicinemedicine.diseasePhenotypeComputer Science ApplicationsCCT5; chaperoning system; chaperonins; genetic chaperonopathies; genetic variants; motor neuropathy; mutationPhenotypelcsh:Biology (General)lcsh:QD1-999chaperoninsFemaleCCT5mutationHereditary Sensory and Motor Neuropathygenetic chaperonopathiesChaperonin Containing TCP-1International Journal of Molecular Sciences
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Hsp60 as a Novel Target in IBD Management: A Prospect

2019

Inflammatory bowel disease (IBD) encompasses various pathological conditions similar but distinct that share a multifactorial etiology, including involvement of the intestinal barrier function, the immune system, and intestinal microorganisms. Hsp60 is a chaperonin component of the chaperoning system, present in all cells and tissues, including the intestine. It plays important roles in cell physiology outside and inside mitochondria, its canonical place of residence. However, Hsp60 can also be pathogenic in many conditions, the Hsp60 chaperonopathies, possibly including IBD. The various clinico-pathological types of IBD have a complicated mix of causative factors, among which Hsp60 can be …

0301 basic medicineColorectal cancerMini Reviewchaperoning systemDiseaseBioinformaticsInflammatory bowel diseasePathogenesis03 medical and health sciences0302 clinical medicineImmune systemintestinal wallinflammatory bowel diseasemedicinemicrobiotaPharmacology (medical)PathologicalchaperonotherapyPharmacologybusiness.industrylcsh:RM1-950fungimedicine.diseaseHsp60Biomarkerimmune systemlcsh:Therapeutics. Pharmacology030104 developmental biology030220 oncology & carcinogenesisEtiologychaperonopathybusinessFrontiers in Pharmacology
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HSP60 is a ubiquitous player in the physiological and pathogenic interactions between the chaperoning and the immune systems

2017

HSP60 participates in many interactions between the system integrated by all chaperones and closely associated molecules (chaperoning system or CS) and the immune system (IS). These interactions occur constantly to maintain normal cell physiology but, occasionally, they are perturbed and become mediators of pathologic events that may lead to disease. This switch to pathology may be initiated by various factors, genetic or acquired, which cause qualitative and/or quantitative modifications of HSP60, or immune crossreactivity between the human and microbial chaperonin orthologs, or a break in the balance between the pro- and anti-inflammatory actions of the chaperonin. Thus, autoimmune and ch…

0301 basic medicineInflammationChaperoning systemImmunologyCancerInflammationAutoimmunityBiologymedicine.diseasemedicine.disease_causeMicrovesiclesAutoimmunityExosome03 medical and health sciences030104 developmental biologyImmune systemImmune systemImmunologymedicineImmunology and AllergyHSP60medicine.symptomHSP60Cancer
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Hsp60 molecular anatomy and role in colorectal cancer diagnosis and treatment

2011

Quantitative changes in Hsp60 during the development of some tumors suggest that this chaperonin plays a role in carcinogenesis. A description of the specific role(s) of Hsp60 in tumor-cell growth and proliferation is still incomplete, but it is already evident that monitoring its levels and distribution in tissues and fluids has potential for diagnosis and staging, and for assessing prognosis and response to treatment. Although Hsp60 is considered an intramitochondrial protein, it has been demonstrated in the cytosol, cell membrane, vesicles, cell surface, extracellular space, and blood. The knowledge that Hsp60 occurs at all these locations opens new avenues for basic and applied research…

Clinical OncologyOncologymedicine.medical_specialtyGeneral Immunology and Microbiologybusiness.industryColorectal cancerCellChaperonin 60medicine.disease_causeBioinformaticsmedicine.diseaseResponse to treatmentGeneral Biochemistry Genetics and Molecular BiologyChaperoninmedicine.anatomical_structureInternal medicineBiomarkers TumorHumansMedicineHSP60Chaperoning system Chaperonology Chaperonopathies Chaperonotherapy Hsp60 Clinical oncology Colorectal cancer ReviewColorectal NeoplasmsbusinessCarcinogenesisFrontiers in Bioscience
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