Search results for "Chaperones"

showing 10 items of 127 documents

Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible…

2020

Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins. We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endotheli…

0301 basic medicineMolecular chaperonesShort CommunicationPneumonia ViralAutoimmunityBiologymedicine.disease_causeAutoantigensBiochemistryEpitopeAutoimmunity03 medical and health sciencesBetacoronavirusViral Proteins0302 clinical medicineImmune systemEndothelialitisAntigenHeat shock proteinmedicineHumansSevere acute respiratory syndrome coronavirus 2Amino Acid SequenceDatabases ProteinPandemicsHeat-Shock ProteinsEffectorImmunodominant EpitopesSARS-CoV-2Settore BIO/16 - Anatomia UmanaEndothelial CellsCOVID-19Cell BiologyCell biologyEndothelial stem cellMolecular mimicry030104 developmental biologyCoronavirus Infections030217 neurology & neurosurgeryMolecular mimicryCell Stress and Chaperones
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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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Circulating Molecular Chaperones in Subjects with Amnestic Mild Cognitive Impairment and Alzheimer’s Disease: Data from the Zabùt Aging Project

2022

Molecular chaperones play essential roles in many processes such as cell differentiation, tissue homeostasis, and organ remodeling. Recent data indicate that chaperones can act as cytoprotectants for brain cells during the progression of neurodegenerative diseases, including Alzheimer’s disease (AD). However, very few data on the levels of chaperones in dementia, including its prodromal phases, have been reported. In this study, we used biological samples and epidemiological data collected during the Zabùt Aging Project (a prospective, community-based, cohort study of normal/pathological aging conducted in Sicily, Italy, with a follow-up of ten years) to determine if there is an association…

0301 basic medicineOncologyAgingmedicine.medical_specialtySettore MED/09 - Medicina InternaHsp90DiseaseNeuropsychological Testsmedicine.disease_causeHsp70Cohort Studies03 medical and health sciences0302 clinical medicineAlzheimer DiseaseInternal medicineEpidemiologyoxidative stressHumansMedicineDementiaCognitive DysfunctionProspective StudiesPathologicalTissue homeostasiscognitive impairmentSettore MED/04 - Patologia Generalebusiness.industryGeneral NeuroscienceNeurodegenerationneurodegenerationGeneral Medicinemolecular chaperoneHsp60medicine.diseasePsychiatry and Mental healthClinical Psychology030104 developmental biologySettore MED/26 - NeurologiaGeriatrics and GerontologybusinessAlzheimer’s disease030217 neurology & neurosurgeryOxidative stressMolecular ChaperonesCohort studyJournal of Alzheimer's Disease
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Oxidative signature of cerebrospinal fluid from mild cognitive impairment and Alzheimer disease patients

2015

Abstract Background Several studies suggest that pathological changes in Alzheimer’s disease (AD) brain begin around 10–20 years before the onset of cognitive impairment. Biomarkers that can support early diagnosis and predict development of dementia would, therefore, be crucial for patient care and evaluation of drug efficacy. Although cerebrospinal fluid (CSF) levels of Aβ42, tau, and p-tau are well-established diagnostic biomarkers of AD, there is an urgent need to identify additional molecular alterations of neuronal function that can be evaluated at the systemic level. Objectives This study was focused on the analysis of oxidative stress-related modifications of the CSF proteome, from …

0301 basic medicineOncologyPathologyDiseasephysiology (medical)medicine.disease_causeProtein oxidationtau proteins0302 clinical medicineCerebrospinal fluidmiddle aged80 and overoxidative stresshumansAged 80 and overamyloid beta-peptidesredox proteomicsagedfemale030220 oncology & carcinogenesisBiomarker (medicine)Alzheimer's diseaseAlzheimer diseaseAPOEmedicine.medical_specialtyoxidation-reductionproteomeCSFmolecular sequence data03 medical and health sciencesmalecognitive dysfunctionInternal medicinemental disordersmedicineDementiabiochemistryprotein oxidationbusiness.industrypeptide fragmentscase-control studiesCase-control studybiomarkersmedicine.diseaseAPOE; biomarkers; CSF; extracellular chaperones; protein oxidation; redox proteomics; aged; aged 80 and over; Alzheimer disease; amino acid sequence; amyloid beta-peptides; apolipoproteins E; biomarkers; case-control studies; cognitive dysfunction; female; humans; male; middle aged; molecular sequence data; oxidation-reduction; oxidative stress; peptide fragments; proteome; tau proteins; biochemistry; physiology (medical)extracellular chaperonesamino acid sequence030104 developmental biologybusinessOxidative stressapolipoproteins E
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Chaperoning the Mononegavirales: Current Knowledge and Future Directions

2018

This article belongs to the Special Issue Breakthroughs in Viral Replication.

0301 basic medicineProtein Foldingrespiratory syncytial viruslcsh:QR1-502ReviewRespiratory syncytial virusVirus Replicationmedicine.disease_causelcsh:MicrobiologyHsp70Ebola virusantiviralsChaperonesMononegaviralesOrder MononegaviralesbiologyAntivirals<i>Mononegavirales</i>Hsp90Respiratory Syncytial VirusesInfectious DiseasesMumps virusHost-Pathogen InteractionsProtein foldingHsp90biology_otherComputational biologyAntiviral Agents03 medical and health sciencesEmerging infectionsVirologymedicineHumanschaperonesHSP70 Heat-Shock Proteinsrabies virusHSP90 Heat-Shock ProteinsEbola virusObligatebiology.organism_classificationCCT030104 developmental biologyMeasles virusRabies virusChaperone (protein)measles virusbiology.proteinmumps virusMononegaviralesMolecular ChaperonesViruses
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Molecular chaperones in the brain endothelial barrier: neurotoxicity or neuroprotection?

2019

Brain microvascular endothelial cells (BMECs) interact with astrocytes and pericytes to form the blood-brain barrier (BBB). Their compromised function alters the BBB integrity, which is associated with early events in the pathogenesis of cancer, neurodegenerative diseases, and epilepsy. Interestingly, these conditions also induce the expression of heat shock proteins (HSPs). Here we review the contribution of major HSP families to BMEC and BBB function. Although investigators mainly report protective effects of HSPs in brain, contrasted results were obtained in BMEC, which depend both on the HSP and on its location, intra- or extracellular. The therapeutic potential of HSPs must be scrupulo…

0301 basic medicineReviewBiochemistryNeuroprotectionPathogenesis03 medical and health sciencesEpilepsy0302 clinical medicineHeat shock proteinGeneticsExtracellularMedicineAnimalsHumansMolecular Biologybusiness.industryNeurotoxicityCancerBrainEndothelial CellsBiological TransportCell Differentiationmedicine.diseaseNeuroprotectionCell biology030104 developmental biologyBlood-Brain Barriercardiovascular systembusiness030217 neurology & neurosurgeryFunction (biology)BiotechnologyMolecular ChaperonesFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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The ribosome assembly gene network is controlled by the feedback regulation of transcription elongation

2017

Ribosome assembly requires the concerted expression of hundreds of genes, which are transcribed by all three nuclear RNA polymerases. Transcription elongation involves dynamic interactions between RNA polymerases and chromatin. We performed a synthetic lethal screening in Saccharomyces cerevisiae with a conditional allele of SPT6, which encodes one of the factors that facilitates this process. Some of these synthetic mutants corresponded to factors that facilitate pre-rRNA processing and ribosome biogenesis. We found that the in vivo depletion of one of these factors, Arb1, activated transcription elongation in the set of genes involved directly in ribosome assembly. Under these depletion c…

0301 basic medicineRibosomal ProteinsSaccharomyces cerevisiae ProteinsTranscription Elongation GeneticCèl·lulesÀcids nucleicsGene regulatory networkRibosome biogenesisSaccharomyces cerevisiaeBiologyRibosome assembly03 medical and health sciencesRegulació genèticaGeneticsGene Regulatory NetworksHistone ChaperonesRNA Processing Post-TranscriptionalGeneAdenosine TriphosphatasesFeedback PhysiologicalMessenger RNAOrganelle BiogenesisGene regulation Chromatin and EpigeneticsRNAChromatinCell biology030104 developmental biologyRNA RibosomalMutationATP-Binding Cassette TransportersOrganelle biogenesisTranscriptional Elongation FactorsSynthetic Lethal MutationsTranscriptomeRibosomes
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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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Fluorinated Chaperone−β-Cyclodextrin Formulations for β-Glucocerebrosidase Activity Enhancement in Neuronopathic Gaucher Disease

2017

Amphiphilic glycomimetics encompassing a rigid, undistortable nor-tropane skeleton based on 1,6-anhydro-L-idonojirimycin and a polyfluorinated antenna, when formulated as the corresponding inclusion complexes with β-cyclodextrin (βCD), have been shown to behave as pharmacological chaperones (PCs) that efficiently rescue lysosomal β- glucocerebrosidase mutants associated to the neuronopathic variants of Gaucher disease (GD), including the highly refractory L444P/L444P and L444P/P415R single nucleotide polymorphs, in patient fibroblasts. The body of work here presented includes the design criteria for the PC prototype, the synthesis of a series of candidates, the characterization of the PC:βC…

0301 basic medicineStereochemistryMutantNeuronopathic Gaucher Disease03 medical and health sciencesGlucocerebrosidase activityDrug DiscoveryAmphiphileHumansIn patientNucleotideCells Culturedchemistry.chemical_classificationGaucher DiseasebiologyCyclodextrinChemistrybeta-CyclodextrinsFluorine3. Good healthMolecular Docking Simulation030104 developmental biologyBiochemistryChaperone (protein)biology.proteinGlucosylceramidaseMolecular MedicineMolecular ChaperonesJournal of Medicinal Chemistry
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BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72

2016

The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity. Here, we examined the functional correlation of HSP72, CHIP, and BAG2, employing human primary fibroblasts.…

0301 basic medicineTime FactorsUbiquitin-Protein LigasesImmunoblottingHSP72 Heat-Shock ProteinsUbiquitin-conjugating enzymeProtein degradationArticleCatalysisCell Linelcsh:ChemistryInorganic Chemistry03 medical and health sciencesUbiquitinddc:570Humansaging; BAG2; CHIP; HSP72; proteostasis; ubiquitinationPhysical and Theoretical ChemistryHSP72lcsh:QH301-705.5Molecular BiologyCellular SenescenceSpectroscopySTUB1proteostasisBAG2biologyCHIPagingOrganic ChemistryUbiquitinationGeneral MedicineComputer Science ApplicationsUbiquitin ligaseCell biology030104 developmental biologyProteostasislcsh:Biology (General)lcsh:QD1-999Chaperone (protein)biology.proteinRNA InterferenceProtein foldingMolecular ChaperonesInternational Journal of Molecular Sciences
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