Search results for "Molecular Chaperones"

showing 10 items of 112 documents

AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7

2005

AbstractIn plant chloroplasts two superoxide dismutase (SOD) activities occur, FeSOD and Cu/ZnSOD, with reciprocal regulation in response to copper availability. This system presents a unique model to study the regulation of metal-cofactor delivery to an organelle. The Arabidopsis thaliana gene AtCCS encodes a functional homolog to yeast Ccs1p/Lys7p, a copper chaperone for SOD. The AtCCS protein was localized to chloroplasts where it may supply copper to the stromal Cu/ZnSOD. AtCCS mRNA expression levels are upregulated in response to Cu-feeding and senescence. We propose that AtCCS expression is regulated to allow the most optimal use of Cu for photosynthesis.

0106 biological sciencesCu/Zn superoxide dismutaseChloroplastsSaccharomyces cerevisiae ProteinsMolecular Sequence DataArabidopsisBiophysicsSaccharomyces cerevisiaeMetallo chaperoneChloroplastModels Biological01 natural sciencesBiochemistryGreen fluorescent proteinSuperoxide dismutase03 medical and health sciencesDownregulation and upregulationGene Expression Regulation PlantStructural BiologyOrganelleGeneticsAmino Acid SequenceRNA MessengerMolecular BiologyGene030304 developmental biology0303 health sciencesbiologyArabidopsis ProteinsGene Expression ProfilingGenetic Complementation TestCell BiologyYeastChloroplastProtein TransportBiochemistryChaperone (protein)Mutationbiology.proteinSequence AlignmentCopperMolecular Chaperones010606 plant biology & botanyFEBS Letters
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Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis

2020

14 p.-7 fig.-2 tab.

0106 biological sciencesSpliceosomeAcademicSubjects/SCI00010RNA SplicingMutantArabidopsis01 natural sciencesChaperonin//purl.org/becyt/ford/1 [https]03 medical and health sciencesGene Expression Regulation PlantArabidopsisRNA and RNA-protein complexesGeneticsHSP90 Heat-Shock Proteins//purl.org/becyt/ford/1.6 [https]030304 developmental biologyprefoldins0303 health sciencesbiologyArabidopsis ProteinsRNA-Binding Proteinsbiology.organism_classificationHsp903. Good healthCell biologyProteostasisMultiprotein ComplexesMutationRNA splicingSpliceosomesbiology.proteinLSM2-8 complexspliceosomeSmall nuclear RNAMolecular ChaperonesProtein Binding010606 plant biology & botany
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In vivoanalysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain

2007

International audience; The endoplasmic reticulum (ER) chaperone binding protein (BiP) binds exposed hydrophobic regions of misfolded proteins. Cycles of ATP hydrolysis and nucleotide exchange on the ATPase domain were shown to regulate the function of the ligand-binding domain in vitro. Here we show that ATPase mutants of BiP with defective ATP-hydrolysis (T46G) or ATP-binding (G235D) caused permanent association with a model ligand, but also interfered with the production of secretory, but not cytosolic, proteins in vivo. Furthermore, the negative effect of BiP(T46G) on secretory protein synthesis was rescued by increased levels of wild-type BiP, whereas the G235D mutation was dominant. U…

0106 biological sciencesgenetic structuresRecombinant Fusion ProteinsATPaseBlotting WesternGreen Fluorescent ProteinsPlant ScienceBINDING PROTEINEndoplasmic ReticulumModels Biological01 natural sciencesChromatography Affinity[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesAdenosine TriphosphateTobaccoPROTEIN FOLDINGGeneticsImmunoprecipitationEndoplasmic Reticulum Chaperone BiPHSP70Heat-Shock Proteins030304 developmental biologyCHAPERONEAdenosine Triphosphatases0303 health sciencesbiologyHydrolysisProtoplastsEndoplasmic reticulumBinding proteinCell BiologyPlants Genetically ModifiedLigand (biochemistry)Secretory proteinBiochemistryChaperone (protein)MutationChaperone bindingbiology.proteinATPASEElectrophoresis Polyacrylamide GelProtein foldingMolecular ChaperonesProtein BindingSignal Transduction010606 plant biology & botanyThe Plant Journal
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Hsp60, amateur chaperone in amyloid-beta fibrillogenesis

2016

BACKGROUND: Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD. METHODS: Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), t…

0301 basic medicineAmyloidMolecular chaperonesAmyloid betaBiophysicsPlasma protein bindingInhibition mechanismsBiochemistryChaperoninChaperonin03 medical and health sciences0302 clinical medicinemedicineHumansInhibition mechanismMolecular BiologyAmyloid aggregationAmyloid beta-PeptidesbiologyNeurodegenerationP3 peptideFibrillogenesisChaperonin 60medicine.diseaseAlzheimer's disease treatmentCell biology030104 developmental biologyChaperone (protein)biology.proteinHSP60030217 neurology & neurosurgeryProtein BindingBiochimica et Biophysica Acta (BBA) - General Subjects
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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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Hsp40 Is Involved in Cilia Regeneration in Sea Urchin Embryos

2003

In a previous paper we demonstrated that, in Paracentrotus lividus embryos, deciliation represents a specific kind of stress that induces an increase in the levels of an acidic protein of about 40 kD (p40). Here we report that deciliation also induces an increase in Hsp40 chaperone levels and enhancement of its ectodermal localization. We suggest that Hsp40 might play a chaperoning role in cilia regeneration.

0301 basic medicineEmbryo NonmammalianHistologyParacentrotus lividus03 medical and health sciences0302 clinical medicineStress PhysiologicalCulture Techniquesbiology.animalEctodermBotanyAnimalsRegenerationElectrophoresis Gel Two-DimensionalCiliaSettore BIO/06 - Anatomia Comparata E CitologiaSea urchinHeat-Shock ProteinsCentrosomebiologyCiliumEmbryoHSP40 Heat-Shock ProteinsSea urchin embryobiology.organism_classificationHsp40 deciliation sea urchinCell biology030104 developmental biologySea UrchinsAnatomy030217 neurology & neurosurgeryMolecular Chaperones
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Treatment strategies for lysosomal storage disorders.

2017

Over the past several years the number of treatments available for patients with lysosomal storage disorders has rapidly increased. Haematopoietic stem cell transplantation, enzyme replacement therapy, substrate reduction, and chaperone therapies are currently available, and gene therapies and other treatments are rapidly advancing. Despite remarkable advances, the efficacy of most of these therapies is limited, particularly because the treatments are usually initiated when organ damage has already occurred. To circumvent this limitation, screening in newborn infants for lysosomal storage disorders has been introduced in many countries. However, this screening is complicated by the broad cl…

0301 basic medicineGenetic enhancementLysosomal storage disordersBioinformatics03 medical and health sciences0302 clinical medicineDevelopmental NeuroscienceSlow progressionMedicineHumansEnzyme Replacement Therapybusiness.industryHematopoietic Stem Cell TransplantationEnzyme replacement therapyGenetic TherapyOrgan damageTransplantationLysosomal Storage Diseases030104 developmental biologyPediatrics Perinatology and Child HealthImmunologyTreatment strategyNeurology (clinical)Stem cellbusiness030217 neurology & neurosurgeryMolecular ChaperonesDevelopmental medicine and child neurology
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The neurochaperonopathies: Anomalies of the chaperone system with pathogenic effects in neurodegenerative and neuromuscular disorders

2021

The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as the chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal molecular chaperones. Since the CS is ubiquitous, chaperonopathies are systemic, affecting various tissues and organs, playing an etiologic-pathogenic role in diverse conditions. In this review, we focus on chaperonopathies involved in the pathogenic mechanisms of diseases of the central and peripheral nervous systems: the neurochaperonopathies (NCPs). Genetic …

0301 basic medicineHspsDiseasechaperonopathieslcsh:Technologylcsh:Chemistry03 medical and health sciences0302 clinical medicineneurochaperonopathieschaperone systemchaperonotherapy.medicineGeneral Materials ScienceReceptorInstrumentationGenelcsh:QH301-705.5Fluid Flow and Transfer Processesbiologylcsh:TSettore BIO/16 - Anatomia UmanaProcess Chemistry and TechnologyNeurodegenerationmolecular chaperonesnervous systemGeneral Engineeringmedicine.diseaseHsp90lcsh:QC1-999Computer Science ApplicationsCell biologyPatient management030104 developmental biologylcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040Chaperone (protein)biology.proteinChaperone system ChaperonopathiesChaperonotherapy Hsps Molecular chaperones Nervous system Neurochaperonopathies Neurodegeneration neuromuscular disorderHSP60lcsh:Engineering (General). Civil engineering (General)030217 neurology & neurosurgerylcsh:Physics
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Assessment of Targeted Next-Generation Sequencing as a Tool for the Diagnosis of Charcot-Marie-Tooth Disease and Hereditary Motor Neuropathy

2016

Charcot-Marie-Tooth disease is characterized by broad genetic heterogeneity with >50 known disease-associated genes. Mutations in some of these genes can cause a pure motor form of hereditary motor neuropathy, the genetics of which are poorly characterized. We designed a panel comprising 56 genes associated with Charcot-Marie-Tooth disease/hereditary motor neuropathy. We validated this diagnostic tool by first testing 11 patients with pathological mutations. A cohort of 33 affected subjects was selected for this study. The DNAJB2 c.352+1G>A mutation was detected in two cases; novel changes and/or variants with low frequency (50 known disease-associated genes. Mutations in some of these gene…

0301 basic medicineMaleDiseaseBioinformaticsDNA sequencingPathology and Forensic Medicine03 medical and health sciences0302 clinical medicineCharcot-Marie-Tooth DiseaseMedicineHumansGeneGeneticsbusiness.industryGenetic heterogeneityHaplotypeCase-control studyHigh-Throughput Nucleotide SequencingReproducibility of ResultsHSP40 Heat-Shock Proteins030104 developmental biologyHaplotypesCase-Control StudiesMutation (genetic algorithm)MutationMolecular MedicineFemalebusinessHereditary Sensory and Motor Neuropathy030217 neurology & neurosurgeryFounder effectMolecular Chaperones
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Exosomal Chaperones and miRNAs in Gliomagenesis: State-of-Art and Theranostics Perspectives

2018

Gliomas have poor prognosis no matter the treatment applied, remaining an unmet clinical need. As background for a substantial change in this situation, this review will focus on the following points: (i) the steady progress in establishing the role of molecular chaperones in carcinogenesis; (ii) the recent advances in the knowledge of miRNAs in regulating gene expression, including genes involved in carcinogenesis and genes encoding chaperones; and (iii) the findings about exosomes and their cargo released by tumor cells. We would like to trigger a discussion about the involvement of exosomal chaperones and miRNAs in gliomagenesis. Chaperones may be either targets for therapy, due to their…

0301 basic medicineMolecular ChaperoneCellReviewmedicine.disease_causelcsh:ChemistryGene expressiontheranostic toolslcsh:QH301-705.5SpectroscopyChaperone GeneSettore MED/27 - Neurochirurgiamolecular chaperonesGliomaGeneral MedicineHsp60Extracellular MatrixComputer Science ApplicationsCell Transformation Neoplasticmedicine.anatomical_structuregliomas; molecular chaperones; Hsps (Heat shock proteins); Hsp60; miRNA; exosomes; extracellular vesicles; theranostic toolsextracellular vesiclesHumanexosomesBiologyCatalysisInorganic Chemistry03 medical and health sciencesGliomamicroRNAmedicineAnimalsHumansHsps (Heat shock proteins)Physical and Theoretical ChemistryMolecular BiologyGenemiRNAAnimalSettore BIO/16 - Anatomia UmanaOrganic ChemistryBiological Transportmedicine.diseaseMicrovesiclesExosomegliomasMicroRNAs030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Cancer researchextracellular vesicleTheranostic toolCarcinogenesisInternational Journal of Molecular Sciences
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