Search results for "molecular chaperone"

showing 10 items of 117 documents

Identification of a copper chaperone from tomato fruits infected with Botrytis cinerea by differential display

2003

Differential display was used to isolate tomato genes responding to fungal infection. Here we describe the isolation and characterization of a gene that is down-regulated in tomato fruits infected with the phytopathogen Botrytis cinerea. The cDNA identified encodes a protein that shares sequence similarity to the amino terminal region of CCH, a copper chaperone from Arabidopsis thaliana, that participates in intracellular copper homeostasis by delivering Cu to the secretory pathway. The fact that this newly characterized tomato gene, referred to as LeCCH (Lycopersicon esculentum copper chaperone), be differentially expressed after fungal infection, suggests an interesting relationship betwe…

Molecular Sequence DataBiophysicsGenes PlantBiochemistryLycopersiconSolanum lycopersicumComplementary DNAMetalloproteinsPlant defense against herbivoryAnimalsHomeostasisHumansAmino Acid SequenceMolecular BiologyGenePlant ProteinsBotrytis cinereaDifferential displaybiologyGene Expression ProfilingIntercellular transportfungifood and beveragesCell Biologybiology.organism_classificationBiochemistryFruitChaperone (protein)biology.proteinBotrytisSequence AlignmentCopperMolecular ChaperonesBiochemical and Biophysical Research Communications
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The triad hsp60-mirnas-extracellular vesicles in brain tumors: Assessing its components for understanding tumorigenesis and monitoring patients

2021

Brain tumors have a poor prognosis and progress must be made for developing efficacious treatments, but for this to occur their biology and interaction with the host must be elucidated beyond current knowledge. What has been learned from other tumors may be applied to study brain tumors, for example, the role of Hsp60, miRNAs, and extracellular vesicles (EVs) in the mechanisms of cell proliferation and dissemination, and resistance to immune attack and anticancer drugs. It has been established that Hsp60 increases in cancer cells, in which it occurs not only in the mitochondria but also in the cytosol and plasma-cell membrane and it is released in EVs into the extracellular space and in cir…

Molecular chaperonesCellBrain tumorBiologymedicine.disease_causelcsh:Technologylcsh:Chemistry03 medical and health sciences0302 clinical medicineImmune systemHigh-grade gliomaExtracellularmedicineGeneral Materials Sciencelcsh:QH301-705.5Instrumentation030304 developmental biologyFluid Flow and Transfer Processes0303 health sciencesLiquid biopsylcsh:TProcess Chemistry and TechnologyGeneral EngineeringCancerTumor biomarkersChaperonopathiesExtracellular vesiclesmedicine.diseaseHsp60lcsh:QC1-999Computer Science ApplicationsCrosstalk (biology)medicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040030220 oncology & carcinogenesisCancer cellCancer researchChaperone systemMiRNAslcsh:Engineering (General). Civil engineering (General)CarcinogenesisGlioblastomaMeningiomalcsh:Physics
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Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone.

1997

Abstract Histones are thought to play a key role in regulating gene expression at the level of DNA packaging. Recent evidence suggests that transcriptional activation requires competition of transcription factors with histones for binding to regulatory regions and that there may be several mechanisms by which this is achieved. We have characterized a human nucleosome assembly protein, NAP-2, previously identified by positional cloning at 11p15.5, a region implicated in several disease processes including Wilms tumor (WT) etiology. The deduced amino acid sequence of NAP-2 indicates that it encodes a protein with a potential nuclear localization motif and two clusters of highly acidic residue…

NAP1L4DNA ComplementaryNucleosome assemblyPositional cloningMolecular Sequence DataMice NudeWilms TumorHistonesMicemental disordersGeneticsNucleosomeAnimalsHumansAmino Acid SequenceCloning MolecularRegulation of gene expressionbiologyBase Sequencemusculoskeletal neural and ocular physiologyfungiGene Transfer TechniquesNuclear ProteinsMolecular biologyRecombinant ProteinsChromatinCell biologyNucleosomesDNA-Binding ProteinsHistoneChaperone (protein)biology.proteinpsychological phenomena and processesMolecular ChaperonesProtein BindingSubcellular FractionsGenomics
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Localization of mitochondrial Hsp56 chaperonin during sea urchin development.

2001

We have previously demonstrated that Paracentrotus lividus nuclear genome encodes for the heat shock inducible chaperonin homolog Hsp 56 (1) and that the mature protein is localized in the mitochondrial matrix (2). In this paper we report that constitutive Hsp56 is maternally inherited, in fact it is present in the in unfertilized eggs, and that it has a perinuclear specific localization during cleavage. In the later stages both the constitutive and the heat shock inducible chaperonin has a specific territorial distribution. Moreover following heat shock, the Hsp56 appears in the cytoplasm and in the postmitochondrial supernatant beside the mitochondrial fraction.

Nuclear geneEmbryo NonmammalianBlotting WesternBiophysicsMitochondrionCell FractionationBiochemistryParacentrotus lividusChaperoninTacrolimus Binding Proteinsbiology.animalAnimalsMolecular BiologySea urchinbiologyCell Biologybiology.organism_classificationMolecular biologyImmunohistochemistryCell biologyMitochondriaMitochondrial matrixCytoplasmSea UrchinsHSP60Molecular ChaperonesBiochemical and biophysical research communications
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SPECIAL ISSUE: The clinical relevance of exosomes in cancer

2021

OncologyCancer Researchmedicine.medical_specialtybusiness.industryMicrovesicles exosomesmolecular chaperones.CancerExosomesmedicine.diseaseMicrovesiclesNeoplasmsInternal medicineBiomarkers TumormedicineHumansClinical significancebusinessSeminars in Cancer Biology
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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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Multiple Receptors Mediate apoJ-Dependent Clearance of Cellular Debris into Nonprofessional Phagocytes

2001

Phagocytosis of apoptotic, senescent, and dying cells by macrophages is a well characterized process. More recently it has been shown that in addition to macrophages vital neighboring cells in the affected tissue participate in the cellular clearance. While scavenger receptors have been shown to mediate uptake into macrophages, it is poorly understood how cellular debris is internalized by nonprofessional phagocytes. We here analyze the endocytic activity of vital fibroblasts and epithelial cells exposed to cellular debris and membrane remnants. We show a mutual stimulation in the endocytosis of debris and apolipoproteinJ (clusterin) in these cells. Experiments using RAP (receptor-associate…

Phagocytosismedia_common.quotation_subjectEndocytic cycleAntineoplastic AgentsApoptosisTretinoinBiologyEndocytosisCulture Media Serum-FreeCell LineTumor Cells CulturedAnimalsScavenger receptorReceptorInternalizationGlycoproteinsReceptors LipoproteinYolk Sacmedia_commonPhagocytesClusterinEpithelial CellsCell BiologyFibroblastsEndocytosisCell biologyLow Density Lipoprotein Receptor-Related Protein-2ClusterinBucladesineCell culturebiology.proteinLow Density Lipoprotein Receptor-Related Protein-1Molecular ChaperonesExperimental Cell Research
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Zebrafish as a Model for the Study of Chaperonopathies.

2016

There is considerable information on the clinical manifestations and mode of inheritance for many genetic chaperonopathies but little is known on the molecular mechanisms underlying the cell and tissue abnormalities that characterize them. This scarcity of knowledge is mostly due to the lack of appropriate animal models that mimic closely the human molecular, cellular, and histological characteristics. In this article we introduce zebrafish as a suitable model to study molecular and cellular mechanisms pertaining to human chaperonopathies. Genetic chaperonopathies manifest themselves from very early in life so it is necessary to examine the impact of mutant chaperone genes during developmen…

PhysiologyClinical BiochemistryModels AnimalMutationAnimalsHumansClinical Biochemistry; Cell Biology; PhysiologyGenetic Predisposition to DiseaseCell BiologyGenetic TestingZebrafishMolecular ChaperonesJournal of cellular physiology
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Heat shock proteins: essential proteins for apoptosis regulation

2008

Abstract Many different external and intrinsic apoptotic stimuli induce the accumulation in the cells of a set of proteins known as stress or heat shock proteins (HSPs). HSPs are conserved proteins present in both prokaryotes and eukaryotes. These proteins play an essential role as molecular chaperones by assisting the correct folding of nascent and stress-accumulated misfolded proteins, and by preventing their aggregation. HSPs have a protective function, that is they allow the cells to survive to otherwise lethal conditions. Various mechanisms have been proposed to account for the cytoprotective functions of HSPs. Several of these proteins have demonstrated to directly interact with compo…

Programmed cell deathCell signalingReviewsMitochondrionBiologyModels BiologicallysosomesLysosomeHeat shock proteindeath receptorsmedicineAnimalsHumansemerging chemotherapeutic treatmentsHeat-Shock ProteinsCell Deathhaematopoietic malignanciesapoptosiscell signallingCell BiologyMitochondriaNeoplasm ProteinsCell biologymedicine.anatomical_structurecaspasesHematologic Neoplasmsheat shock proteinsMolecular MedicineProtein foldingHSP60Signal transductionMolecular ChaperonesSignal TransductionJournal of Cellular and Molecular Medicine
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Apoptotic Cell Debris and Phosphatidylserine-Containing Lipid Vesicles Induce Apolipoprotein J (Clusterin) Gene Expression in Vital Fibroblasts

2001

The molecular events in cells undergoing programmed cell death (apoptosis) are well studied; however, the response of the surviving neighbor cells to local cell death is largely uncharacterized. Apolipoprotein J (clusterin) is an 80-kDa glycoprotein that has been implied in cytoprotection of the vital cells, presumably by assisting in the clearance of apoptotic vesicles and membrane remnants. Its mRNA is specifically up-regulated in the vital cells of apoptotic tissues. The molecular mechanisms, however, leading to this response are not known. We here show that exposure of vital fibroblasts to apoptotic vesicles, disrupted vital cells, and trypsin-treated membrane remnants induces apoJ mRNA…

Programmed cell deathEndocytic cycleGene ExpressionApoptosisPhosphatidylserinesCell Linechemistry.chemical_compoundCricetinaeAnimalsTrypsinGlycoproteinsClusterinbiologyVesicleCell BiologyPhosphatidylserinePhosphatidic acidFibroblastsLipid MetabolismMolecular biologyCytoprotectionRatsCell biologyClusterinchemistryApoptosisbiology.proteinMolecular ChaperonesExperimental Cell Research
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