Search results for "Chaperones"

showing 10 items of 127 documents

Poly-Xaa Sequences in Proteins - Biological Role and Interactions with Metal Ions: Chemical and Medical Aspects

2016

Background: The understanding of the bioinorganic and coordination chemistry of metalloproteins containing unusual poly-Xaa sequences, in which a single amino acid is repeated consecutively, is crucial for describing their metal binding-structure-function relationship, and therefore also crucial for understanding their medicinal potential. To the best of our knowledge, this is the first systematic review on metal complexes with polyXaa sequences. Methods: We performed a thorough search of high quality peer reviewed literature on poly-Xaa type of sequences in proteins, focusing on their biological importance and on their interactions with metal ions. Results: 228 papers were included in the…

Metal ions in aqueous solutionComputational biology010402 general chemistry01 natural sciencesBiochemistryCoordination complexTurn (biochemistry)metal chaperonesCoordination ComplexesDrug DiscoveryMetalloproteinHumansAmino Acid SequenceSingle amino acidAmino AcidsBinding siteantimicrobial therapeuticsIonsPharmacologychemistry.chemical_classification010405 organic chemistryMetal bindingOrganic Chemistrymetal ionsProteinsBioinorganic chemistry0104 chemical scienceschemistryChemical physicsMetal-protein complexespoly-Xaa peptide sequencesMolecular MedicineCurrent Medicinal Chemistry
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Gut microbiota imbalance and chaperoning system malfunction are central to ulcerative colitis pathogenesis and can be counteracted with specifically …

2013

In this work, we propose that for further studies of the physiopathology and treatment for inflammatory bowel diseases, an integral view of the conditions, including the triad of microbiota-heat shock proteins (HSPs)-probiotics, ought to be considered. Microbiota is the complex microbial flora that resides in the gut, affecting not only gut functions but also the health status of the whole body. Alteration in the microbiota's composition has been implicated in a variety of pathological conditions (e.g., ulcerative colitis, UC), involving both gut and extra-intestinal tissues and organs. Some of these pathologies are also associated with an altered expression of HSPs (chaperones) and this is…

Microbiology (medical)medicine.medical_specialtyImmunologyInflammationBiologyGut floradigestive systemMedical microbiologyFlora (microbiology)Heat shock proteinmedicineHumansImmunology and AllergyColitisCrohn's diseaseMicrobiotaProbioticsGeneral Medicinemedicine.diseasebiology.organism_classificationMicrobiota Probiotics Ulcerative colitis Heat shock proteins Molecular chaperones InflammationUlcerative colitisGastrointestinal TractImmunologyColitis Ulcerativemedicine.symptomMolecular ChaperonesMedical Microbiology and Immunology
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Biophysical investigation on therapeutic proteins (Chaperonins, Hsp60 and CCT/TRiC) involved in human diseases

Molecular chaperones are indispensable cellular components that assist folding and assembly of newly synthesized proteins, translocation of proteins across membranes, as well as refolding and degrading of misfolded and aggregated proteins. In the last few years, innovative therapeutic strategies targeting stability and functionality of chaperones have received great attention, particularly in the field of neurodegenerative diseases. Moreover, the growing number of diseases found linked to chaperone mutations, testifies to the importance of their role in the cellular protein-quality control mechanism. The investigation of the biophysical interactions between chaperones and specific proteins …

Molecolar chaperones HSP CCT TRiC DSC ITC FS HPLC-SEC Circular DichroismSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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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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