Search results for "Erythroblasts"

showing 5 items of 5 documents

Mitochondrial Changes in β0-Thalassemia/Hb E Disease.

2015

The compound β°-thalassemia/Hb E hemoglobinopathy is characterized by an unusually large range of presentation from essentially asymptomatic to a severe transfusion dependent state. While a number of factors are known that moderate presentation, these factors do not account for the full spectrum of presentation. Mitochondria are subcellular organelles that are pivotal in a number of cellular processes including oxidative phosphorylation and apoptosis. A mitochondrial protein enriched proteome was determined and validated from erythroblasts from normal controls and β°-thalassemia/Hb E patients of different severities. Mitochondria were evaluated through the use of mitotracker staining, analy…

0301 basic medicineMetabolic ProcessesErythroblastsProteomeProteomesCelllcsh:MedicineGene ExpressionAntigens CD34ApoptosisMitochondrionBiochemistryOxidative Phosphorylation0302 clinical medicineAnimal Cellshemic and lymphatic diseasesRed Blood CellsGene expressionlcsh:ScienceErythroid Precursor CellsEnergy-Producing OrganellesErythroid Precursor CellsStainingMultidisciplinaryCell DeathHemoglobin ECell StainingCell biologyGlobinsMitochondriamedicine.anatomical_structureCell Processes030220 oncology & carcinogenesisCellular Structures and OrganellesCellular TypesResearch ArticleMitochondrial DNAPrecursor CellsBone Marrow CellsOxidative phosphorylationBiologyBioenergeticsResearch and Analysis Methods03 medical and health sciencesmedicineHumansGlobinBlood Cellslcsh:Rbeta-ThalassemiaBiology and Life SciencesProteinsCell BiologyMolecular biologyChaperone ProteinsHemoglobinopathies030104 developmental biologyMetabolismApoptosisSpecimen Preparation and TreatmentCase-Control Studieslcsh:QPloS one
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The severe phenotype of Diamond-Blackfan anemia is modulated by heat shock protein 70.

2017

International audience; Diamond-Blackfan anemia (DBA) is a rare congenital bone marrow failure syndrome that exhibits an erythroid-specific phenotype. In at least 70% of cases, DBA is related to a haploinsufficient germ line mutation in a ribosomal protein (RP) gene. Additional cases have been associated with mutations in GATA1. We have previously established that the RPL11+/Mut phenotype is more severe than RPS19+/Mut phenotype because of delayed erythroid differentiation and increased apoptosis of RPL11+/Mut erythroid progenitors. The HSP70 protein is known to protect GATA1, the major erythroid transcription factor, from caspase-3 mediated cleavage during normal erythroid differentiation.…

0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesIdentificationApoptosis-Inducing FactorGata1 MutationsInhibits ApoptosisBiologyHsp7003 medical and health sciencesGermline mutationRed Cells Iron and Erythropoiesishemic and lymphatic diseasesmedicine[ SDV.MHEP.HEM ] Life Sciences [q-bio]/Human health and pathology/HematologyNuclear ImportErythropoiesisDiamond–Blackfan anemiaHuman ErythroblastsBone marrow failure[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/HematologyGATA1Hematologymedicine.diseasePhenotypeMolecular biology3. Good healthHsp70030104 developmental biologyRibosomal-ProteinsProtein Gene DeletionsErythropoiesisHaploinsufficiencyBlood advances
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HSP70 sequestration by free α-globin promotes ineffective erythropoiesis in β-thalassaemia

2014

International audience; β-Thalassaemia major (β-TM) is an inherited haemoglobinopathy caused by a quantitative defect in the synthesis of β-globin chains of haemoglobin, leading to the accumulation of free α-globin chains that form toxic aggregates. Despite extensive knowledge of the molecular defects causing β-TM, little is known of the mechanisms responsible for the ineffective erythropoiesis observed in the condition, which is characterized by accelerated erythroid differentiation, maturation arrest and apoptosis at the polychromatophilic stage. We have previously demonstrated that normal human erythroid maturation requires a transient activation of caspase-3 at the later stages of matur…

Ineffective erythropoiesisCytoplasmErythroblastsCell SurvivalMutantApoptosis[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyalpha-globin[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Biologymedicine.disease_causeProtein Refolding03 medical and health sciences0302 clinical medicinealpha-GlobinsBone Marrowhemic and lymphatic diseasesmedicineHumans[ SDV.MHEP.HEM ] Life Sciences [q-bio]/Human health and pathology/HematologyErythropoiesisGATA1 Transcription FactorHSP70 Heat-Shock ProteinsMolecular Targeted TherapyCells CulturedHSP70030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesMultidisciplinaryCaspase 3beta-Thalassemia[ SDV.BC.BC ] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]GATA1[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/Hematology[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMolecular biologyHsp70Enzyme ActivationKineticsGene Expression RegulationCytoplasm030220 oncology & carcinogenesisChaperone (protein)biology.proteinErythropoiesisbeta-ThalassaemiaProtein Binding
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Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes.

2012

Abstract Normal human erythroid cell maturation requests the transcription factor GATA-1 and a transient activation of caspase-3, with GATA-1 being protected from caspase-3–mediated cleavage by interaction with the chaperone heat shock protein 70 (Hsp70) in the nucleus. Erythroid cell dysplasia observed in early myelodysplastic syndromes (MDS) involves impairment of differentiation and excess of apoptosis with a burst of caspase activation. Analysis of gene expression in MDS erythroblasts obtained by ex vivo cultures demonstrates the down-regulation of a set of GATA-1 transcriptional target genes, including GYPA that encodes glycophorin A (GPA), and the up-regulation of members of the HSP70…

MaleErythroblasts[SDV]Life Sciences [q-bio]Biochemistry0302 clinical medicineTranscription (biology)hemic and lymphatic diseasesGene expressionErythropoiesisGATA1 Transcription FactorCells CulturedCaspaseComputingMilieux_MISCELLANEOUSOligonucleotide Array Sequence AnalysisAged 80 and over0303 health sciencesbiologyCaspase 3Reverse Transcriptase Polymerase Chain ReactionCell DifferentiationU937 CellsHematologyMiddle Agedmedicine.anatomical_structure030220 oncology & carcinogenesisFemaleAdultGreen Fluorescent ProteinsImmunoblottingImmunology03 medical and health sciencesErythroid CellsmedicineHumansHSP70 Heat-Shock ProteinsTranscription factorAged030304 developmental biologyCell NucleusGene Expression ProfilingCell BiologyMolecular biologyCell nucleusMicroscopy FluorescenceApoptosisMyelodysplastic SyndromesChaperone (protein)Mutationbiology.proteinNuclear localization sequence
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Identification and purification of human erythroid progenitor cells by monoclonal antibody to the transferrin receptor (T� 67)

1988

Anti-TU 67 is a murine monoclonal antibody that recognizes the transferrin receptor. With respect to hematopoietic cells TU 67 is expressed by human multipotent colony-forming cells (CFU-Mix), erythroid progenitor cells (BFU-E and CFU-E) and a fraction of granulocyte/monocyte colony forming cells, but is not expressed by mature hematopoietic cells including erythrocytes, platelets, lymphocytes, and peripheral blood myeloid cells. The TU 67-positive fraction of normal bone marrow, separated by fluorescence-activated cell sorting (FACS) or immune rosettes, contained 87% of the erythroid progenitor cells. Erythroid progenitor cells were enriched up to 50-fold by using a combination of monoclon…

Rosette FormationErythroblastsmedicine.drug_classMonocyteAntibodies MonoclonalFluorescent Antibody TechniqueTransferrin receptorCell SeparationHematologyGeneral MedicineCell sortingBiologyFlow CytometryMonoclonal antibodyMolecular biologyHaematopoiesismedicine.anatomical_structurehemic and lymphatic diseasesReceptors TransferrinMonoclonalmedicinebiology.proteinAntibodyInterleukin 3Blut
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