Search results for "Transferrin receptor"

showing 10 items of 30 documents

Iron Metabolism Contributes to Prognosis in Coronary Artery Disease: Prognostic Value of the Soluble Transferrin Receptor Within the AtheroGene Study

2020

Background Coronary heart disease is a leading cause of mortality worldwide. Iron deficiency, a frequent comorbidity of coronary heart disease, causes an increased expression of transferrin receptor and soluble transferrin receptor levels (sTfR) levels, while iron repletion returns sTfR levels to the normal physiological range. Recently, sTfR levels were proposed as a potential new marker of iron metabolism in cardiovascular diseases. Therefore, we aimed to evaluate the prognostic value of circulating sTfR levels in a large cohort of patients with coronary heart disease. Methods and Results The disease cohort comprised 3423 subjects who had angiographically documented coronary heart diseas…

Malemedicine.medical_specialtyTime FactorsIronMyocardial InfarctionCoronary Artery Disease030204 cardiovascular system & hematologyCoronary AngiographyRisk AssessmentGastroenterologyCoronary artery disease03 medical and health sciences0302 clinical medicinePredictive Value of TestsRisk FactorsGermanyInternal medicineReceptors TransferrinmedicineHumansCoronary Heart Diseasesoluble transferrin receptorAgedOriginal Research030304 developmental biologySoluble transferrin receptorchemistry.chemical_classification0303 health sciencesbiologybusiness.industryMyocardiumMetabolismIron deficiencyMiddle AgedPrognosismedicine.diseaseComorbidityCoronary heart diseasechemistryTransferrinbiology.proteinbiomarkerBiomarker (medicine)FemaleCardiology and Cardiovascular MedicinebusinessBiomarkersJournal of the American Heart Association
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Bio-profiling and bio-prognostication of chronic heart failure with mid-range ejection fraction.

2018

Abstract Background Recent ESC guidelines on heart failure (HF) have introduced a new phenotype based on left ventricular ejection fraction (LVEF), called the mid-range (HFmrEF). This phenotype falls between the classical reduced (HFrEF) and preserved (HFpEF) HF phenotypes. We aimed to characterize the HFmrEF biomarker profile and outcomes. Methods 1069 consecutive ambulatory patients were included in the study (age 66.2 ± 12.8 years); 800 with HFrEF (74.8%), 134 with HFmrEF (12.5%), and 135 with HFpEF (12.5%). We measured serum concentrations of N-terminal pro-brain natriuretic peptide (NT-proBNP), high-sensitivity troponin T (hs-TnT), soluble suppression of tumorigenicity (ST2), galectin-…

Malemedicine.medical_specialtymedicine.drug_classGalectin 3030204 cardiovascular system & hematology03 medical and health sciences0302 clinical medicineTroponin TInternal medicineNatriuretic Peptide BrainNatriuretic peptidemedicineHumans030212 general & internal medicineSoluble transferrin receptorAgedAged 80 and overHeart FailureEjection fractionbiologyTroponin Tbusiness.industryHazard ratioStroke VolumeStroke volumeMiddle Agedmedicine.diseasePrognosisPeptide FragmentsDeathHeart failureChronic Diseasebiology.proteinCardiologyBiomarker (medicine)FemaleCardiology and Cardiovascular MedicinebusinessBiomarkersFollow-Up StudiesInternational journal of cardiology
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Endocytosis in skeletal muscle fibers.

1999

Defining the organization of endocytic pathway in multinucleated skeletal myofibers is crucial to understand the routing of membrane proteins, such as receptors and glucose transporters, through this system. Here we analyzed the organization of the endocytic trafficking pathways in isolated rat myofibers. We found that sarcolemmal-coated pits and transferrin receptors were concentrated in the I band areas. Fluid phase markers were taken up into vesicles in the same areas along the whole length of the fibers and were then delivered into structures around and between the nuclei. These markers also accumulated beneath the neuromuscular and myotendinous junctions. The recycling compartment, lab…

Monosaccharide Transport ProteinsEndosomeEndocytic cycleMuscle Fibers SkeletalFluorescent Antibody TechniqueGene ExpressionMuscle ProteinsTransferrin receptorEndosomesBiologyEndocytosisMicrotubulesSarcolemmaMicrotubuleReceptors TransferrinMyocyteAnimalsMuscle SkeletalCells Culturedchemistry.chemical_classificationGlucose Transporter Type 4Cell MembraneCoated Pits Cell-MembraneCell BiologyEndocytosisCell biologyCell CompartmentationRatsMicroscopy ElectronMembrane proteinchemistryTransferrinLysosomesExperimental cell research
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The influence of leflunomide on cell cycle, IL-2-receptor (IL-2-R) and its gene expression

1994

Leflunomide is a novel immunomodulatory drug shown to be very effective in animal models of autoimmune diseases and transplantation rejection, as well as in human rheumatoid arthritis. Leflunomide's main metabolite, A77 1726, has been shown to be reversibly antiproliferativein vitro. Pursuing this, we performed cell cycle analysis by flow cytometry of a B-cell lymphoma line and found that at concentrations >2.5 μM cells accumulated in the early S-phase. In order to determine A77 1726's effects on cell activation, human peripheral blood lymphocytes (PBL) were cultured in the presence of PHA or OKT 3 antibody. Flow cytometric evaluation of IL-2 and transferrin receptor expression exhibited a …

Pharmacologymedicine.diagnostic_testImmunologyTransferrin receptorBiologyCell cycleToxicologyMolecular biologyFlow cytometryTransplantationGene expressionmedicinePharmacology (medical)IL-2 receptorCell activationLeflunomidemedicine.drugAgents and Actions
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Effect of Caseinophosphopeptides from αs- and β-Casein on Iron Bioavailability in HuH7 Cells

2015

International audience; Two pools of caseinophosphopeptides (CPPs) obtained from αs- and β-casein fractions (α-CPPs and β-CPPs) were characterized. A total of 16 CPPs were identified in the α-CPPs pool, 9 of them derived from αs1-casein and 7 from αs2-casein. A total of 18 CPPs were identified in the β-CPPs pool. Four of the identified CPPs contained the characteristic phosphoseryl-glutamic acid cluster SpSpSpEE. Calcein assay was used to compare the iron-binding capacity of the α- and β-CPPs pools. At the concentration of 12.5 μM CPPs used in the iron bioavailability assays, β-CPPs pools show greater iron-binding capacity than α-CPPs pools. HuH7 human hepatoma cells show many differentiate…

PhosphopeptidesIronBiological AvailabilitydigestionModels BiologicalMass Spectrometryproduit laitierchemistry.chemical_compoundcaséinophosphopeptideIn vivoCell Line TumorReceptors Transferrinferritine[SDV.IDA]Life Sciences [q-bio]/Food engineeringHumanscellule HuH7Chromatography High Pressure LiquidComputingMilieux_MISCELLANEOUSSoluble transferrin receptorbiologytransferrine solubleCaseinsGeneral ChemistryMolecular biologyBioavailabilityFerritinCalceinnutritionchemistryβ caseinBiochemistryFerritinsbiology.proteinGeneral Agricultural and Biological Sciences[SDV.AEN]Life Sciences [q-bio]/Food and NutritionJournal of Agricultural and Food Chemistry
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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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Novel host-specific iron acquisition system in the zoonotic pathogenVibrio vulnificus

2015

Summary Vibrio vulnificus is a marine bacterium associated with human and fish (mainly farmed eels) diseases globally known as vibriosis. The ability to infect and overcome eel innate immunity relies on a virulence plasmid (pVvbt2) specific for biotype 2 (Bt2) strains. In the present study, we demonstrated that pVvbt2 encodes a host-specific iron acquisition system that depends on an outer membrane receptor for eel transferrin called Vep20. The inactivation of vep20 did not affect either bacterial growth in human plasma or virulence for mice, while bacterial growth in eel blood/plasma was abolished and virulence for eels was significantly impaired. Furthermore, vep20 is an iron-regulated ge…

chemistry.chemical_classificationbiologyVibrio harveyiVirulenceTransferrin receptorVibrio vulnificusbiology.organism_classificationMicrobiologyMicrobiologyPlasmidPhotobacterium damselaechemistryTransferrinPathogenEcology Evolution Behavior and SystematicsEnvironmental Microbiology
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Genetische Hämochromatose und das HFE-Gen: von der Molekulargenetik zur klinischen Diagnostik

2000

More than 90% of patients with genetic hemochromatosis carry a characteristic mutation in the HFE-gene (C282Y). HFE modulates the iron uptake by the transferrin receptor. Duodenal crypt cells of HFE-knockout mice show low intracellular iron concentrations which lead to an upregulation of the divalent metal transporter and enhanced iron uptake by duodenal enterocytes. Heterozygosity for the C282Y mutation appears to alter the course of other liver diseases like porphyria cutanea tarda and nonalcoholic steatohepatitis.

congenital hereditary and neonatal diseases and abnormalitiesmedicine.medical_specialtyMutationdigestive oral and skin physiologyGastroenterologynutritional and metabolic diseasesTransferrin receptorBiologymedicine.diseasemedicine.disease_causedigestive systemPathogenesisLoss of heterozygosityEndocrinologyDownregulation and upregulationInternal medicineMolecular geneticsmedicinePorphyria cutanea tardaskin and connective tissue diseasesHemochromatosisZeitschrift für Gastroenterologie
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Regulation of the Transferrin Receptor Recycling in Hepatitis C Virus-Replicating Cells

2020

After binding of its ligand transferrin, the transferrin receptor (TfR) is internalized via early endosomes. Ligand and receptor can be recycled. α-Taxilin was identified as an essential factor for TfR recycling. Apart from its role for iron uptake, TfR is a coreceptor for hepatitis C virus (HCV) infection. In HCV-replicating cells, the amount of a-taxilin is decreased. This study aims to investigate the effect of decreased α-taxilin levels in HCV-replicating cells on recycling of TfR, its amount on the cell surface, on iron uptake, and the impact of a disturbed TfR recycling on HCV superinfection exclusion. TfR amount and localization were determined by CLSM and surface biotinylation. α-ta…

hepatitis C virus0301 basic medicineEndosomemedia_common.quotation_subjectTransferrin receptorSuperinfection exclusionCell and Developmental Biology03 medical and health sciences0302 clinical medicineiron metabolismInternalizationReceptorlcsh:QH301-705.5iron metabolism ; transferrin receptor ; α-taxilin ; HCV superinfection ; Hepatitis C ; hepatitis C virusOriginal Researchmedia_commonchemistry.chemical_classificationα-taxilinHCV superinfectionvirus diseasesCell Biologytransferrin receptorLigand (biochemistry)Cell biology030104 developmental biologylcsh:Biology (General)chemistryTransferrin030220 oncology & carcinogenesisIntracellularDevelopmental BiologyFrontiers in Cell and Developmental Biology
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Fluorescent quantum dot labeling of canine transferrin receptor with biotin ligase

2007

koiran parvoviruscanine transferrin receptorcanine parvovirusquantum dotbiotin ligaseparvoviruksetBirA
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