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RESEARCH PRODUCT
Effect of Caseinophosphopeptides from αs- and β-Casein on Iron Bioavailability in HuH7 Cells
María José García-nebotSaïd BouhallabFrançois GaboriauReyes BarberáAmparo Alegríasubject
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 Nutritiondescription
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 differentiated functions of liver cells in vivo and can be used to evaluate iron bioavailability (ferritin content and soluble transferrin receptor) from Fe−α-CPPs and Fe−β-CPPs complexes. The α-CPPs and β-CPPs pools did not improve ferritin content or soluble transferrin receptor in HuH7 cells.
year | journal | country | edition | language |
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2015-01-01 | Journal of Agricultural and Food Chemistry |