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Effect of Caseinophosphopeptides from αs- and β-Casein on Iron Bioavailability in HuH7 Cells

Garcia-Nebot, Maria Jose, Alegria, Amparo, Barbera, Reyes, Gaboriau, Francois, Bouhallab, Said
Journal of agricultural and food chemistry 2015 v.63 no.30 pp. 6757-6763
alphaS1-casein, alphaS2-casein, beta-casein, bioavailability, ferritin, hepatocytes, hepatoma, humans, transferrin
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.