Transport of iron bound to recombinant human lactoferrin from rice and iron citrate across Caco-2 cell monolayers.
The possibility of using recombinant human lactoferrin from rice (rhLF) makes it necessary to study its differences from the protein of milk. In this work, the binding of different iron-saturated forms of rhLF to Caco-2 cells was studied. Iron-saturated rhLF bound in higher proportion than the apo-form, but, the data obtained for specific binding were not compatible with receptor-mediated binding. Competition assays showed the same binding capacity for human milk lactoferrin as for rhLF to Caco-2 cells. Another basic protein of milk, lactoperoxidase, was found to compete with rhLF for binding to Caco-2 cell membranes, suggesting an electrostatic interaction. The transport of iron ((59)Fe) bound to rhLF and to citrate and the transport of rhLF ((125)I-labeled) were studied on Caco-2 monolayers. Transport of iron was found to be significantly greater when bound to citrate than to rhLF. The amount of intact lactoferrin that traversed the Caco-2 monolayers was very low, suggesting degradation of it across these cells.
Conesa
Celia
C
Department of Animal Production and Food Science, Food Technology Unit, Veterinary Faculty, University of Zaragoza, Spain.
Pocoví
Coloma
C
Pérez
María-Dolores
MD
Calvo
Miguel
M
Sánchez
Lourdes
L
D000818:Animals; D001692:Biological Transport; D018938:Caco-2 Cells; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D005290:Ferric Compounds / Q000378:metabolism*; D006801:Humans; D007501:Iron / Q000378:metabolism*; D007781:Lactoferrin / Q000378:metabolism*; D012275:Oryza; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism*
D005290:Ferric Compounds; D010940:Plant Proteins; D011994:Recombinant Proteins; C025314:ferric citrate; D007501:Iron; D007781:Lactoferrin