Evidence for a different mechanism of lactoferrin and transferrin translocation on HT 29-D4 cells.
The fate of [125I] lactoferrin after binding on its specific receptor on HT29-D4 cells, a clone of HT29 cells, was studied and compared with that of [125I]transferrin. Time courses of protein binding in relation with temperature clearly show that different mechanisms of ligand-transportation for the two glycoproteins exist on these cells: whereas transferrin would enter into the cell probably by a relatively classic pathway of receptor-mediated endocytosis, lactoferrin and its specific receptor would not be internalized. Thus the mechanism by which lactoferrin promotes HT29 cell growth seems quite different from that of transferrin on the same cells.
Roiron-Lagroux
D
D
Groupe de Recherche sur les Glandes Exocrines, Marseille, France.
Figarella
C
C
D001692:Biological Transport; D004705:Endocytosis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000378:metabolism; D007700:Kinetics; D007781:Lactoferrin / Q000378:metabolism*; D007782:Lactoglobulins / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011990:Receptors, Transferrin / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D007782:Lactoglobulins; D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin; C038340:lactoferrin receptors; D007501:Iron; D007781:Lactoferrin