Roiron-Lagroux D, Figarella C
Groupe de Recherche sur les Glandes Exocrines, Marseille, France.
Biochem Biophys Res Commun. 1990 Jul 31;170(2):837-42. doi: 10.1016/0006-291x(90)92167-x.
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.
研究了[125I]乳铁蛋白与HT29细胞克隆HT29-D4细胞上的特异性受体结合后的命运,并与[125I]转铁蛋白进行了比较。蛋白质结合与温度的时间进程清楚地表明,这些细胞上存在两种糖蛋白的不同配体转运机制:转铁蛋白可能通过相对经典的受体介导的内吞作用途径进入细胞,而乳铁蛋白及其特异性受体不会被内化。因此,乳铁蛋白促进HT29细胞生长的机制似乎与同一细胞上的转铁蛋白机制有很大不同。