title: Receptor-mediated endocytosis of transferrin and ferritin by guinea-pig reticulocytes. Uptake by a common endocytic pathway.
abstract: Earlier studies have shown that transferrin binds to specific receptors on the reticulocyte surface, clusters in coated pits and is then internalized via endocytic vesicles. Guinea-pig reticulocytes also have specific receptors for ferritin. In this paper ferritin and transferrin endocytosis by guinea-pig reticulocytes was studied by electron microscopy using the natural electron density of ferritin and colloidal gold-transferrin (AuTf). At 4 degrees C both ligands bound to the cell surface. At 37 degrees C progressive uptake occurred by endocytosis. AuTf and ferritin clustered in the same coated pits and small intracellular vesicles. After 60 min incubations the ligands colocalized to large multivesicular endosomes (MVE), still membrane-bound. MVE subsequently fused with the plasma membrane and released AuTf, ferritin and inclusions by exocytosis. All endocytic structures labelled with AuTf contained ferritin, but 23 to 35% of ferritin-labelled endocytic structures contained no AuTf. These data suggest that ferritin and transferrin are internalized through the same pathway involving receptors, coated pits and vesicles, but that these proteins are recycled only partly in common.
mesh_terms: D000818:Animals; D004705:Endocytosis; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D005293:Ferritins / Q000097:blood*; D006168:Guinea Pigs; D033862:Iron-Binding Proteins; D007700:Kinetics; D008854:Microscopy, Electron; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011990:Receptors, Transferrin / Q000378:metabolism*; D012156:Reticulocytes / Q000378:metabolism* / Q000648:ultrastructure; D014168:Transferrin / Q000378:metabolism*
chemical_list: D033862:Iron-Binding Proteins; D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin; C027293:ferritin receptor; D005293:Ferritins