Friend erythroleukemia cell membrane transferrin receptors.
We have compared the uptake of transferrin by murine Friend erythroleukemia cells with the uptake of transferrin by murine reticulocytes. Friend cells which had been induced to erythroid differentiation by dimethyl sulfoxide took up transferrin in a manner qualitatively and quantitatively similar to the uptake of transferrin by reticulocytes, while uninduced Friend cells took up only negligible amounts of transferrin. Specific transferrin-binding activity could be demonstrated in detergent extracts of membranes from induced cells and this activity was isolated from membrane extracts by the use of antibody to transferrin. The isolated membrane component(s) with transferrin-binding activity migrated electrophoretically as a single protein on sodium dodecyl sulfate gels and had similar properties to a transferrin-binding protein isolated previously from reticulocytes.
D000818:Animals; D001692:Biological Transport; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D002999:Clone Cells; D006801:Humans; D007501:Iron / Q000378:metabolism; D007700:Kinetics; D007942:Leukemia, Experimental / Q000378:metabolism*; D051379:Mice; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011990:Receptors, Transferrin; D012156:Reticulocytes / Q000378:metabolism; D013696:Temperature; D014168:Transferrin / Q000378:metabolism*
D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin; D007501:Iron