Evidence for a pool of non-recycling transferrin receptors in peripheral sheep reticulocytes.
Sheep reticulocytes from phlebotomized animals have a total transferrin binding potential that may exceed by an order of magnitude the surface binding capacity. Steady state uptake of transferrin at 37 degrees C is generally less than 50% of the total transferrin binding capacity. During long-term incubation of the reticulocytes, all transferrin binding ability is lost, the ability to internalize being lost most rapidly. The loss in ability to bind transferrin during long-term incubation is independent of the number of surface transferrin binding sites, since removal of surface receptors with pronase does not affect the rate of loss of the internal pool of receptors during long-term incubation. Moreover, after removing surface receptors with pronase, only a fraction of the original number of receptors is restored to the surface, despite the presence of a large pool of internal receptors. These data suggest that only a fraction of the internal pool of receptors is capable of recycling to the cell surface in sheep reticulocytes.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D005290:Ferric Compounds / Q000378:metabolism; D011402:Pronase / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011990:Receptors, Transferrin; D012156:Reticulocytes / Q000378:metabolism*; D012756:Sheep; D013696:Temperature; D014168:Transferrin / Q000378:metabolism*
D005290:Ferric Compounds; D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin; D011402:Pronase