Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: selective externalization of the receptor

Cell. 1983 Jul;33(3):967-78. doi: 10.1016/0092-8674(83)90040-5.


The fate of the transferrin receptor during in vitro maturation of sheep reticulocytes has been followed using FITC- and 125I-labeled anti-transferrin-receptor antibodies. Vesicles containing peptides that comigrate with the transferrin receptor on polyacrylamide gels are released during incubation of sheep reticulocytes, tagged with anti-transferrin-receptor antibodies. Vesicle formation does not require the presence of the anti-transferrin-receptor antibodies. Using 125I-surface-labeled reticulocytes, it can be shown that the 125I-labeled material which is released is retained by an immunoaffinity column of the anti-transferrin-receptor antibody. Using reticulocytes tagged with 125I-labeled anti-transferrin-receptor antibodies to follow the formation of vesicles, it can be shown that at 0 degree C or in phosphate-buffered saline the rate of vesicle release is less than that at 37 degrees C in culture medium. There is selective externalization of the antibody-receptor complex since few other membrane proteins are found in the externalized vesicles. The anti-transferrin-receptor antibodies cause redistribution of the receptor into patches that do not appear to be required for vesicle formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Differentiation
  • Culture Media
  • Erythropoiesis*
  • Exocytosis
  • Extracellular Space / physiology
  • Fluorescent Antibody Technique
  • Kinetics
  • Membranes / physiology
  • Molecular Weight
  • Receptors, Cell Surface / physiology*
  • Receptors, Transferrin
  • Reticulocytes / physiology*
  • Sheep
  • Transferrin / physiology*


  • Culture Media
  • Receptors, Cell Surface
  • Receptors, Transferrin
  • Transferrin