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Anemia of the Belgrade rat: evidence for defective membrane transport of
iron
BJ Bowen and EH Morgan
The mechanisms underlying the impaired utilization of transferrin-bound
iron by erythroid cells in the anemia of the Belgrade laboratory rat were
investigated using reticulocytes from homozygous anemic animals and
transferrin labeled with 59Fe and 125I. The results were compared with
those obtained using reticulocytes from phenylhydrazine-treated rats and
iron-deficient rats. Each step in the iron uptake mechanism was
investigated, ie, transferrin-receptor interaction, transferrin
endocytosis, iron release from transferrin, and transferrin exocytosis.
Although there were quantitative differences, no fundamental difference was
found in any of the abovementioned aspects of cellular function when the
reticulocytes from Belgrade rats were compared with those from
iron-deficient animals. The basic defect in the Belgrade reticulocytes must
therefore reside in subsequent steps in iron uptake, after it is released
from transferrin within endocytotic vesicles, ie, in the mechanism by which
it is transferred across the lining membrane of the vesicles into the cell
cytosol. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis
(SDS-PAGE) of reticulocyte ghosts extracts demonstrated a prominent protein
band of mol wt 69,000 that was absent or present only in low concentration
extracts from the other two types of reticulocytes. This may be a result of
the genetic defect.
Volume 70,
Issue 1,
pp. 38-44,
07/01/1987
Copyright © 1987 by The American Society of Hematology

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