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The association of erythroblasts with macrophages promotes erythroid
proliferation and maturation: a 30-kD heparin-binding protein is involved
in this contact
M Hanspal and JS Hanspal
Department of Biomedical Research, St Elizabeth's Medical Center, Tufts
University School of Medicine, Boston, MA 02135.
Although the association of erythroblasts with macrophages has been well
documented in the human bone marrow, the function and identification of the
intimate contacts occurring between the membranes of these two cell types
in the physiology of erythropoiesis is not known. Using in vitro cultures
of human peripheral blood derived erythroid progenitors, we have shown the
presence of erythroblastic islands consisting of a central macrophage
surrounded by a ring of erythroblasts that undergo terminal maturation
leading to enucleation. However, when cultures were carried in the absence
of intact macrophages, erythroid cells matured to the late erythroblast
stage but failed to enucleate. Furthermore, the number of erythroid cells
was markedly reduced in macrophage-depleted cultures, suggesting that the
erythroblast-macrophage contact promotes proliferation and terminal
maturation of erythroid cells leading to their enucleation. To examine the
molecule(s) involved in the interaction between erythroblasts and
macrophages, we have used a cell attachment assay involving incubation of
solubilized surface-labeled erythroblasts with macrophage membrane proteins
separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and
transferred to a nitrocellulose membrane. Erythroblast surface proteins
specifically attached to a 30-kD protein from macrophage membranes, whereas
no adhesion was seen to the protein standards. An apparently similar
protein of 30 kD was also detected on erythroblasts and was shown to
mediate erythroblast-erythroblast contact in addition to the
erythroblast-macrophage contact. The extraction of plasma membranes with
Triton X-100 showed that the 30-kD protein is linked to the membrane
skeleton via an integral membrane protein both in erythroblasts and
macrophages. Furthermore, our results show that the cell:cell interactions
mediated by the 30-kD protein are calcium-independent and could be
specifically inhibited by heparin. We conclude that the association of
erythroblasts with macrophages promotes erythroid proliferation and
maturation leading to erythroblast enucleation and that a 30-kD
heparin-binding protein present on the surface of macrophages and
erythroblasts is involved in this contact. This protein is capable of
binding homotypic and heterotypic cells.
Volume 84,
Issue 10,
pp. 3494-3504,
11/15/1994
Copyright © 1994 by The American Society of Hematology
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