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Effect of activin A on globin gene expression in purified human erythroid
progenitors
L Shao, NL Frigon , AL Young, AL Yu, LS Mathews, J Vaughan, W Vale and J Yu
Department of Molecular and Experimental Medicine, Scripps Research
Institute, La Jolla, CA 92037.
The regulatory control of human erythropoiesis through a purified protein,
activin A, was examined. Previous studies using mixed populations of bone
marrow cells suggested that activin A has an indirect effect on cellular
proliferation and DNA synthesis of erythroid progenitors through the
mediation of accessory cells. In present studies, the cultures of purified
erythroid progenitors were used to examine the effect of activin A on
globin gene expression. Human erythroid burst-forming units (BFU-E) were
partially purified from peripheral blood, and after 8 days of culture the
cells generated consisted mainly of erythroid colony-forming units (CFU-E).
It was found that the subsequent 7-day cultures of these purified
progenitors yielded similar numbers and size distributions of erythroid
colonies, regardless of the presence of activin A in the cultures. In
addition, these erythroid progenitor cells were responsive, in terms of
stimulation of DNA synthesis, to the addition of erythropoietin, but not to
treatment by activin A. Therefore, once the erythroid progenitors are
depleted of accessory cells, activin A has little effect on both the
proliferation and the DNA synthesis of these progenitors. However, when
these purified erythroid progenitors were cultured in the presence of
activin A, the levels of all alpha, beta, and epsilon globin transcripts
and hemoglobins were significantly increased. In addition, disuccinimidyl
suberate was found to chemically cross-link 125I-activin A to cell surface
binding proteins (45 to 54 Kd) in both purified erythroid progenitors and
K562 cells. The labeling of these binding proteins was specifically
inhibited by the presence of unlabeled activin A, but not transforming
growth factor-beta. These results suggest that, in addition to its indirect
effect on DNA synthesis and cellular proliferation of erythroid
progenitors, activin A directly affects the levels of globin mRNAs and
hemoglobins in developing human erythroid cells through its specific
surface binding receptor(s).
Volume 79,
Issue 3,
pp. 773-781,
02/01/1992
Copyright © 1992 by The American Society of Hematology
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