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Coordinate expression and developmental role of Id2 protein and TAL1/E2A
heterodimer in erythroid progenitor differentiation
G Condorelli, L Vitelli, M Valtieri, I Marta, E Montesoro, V Lulli, R Baer and C Peschle
Thomas Jefferson Cancer Institute, Thomas Jefferson University,
Philadelphia, PA 19107-5541, USA.
The Id proteins and basic helix-loop-helix (bHLH) proteins play major roles
in specifying cell fate decisions in diverse biologic settings. A potential
role for Id and TAL1/E2A bHLH genes in hematopoiesis has been suggested by
studies on immortalized cell lines. However, it is uncertain whether these
observations reflect normal hematopoiesis. We have investigated the
expression pattern of Id2 and TAL1/E2A genes in liquid suspension culture
of purified hematopoietic progenitor cell (HPCs) undergoing erythroid or
granulopoietic differentiation in the first culture week and maturation to
terminal cells in the second week. In quiescent, freshly purified HPCs, Id2
mRNA is detected by reverse transcriptase-polymerase chain reaction
(RT-PCR), whereas TAL1 and E2A mRNAs are not. At the onset of erythroid
differentiation, Id2 mRNA is downregulated, while E2A and TAL1 mRNAs are
concomitantly upregulated: their expression is further increased at
erythroblast level. Conversely, Id2 is not downmodulated in granulopoietic
culture, except for a late decline at day 10 to 12, while TAL1 and E2A are
only transiently induced in the first week of granulopoietic
differentiation. The expression pattern of the TAL1/E2A heterodimer, as
evaluated by mobility shift assay, is consistent with RT-PCR results
(except for lower levels of the heterodimer in late erythroid maturation).
TAL1 protein level, analyzed by Western blot, shows a pattern consistent
with gelshift results. Functional experiments were performed on purified
HPCs treated with phosphorothioate antisense oligodeoxynucleotides to Id2
or TAL1 mRNA. The results are strictly consistent with the expression
studies: anti-Id2 oligomer (alpha-Id2) causes a significant dose-dependent
increase of erythroid colony formation, whereas alpha-TAL1 induces a
selective dose-related inhibitory effect on erythroid colonies, as compared
with untreated or scrambled oligomer-treated control HPCs. Finally, murine
and human glutathione-S-transferase (GST)-Id2 polypeptides compete the
TAL1/E2A- specific DNA binding activity when added to the nuclear extracts
derived from erythroid culture cells, thus indicating biochemical and
suggesting functional interaction of Id2 with the TAL1/E2A complex. These
novel observations indicate a coordinate expression and function of an
inhibitory Id protein (Id2) and a stimulatory bHLH/bHLH heterodimer
(TAL1/E2A) in normal erythroid differentiation.
Volume 86,
Issue 1,
pp. 164-175,
07/01/1995
Copyright © 1995 by The American Society of Hematology
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