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Dissociation between p93B-myb and p75c-myb expression during the
proliferation and differentiation of human myeloid cell lines
M Arsura, MM Luchetti, E Erba, J Golay, A Rambaldi and M Introna
Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy.
Direct and indirect evidence strongly indicates that the proto-oncogene
c-myb plays an important role in the regulation of both the proliferation
and differentiation of hematopoietic cells. In addition, recent data
suggest that the structurally related B-myb gene is also necessary for the
proliferation of these cells. To help understand the relationship between
these two related gene products during proliferation and differentiation of
myeloid cells, we have studied in parallel the regulated expression of
c-myb and B-myb RNAs and proteins in human myeloid cells that were either
growth-arrested or induced to differentiate along different pathways. For
this purpose, we have produced a polyclonal antibody directed against a
fragment of the recombinant B-myb protein. We have thus been able to detect
the B-myb protein in human cell lines and have found it to be a 93-kD
protein localized in the nucleus. We have chosen two models to study the
expression of both c-myb and B-myb mRNAs and proteins during myeloid
proliferation and differentiation. One of the models was the HL-60 cell
line, which can be induced to differentiate towards the monocytic pathway
with either phorbol ester (phorbol myristate acetate) or vitamin D3 and
towards the granulocytic pathway with either dimethyl sulfoxide or retinoic
acid. In addition, we have studied another recently established human
leukemic cell line, called GF-D8, which is strictly dependent on
granulocyte-macrophage colony-stimulating factor (GM-CSF) for
proliferation. The results show that the expression of B- myb RNA and
protein closely correlates with proliferation in all experimental setups
studied, whereas the c-myb protein levels do not always do so. We observed
that the c-myb protein levels decreased well before the decrease of B-myb
protein and of proliferation itself during differentiation toward
monocytes. Such a difference was not present during granulocytic
differentiation, in which c-myb levels decreased, if anything, later than
those of B-myb and proliferation. Most striking was the finding that high
levels of c-myb RNA and protein, but not of B- myb, were present in the
GF-D8 cell line, even after growth arrest by GM-CSF deprivation. These data
suggest that B-myb may function solely in the regulation of cellular
proliferation, whereas c-myb has additional functions, for example, in the
maintenance of an undifferentiated state.
Volume 83,
Issue 7,
pp. 1778-1790,
04/01/1994
Copyright © 1994 by The American Society of Hematology
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