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Loss of attachment to fibronectin with terminal human erythroid
differentiation
MH Vuillet-Gaugler, J Breton-Gorius, W Vainchenker, J Guichard, C Leroy, G Tchernia and L Coulombel
Hematology Laboratory, Hopital Bicetre, Kremlin-Bicetre, France.
Human erythroblastic progenitors (colony-forming unit-erythroid [CFU-E] and
burst-forming unit-erythroid [BFU-E]) have been shown to attach to
fibronectin (Fn), a property that might be involved in the local regulation
of erythropoiesis. In this study, we have investigated changes in cell
attachment to Fn upon terminal erythroid differentiation. We first purified
CFU-E from human marrow by avidin- biotin immune rosetting. This negative
selection procedure yielded a cell population containing approximately 80%
blasts that, after characterization by colony-assays and electron
microscopy, appeared to consist of CFU-E (10% to 15%) and their immediate
progeny (85% to 90%), here defined as "preproerythroblasts." In the
presence of erythropoietin, purified cells differentiated into
reticulocytes in 7 to 10 days. Cell attachment to Fn was inversely
correlated to the stage of differentiation of the erythroid cell: more than
50% of the CFU-E population reproducibly adhered to Fn, whereas at most 30%
of the preproerythroblasts had the same capacity. Adhesion was further lost
at late maturation stages, and a constant finding was the inability of
reticulocytes to adhere to Fn. Finally, CFU-E adhesion to Fn was blocked by
polyclonal lgG raised against the Fn receptor and by a monoclonal antibody
against VLA-5. These results demonstrate that adhesion to Fn is
developmentally regulated during normal human erythropoiesis. Restriction
of its expression to CFU-E and its first divisions strikingly correlates
with the migratory capacity of these cells.
Volume 75,
Issue 4,
pp. 865-873,
02/15/1990
Copyright © 1990 by The American Society of Hematology
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