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Adhesion of committed human hematopoietic progenitors to synthetic peptides
from the C-terminal heparin-binding domain of fibronectin: cooperation
between the integrin alpha 4 beta 1 and the CD44 adhesion receptor
CM Verfaillie, A Benis, J Iida, PB McGlave and JB McCarthy
Department of Medicine, University of Minnesota, Minneapolis.
Close interaction of human hematopoietic progenitors with the bone marrow
microenvironment is important for the ordered progression of human
hematopoiesis. Progenitor cell adhesion to stroma has a complex molecular
basis, involving various cell-extracellular matrix and cell- cell
interactions. We have previously shown that adhesion of colony- forming
cells (CFC) to fibronectin, present in stromal extracellular matrix,
involves multiple sites, including two heparin-binding synthetic peptides
(FN-C/H I and FN-C/H II) and the alpha 4 beta 1 integrin-binding peptide
CS1. These synthetic peptides are located in close proximity in the type
III repeat 14 and the immediately adjacent type IIIcs region of
fibronectin. In the current study, we evaluate receptors expressed by CFC
responsible for their adhesion to fibronectin. We show that the alpha 4
beta 1 integrin mediates adhesion to CFC to the peptides FN-C/H I and CS1.
Adhesion of CFC to fibronectin is also mediated by proteoglycans, because
removal of cell surface chondroitin-sulfate proteoglycans resulted in
decreased adhesion of CFC to FN-C/ I and FN-C/H II. The core protein of
this proteoglycan was identified by immunoprecipitation as a 90-kD member
of the CD44 group of adhesion molecules. Interestingly, although the
proteoglycan core protein failed to adhere to FN-C/H II affinity columns,
anti-CD44 monoclonal antibodies blocked CFC adhesion to FN-C/H II,
indicating that these monoclonal antibodies may interfere with core
protein- mediated intracellular signalling. Finally, we show that CD44 and
alpha 4 beta 1 may cooperate in establishing progenitor adhesion, because
anti-CD44 antibodies potentiated the adhesion-inhibitory effects of
suboptimal concentrations of anti-alpha 4 or anti-beta 1 monoclonal
antibodies. These results provide a working model for progenitor cell
recognition of fibronectin (and possibly the marrow micro-environment) in
which the coordinated action of integrins and cell surface proteoglycans is
necessary for cell adhesion. This model can now be used to study the
complex relationship between progenitor cell adhesion and the regulation of
their proliferation and differentiation.
Volume 84,
Issue 6,
pp. 1802-1811,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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