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Myeloid and erythroid progenitor cells from normal bone marrow adhere to
collagen type I
M Koenigsmann, JD Griffin, J DiCarlo and SA Cannistra
Division of Tumor Immunology, Dana-Farber Cancer Institute, Harvard Medical
School, Boston, MA.
One of the mechanisms by which normal hematopoietic progenitor cells remain
localized within the bone marrow microenvironment is likely to involve
adhesion of these cells to extracellular matrix (ECM) proteins. For
example, there is evidence that uncommitted, HLA-DR-negative progenitor
cells and committed erythroid precursors (BFU-E) bind to fibronectin.
However, fibronectin is not known to mediate binding of committed myeloid
(granulocyte-macrophage) progenitors, raising the possibility that other
ECM proteins may be involved in this process. We investigated the binding
of the MO7 myeloid cell line to a variety of ECM proteins and observed
significant specific binding to collagen type I (56% +/- 5%), minimal
binding to fibronectin (18% +/- 4%) or to laminin (19% +/- 5%), and no
binding to collagen type III, IV, or V. Similarly, normal bone marrow
myeloid progenitor cells (CFU-GM) demonstrated significant specific binding
to collagen type I (46% +/- 8% and 47% +/- 12% for day 7 CFU-GM and day 14
CFU-GM, respectively). The ability of collagen to mediate binding of
progenitor cells was not restricted to the myeloid lineage, as BFU-E also
showed significant binding to this ECM protein (40% +/- 10%). The binding
of MO7 cells and CFU-GM was collagen-mediated, as demonstrated by complete
inhibition of adherence after treatment with collagenase type VII, which
was shown to specifically degrade collagen. Binding was not affected by
anti-CD29 neutralizing antibody (anti-beta-1 integrin), the RGD-containing
peptide sequence GRGDTP, or divalent cation chelation, suggesting that
collagen binding is not mediated by the beta-1 integrin class of adhesion
proteins. Finally, mature peripheral blood neutrophils and monocytes were
also found to bind to collagen type I (25% +/- 8% and 29% +/- 6%,
respectively). These data suggest that collagen type I may play a role in
the localization of committed myeloid and erythroid progenitors within the
bone marrow microenvironment.
Volume 79,
Issue 3,
pp. 657-665,
02/01/1992
Copyright © 1992 by The American Society of Hematology
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