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Dual role of fibronectin in hematopoietic differentiation
R Weinstein, MA Riordan, K Wenc, S Kreczko, M Zhou and N Dainiak
Department of Biomedical Research, St. Elizabeth's Hospital, Brighton, MA
02135.
The adhesive glycoprotein fibronectin provides anchorage for fibroblasts
and hematopoietic progenitor cells in vitro. Fibronectin also demonstrates
growth factor activity for fibroblasts; however, there is no available
information regarding its role as a hematopoietic growth factor. To
distinguish growth factor activity of fibronectin from its anchorage
activity for hematopoietic progenitors, we assessed the ability of purified
human plasma fibronectin to promote human bone marrow erythroid,
granulocyte-macrophage (GM) and mixed granulocyte-
erythroid-macrophage-megakaryocyte (GEMM) colony formation in liquid
suspension, methylcellulose, and fibrin clots under serum-free conditions.
Addition of fibronectin to methylcellulose cultures, or to cultures formed
in fibrin clots, using fibrinogen depleted of fibronectin by preadsorption
over gelatin-Sepharose and clotted with thrombin, resulted in up to a
twofold enhancement of proliferation of erythroid burst-forming units
(BFU-E), erythroid colony-forming units (CFU-E), and CFU-GEMM. This effect
was concentration-dependent up to a fibronectin supplement of 100
micrograms/mL. By contrast, CFU-GM proliferation was not affected by the
addition of fibronectin to the cultures. Fibronectin-adherent marrow cells
overlaid with liquid medium formed both early and late-appearing erythroid
colonies, whereas similarly cultured plastic-adherent marrow cells did not.
Erythroid colony formation was observed in cultures of fibronectin-adherent
marrow cells overlaid with methylcellulose but not in cultures of
plastic-adherent marrow cells under the same conditions. Finally, the
erythroid growth-promoting activity of fibronectin was inhibited by
arginyl-glycyl-aspartyl-serine (RGDS), a tetrapeptide that competitively
blocks the interaction of fibronectin with its receptor. We conclude that
fibronectin plays a dual role in hematopoiesis: providing (a) anchorage for
erythroid and primitive progenitors, and (b) as a proliferative stimulus
for these hematopoietic cells. Both activities may be mediated by the cell
adhesion domain of the molecule.
Volume 73,
Issue 1,
pp. 111-116,
01/01/1989
Copyright © 1989 by The American Society of Hematology
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