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In vitro characterization of the human recombinant soluble granulocyte-
macrophage colony-stimulating factor receptor
CB Brown, P Beaudry, TD Laing, S Shoemaker and K Kaushansky
Department of Medicine, University of Calgary, Alberta, Canada.
We have cloned, expressed, and partially purified a naturally occurring,
truncated, soluble form of the human granulocyte-macrophage
colony-stimulating factor (GM-CSF) receptor alpha subunit to investigate
its biochemical and biologic properties. The soluble receptor species lacks
the transmembrane and cytoplasmic domains that are presumably removed from
the intact receptor cDNA by a mechanism of alternative splicing. The
resulting soluble 55- to 60-kD glycosylated receptor species binds GM-CSF
with a dissociation constant (kd) of 3.8 nmol/L. The soluble GM-CSF
receptor successfully competes for GM-CSF binding not only with the
transmembrane-anchored GM-CSF receptor alpha subunit but also with the
native oligomeric high-affinity receptor complex. In addition, in human
bone marrow colony-forming assays, the soluble GM-CSF receptor species can
antagonize the activity of GM-CSF. Our data suggest that the soluble GM-CSF
receptor may be capable of acting in vivo as a modulator of the biologic
activity of GM-CSF.
Volume 85,
Issue 6,
pp. 1488-1495,
03/15/1995
Copyright © 1995 by The American Society of Hematology
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