In vitro characterization of the human recombinant soluble granulocyte-macrophage colony-stimulating factor receptor.

Abstract:

: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.

journal_name

Blood

journal_title

Blood

authors

Brown CB,Beaudry P,Laing TD,Shoemaker S,Kaushansky K

subject

Has Abstract

pub_date

1995-03-15 00:00:00

pages

1488-95

issue

6

eissn

0006-4971

issn

1528-0020

journal_volume

85

pub_type

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