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The active monomeric form of macrophage inflammatory protein-1 alpha
interacts with high- and low-affinity classes of receptors on human
hematopoietic cells
BR Avalos, KJ Bartynski, PJ Elder, MS Kotur, WG Burton and NM Wilkie
Department of Internal Medicine, Ohio State University Hospitals, Columbus.
Macrophage inflammatory protein-1 alpha (MIP-1 alpha) and its human
homologue GOS19.1/LD78 are members of the C-C chemokine/intercrine family
of secreted proteins. They have proinflammatory properties and also inhibit
cell cycle progression of hematopoietic stem cells. Characterization of
MIP-1 alpha receptor(s) has been confused because of its reported
aggregation to inactive forms. Using a defined monomeric form of MIP-1
alpha that is biologically active for stem cell inhibition and induction of
oxidative metabolism in polymorphonuclear cells, we report the detection of
high- and low-affinity receptor classes on human leukemic CD34+ blast
cells, promyelocytic cells, monocytes, peripheral blood neutrophils, and T
cells. Both high- and low-affinity classes are expressed simultaneously in
promyelocytes and neutrophils. The calculated kd for high-affinity
receptors correlates with the concentrations of MIP-1 alpha required to
induce a biologic effect on stem cells and neutrophils. Cross-linking
studies show that MIP-1 alpha associates with two cell surface proteins
with apparent molecular masses of 92 kD and 52 kD. Direct competition
binding studies combined with studies on the inhibition of stem cells show
that human and murine MIP-1 alpha have different receptor-binding and
biologic properties.
Volume 84,
Issue 6,
pp. 1790-1801,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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