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Identification of a novel low-affinity receptor for human interleukin-7
RJ Armitage, SF Ziegler, DJ Friend, LS Park and WC Fanslow
Immunex Research and Development Corporation, Seattle, WA 98101.
Human recombinant interleukin-7 (IL-7) was labeled with biotin and used to
examine IL-7 receptor (IL-7R) expression and regulation on human primary
hematopoietic cells, the monocytoid line THP1, and a range of B- and
pre-B-celi lines by flow cytometry. A strong intensity of staining was
observed using relatively high (greater than 1 x 10(-7) mol/L)
concentrations of biotinylated IL-7 on the majority of cell types examined.
This reactivity, which could be effectively competed with excess unlabeled
IL-7, did not correlate with either mRNA levels for the cloned receptor or
with estimates of IL-7R expression determined by [125I]IL-7 binding.
Staining of cells with a titration of biotinylated IL-7 showed, at
concentrations greater than 1 x 10(-7) mol/L binding with a Ka in the range
of 1 x 10(6) mol/L-1, to 1 x 10(7) mol/L-1, an affinity 100 to 1,000 times
lower than that reported for the cloned IL- 7 receptor. Further data
suggesting the existence of a distinct low- affinity IL-7R were provided by
two antibodies specific for the cloned IL-7R. Staining with these
monoclonal antibodies (MoAbs) correlated with both IL-7R mRNA levels and
receptor expression determined by [125I]IL-7 binding, but was not
compatible with the distribution of reactivity seen with biotinylated IL-7.
Using tritiated biotin to label IL-7, it was estimated that the total
number of IL-7 binding sites on the cell lines examined ranged from 1 x
10(4) to at least 5 x 10(5)/cell. Cross-linking studies showed that
[125I]IL-7 associated with two major proteins of approximately 62 Kd and 70
Kd on the surface of RPMI 1788 and THP1 cells, in contrast to the 75- to 80
Kd molecule characteristic of the previously cloned receptor, expressed on
the surface of Daudi cells. Proliferation of THP1 cells, expressing only
the low-affinity form of IL-7R and lacking detectable IL-7R mRNA, could be
inhibited by the addition of IL-7 in a concentration-dependent fashion,
indicating that, at least on this cell line, binding of IL-7 with a Ka of 1
x 10(6) mol/L-1 to 1 x 10(7) mol/L-1 can transduce a biological signal.
Taken together, the data contained in this report demonstrate the existence
of a low-affinity IL-7R, expressed in high numbers on hematopoietic cells
of different lineages, which is the product of a gene distinct from that
encoding the cloned IL-7R.
Volume 79,
Issue 7,
pp. 1738-1745,
04/01/1992
Copyright © 1992 by The American Society of Hematology
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