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Interleukin-4 receptor regulation in human monocytic cells
H de Wit, DW Hendriks, MR Halie and E Vellenga
Department of Internal Medicine, University of Groningen, The Netherlands.
The regulation of the interleukin-4 receptor (IL-4R) was studied at mRNA
and protein level in monocytic cells on stimulation with activators of
different intracellular signaling pathways and IL-4. Activation of protein
kinase C-dependent pathways with phorbol myristate acetate (PMA) or
activation of protein kinase A-dependent pathways with DBcAMP and
prostaglandin E2 resulted in an augmented IL- 4R expression at mRNA and
protein level. Transcriptional and posttranscriptional mechanisms seemed to
be involved in the promotive effect of DBcAMP because the transcription
rate increased 1.8-fold, and the half-life of IL-4R mRNA was prolonged to
150 minutes compared with 120 minutes in unstimulated cells. In contrast,
the effect of PMA could only be ascribed to changes at transcriptional
level. However, activation of Ca(2+)-dependent pathways with A23187 or
stimulation with IL-4 had no effect on the IL-4R expression. The
unresponsiveness to IL- 4 could not be ascribed to a nonfunctional receptor
because IL-4 did modulate the CD14, CD23, and HLA-DR antigen expression.
These results are in contrast with IL-4R regulation in T cells, which is
affected by IL-4- and Ca(2+)-dependent pathways. The discrepancy might be
caused by the presence of the common IL-2 receptor gamma chain (gamma c) in
T cells and the absence of the gamma c in monocytic cells, as has been
shown by polymerase chain reaction. These data indicate that IL-4Rs are
differentially regulated, depending on the cell type studied.
Volume 84,
Issue 2,
pp. 608-615,
07/15/1994
Copyright © 1994 by The American Society of Hematology
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