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Blood, Vol. 95 No. 12 (June 15), 2000:
pp. 3868-3877
Engagement of CD11b and CD11c  2 integrin by antibodies or
soluble CD23 induces IL-1 production on primary human monocytes
through mitogen-activated protein kinase-dependent pathways
Roger Rezzonico,
Rachel Chicheportiche,
Veronique Imbert, and
Jean-Michel Dayer
From the Division of Immunology and Allergy, Clinical Immunology
Unit (Hans Wilsdorf Laboratory), Department of Internal Medicine,
University Hospital, Geneva, Switzerland; and INSERM CJF 96-05, Facultè de Mèdecine, Nice, France.
 2 integrins are involved in the recruitment of leukocytes to
inflammatory sites and in cellular activation. We demonstrate that
ligation of CD11b (Mac-1, CR3) or CD11c (p150, CR4) alpha chains of
2 integrins by mAbs or soluble chimeric CD23 (sCD23) on human
freshly isolated monocytes rapidly stimulates high levels of
interleukin-1 production. This induction takes place at the transcriptional level and is regulated by members of the
mitogen-activated protein kinase (MAPK) family. Indeed, stimulation of
monocytes through engagement of CD11b or CD11c results in the
phosphorylation and activation of ERK1, ERK2, and p38/SAPK2 MAP
kinases. U0126, a potent inhibitor of the upstream activator of ERK1/2,
ie, MEK1/2, suppresses IL-1 messenger RNA (mRNA) expression in a
dose-dependent fashion, showing the implication of this pathway in the
transcriptional control of IL-1 production. On the other hand,
inhibition of p38 by SB203580 indicates that this MAPK is involved in
the control of IL-1 production at both transcriptional and
translational levels. Together these data demonstrate that ligation of
CD11b and CD11c 2 integrins by mAbs or sCD23 fusion proteins
triggers the activation of 2 distinct MAPK signaling pathways that
cooperate in controlling IL-1 synthesis at different levels.
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