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*
Institut National de la Santé et de la Recherche Médicale, Unité 429, Hôpital Necker-Enfants Malades, Paris, France;
Institut National de la Santé et de la Recherche Médicale Unité 520, Institut Curie, Paris, France;
Etablissement de Transfusion Sanguine de l’Assistance Publique-Hôpitaux de Paris, Site Saint-Antoine, Paris, France; and
§
Serono Pharmaceuticals Research Institute, Geneva, Switzerland
CD40/CD40 ligand interactions play a key role in the immune
responses of B lymphocytes, monocytes, and dendritic cells. The signal
transduction events triggered by cross-linking of the CD40 receptor
have been widely studied in B cell lines, but little is known about
signaling following CD40 stimulation of monocytes and resting tonsillar
B cells. Therefore, we studied the CD40 pathway in highly purified
human monocytes and resting B cells. After CD40 triggering, a similar
activation of the NF-
B (but not of the AP-1) transcription factor
complex occurred in both cell preparations. However, the components of
the NF-B complexes were different in monocytes and B cells, because
p50 is part of the NF-B complex induced by CD40 triggering in both
monocytes and B cells, whereas p65 was only induced in B cells. In
contrast, although the Janus kinase 3 tyrosine kinase was associated
with CD40 molecules in both monocytes and resting B cells, Janus kinase
3 phosphorylation induction was observed only in CD40-activated
monocytes, with subsequent induction of STAT5a DNA binding activity in
the nucleus. These results suggest that the activation signals in human
B cells and monocytes differ following CD40 stimulation. This
observation is consistent with the detection of normal CD40-induced
monocyte activation in patients with CD40 ligand+ hyper IgM
syndrome in whom a defect in CD40-induced B cell activation has been
reported.
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