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*
Section of Toxicology and Biomedicine, Ente per le Nuove Tecnologie, l’Energia et l’Ambiente C.R. Casaccia; and
Department of Biology, University of Tor Vergata, Rome, Italy
Although a large amount of information is available on the activity
of CTLA-4 in T cells, the role of this receptor in B cells has not been
previously characterized. Our results show that CD40 or LPS stimulation
in the presence of IL-4 induces CTLA-4 expression in purified B cells;
the maximum level is reached in both membrane and intracellular
compartments after 48–72 h. Engagement of the B cell CTLA-4 by
immobilized mAb inhibits IgG1 and IgE production and reduces the
frequency of IgG1- and IgE-expressing B cells. C
and
C
1 germline mRNA expression as well as NF-
B and STAT6
activation, events required for isotype switching, are also inhibited
by CTLA-4 engagement. Together these findings show the critical role of
CTLA-4 in the control of IL-4-driven isotype switching and suggest new
approaches for modulating immediate-type hypersensitivity
responses.
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