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*
Department of Immunology, Medical Research Institute, Tokyo Medical and Dental University, Tokyo, Japan;
Department of Molecular Immunology, Graduate School of Medicine, Chiba University, Chiba, Japan; and
Tokyo Metropolitan Institute for Neuroscience, Fuchu, Tokyo, Japan
The immunoreceptor tyrosine-based inhibition motif (ITIM) is found
in various membrane molecules such as CD22 and the low-affinity Fc
receptor for IgG in B cells and the killer cell-inhibitory receptor and
Ly-49 in NK cells. Upon tyrosine phosphorylation at the ITIMs, these
molecules recruit SH2 domain-containing phosphatases such as
SH2-containing tyrosine phosphatase-1 and negatively regulate cell
activity. The B cell surface molecule CD72 carries an ITIM and an
ITIM-like sequence. We have previously shown that CD72 is
phosphorylated and recruits SH2-containing tyrosine phosphatase-1 upon
cross-linking of the Ag receptor of B cells (BCR). However, whether
CD72 modulates BCR signaling has not yet been elucidated. In this paper
we demonstrate that expression of CD72 down-modulates both
extracellular signal-related kinase (ERK) activation and
Ca2+ mobilization induced by BCR ligation in the mouse B
lymphoma line K46µm
, whereas BCR-mediated ERK activation was not
reduced by the ITIM-mutated form of CD72. Moreover, coligation with
CD72 with BCR reduces BCR-mediated ERK activation in spleen B cells of
normal mice. These results indicate that CD72 negatively regulates BCR
signaling. CD72 may play a regulatory role in B cell activation,
probably by setting a threshold for BCR
signaling.
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