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*
Laboratory for Immunological Research, Schering-Plough, Dardilly, France;
DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304
In this study, we describe human FDF03, a novel member of the Ig
superfamily expressed as a monomeric 44-kDa transmembrane glycoprotein
and containing a single extracellular V-set Ig-like domain. Two
potential secreted isoforms were also identified. The gene encoding
FDF03 mapped to chromosome 7q22. FDF03 was mostly detected in
hemopoietic tissues and was expressed by monocytes, macrophages, and
granulocytes, but not by lymphocytes (B, T, and NK cells), indicating
an expression restricted to cells of the myelomonocytic lineage. FDF03
was also strongly expressed by monocyte-derived dendritic cells (DC)
and preferentially by CD14+/CD1a- DC derived
from CD34+ progenitors. Moreover, flow cytometric analysis
showed FDF03 expression by CD11c+ blood and tonsil DC, but
not by CD11c- DC precursors. The FDF03 cytoplasmic tail
contained two immunoreceptor tyrosine-based inhibitory motif
(ITIM)-like sequences. When overexpressed in pervanadate-treated U937
cells, FDF03 was tyrosine-phosphorylated and recruited Src homology-2
(SH2) domain-containing protein tyrosine phosphatase (SHP)-2 and to a
lesser extent SHP-1. Like engagement of the ITIM-bearing receptor
LAIR-1/p40, cross-linking of FDF03 inhibited calcium mobilization in
response to CD32/Fc
RII aggregation in transfected U937 cells, thus
demonstrating that FDF03 can function as an inhibitory receptor.
However, in contrast to LAIR-1/p40, cross-linking of FDF03 did not
inhibit GM-CSF-induced monocyte differentiation into DC. Thus, FDF03 is
a novel ITIM-bearing receptor selectively expressed by cells of myeloid
origin, including DC, that may regulate functions other than that of
the broadly distributed LAIR-1/p40 molecule.
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