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J Biol Chem, Vol. 274, Issue 32, 22729-22738, August 6, 1999
From the Molecular Biology Department, DNAX Research Institute,
Palo Alto, California 94304 and the c Divisions of
Hematology-Oncology and Cellular and Molecular Medicine, University of
California at San Diego, La Jolla, California 92093
We report the expression cloning of a novel
leptin-binding protein of the immunoglobulin superfamily (OB-BP1) and a
cross-hybridizing clone (OB-BP2) that is identical to a recently
described sialic acid-binding I-type lectin called Siglec-5.
Comparisons to other known Siglec family members (CD22, CD33,
myelin-associated glycoprotein, and sialoadhesin) show that OB-BP1,
OB-BP2/Siglec-5, and CD33/Siglec-3 constitute a unique related subgroup
with a high level of overall amino acid identity: OB-BP1
versus Siglec-5 (59%), OB-BP1 versus CD33
(63%), and OB-BP2/Siglec-5 versus CD33 (56%). The
cytoplasmic domains are not as highly conserved, but display novel
motifs which are putative sites of tyrosine phosphorylation, including an immunoreceptor tyrosine kinase inhibitory motif and a motif found in
SLAM and SLAM-like proteins. Human tissues showed high levels of OB-BP1
mRNA in placenta and moderate expression in spleen, peripheral
blood leukocytes, and small intestine. OB-BP2/Siglec-5 mRNA was
detected in peripheral blood leukocytes, lung, spleen, and placenta. A
monoclonal antibody specific for OB-BP1 confirmed high expression in
the cyto- and syncytiotrophoblasts of the placenta. Using this antibody
on peripheral blood leukocytes showed an almost exclusive expression
pattern on B cells. Recombinant forms of the extracellular domains of
OB-BP1, OB-BP2/Siglec-5, and CD33/Siglec-3 were assayed for specific
binding of leptin. While OB-BP1 exhibited tight binding
(Kd 91 nM), the other two showed weak
binding with Kd values in the 1-2 µM
range. Studies with sialylated ligands indicated that OB-BP1
selectively bound Neu5Ac
2-6GalNAc (sialyl-Tn) allowing its
formal designation as Siglec-6. The identification of OB-BP1/Siglec-6
as a Siglec family member, coupled with its restricted expression
pattern, suggests that it may mediate cell-cell recognition events by
interacting with sialylated glycoprotein ligands expressed on specific
cell populations. We also propose a role for OB-BP1 in leptin
physiology, as a molecular sink to regulate leptin serum levels.
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