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J. Biol. Chem., Vol. 275, Issue 29, 22127-22135, July 21, 2000
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From the Glycobiology Research and Training Center, Department of
Medicine and Cancer Center, University of California, San Diego,
La Jolla, California 92093
The Siglecs are a subfamily of I-type lectins
(immunoglobulin superfamily proteins that bind sugars) that
specifically recognize sialic acids. We report the cloning and
characterization of human Siglec-9. The cDNA encodes a type 1 transmembrane protein with three extracellular immunoglobulin-like
domains and a cytosolic tail containing two tyrosines, one within a
typical immunoreceptor tyrosine-based inhibitory motif (ITIM). The
N-terminal V-set Ig domain has most amino acid residues typical of
Siglecs. Siglec-9 is expressed on granulocytes and monocytes.
Expression of the full-length cDNA in COS cells induces sialic-acid
dependent erythrocyte binding. A recombinant soluble form of the
extracellular domain binds to The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF227924.
Cloning, Characterization, and Phylogenetic Analysis of
Siglec-9, a New Member of the CD33-related Group of Siglecs
EVIDENCE FOR CO-EVOLUTION WITH SIALIC ACID SYNTHESIS
PATHWAYS*
and
2-3 and 2-6-linked sialic acids.
Typical of Siglecs, the carboxyl group and side chain of sialic acid
are essential for recognition, and mutation of a critical arginine
residue in domain 1 abrogates binding. The underlying glycan structure
also affects binding, with Gal
1-4Glc[NAc] being preferred.
Siglec-9 shows closest homology to Siglec-7 and both belong to a
Siglec-3/CD33-related subset of Siglecs (with Siglecs-5, -6, and -8).
The Siglec-9 gene is on chromosome 19q13.3-13.4, in a cluster with all
Siglec-3/CD33-related Siglec genes, suggesting their origin by gene
duplications. A homology search of the Drosophila
melanogaster and Caenorhabditis elegans genomes
suggests that Siglec expression may be limited to animals of
deuterostome lineage, coincident with the appearance of the genes of
the sialic acid biosynthetic pathway.
*
This work was supported by United States Public Health
Service Grants R01-GM323373 and P01-HL57345.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Partially supported by the Naito Foundation (Tokyo, Japan).
§
To whom correspondence should be addressed: Glycobiology Research
and Training Center, La Jolla, CA 92093-0687. Tel.: 858-534-3296; Fax:
858-534-5611; E-mail: avarki@ucsd.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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