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Blood, Vol. 92 No. 6 (September 15), 1998:
pp. 2123-2132
Characterization of Siglec-5, a Novel Glycoprotein Expressed on
Myeloid Cells Related to CD33
Ann L. Cornish,
Sylvie Freeman,
Gareth Forbes,
Jian Ni,
Mei Zhang,
Mario Cepeda,
Reiner Gentz,
Meena Augustus,
Kenneth C. Carter, and
Paul R. Crocker
From The Wellcome Trust Building, Department of Biochemistry,
University of Dundee, Dundee, Scotland, UK; the Institute of Molecular
Medicine, John Radcliffe Hospital, University of Oxford, Oxford, UK;
and Human Genome Sciences Inc, Rockville, MD.
We describe the characterization of siglec-5 (sialic acid-binding
Ig-like lectin-5), a novel transmembrane member of the immunoglobulin superfamily, highly related to the myeloid antigen, CD33. A full-length cDNA encoding siglec-5 was isolated from a human activated monocyte cDNA library. Sequencing predicted that siglec-5 contains four extracellular immunoglobulin-like domains, the N-terminal two of which
are 57% identical to the corresponding region of CD33. The cytoplasmic
tail is also related to that of CD33, containing two tyrosine residues
embodied in immunoreceptor tyrosine-based inhibitory motif-like motifs.
The siglec-5 gene was shown to map to chromosome 19q13.41-43, closely
linked to the CD33 gene. When siglec-5 was expressed on COS cells or as
a recombinant protein fused to the Fc region of human IgG1, it was able
to mediate sialic acid-dependent binding to human erythrocytes and
soluble glycoconjugates, suggesting that it may be involved in
cell-cell interactions. By using specific antibodies, siglec-5 was
found to have an expression pattern distinct from that of CD33, being
present at relatively high levels on neutrophils but absent from
leukemic cell lines representing early stages of myelomonocytic
differentiation. Western blot analysis of neutrophil lysates indicated
that siglec-5 exists as a disulfide-linked dimer of approximately 140 kD.
© 1998 by The American Society of Hematology.
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