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J Biol Chem, Vol. 275, Issue 2, 861-866, January 14, 2000
From We describe the characterization of siglec-8, a
novel sialic acid-binding immunoglobulin-like lectin that is expressed
specifically by eosinophils. A full-length cDNA encoding siglec-8
was isolated from a human eosinophil cDNA library. Siglec-8 is
predicted to contain three extracellular immunoglobulin-like domains, a
transmembrane region, and a cytoplasmic tail of 47 amino acids. The
siglec-8 gene mapped on chromosome 19q13.33-41, closely
linked to genes encoding CD33 (siglec-3), siglec-5, siglec-6, and
siglec-7. When siglec-8 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 to soluble sialoglycoconjugates. Using specific
monoclonal antibodies, siglec-8 could be detected only on eosinophils
and hence appears to be the first example of an eosinophil-specific
transmembrane receptor.
Siglec-8
A NOVEL EOSINOPHIL-SPECIFIC MEMBER OF THE IMMUNOGLOBULIN
SUPERFAMILY*
,
,
The Wellcome Trust Biocentre at Dundee,
Department of Biochemistry, University of Dundee, Dundee DD1 5EH,
Scotland, United Kingdom, § Human Genome Sciences, Inc.,
Rockville, Maryland 20850-3338, and the ¶ Imperial Cancer
Research Fund, 44 Lincoln's Inn Fields, London WC1, United Kingdom
*
This work was supported by The Wellcome Trust and the
Imperial Cancer Research Fund.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.
To whom correspondence should be addressed. Tel.:
44-1382-345781; Fax: 44-1382-345855; E-mail:
p.r.crocker@dundee.ac.uk.
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