Siglec-8. A novel eosinophil-specific member of the immunoglobulin superfamily - PubMed (original) (raw)

. 2000 Jan 14;275(2):861-6.

doi: 10.1074/jbc.275.2.861.

Affiliations

• PMID: 10625619
• DOI: 10.1074/jbc.275.2.861

Free article

Siglec-8. A novel eosinophil-specific member of the immunoglobulin superfamily

H Floyd et al. J Biol Chem. 2000.

Free article

Abstract

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 IgG(1), 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.

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