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PMID: 7532186 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Sialoadhesin binds preferentially to cells of the granulocytic lineage.

The Journal of clinical investigation ·Vol. 95 ·No. 2 ·1995-02-00 ·Pages 635-43

Crocker PR, Freeman S, Gordon S, Kelm S

Abstract

Sialoadhesin is a macrophage-restricted, sialic acid-dependent receptor of 185 kD that binds to the oligosaccharide sequence NeuAc alpha 2,3Gal on cell surface glycoconjugates. Recent cDNA cloning has shown that sialoadhesin is a new member of the immunoglobulin superfamily with sequence similarity to CD22, a sialic acid-dependent receptor of B lymphocytes. Sialoadhesin has been implicated in cellular interactions of stromal macrophages with developing myeloid cells. In this study, direct evidence for this interaction was obtained in cell-cell binding assays using both native and recombinant forms of the protein. In all assays, sialoadhesin exhibited specific, differential binding to various murine cell populations of hemopoietic origin. In rank order, sialoadhesin bound neutrophils > bone marrow cells = blood leukocytes > lymphocytes > thymocytes. Single-cell analyses confirmed that sialoadhesin selectively bound myeloid cells in complex cell mixtures obtained from the bone marrow and blood. In comparison, a recombinant Fc-chimeric form of murine CD22 showed high binding to B and T lymphocytes, but very low binding to immature and mature myeloid cells. These results are consistent with the notion that sialoadhesin in involved in interactions with granulocytes at different stages of their life histories.

MeSH Terms
Animals Carbohydrate Conformation Carbohydrate Sequence Cell Adhesion Molecules/immunology,metabolism Cell Line Chlorocebus aethiops Cloning, Molecular DNA, Complementary Epitopes/analysis Erythrocytes/immunology,metabolism Female Glycoconjugates/chemistry,immunology,metabolism Granulocytes/immunology,metabolism Immunoglobulin Fab Fragments/pharmacology Immunoglobulin G/pharmacology Kinetics Male Membrane Glycoproteins/immunology,isolation & purification,metabolism Mice Mice, Inbred C57BL Molecular Sequence Data Receptors, Immunologic/immunology,isolation & purification,metabolism Recombinant Proteins/immunology,isolation & purification,metabolism Sialic Acid Binding Ig-like Lectin 1 Transfection
Chemicals
Cell Adhesion Molecules DNA, Complementary Epitopes Glycoconjugates Immunoglobulin Fab Fragments Immunoglobulin G Membrane Glycoproteins Receptors, Immunologic Recombinant Proteins Sialic Acid Binding Ig-like Lectin 1 Siglec1 protein, mouse
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Crocker P R
Imperial Cancer Research Fund Laboratories, University of Oxford, John Radcliffe Hospital, United Kingdom.
Freeman S
Gordon S
Kelm S
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Article Info
Journal
The Journal of clinical investigation
Abbr.
J Clin Invest
ISSN
0021-9738
DOI
10.1172/JCI117708
Published
1995-02-00
Pages
635-43
Language
English
Region
United States
NLM ID
7802877
PMCID
PMC295529
Subset
IM
External Links
PubMed source DOI: 10.1172/JCI117708 PMC Full Text View journal details
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