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Published online before print October 21, 2004

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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.0704402

Received for publication July 15, 2004.
Revised September 14, 2004.
Accepted for publication September 23, 2004.

Article

Expression of the largest CD97 and EMR2 isoforms on leukocytes facilitates a specific interaction with chondroitin sulfate on B cells

Mark J. Kwakkenbos ^*, Walter Pouwels ^*, Mourad Matmati ^*, Martin Stacey , Hsi-Hsien Lin , Siamon Gordon , René A. W. van Lier ^*, and Jörg Hamann ^*@

*Laboratory for Experimental Immunology, Academic Medical Centre, University of Amsterdam, The Netherlands; and Sir William Dunn School of Pathology, University of Oxford, United Kingdom

^@ To whom correspondence should be addressed. E-mail: j.hamann{at}amc.uva.nl.

	Abstract

The epidermal growth factor (EGF)-seven-span transmembrane receptors CD97 and EGF-like module-containing mucin-like receptor protein (EMR)2 are heptahelical molecules predominantly expressed on leukocytes. A characteristic of these receptors is their ability to interact with cellular ligands via the N-terminal EGF-like domains. The first two EGF domains of CD97 (but not EMR2) bind CD55 (decay-accelerating factor), and the fourth EGF domain of CD97 and EMR2 interacts with the glycosaminoglycan chondroitin sulfate (CS). Using fluorescent beads coated with soluble recombinant CD97 and EMR2 protein and isoform-specific monoclonal antibodies, we have determined the cellular and molecular characteristics of the interaction with CS. The fourth EGF domain of CD97 and EMR2 is expressed on activated lymphocytes and myeloid cells, whereas the ligand is specifically found on B cells within the peripheral blood. The interaction between CD97/EMR2 and CS may therefore play a role in the interaction of activated T cells, dendritic cells, and macrophages with B cells.

Key Words: B cell • EGF-like domain • ligand specificity • multivalent probe • proteoglycan

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