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Secretion: Adhesion Is Mediated by Ig-Like Domain 11
*
Immunology Unit, Department of Cellular Biology and Pathology, Medical School, and Department of
Physiology, Faculty of Biology, University of Barcelona, and
Liver Unit, Hospital Clinic, Institut d’Investigacions Biomèdiques August Pi ySunyer, Barcelona, Spain
CD84 is a member of the CD2 subset of the Ig superfamily of cell
surface molecules. Its cytoplasmic tail binds to Src homology 2
domain-containing protein 1A (signaling lymphocytic activation
molecule-associated protein), a protein encoded by the X-linked
lymphoproliferative disease gene. It is preferentially expressed on B
lymphocytes, monocytes, and platelets. We show that it is also
expressed on thymocytes and T cells. CD84 was positive on
CD4-CD8- thymocytes, and its expression
decreased with cell maturation. It is expressed on mature T cells
preferentially on CD45RO+. To identify the CD84 ligand, we
generated a soluble Ig fusion protein containing the human CD84
extracellular domains (CD84-Ig). Because receptor-ligand interactions
occur between several members of this subfamily, we assayed CD84-Ig
binding with all members of the CD2 family. CD84-Ig bound to
CD84-transfected cells, whereas no binding was detected with cells
expressing other CD2 subfamily receptors, showing that CD84 binds to
itself. Anti-CD84 mAbs recognizing epitopes wholly within domain 1 of
CD84 blocked the binding of the CD84-Ig fusion protein to
CD84-transfected cells and platelets. Data from CD84 domain human/mouse
chimeras further revealed that only the first extracellular domain of
the molecule is involved in the ligand receptor recognition. The
CD84-CD84 interaction was independent of its cytoplasmic tail. Finally,
concurrent ligation of human CD84 with mAbs or CD84-Ig and CD3 enhanced
IFN-
secretion in human lymphocytes. Thus, CD84 is its own ligand
and acts as a costimulatory molecule.
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