cDNA isolated from a human B-cell line Raji library was analyzed and shown to encode the full-length cDNA sequence of a novel cell-surface glycoprotein, initially termed HLy9-beta. The predicted mature 307-amino acid protein was composed of two extracellular Ig-like domains, a hydrophobic transmembrane region, and an 83-amino acid cytoplasmic domain. The extracellular Ig-like domains presented structural and sequence homology with a group of members of the Ig superfamily that included CD2, CD48, CD58, and Ly9. Northern blot analysis showed that the expression of HLy9-beta was predominantly restricted to hematopoietic tissues. Chromosome localization studies mapped the HLy9-beta gene to chromosome 1q24, where other members of this Ig superfamily (CD48 and HumLy9) have been mapped. CD84 monoclonal antibodies (MoAbs) were shown to react with cells transfected with the cloned cDNA. These MoAbs were further used to show that CD84 is expressed as a single chain cell-surface glycoprotein of Mr 64,000 to 82,000, which was highly glycosylated. CD84 had a unique pattern of expression, being found predominantly on lymphocytes and monocytes. Thus, the glycoprotein HLy9-beta is recognized by MoAbs previously clustered as CD84 and represents a newly identified member of the Ig superfamily that may play a significant role in leukocyte activation.
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