| First Author | Tangye SG | Year | 2002 |
| Journal | Eur J Immunol | Volume | 32 |
| Issue | 6 | Pages | 1640-9 |
| PubMed ID | 12115647 | Mgi Jnum | J:77092 |
| Mgi Id | MGI:2180989 | Doi | 10.1002/1521-4141(200206)32:6<1640::AID-IMMU1640>3.0.CO;2-S |
| Citation | Tangye SG, et al. (2002) CD84 is up-regulated on a major population of human memory B cells and recruits the SH2 domain containing proteins SAP and EAT-2. Eur J Immunol 32(6):1640-9 |
| abstractText | CD84 is a member of the CD2 subset of the immunoglobulin superfamily of cell surface receptors. Several members of this family are involved in the activation of T cells and NK cells. Although CD84 was originally cloned from a human B cell line cDNA library, very little is known regarding its biology on primary human leukocytes. We investigated the expression and biochemistry of CD84 on human B cells. CD84 was expressed on B cells in peripheral blood, spleen and cord blood. Two populations of splenic B cells could be resolved, CD84(lo) and CD84(hi). CD84(hi) B cells represented a subset of memory B cells as demonstrated by increased cell size, co-expression of the memory B cell-specific marker CD27, somatically mutated Ig variable region genes, and increased proliferation compared to CD84(lo) B cells. CD84 became rapidly phosphorylated on tyrosine residues following ligation with a specific monoclonal antibody and recruited the cytoplasmic adaptor proteins SAP and EAT-2. The ability of CD84 to undergo tyrosine phosphorylation and to recruit these SH2 domain-containing proteins suggests it may function in the activation of B cells, particularly memory cells, and its signal transduction pathway may utilize SAP and/or EAT-2. Thus, investigation of expression and function of CD84 and CD27 is likely to contribute to a greater understanding of the development and biology of memory B cells in normal and immunocompromised hosts. |
