CEACAM1 is a potent regulator of B cell receptor complex-induced activation

被引:54
作者
Greicius, G
Severinson, E
Beauchemin, N
Öbrink, B
Singer, BB
机构
[1] Karolinska Inst, CMB, Med Nobel Inst, Dept Cell & Mol Biol, SE-17177 Stockholm, Sweden
[2] McGill Univ, McGill Canc Ctr, Montreal, PQ, Canada
关键词
rodent; B lymphocytes; coregulation; cellular proliferation; adhesion molecules;
D O I
10.1189/jlb.1202594
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1, CD66a) is a member of the immunoglobulin (Ig) superfamily, previously characterized as an adhesion and signaling molecule in epithelial, endothelial, and hematopoietic cells. Here, we show that the CEACAM1 isoform expression pattern is different in nonactivated and activated primary mouse B lymphocytes and that CEACAM1 influences B cell receptor complex-mediated activation. A CEACAM1-specific monoclonal antibody strongly triggered proliferation of mouse B cells when combined with surface IgM cross-linking. However, anti-CEACAM1 was not mitogenic when added alone. The proliferation was more pronounced and lasted longer as compared with other activators of B cells, such as anti-IgM in the presence of interleukin-4 or lipopolysaccharide. A similar, costimulatory effect was exerted by CEACAM1-expressing fibroblasts, indicating that homophilic CEACAM1-CEACAM1 cell-mediated binding is the physiological stimulus for CEACAM1-triggered B cell signaling. The anti-CEACAM1/anti-IgM-activated cells aggregated in a lymphocyte function-associated antigen-1-dependent manner. Furthermore, cells that were activated by anti-CEACAM1/anti-IgM secreted Ig but did not go through Ig class-switching. Anti-CEACAM1 induced phosphorylation of c-Jun N-terminal kinase (stress-activated protein kinase) but did not activate the extracellular signal-regulated kinase or p38 mitogen-activated protein kinases.
引用
收藏
页码:126 / 134
页数:9
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