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Juha Punnonen^*, Benjamin G. Cocks^*, José M. Carballido^*, Bruce Bennett^*, David Peterson, Gregorio Aversa^*, and Jan E. de Vries^*

From ^* Department of Human Immunology and Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, California 94304

In this study it is shown that both membrane-bound and soluble forms of signaling lymphocytic activation molecule (SLAM) induce proliferation and Ig synthesis by activated human B cells. Activated B cells express the membrane-bound form of SLAM (mSLAM), the soluble (s) and the cytoplasmic (c) isoforms of SLAM, and the expression levels of mSLAM on B cells are rapidly upregulated after activation in vitro. Importantly, recombinant sSLAM and L cells transfected with mSLAM efficiently enhance B cell proliferation induced by anti-µ mAbs, anti-CD40 mAbs or Staphylococcus aureus Cowan I (SAC) in the presence or absence of IL-2, IL-4, IL-10, IL-12, or IL-15. sSLAM strongly enhances proliferation of both freshly isolated B cells and B cells derived from long-term in vitro cultures, indicating that SLAM acts not only during the initial phase of B cell activation but also during the expansion of preactivated B cells. In addition, sSLAM enhances production of IgM, IgG, and IgA by B cells activated by antiCD40 mAbs. SLAM has recently been shown to be a high affinity self-ligand, and the present data suggest that signaling through homophilic SLAM–SLAM binding during B–B and B–T cell interactions enhances the expansion and differentiation of activated B cells.

DNAX Research Institute is supported by Schering-Plough, Inc.

¹ Abbreviations used in this paper: aa, amino acid; CD40L, CD40 ligand; MC, mononuclear cells; HPRT, hypoxanthine phosphoribosyltransferase; PB, peripheral blood; PI, propidium iodide; RA, rheumatoid arthritis; SAC, Staphylococcus aureus Cowan I; SH2, Src homology 2; SLAM, signaling lymphocytic activation molecule.

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