Aversa G, Carballido J, Punnonen J, Chang C C, Hauser T, Cocks B G, De Vries J E
Department of Human Immunology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, California 94304-1104, USA.
Immunol Cell Biol. 1997 Apr;75(2):202-5. doi: 10.1038/icb.1997.30.
Following the initial events of T cell activation, triggered by binding of specific peptide-MHC complex to the TCR for antigen and engagement of costimulatory molecules, a number of activation molecules are expressed on the cell surface. Many of these molecules regulate T cell function, T-T cell interactions and the interaction of T cells with other cells. One such molecule is SLAM, a multifunctional 70 kDa glycoprotein member of the Ig superfamily with multiple isoforms. SLAM is rapidly induced on naive T cells and B cells following activation. Engagement of SLAM by a specific antibody (mAb A12) results in IL-2-independent T cell expansion and induction/up-regulation of IFN-gamma by activated T cells, including Th2 cells. SLAM was found to be a high-affinity self-ligand mediating molecular and cellular homophilic interactions. In this review we discuss SLAM as a receptor involved in T cell expansion and in directing immune responses to a Th0-Th1 pathway.