SLAM and its role in T cell activation and Th cell responses
- 1 April 1997
- journal article
- Published by Wiley in Immunology & Cell Biology
- Vol. 75 (2) , 202-205
- https://doi.org/10.1038/icb.1997.30
Abstract
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 natve 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‐γ 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‐Th 1 pathway.Keywords
This publication has 29 references indexed in Scilit:
- One Step Ahead of the Game: Viral Immunomodulatory MoleculesAnnual Review of Immunology, 1996
- CD28/B7 SYSTEM OF T CELL COSTIMULATIONAnnual Review of Immunology, 1996
- Lymphoproliferative Disorders with Early Lethality in Mice Deficient in Ctla-4Science, 1995
- Cytokine receptors encoded by poxviruses: a lesson in cytokine biologyImmunology Today, 1995
- CTLA-4 can function as a negative regulator of T cell activationImmunity, 1994
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993
- Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM.The Journal of cell biology, 1992
- Molecular and biological characterization of a murine ligand for CD40Nature, 1992
- Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23.The Journal of Experimental Medicine, 1989
- The Immunoglobulin Superfamily—Domains for Cell Surface RecognitionAnnual Review of Immunology, 1988