CD48 can have activating roles on T cells, antigen presenting cells and granulocytes, by binding to CD2 or bacterial FimH, and through cell intrinsic effects. Interactions between CD48 and its high affinity ligand CD244 are more complex, with both stimulatory and inhibitory outcomes.

CD48 antigen (cluster of differentiation 48) also known as B-lymphocyte activation marker (BLAST-1) or signaling lymphocytic activation molecule 2 (SLAMF2) is a protein that in humans is encoded by the CD48 gene.

Jul 7, 2011 · CD48 is broadly expressed on hematopoietic cells but excluded from quiescent long-term murine HSCs. Through its interactions with CD244 on progenitor cells, it influences HSC function by altering the BM cytokine milieu, particularly IFNγ.

The HM48-1 mAb blocks binding of soluble CD2 to CD48-bearing cells, blocks the interaction of CD2 and CD244, inhibits spleen cell proliferative responses to mitogens, augments the proliferative response of spleen cells when cross-linked …

CD48 binds CD2 and other molecules, yet its high-affinity ligand in both mouse and human systems is 2B4. Despite its lack of an intracellular domain, stimulation of CD48 induces rearrangement of signaling factors in lipid rafts, Lck-kinase activity, and tyrosine phosphorylation.

Jul 1, 2005 · Cell surface receptors of the SLAM family, including CD150, CD244, and CD48, were differentially expressed among functionally distinct progenitors. HSCs were highly purified as CD150+CD244−CD48− cells while MPPs were CD244+CD150−CD48− and most restricted progenitors were CD48+CD244+CD150−.

We provide evidence that NK and ILC progenitors can be better defined using CD48 and CD52 staining, and that 2B4 ligation by CD48 is required for the development of ILC2 lineage cells, …

These results indicate that CD48 is a ligand for mouse CD2 and is involved in regulating T cell activation. The Full Text of this article is available as a PDF (1.1 MB). These references are in PubMed. This may not be the complete list of references from this article.

We show that CD2 binds to the GFCC′C″ face of the V-set domain of CD48, and we use a complementary mutagenesis strategy to determine the orientation of the interacting CD2 and CD48 binding sites. Our results strongly support a head-to-head interaction and rule out a three-layer packing interaction.

CD48 can have activating roles on T cells, antigen presenting cells and granulocytes, by binding to CD2 or bacterial FimH, and through cell intrinsic effects. Interactions between CD48 and its high affinity ligand CD244 are more complex, with both stimulatory and inhibitory outcomes.