CD11c is a 150 kD glycoprotein also known as αX integrin, CR4, and p150. CD11c forms a αXβ2 heterodimer with β2 integrin (CD18). It is primarily expressed on dendritic cells, NK cells, a subset of intestinal intraepithelial lymphocytes (IEL), and some activated T cells. The αXβ2 integrin plays an important role in cell-cell contact by binding its ligands: iC3b, fibrinogen, and CD54.
CD120b is a 75 kD type I transmembrane protein, also known as Tumor Necrosis Factor Receptor Type II (TNFRII) or p75. It is expressed on a variety of cells at low levels; the expression is upregulated upon activation. This receptor binds both TNF-α and LT-α (also known as TNF-β). In association with TRAF1 and TRAF2, the receptor crosslinking induced by TNF-α or LT-α trimers is critical for signal transduction, leading to apoptosis, NF-kB activation, increased expression of proinflammatory genes, tumor necrosis, and cell differentiation depending on cell type and differentiation state.
CD122 is a 70-75 kD IL-2 receptor β chain also known as IL-2Rβ, which is also shared by the IL-15 receptor. It is constitutively expressed by NK cells and at lower levels by T cells, B cells, monocytes, and macrophages. The IL-2Rβ chain can combine with either the common γ subunit (γc, CD132) alone or with the γc subunit and the IL-2Rα subunit (CD25) to generate intermediate or high affinity IL-2 receptor complexes, respectively. CD122 expression levels can be upregulated by activation. The 5H4 antibody does not block IL-2 binding to the IL-2 receptor. CD122 is expressed on murine, but not human, CD8+ Tregs involved in the maintenance of T cell homeostasis.
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