CD11b is a 165-170 kD type I transmembrane glycoprotein also known as αMintegrin, Mac-1, CR3, and C3biR. CD11b non-covalently associates with integrin β2(CD18) and is expressed on granulocytes, monocytes/macrophages, dendritic cells, NK cells, and subsets of T and B cells. CD11b/CD18 is critical for the transendothelial migration of monocytes and neutrophils. It is also involved in granulocyte adhesion, phagocytosis, and neutrophil activation. CD11b/CD18 interacts with ICAM-1 (CD54), ICAM-2 (CD102), ICAM-4, CD14, CD23, heparin, iC3b, fibrinogen, and factor X.
CD11c is a 145-150 kD type I transmembrane glycoprotein also known as integrin αX and CR4. CD11c non-covalently associates with integrin β2 (CD18) and is expressed on monocytes/macrophages, dendritic cells, granulocytes, NK cells, and subsets of T and B cells. CD11c has been reported to play a role in adhesion and CTL killing through its interactions with fibrinogen, CD54, and iC3b.
CD122 is a 70-75 kD type I transmembrane glycoprotein and member of the Ig superfamily. It is IL-2 receptor β chain also known as IL-2Rβ, which is also shared by the IL-15 receptor. CD122 is constitutively expressed by NK cells and at lower levels by a subset of T cells. Its expression is upregulated upon activation. 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.
CD123 is the 70 kD transmembrane α chain of the IL-3 receptor. Alone, CD123 binds IL-3 with low affinity; when CD123 associates with CDw131 (common β chain), it binds IL-3 with high affinity. CD123 does not transduce intracellular signals upon binding IL-3 and requires the β chain for this function. CD123 is expressed by myeloid precursors, macrophages, dendritic cells, mast cells, basophils, megakaryocytes, and some B cells.
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