CD123; also known as Interleukin-3 receptor subunit alpha; belongs to the type I cytokine receptor family. In mouse; there are two classes of high-affinity IL3 receptors. One contains an IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. CD123 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage-committed cells. CD123 is a heterodimer consisting of an alpha and a beta subunit. The alpha subunit alone binds IL-3 with low affinity. The beta subunit does not bind IL-3 by itself but is required for the high-affinity binding of IL-3 to the heterodimeric receptor complex.
Interleukin-3 receptor subunit alpha, also known as IL-3 receptor subunit alpha, IL-3R-alpha, CD123, and IL3RA, is a single-pass type I membrane protein which belongs to the type I cytokine receptor family and Type 5 subfamily. The WSXWS motif of IL3RA appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box one motif of IL3RA is required for JAK interaction and / or activation. IL3RA represents a unique marker for primitive leukemic stem cells. Targeting of IL3RA may be a promising strategy for the preferential ablation of AML cells. Aberrant IL3RA expression is a good marker for monitoring of minimal residual disease. IL3RA is strongly expressed in various leukemic blasts and leukemic stem cells and seems to be an excellent target for the therapy of leukemias. Recent studies have shown that interleukin-3 receptor alpha (CD123) is highly expressed on leukemia stem cells of patients with acute myeloid leukemia, and is correlated with tumor load and poor prognosis. CD123 was highly expressed in the bone marrow of the patients with myelodysplastic syndrome (MDS), significantly correlated with the proportion of bone marrow blasts, and thus might be the marker of MDS malignant clone. IL3RA is also a useful new marker for distinguishing B-cell disorders with circulating villous lymphocytes as its expression is characteristic of typical hairy cell leukemia (HCL) with high sensitivity and specificity.
CD123, also known as Interleukin-3 receptor subunit alpha, belongs to the type I cytokine receptor family. In mouse, there are two classes of high-affinity IL3 receptors. One contains an IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. CD123 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage‑committed cells. CD123 is a heterodimer consisting of an alpha and a beta subunit. The alpha subunit alone binds IL‑3 with low affinity. The beta subunit does not bind IL‑3 by itself but is required for the high‑affinity binding of IL‑3 to the heterodimeric receptor complex.
Interleukin-4 (IL-4) is a pleiotropic cytokine that regulates diverse T and B cell responses including cell proliferation, survival and gene expression. IL-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of naive CD4+ T cells into helper Th2 cells, characterized by their cytokine-secretion profile that includes secretion of IL-4, IL-5, IL-6, IL-10, and IL-13, which favor a humoral immune response. Another dominant function of IL-4 is the regulation of immunoglobulin class switching to the IgG1 and IgE isotypes. Excessive IL-4 production by Th2 cells has been associated with elevated IgE production and allergic response.
Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
Interleukin 4 Receptor alpha (IL4-Ra) is a widely expressed 140 kDa transmembrane glycoprotein in the class I cytokine receptor family. Mature human IL4-Ra consists of a 207 amino acid (aa) extracellular domain (ECD) that contains a cytokine binding region and one fibronectin type III domain; a 24 aa transmembrane segment; and a 569 aa cytoplasmic domain that contains one Box 1 motif and one ITIM motif. IL4-Ra plays an important role in Th2-biased immune responses; alternative macrophage activation; mucosal immunity; allergic inflammation; tumor progression; and atherogenesis. Soluble forms of IL4-Ra; generated by alternate splicing or proteolysis; retain ligand binding properties and inhibit IL-4 bioactivity. IL4-Ra is a component of two distinct receptor complexes and shows species selectivity between human and mouse. It can associate with the common gamma chain (γc) to form the IL-4 responsive type I receptor in which γc increases the affinity for IL-4 and enables signaling. It can alternatively associate with IL13-Ra1 to form the type II receptor which is responsive to both IL-4 and IL-13. The use of shared receptor components contributes to the overlapping biological effects of IL-4 and IL-13 as well as other cytokines that utilize γc.
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