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.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD124, also known as interleukin 4 receptor (IL4R), is a typeⅠ transmembrane protein that can regulate IgE antibody production in B cells through binding to interleukin 4 and interleukin 13 and promote differentiation of Th2 cells through binding to interleukin 4. The membrane-bound form of CD124 can be hydrolyzed to soluble form which can inhibit IL4-mediated cell proliferation and IL5 upregulation by T-cells.
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.
IL-5 is expressed in eosinophils, NK cells, TC2 CD8+ T cells, mast cells, CD45+ CD4+ T cells, gamma delta T cells and IL-1 beta activated endothelial cells. IL-5 acts as a growth and differentiation factor for both B cells and eosinophils. Relative to B cells, IL-5 appears to induce the differentiation of activated conventional B-2 cells into Ig-secreting cells. In addition, it induces the growth of B-1 progenitors as well as IgM production by B-1 cells.IL-5 appears to perform a number of functions on eosinophils. These include the down modulation of Mac-1,the upregulation of receptors for IgA and IgG,the stimulation of lipid mediator (leukotriene C4 and PAF) secretion and the induction of granule release.IL-5 also promotes the growth and differentiation of eosinophils.
Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells.
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