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.
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.
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