Interleukin4 (IL-4), also known as B cell-stimulatory factor-1, is a cytokine that shows pleiotropic effects during immune responses. It is a glycosylated polypeptide that contains three intrachain disulfide bridges and adopts a bundled four α helix structure. Human IL-4 is synthesized with a 24 aa signal sequence. Alternate splicing generates an isoform with a 16 aa internal deletion. Mature human IL-4 shares 55%, 39% and 43% aa sequence identity with bovine, mouse, and rat IL-4, respectively. Human, mouse, and rat IL-4 are species specific in their activities. IL-4 exerts its effects through two receptor complexes. The type I receptor, which is expressed on hematopoietic cells, is a heterodimer of the ligand binding IL-4 Rα and the common γ chain (a shared subunit of the receptors for IL-2,7,9,15, and 21). The type II receptor on nonhematopoietic cells consists of IL-4 Rα and IL13 Rα1. The type II receptor also transduces IL-13 mediated signals. IL-4 is primarily expressed by Th2-biased CD4+ T cells, mast cells, basophils, and eosinophils. It promotes cell proliferation, survival, and immunoglobulin class switch to IgG4 and IgE in human B cells, acquisition of the Th2 phenotype by naïve CD4+ T cells, priming and chemotaxis of mast cells, eosinophils, and basophils, and the proliferation and activation of epithelial cells. IL-4 plays a dominant role in the development of allergic inflammation and asthma.
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