Interleukin-4 receptor subunit alpha (IL-4Rα) (IL-4Rα)

Interleukin-4 receptor subunit alpha (IL-4Rα), also known as CD124, is a critical component of the receptor complexes for both interleukin-4 (IL-4) and interleukin-13 (IL-13) [6, 13]. It is a type I transmembrane protein that pairs with the common gamma chain to form the Type I IL-4 receptor or with IL-13Rα1 to form the Type II IL-4 receptor [3, 6]. This subunit is a central mediator of Type 2 (Th2) inflammation, driving processes such as IgE class switching in B cells, Th2 cell differentiation, and alternative macrophage activation [1, 12]. Dysregulation of the IL-4Rα signaling pathway is strongly linked to various allergic and inflammatory diseases, including asthma, atopic dermatitis, and eosinophilic esophagitis [5, 15]. Therapeutic targeting of IL-4Rα, most notably by the monoclonal antibody dupilumab, has revolutionized the treatment of these conditions by simultaneously blocking the pro-inflammatory effects of both IL-4 and IL-13 [7, 15]. Clinical use of IL-4Rα inhibitors is generally well-tolerated, though it is uniquely associated with side effects like conjunctivitis in certain patient populations [5, 15]. Beyond allergic diseases, IL-4Rα is being investigated for its role in other conditions such as chronic obstructive pulmonary disease (COPD) and certain cancers [1, 17]. The receptor's ability to modulate both innate and adaptive immune responses makes it a versatile target for precision medicine in immunology [11, 18].

Other names

CD124IL4RIL-4RAIL4RAInterleukin-4 receptor alpha chainBSF receptor

Antagonist; monoclonal antibody that binds to the IL-4Rα subunit, blocking the signaling of both IL-4 and IL-13 by preventing the formation of Type I and Type II receptor complexes.