Interleukin-12 subunit beta (IL-12B) belongs to the type I cytokine receptor family. It contains 1 fibronectin type-III domain and 1 Ig-like C2-type domain. IL-12B is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. IL-12 is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor encoded by IL12B and a 35 kD subunit encoded by IL12A. IL12 is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. It has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen.
The IL12 receptor complex, formed by IL12RB1 and IL12RB2, mediates the type I immune responses of various types of lymphocytes. Its ligand, IL12, is a heterodimeric cytokine composed of IL-12p35 and IL-12p40 subunits that are linked via disulfide bonds. Ligation of IL-12 to its receptor involves the binding of IL-12p35 to IL12RB1 and IL-12p40 to IL12RB2. This will result in the activation of tyrosine kinase 2 (TYK2), which is associated with the IL12RB1 chain and Janus kinase 2 (JAK2), which is associated with the IL12RB2 chain. Activated TYK2 and JAK2 direct the phosphorylation of STAT4. IL12RB1 is present on all lymphocytes, while the expression of IL12RB2 is tightly regulated. It has shown that the expression of IL12RB2 is limited to Th2 cells. IL12RB2 subunit plays an important role in Th1 cell differentiation, since its absence leads to an abortive Th1 differentiation that has dysfunctional production of Th1 effector molecules.
Interleukin-12 receptor subunit beta-2 (IL12RB2), also known as IL-12 receptor subunit beta-2, IL-12R subunit beta-2, IL-12R-beta-2, and IL-12RB2, is a type I transmembrane protein identified as a subunit of the interleukin 12 receptor complex. IL12RB2 belongs to the type I cytokine receptor family. The coexpression of IL12RB2 and IL12RB1 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. The expression of IL12RB2 is up-regulated by IFN gamma in Th1 cells, and plays a role in Th1 cell differentiation. The up-regulation of IL12RB2 is found to be associated with a number of infectious diseases, such as Crohn's disease and leprosy, which is thought to contribute to the inflammatory response and host defense. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. IL12RB2 promotes the proliferation of T-cells as well as NK cells. IL12RB2 induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production.
Interleukin 13 (IL-13) is a single-chain glycosylated polypeptide, which belongs to the IL-13/IL-4 family. IL-13 protein is secreted by many cell types, but especially by T helper type 2 (Th2) cells. IL-13 exerts its effects through a multi-subunit receptor comprising the alpha chain of the IL-4 receptor (IL-4Rα) and at least one of two known IL-13-specific binding chains (IL-13 Rα1 and IL-13 Rα2). As a cytokine, IL-13 protein is critical in regulating inflammatory, immune responses, and diseases. Also, it inhibits the production of pro-inflammatory cytokines and chemokines, and thus down-regulates macrophage activity. IL-13 protein and antibody are more importantly implicated as a central mediator of immunoregulatory processes in various cell types.
Interleukin-13 receptor subunit alpha-1(IL-13RA1), also known as NR4, belongs to the hemopoietin receptor family. Interleukin-13 receptor is a complex of IL4R, IL13RA1, and possibly other components. It interacts with TRAF3IP1 and binds with low affinity to interleukin-13(IL3). IL-13RA1, together with IL4RA, can form a functional receptor for IL13. It also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity. The WSXWS motif in domains appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
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