IL-5 (Interleukin-5) is a secreted cytokine that is expressed as a covalent dimer. It is produced by activated Th2 cells, eosinophils, mast cells, and iNKT cells and promotes eosinophilic and basophilic differentiation and activation. IL-5 signals through a receptor complex containing IL-5 R alpha and the Common beta Chain/CD131 on eosinophils and basophils. Naturally occurring soluble forms of IL-5 R alpha retain the ability to bind IL-5 and limit its bioavailability.
Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells.
Interleukin 5 receptor, alpha (IL5RA) also known as CD125 (Cluster of Differentiation 125) is a subunit of the Interleukin-5 receptor. IL5RA (CD125) is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Six alternatively spliced transcript variants encoding three distinct isoforms have been reported. IL5RA (CD125) is a T-cell-derived cytokine which is particularly important in the development of asthma for the lerminal differentiation, activation and survival of committed cosinophil precursors.
Interleukin 5 Receptor alpha (IL-5 Rα), also known as CD125, is a hematopoietin receptor that plays a dominant role in eosinophil biology. Mature mouse IL-5 Rα consists of a 322 amino acid (aa) extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 22 aa transmembrane segment, and a 54 aa cytoplasmic domain. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GM-CSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling-competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5 Rα followed by eosinophilic differentiation and activation. IL-5 Rα also promotes the differentiation of basophils and B cells. Exposure of mature eosinophils to IL-5 attenuates their IL-5 responsiveness by inducing the down-regulation of surface IL-5 Rα and increased production of soluble IL-5 Rα.
Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism (Probable). Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway.The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells.
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