Interleukin-2 receptor subunit alpha (IL2RA) is a single-pass type I membrane protein; contains 2 Sushi (CCP/SCR) domains. The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains; together with the common gamma chain (IL2RG); constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor; while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein; soluble IL2RA has been isolated and determined to result from extracellular proteolyisis.
CD25 (alpha-chain of IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells, and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covelently with the IL2 receptor beta and gamma chain, and subsequently initiates the intacellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development is associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of sIL-2Ralpha. In most haematological malignancies, including different types of leukaemias and lymphomas, sIL-2Ralpha has been found to be released directly from the surface of neoplastic cells thus reflecting the tumour bulk, turnover and activity.
The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with an the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolyisis. Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is presently unknown. Mutations in this gene are associated with an interleukin 2 receptor alpha deficiency.
Human IL-2RB; also known asinterleukin-2 receptor subunit beta;is the receptor for interleukin-2. IL2 receptor complex is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. IL2 receptor complex has three forms with respect to ability to bind IL2. IL-2RB is belonged to a type I membrane protein;and has a 26 residue signal peptide; a 214 residue extracellular region; a 25 residue transmembrane region and a 286 residue cytoplasmic domain. IL-2RB is the subunit critical for receptor-mediated signaling via physically or functionally coupling to other signaling molecules; such as the Jak-STAT and Src-family protein tyrosine kinase although it lacks apparent catalytic motifs.
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