Interleukin 1 receptor, type I (IL-1R1) is an interleukin receptor that belongs to the interleukin-1 receptor family. IL-1R1 is an 80 kDa transmembrane protein that is expressed predominantly by T cells, fibroblasts, and endothelial cells. This gene along with IL1R2, IL1RL2, and IL1RL1 form a cytokine receptor gene cluster in a region mapped to chromosome 2q12. IL-1R1 is an important mediator involved in many cytokine induced immune and inflammatory responses. It binds to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. The signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. It also binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. An IL1 receptor accessory protein that can heterodimerize with the Type I receptor in the presence of IL1α or IL1β but not IL1ra, was identified. Recombinant IL1 soluble receptor Type I is a potent antagonist of IL1 action.
Interleukin 1 receptor, type I (IL-1R1) also known as CD121a (Cluster of Differentiation 121a), is an interleukin receptor. IL-1R1/CD121a is a cytokine receptor that belongs to the interleukin 1 receptor family. This protein is a receptor for interleukin alpha (IL1A), interleukin beta (IL1B), and interleukin 1 receptor, type I (IL1R1/IL1RA). IL-1R1/CD121a is an important mediator involved in many cytokine induced immune and inflammatory responses. This protein has been characterized by pharmacological and molecular techniques in the mouse brain. The spindle-shaped astrocytes enclose the wound, separating the healthy from damaged neural tissue. The shape change and subsequent repair processes are IL-1β activity-dependent, acting through the IL-1 type 1 receptor (IL-1R1), as co-application of the IL-1type 1 receptor antagonist protein (IL-1ra) blocks IL-1β induced effects. In the spleen, a slight increase in IL-1R AcP and IL-1R1 was observed during the first hours following LPS stimulation. In conclusion, IL-1R AcP mRNA is expressed in the brain and in other tissues where IL-1R1/CD121a transcripts are found. However, the regulation of its expression is distinct from IL-1R1/CD121a. The high level of expression and the lack of regulation of IL-1R AcP transcripts in the brain under inflammatory conditions suggest that the protein might be constitutively expressed in excess.
Interleukin 1 receptor; type II (IL1R2) also known as CD121b (Cluster of Differentiation 121b) is a cytokine receptor that belongs to the interleukin-1 receptor family. This protein binds interleukin alpha (IL1A); interleukin beta (IL1B); and interleukin 1 receptor; type I (IL1R1/IL1RA); and acts as a decoy receptor that inhibits the activity of its ligands. The pleiotropic cytokine IL1 is produced to regulate development and maintenance of the inflammatory responses; and binds to specific plasma membrane receptors on cells. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified; designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1R1 contributes to IL-1 signaling; whereas the IL-1R2/CD121b has no signaling property and acts as a decoy for IL-1. IL-1R2/CD121b structurally consisting of a ligand binding portion comprised of three Ig-like domains; a single transmembrane region; and a short cytoplasmic domain; is expressed in a variety of cell types including B lymphocytes; neutrophils; monocytes; large granular leukocytes and endothelial cells. Interleukin 4 (IL4) is reported to antagonize the activity of interleukin 1 by inducing the expression and release of this cytokine.
Interleukin-1 receptor type 2 (IL1R2) belongs to the interleukin-1 receptor family. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified, designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1 receptor type II is a 68 kDa transmembrane protein found on B lymphocytes, neutrophils, monocytes, large granular leukocytes and endothelial cells. IL1R2 is non-signaling receptor forIL1A, IL1B and IL1RN, reduces IL1B activities. IL1R2 serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. IL1R2 modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.
Interleukin-1 receptor type 2 (IL1R2) belongs to the interleukin-1 receptor family. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified; designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1 receptor type II is a 68 kDa transmembrane protein found on B lymphocytes; neutrophils; monocytes; large granular leukocytes and endothelial cells. IL1R2 is non-signaling receptor forIL1A; IL1B and IL1RN; reduces IL1B activities. IL1R2 serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. IL1R2 modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors.
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