The protein encoded by this gene is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of this cytokine is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. The cytokine function is exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Alternate splicing results in multiple transcript variants.
The protein encoded by this gene is a proinflammatory cytokine that augments natural killer cell activity in spleen cells, and stimulates interferon gamma production in T-helper type I cells. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Interleukin 18 receptor accessory protein, also known as IL18RAP and CDw218b (cluster of differentiation w218b), is an accessory subunit of the heterodimeric receptor for IL18. This protein enhances the IL18 binding activity of IL18R1 (IL1RRP), a ligand-binding subunit of the IL18 receptor. The coexpression of IL18R1 and this protein is required for the activation of NF-kappaB and MAPK8 (JNK) in response to IL18. IL18RAP is required for the high-affinity binding of interleukin 18 (IL-18) to its receptor complex. IL18RAP together with IL18R1 mediates IL-18-dependent activation of NF-kappa-B and JNK. Two putative isoforms of IL18RAP were detected and the ratios and total levels of these isoforms may contribute to the etiology of coeliac disease. IL18R1 and IL18RAP polymorphisms have been found associated with diseases such as schizophrenia, HSV1 seropositivity, and atopic asthma. Analysis of IL18R1 and IL18RAP SNPs in 5 European prospective cohorts suggests that the variability of these genes are unlikely to contribute to modulate the risk of CVD in European populations.
IL-1ra was originally isolated from the urine of patients with monocytic leukemia and has also been purified from adherent monocytes. The naturally occurring, fully glycosylated form has an apparent molecular weight of about 25,000 Daltons. The protein shows 26% amino acid homology to IL-1 beta and 19% homology to IL-1 alpha. It will compete with either factor for receptor binding, but does not interact with either one. Human IL-1ra will bind to both types of IL-1 receptor (I and II) on human cells, but reportedly will not block binding to the type II receptor on murine pre-B cell lines. The recombinant, non-glycosylated form of IL-1ra blocks binding of IL-1 to its receptor equally as well as the naturally-occurring, glycosylated form. The IL-1ra has been shown to block the inflammatory responses induced by IL-1 both in vitro and in vivo. Currently, pre-clinical and clinical studies are underway to test possible therapeutic applications for IL-1ra in the treatment of sepsis, rheumatoid arthritis and chronic myelogenous leukemia.
The founding members of the interleukin-1 (IL-1) superfamily include pro-inflammatory cytokines IL-1α, IL-1β and IL-1 receptor antagonist (IL-1RA). At least six similar proteins have been recently identified, including a homolog of IL-1RA (IL1F5). IL-1a, IL-1b and IL-1RA are mainly expressed in macrophages, monocytes, and dendritic cells. IL-1RA acts as an anti-inflammatory cytokine, binding the IL-1 receptor to limit the response to inflammation. Because it plays a key role in regulating the inflammatory response, recombinant IL-1RA is a therapeutic agent used in the treatment of diseases such as rheumatoid arthritis. Alternatively, mutation of the corresponding IL-1RA gene may be associated with susceptibility to the development of specific cancers.
IL1B(interleukin 1 beta) Homo sapiens The protein encoded by this gene is a member of the interleukin 1 cytokine family. This cytokine is produced by activated macrophages as a proprotein, which is proteolytically processed to its active form by caspase 1 (CASP1/ICE). This cytokine is an important mediator of the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. The induction of cyclooxygenase-2 (PTGS2/COX2) by this cytokine in the central nervous system (CNS) is found to contribute to inflammatory pain hypersensitivity. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2.
Interleukin 20 receptor, alpha subunit (IL20RA/IL-20RA) also known as IL-20 receptor subunit alpha, Cytokine receptor class-II member 8, interleukin-20 receptor I, and interleukin-20 receptor subunit alpha, is a subunit for the interleukin-20 receptor. IL20RA/IL-20RA belongs to the type II cytokine receptor family. This cytokine is a receptor for interleukin 20 (IL20), a cytokine that may be involved in the epidermal function. The receptor of IL20 is a heterodimeric receptor complex consisting of this protein and interleukin 20 receptor beta (IL20B). IL20RA forms heterodimer with IL20RB and the complex serves as a receptor for IL19, IL20, and IL24. All three are capable of signaling through the IL-20RA/IL-20RB complex. The ligand binding to receptor B creating a high-affinity binding site for receptor A which is recruited to complete the complex. Besides, IL20RA also forms a heterodimer with the unique and specific receptor IL10RB and functions as the receptor for IL26. IL20RA is widely expressed with the highest levels in skin, testis, and brain. The expression of both IL20RA and IL20RB is found to be upregulated in psoriatic skin lesions on keratinocytes.
IL26 (Interleukin 26) is a Protein Coding gene. Among its related pathways are PEDF Induced Signaling and TGF-Beta Pathway. GO annotations related to this gene include cytokine activity.This gene was identified by its overexpression specifically in herpesvirus samimiri-transformed T cells. The encoded protein is a member of the IL10 family of cytokines. It is a secreted protein and may function as a homodimer. This protein is thought to contribute to the transformed phenotype of T cells after infection by herpesvirus samimiri.
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