Type I Cytokine Receptor
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Type I Cytokine Receptor
Type I cytokine receptors are transmembrane receptors expressed on the surface of cells that recognize and respond to cytokines with four α-helical strands. These receptors are also known under the name '' hemopoietin receptors'', and share a common amino acid motif ( WSXWS) in the extracellular portion adjacent to the cell membrane. Members of the type I cytokine receptor family comprise different chains, some of which are involved in ligand/cytokine interaction and others that are involved in signal transduction. The common cytokine-binding domain is related to the Fibronectin type III domain. Signal transduction chains The signal transducing chains are often shared between different receptors within this receptor family. * The IL-2 receptor common gamma chain (also known as CD132) is shared between: ** IL-2 receptor ** IL-4 receptor ** IL-7 receptor ** IL-9 receptor ** IL-13 receptor ** IL-15 receptor ** IL-21 receptor * The common beta chain ( CD131 or CDw131 ...
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Cytokine Receptor
Cytokine receptors are receptors that bind to cytokines. In recent years, the cytokine receptors have come to demand the attention of more investigators than cytokines themselves, partly because of their remarkable characteristics, and partly because a deficiency of cytokine receptors has now been directly linked to certain debilitating immunodeficiency states. In this regard, and also because the redundancy and pleiotropy of cytokines are a consequence of their homologous receptors, many authorities are now of the opinion that a classification of cytokine receptors would be more clinically and experimentally useful. Classification A classification of cytokine receptors based on their three-dimensional structure has been attempted. (Such a classification, though seemingly cumbersome, provides several unique perspectives for attractive pharmacotherapeutic targets.) * Type I cytokine receptors, whose members have certain conserved motifs in their extracellular amino-acid domain. Th ...
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Interleukin-21 Receptor
Interleukin 21 receptor is a type I cytokine receptor. IL21R is its human gene. The protein encoded by this gene is a cytokine receptor for interleukin 21 Interleukin 21 (IL-21) is a protein that in humans is encoded by the ''IL21'' gene. Interleukin-21 is a cytokine that has potent regulatory effects on cells of the immune system, including natural killer (NK) cells and cytotoxic T cells that can ... (IL21). It belongs to the type I cytokine receptors, and has been shown to form a heterodimeric receptor complex with the common gamma chain (γc), a receptor subunit also shared by the receptors for interleukin 2 (IL2), interleukin 7 (IL7) and interleukin 15 (IL15). This receptor transduces the growth promoting signal of IL21, and is important for the proliferation and differentiation of T cells, B cells, and natural killer (NK) cells. The ligand binding of this receptor leads to the activation of multiple downstream signaling molecules, including JAK1, JAK3, STAT1, and STAT3. K ...
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Colony Stimulating Factor
Colony-stimulating factors (CSFs) are secreted glycoproteins that bind to receptor proteins on the surfaces of hemopoietic stem cells, thereby activating intracellular signaling pathways that can cause the cells to proliferate and differentiate into a specific kind of blood cell (usually white blood cells. For red blood cell formation, see erythropoietin). They may be synthesized and administered exogenously. However, such molecules can at a latter stage be detected, since they differ slightly from the endogenous ones in, e.g., features of post-translational modification. Etymology The name "colony-stimulating factors" comes from the method by which they were discovered. Hematopoietic stem cells were cultured (see cell culture) on a so-called semisolid matrix, which prevents cells from moving around, so that, if a single cell starts proliferating, all of the cells derived from it will remain clustered around the spot in the matrix where the first cell was originally locate ...
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Interleukin
Interleukins (ILs) are a group of cytokines (secreted proteins and signal molecules) that are expressed and secreted by white blood cells (leukocytes) as well as some other body cells. The human genome encodes more than 50 interleukins and related proteins. The function of the immune system primarily depends on interleukins, and rare deficiencies of a number of them have been described, all featuring autoimmune diseases or immune deficiency. The majority of interleukins are synthesized by CD4 helper T-lymphocyte, as well as through monocytes, macrophages, and endothelial cells. They promote the development and differentiation of T and B lymphocytes, and hematopoietic cells. Interleukin receptors on astrocytes in the hippocampus are also known to be involved in the development of spatial memories in mice. History and name The name "interleukin" was chosen in 1979, to replace the various different names used by different research groups to designate interleukin 1 (lymphocyte ...
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Oncostatin M Receptor
Oncostatin-M specific receptor subunit beta also known as the Oncostatin M receptor (OSMR) , is one of the receptor proteins for oncostatin M, that in humans is encoded by the ''OSMR'' gene. OSMR is a member of the type I cytokine receptor family. This protein heterodimerizes with interleukin 6 signal transducer to form the type II oncostatin M receptor and with interleukin 31 receptor A to form the interleukin 31 receptor, and thus transduces oncostatin M and interleukin 31 induced signaling events. Expression OSMR is widely expressed across non-haematopoietic, hepatocytes, mesothelial cells, glial cells and epithelial cell types across various organs and mammary glands. OSM receptor is abundantly expressed on endothelial and stromal/fibroblast cells in the lung of mice.= In vitro expression of OSMR  in fetal hepatocytes is upregulated by OSM stimulation. OSMR expression has been shown to be induced by parathyroid hormone in osteoblasts and OSM. Signaling Intracellula ...
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Leukemia Inhibitory Factor Receptor
LIFR also known as CD118 (Cluster of Differentiation 118), is a subunit of a receptor for leukemia inhibitory factor. Function The leukemia inhibitory factor (LIF) is a polyfunctional cytokine that affects the differentiation, survival, and proliferation of a wide variety of cells in the adult and the embryo. LIF action appears to be mediated through a high-affinity receptor complex composed of a low-affinity LIF binding chain (LIF receptor) and a high-affinity converter subunit, glycoprotein 130 (IL6ST, gp130). Both LIFR and gp130 are members of a family of cytokine receptors that includes components of the receptors for the majority of hematopoietic cytokines and for cytokines that affect other systems, including the ciliary neurotrophic factor, growth hormone and prolactin. Interactions Leukemia inhibitory factor receptor has been shown to interact with glycoprotein 130. LIFR has also been identified as a breast cancer metastasis suppressor that functions through the ...
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IL-27 Receptor
The interleukin-27 receptor is a type I cytokine receptor for interleukin-27. It is a heterodimer composed of the interleukin 27 receptor, alpha subunit and glycoprotein 130. IL27RA essential for transcriptional activation of STAT1 and for augmenting the induction of T-bet expression during initiation of Th1 cell The T helper cells (Th cells), also known as CD4+ cells or CD4-positive cells, are a type of T cell that play an important role in the adaptive immune system. They aid the activity of other immune cells by releasing cytokines. They are consider ... differentiation. References External links * Type I cytokine receptors {{membrane-protein-stub ...
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IL-12 Receptor
Interleukin 12 receptor is a type I cytokine receptor, binding interleukin 12. It consists of interleukin 12 receptor, beta 1 subunit, beta 1 and interleukin 12 receptor, beta 2 subunit, beta 2 subunits. References External links

* Type I cytokine receptors {{membrane-protein-stub ...
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IL-11 Receptor
The interleukin 11 receptor is a type I cytokine receptor, binding interleukin 11 Interleukin 11 (IL-11) is a protein that in humans is encoded by the ''IL11'' gene. IL-11 is a cytokine and first isolated in 1990 from bone marrow-derived fibrocyte-like stromal cells. It was initially thought to be important for hematopoiesis .... It is a heterodimer composed of an interleukin 11 receptor alpha subunit and an incompletely characterized beta subunit. References External links * Type I cytokine receptors {{membrane-protein-stub ...
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IL-6 Receptor
Interleukin 6 receptor (IL6R) also known as CD126 (Cluster of Differentiation 126) is a type I cytokine receptor. Function Interleukin 6 (IL6) is a potent pleiotropic cytokine that regulates cell growth and differentiation and plays an important role in immune response. Dysregulated production of IL6 and this receptor are implicated in the pathogenesis of many diseases, such as multiple myeloma, autoimmune diseases and prostate cancer. In melanocytes IL6R gene expression may be regulated by MITF. Structure The IL6 receptor is a protein complex consisting of an IL-6 receptor subunit (IL6R) and interleukin 6 signal transducer Glycoprotein 130. IL6R also denotes the human gene encoding this subunit. Alternatively spliced transcript variants encoding distinct isoforms have been reported. IL6R subunit is also shared by many other cytokines. Interactions Interleukin-6 receptor has been shown to interact with Interleukin 6 and ciliary neurotrophic factor. See also * Clu ...
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Glycoprotein 130
Glycoprotein 130 (also known as gp130, IL6ST, IL6R-beta or CD130) is a transmembrane protein which is the founding member of the class of all cytokine receptors. It forms one subunit of the type I cytokine receptor within the IL-6 receptor family. It is often referred to as the common gp130 subunit, and is important for signal transduction following cytokine engagement. As with other type I cytokine receptors, gp130 possesses a WSXWS amino acid motif that ensures correct protein folding and ligand binding. It interacts with Janus kinases to elicit an intracellular signal following receptor interaction with its ligand. Structurally, gp130 is composed of five fibronectin type-III domains and one immunoglobulin-like C2-type (immunoglobulin-like) domain in its extracellular portion. Characteristics The members of the IL-6 receptor family all complex with gp130 for signal transduction. For example, IL-6 binds to the IL-6 Receptor. The complex of these two proteins then associa ...
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IL-5 Receptor
The interleukin-5 receptor is a type I cytokine receptor. It is a heterodimer of the interleukin 5 receptor alpha subunit and CSF2RB. The IL-5 receptor (IL-5R) belongs to the type I cytokine receptor family and is a heterodimer composed of two polypeptide chains, one α subunit, which binds IL-5 and confers upon the receptor cytokine specificity, and one β subunit, which contains the signal transduction domains. α-subunit The IL-5Rα chain is exclusively expressed by eosinophils, some basophils and murine B1 cells or B cell precursors. Like many other cytokine receptors, alternative splicing of the α-chain gene results in expression of either a membrane bound or soluble form of the bα-chain. The soluble form does not lead to signal transduction and therefore has an antagonistic effect on IL-5 signaling. Both monomeric forms of IL-5Rα are low affinity receptors, while dimerization with the β-chain produces a high affinity receptor. In either case, the α-chain exclusively ...
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