Array ( [0] => {{Short description|Group of cytokines}} [1] => '''Interleukins''' (ILs) are a group of [[cytokine]]s (secreted [[proteins]] and [[signal molecule]]s) that are expressed and secreted by [[white blood cell]]s (leukocytes) as well as some other body cells. The [[human genome]] encodes more than 50 interleukins and related proteins.{{cite journal | vauthors = Brocker C, Thompson D, Matsumoto A, Nebert DW, Vasiliou V | title = Evolutionary divergence and functions of the human interleukin (IL) gene family | journal = Human Genomics | volume = 5 | issue = 1 | pages = 30–55 | date = Oct 2010 | pmid = 21106488 | pmc = 3390169 | doi = 10.1186/1479-7364-5-1-30 | doi-access = free }} [2] => [3] => The function of the [[immune system]] primarily depends on interleukins, and [[rare disease|rare]] deficiencies of a number of them have been described, all featuring [[autoimmune disease]]s or [[immune deficiency]]. The majority of interleukins are synthesized by [[CD4 helper T-lymphocyte]]s, as well as through [[monocytes]], [[macrophages]], and [[endothelial]] cells. They promote the development and differentiation of T and [[B lymphocytes]], and [[hematopoietic]] cells. [4] => [5] => Interleukin receptors on [[astrocytes]] in the [[hippocampus]] are also known to be involved in the development of spatial memories in mice. [6] => [7] => == History and name == [8] => [9] => The name "interleukin" was chosen in 1979, to replace the various different names used by different research groups to designate [[interleukin 1]] (lymphocyte activating factor, mitogenic protein, T-cell replacing factor III, B-cell activating factor, B-cell differentiation factor, and "Heidikine") and [[interleukin 2]] (TSF, etc.). This decision was taken during the Second International Lymphokine Workshop in [[Switzerland]] (27–31 May 1979 in [[Ermatingen]]).{{cite journal | vauthors = di Giovine FS, Duff GW | title = Interleukin 1: the first interleukin | journal = Immunology Today | volume = 11 | issue = 1 | pages = 13–20 | date = Jan 1990 | pmid = 2405873 | doi = 10.1016/0167-5699(90)90005-t }}{{cite book| editor =Habenicht A |vauthors=Schindler R, Dinarello CA | title = Growth Factors, Differentiation Factors, and Cytokines |pages=85–102 | year = 1990 | publisher = Springer | location = Berlin, Heidelberg | isbn = 978-3-642-74856-1 | chapter = Interleukin 1 | doi = 10.1007/978-3-642-74856-1_7 }}{{cite journal | title = Revised nomenclature for antigen-nonspecific T cell proliferation and helper factors | journal = Journal of Immunology | volume = 123 | issue = 6 | pages = 2928–9 | date = Dec 1979 | doi = 10.4049/jimmunol.123.6.2928 | pmid = 91646 | url = http://www.jimmunol.org/content/123/6/2928.short | doi-access = free }} [10] => [11] => The term ''interleukin'' derives from (''inter-'') "as a means of communication", and (''-leukin'') "deriving from the fact that many of these proteins are produced by leukocytes and act on leukocytes". The name is something of a relic; it has since been found that interleukins are produced by a wide variety of body cells. The term was coined by Dr Vern Paetkau, [[University of Victoria]]. [12] => [13] => Some interleukins are classified as [[lymphokine]]s, lymphocyte-produced cytokines that mediate immune responses. [14] => [15] => ==Common families== [16] => [17] => ===Interleukin 1=== [18] => {{main|Interleukin 1}} [19] => [20] => Interleukin 1 alpha and interleukin 1 beta ([[IL1A|IL1 alpha]] and [[IL1B|IL1 beta]]) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis.{{cite journal | vauthors = Sims JE, March CJ, Cosman D, Widmer MB, MacDonald HR, McMahan CJ, Grubin CE, Wignall JM, Jackson JL, Call SM | title = cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily | journal = Science | volume = 241 | issue = 4865 | pages = 585–9 | date = Jul 1988 | pmid = 2969618 | doi = 10.1126/science.2969618 | bibcode = 1988Sci...241..585S }} Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors.{{cite journal | vauthors = Liu C, Hart RP, Liu XJ, Clevenger W, Maki RA, De Souza EB | title = Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA | journal = The Journal of Biological Chemistry | volume = 271 | issue = 34 | pages = 20965–72 | date = Aug 1996 | pmid = 8702856 | doi = 10.1074/jbc.271.34.20965 | doi-access = free }} The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors. [21] => [22] => Both IL-1 receptors ([[Interleukin 1 receptor, type I|CD121a/IL1R1]], [[Interleukin 1 receptor, type II|CD121b/IL1R2]]) appear to be well conserved in evolution, and map to the same chromosomal location.{{cite journal | vauthors = McMahan CJ, Slack JL, Mosley B, Cosman D, Lupton SD, Brunton LL, Grubin CE, Wignall JM, Jenkins NA, Brannan CI | title = A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types | journal = The EMBO Journal | volume = 10 | issue = 10 | pages = 2821–32 | date = Oct 1991 | pmid = 1833184 | pmc = 452992 | doi = 10.1002/j.1460-2075.1991.tb07831.x}} The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and [[Interleukin 1 receptor antagonist|IL-1 receptor antagonist]]). [23] => [24] => The crystal structures of IL1A and IL1B{{cite journal | vauthors = Priestle JP, Schär HP, Grütter MG | title = Crystallographic refinement of interleukin 1 beta at 2.0 A resolution | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 24 | pages = 9667–71 | date = Dec 1989 | pmid = 2602367 | pmc = 298562 | doi = 10.1073/pnas.86.24.9667 | doi-access = free }} have been solved, showing them to share the same 12-stranded beta-sheet structure as both the [[heparin]] binding growth factors and the Kunitz-type soybean trypsin inhibitors.{{cite journal | vauthors = Murzin AG, Lesk AM, Chothia C | title = beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors | journal = Journal of Molecular Biology | volume = 223 | issue = 2 | pages = 531–43 | date = Jan 1992 | pmid = 1738162 | doi = 10.1016/0022-2836(92)90668-A }} The beta-sheets are arranged in 4 similar lobes around a central axis, 8 strands forming an anti-parallel beta-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding. [25] => [26] => Molecular cloning of the Interleukin 1 Beta converting enzyme is generated by the proteolytic cleavage of an inactive precursor molecule. A complementary DNA encoding protease that carries out this cleavage has been cloned. Recombinant expression enables cells to process precursor Interleukin 1 Beta to the mature form of the enzyme. [27] => [28] => Interleukin 1 also plays a role in the [[Central Nervous System|central nervous system]]. Research indicates that mice with a genetic deletion of the type I IL-1 receptor display markedly impaired hippocampal-dependent memory functioning and [[long-term potentiation]], although memories that do not depend on the integrity of the [[hippocampus]] seem to be spared.{{cite journal | vauthors = Ben Menachem-Zidon O, Avital A, Ben-Menahem Y, Goshen I, Kreisel T, Shmueli EM, Segal M, Ben Hur T, Yirmiya R | s2cid = 18300021 | title = Astrocytes support hippocampal-dependent memory and long-term potentiation via interleukin-1 signaling | journal = Brain, Behavior, and Immunity | volume = 25 | issue = 5 | pages = 1008–16 | date = Jul 2011 | pmid = 21093580 | doi = 10.1016/j.bbi.2010.11.007 }}{{cite journal | vauthors = Avital A, Goshen I, Kamsler A, Segal M, Iverfeldt K, Richter-Levin G, Yirmiya R | title = Impaired interleukin-1 signaling is associated with deficits in hippocampal memory processes and neural plasticity | journal = Hippocampus | volume = 13 | issue = 7 | pages = 826–34 | year = 2003 | pmid = 14620878 | doi = 10.1002/hipo.10135 | citeseerx = 10.1.1.513.8947 | s2cid = 8368473 }} However, when mice with this genetic deletion have wild-type [[Neurogenesis|neural precursor cells]] injected into their [[hippocampus]] and these cells are allowed to mature into [[astrocytes]] containing the interleukin-1 receptors, the mice exhibit normal hippocampal-dependent memory function, and partial restoration of [[long-term potentiation]]. [29] => [30] => ===Interleukin 2=== [31] => {{main|Interleukin 2}} [32] => [33] => T lymphocytes regulate the growth and differentiation of T cells and certain B cells through the release of secreted protein factors.{{cite journal | vauthors = Yokota T, Arai N, Lee F, Rennick D, Mosmann T, Arai K | title = Use of a cDNA expression vector for isolation of mouse interleukin 2 cDNA clones: expression of T-cell growth-factor activity after transfection of monkey cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 82 | issue = 1 | pages = 68–72 | date = Jan 1985 | pmid = 3918306 | pmc = 396972 | doi = 10.1073/pnas.82.1.68 | bibcode = 1985PNAS...82...68Y | doi-access = free }} These factors, which include [[interleukin 2]] (IL2), are secreted by lectin- or antigen-stimulated T cells, and have various physiological effects. IL2 is a lymphokine that induces the proliferation of responsive T cells. In addition, it acts on some B cells, via receptor-specific binding,{{cite journal | vauthors = Cerretti DP, McKereghan K, Larsen A, Cantrell MA, Anderson D, Gillis S, Cosman D, Baker PE | title = Cloning, sequence, and expression of bovine interleukin 2 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 83 | issue = 10 | pages = 3223–7 | date = May 1986 | pmid = 3517854 | pmc = 323485 | doi = 10.1073/pnas.83.10.3223 | bibcode = 1986PNAS...83.3223C | doi-access = free }} as a growth factor and antibody production stimulant.{{cite journal | vauthors = Mott HR, Driscoll PC, Boyd J, Cooke RM, Weir MP, Campbell ID | title = Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments | journal = Biochemistry | volume = 31 | issue = 33 | pages = 7741–4 | date = Aug 1992 | pmid = 1510960 | doi = 10.1021/bi00148a040 }} The protein is secreted as a single glycosylated polypeptide, and cleavage of a signal sequence is required for its activity. Solution NMR suggests that the structure of IL2 comprises a bundle of 4 helices (termed A-D), flanked by 2 shorter helices and several poorly defined loops. Residues in helix A, and in the loop region between helices A and B, are important for receptor binding. Secondary structure analysis has suggested similarity to IL4 and granulocyte-macrophage colony stimulating factor (GMCSF). [34] => [35] => ===Interleukin 3=== [36] => {{main|Interleukin 3}} [37] => [38] => [[Interleukin 3]] (IL3) is a cytokine that regulates [[hematopoiesis]] by controlling the production, differentiation and function of granulocytes and macrophages.{{cite journal | vauthors = Dorssers L, Burger H, Bot F, Delwel R, Geurts van Kessel AH, Löwenberg B, Wagemaker G | title = Characterization of a human multilineage-colony-stimulating factor cDNA clone identified by a conserved noncoding sequence in mouse interleukin-3 | journal = Gene | volume = 55 | issue = 1 | pages = 115–24 | year = 1987 | pmid = 3497843 | doi = 10.1016/0378-1119(87)90254-X }}{{cite journal | vauthors = Ymer S, Tucker WQ, Sanderson CJ, Hapel AJ, Campbell HD, Young IG | s2cid = 4279226 | title = Constitutive synthesis of interleukin-3 by leukaemia cell line WEHI-3B is due to retroviral insertion near the gene | journal = Nature | volume = 317 | issue = 6034 | pages = 255–8 | year = 1985 | pmid = 2413359 | doi = 10.1038/317255a0 | bibcode = 1985Natur.317..255Y }} The protein, which exists in vivo as a monomer, is produced in activated T cells and mast cells, and is activated by the cleavage of an N-terminal signal sequence. [39] => [40] => IL3 is produced by T lymphocytes and T-cell lymphomas only after stimulation with antigens, mitogens, or chemical activators such as phorbol esters. However, IL3 is constitutively expressed in the myelomonocytic leukaemia cell line WEHI-3B. It is thought that the genetic change of the cell line to constitutive production of IL3 is the key event in development of this leukaemia. [41] => [42] => ===Interleukin 4=== [43] => {{main|Interleukin 4}}[[Interleukin 4]] (IL4) is produced by CD4+ T cells specialized in providing help to B cells to proliferate and to undergo class switch recombination and somatic hypermutation. Th2 cells, through production of IL-4, have an important function in B-cell responses that involve class switch recombination to the IgG1 and IgE isotypes. [44] => [45] => ===Interleukin 5=== [46] => {{main|Interleukin 5}}[[Interleukin 5]] (IL5), also known as [[eosinophil]] differentiation factor (EDF), is a lineage-specific cytokine for eosinophilpoiesis.{{cite journal | vauthors = Campbell HD, Tucker WQ, Hort Y, Martinson ME, Mayo G, Clutterbuck EJ, Sanderson CJ, Young IG | title = Molecular cloning, nucleotide sequence, and expression of the gene encoding human eosinophil differentiation factor (interleukin 5) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 19 | pages = 6629–33 | date = Oct 1987 | pmid = 3498940 | pmc = 299136 | doi = 10.1073/pnas.84.19.6629 | bibcode = 1987PNAS...84.6629C | doi-access = free }}{{cite journal | vauthors = Milburn MV, Hassell AM, Lambert MH, Jordan SR, Proudfoot AE, Graber P, Wells TN | s2cid = 4254991 | title = A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5 | journal = Nature | volume = 363 | issue = 6425 | pages = 172–6 | date = May 1993 | pmid = 8483502 | doi = 10.1038/363172a0 | bibcode = 1993Natur.363..172M }} It regulates eosinophil growth and activation, and thus plays an important role in diseases associated with increased levels of eosinophils, including asthma. IL5 has a similar overall fold to other cytokines (e.g., IL2, IL4 and GCSF), but while these exist as monomeric structures, IL5 is a homodimer. The fold contains an anti-parallel 4-alpha-helix bundle with a left handed twist, connected by a 2-stranded anti-parallel beta-sheet.{{cite journal | vauthors = Proudfoot AE, Davies JG, Turcatti G, Wingfield PT | title = Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein | journal = FEBS Letters | volume = 283 | issue = 1 | pages = 61–4 | date = May 1991 | pmid = 2037074 | doi = 10.1016/0014-5793(91)80553-F | s2cid = 39101523 | doi-access = free }} The monomers are held together by 2 interchain disulphide bonds. [47] => [48] => ===Interleukin 6=== [49] => {{main|Interleukin 6}} [50] => [51] => [[Interleukin 6]] (IL6), also referred to as B-cell stimulatory factor-2 (BSF-2) and interferon beta-2, is a cytokine involved in a wide variety of biological functions.{{cite journal | vauthors = Hirano T, Yasukawa K, Harada H, Taga T, Watanabe Y, Matsuda T, Kashiwamura S, Nakajima K, Koyama K, Iwamatsu A | s2cid = 4367596 | title = Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes to produce immunoglobulin | journal = Nature | volume = 324 | issue = 6092 | pages = 73–6 | year = 1986 | pmid = 3491322 | doi = 10.1038/324073a0 | bibcode = 1986Natur.324...73H }} It plays an essential role in the final differentiation of B cells into immunoglobulin-secreting cells, as well as inducing myeloma/plasmacytoma growth, nerve cell differentiation, and, in hepatocytes, acute-phase reactants.{{cite journal | vauthors = Lütticken C, Krüttgen A, Möller C, Heinrich PC, Rose-John S | title = Evidence for the importance of a positive charge and an alpha-helical structure of the C-terminus for biological activity of human IL-6 | journal = FEBS Letters | volume = 282 | issue = 2 | pages = 265–7 | date = May 1991 | pmid = 2037043 | doi = 10.1016/0014-5793(91)80491-K | s2cid = 42023451 | doi-access = free }} [52] => [53] => A number of other cytokines may be grouped with IL6 on the basis of sequence similarity.{{cite journal | vauthors = Clogston CL, Boone TC, Crandall BC, Mendiaz EA, Lu HS | title = Disulfide structures of human interleukin-6 are similar to those of human granulocyte colony stimulating factor | journal = Archives of Biochemistry and Biophysics | volume = 272 | issue = 1 | pages = 144–51 | date = Jul 1989 | pmid = 2472117 | doi = 10.1016/0003-9861(89)90205-1 }} These include granulocyte colony-stimulating factor (GCSF) and myelomonocytic growth factor (MGF). GCSF acts in hematopoiesis by affecting the production, differentiation, and function of two related white cell groups in the blood. MGF also acts in hematopoiesis, stimulating proliferation and colony formation of normal and transformed avian cells of the myeloid lineage. [54] => [55] => Cytokines of the IL6/GCSF/MGF family are glycoproteins of about 170 to 180 amino acid residues that contain four conserved cysteine residues involved in two disulphide bonds. They have a compact, globular fold (similar to other interleukins), stabilised by the two disulphide bonds. One half of the structure is dominated by a 4-alpha-helix bundle with a left-handed twist;{{cite journal | vauthors = Walter MR, Cook WJ, Zhao BG, Cameron RP, Ealick SE, Walter RL, Reichert P, Nagabhushan TL, Trotta PP, Bugg CE | s2cid = 2310949 | title = Crystal structure of recombinant human interleukin-4 | journal = The Journal of Biological Chemistry | volume = 267 | issue = 28 | pages = 20371–6 | date = Oct 1992 | pmid = 1400355 | doi = 10.2210/pdb2int/pdb }} the helices are anti-parallel, with two overhand connections, which fall into a double-stranded anti-parallel beta-sheet. The fourth alpha-helix is important to the [[biological activity]] of the molecule. [56] => [57] => ===Interleukin 7 === [58] => {{main|Interleukin 7|}} [59] => [60] => [[Interleukin 7]] (IL-7){{cite journal | vauthors = Henney CS | title = Interleukin 7: effects on early events in lymphopoiesis | journal = Immunology Today | volume = 10 | issue = 5 | pages = 170–3 | date = May 1989 | pmid = 2663018 | doi = 10.1016/0167-5699(89)90175-8 }} is a cytokine that serves as a growth factor for early lymphoid cells of both B- and T-cell lineages. [61] => [62] => ===Interleukin 8=== [63] => {{Main|Interleukin 8}} [64] => Interleukin 8 is a [[chemokine]] produced by [[macrophages]] and other cell types such as [[epithelial cells]], airway smooth muscle cells{{cite journal | vauthors = Hedges JC, Singer CA, Gerthoffer WT | title = Mitogen-activated protein kinases regulate cytokine gene expression in human airway myocytes | journal = Am. J. Respir. Cell Mol. Biol. | volume = 23 | issue = 1 | pages = 86–94 | year = 2000 | pmid = 10873157 | doi = 10.1165/ajrcmb.23.1.4014 | citeseerx = 10.1.1.326.6212 }} and endothelial cells. [[Endothelial cells]] store IL-8 in their storage vesicles, the [[Weibel-Palade bodies]].{{cite journal | vauthors = Wolff B, Burns AR, Middleton J, Rot A | title = Endothelial cell "memory" of inflammatory stimulation: human venular endothelial cells store interleukin 8 in Weibel-Palade bodies | journal = J. Exp. Med. | volume = 188 | issue = 9 | pages = 1757–62 | year = 1998 | pmid = 9802987 | pmc = 2212526 | doi = 10.1084/jem.188.9.1757 }}{{cite journal | vauthors = Utgaard JO, Jahnsen FL, Bakka A, Brandtzaeg P, Haraldsen G | title = Rapid secretion of prestored interleukin 8 from Weibel-Palade bodies of microvascular endothelial cells | journal = J. Exp. Med. | volume = 188 | issue = 9 | pages = 1751–6 | year = 1998 | pmid = 9802986 | pmc = 2212514 | doi = 10.1084/jem.188.9.1751 }} In humans, the interleukin-8 [[protein]] is encoded by the ''CXCL8'' [[gene]].{{cite journal | vauthors = Modi WS, Dean M, Seuanez HN, Mukaida N, Matsushima K, O'Brien SJ | s2cid = 2217894 | title = Monocyte-derived neutrophil chemotactic factor (MDNCF/IL-8) resides in a gene cluster along with several other members of the platelet factor 4 gene superfamily | journal = Hum. Genet. | volume = 84 | issue = 2 | pages = 185–7 | year = 1990 | pmid = 1967588 | doi = 10.1007/BF00208938 }} IL-8 is initially produced as a precursor peptide of 99 amino acids which then undergoes cleavage to create several active IL-8 isoforms.{{cite journal |vauthors=Brat DJ, Bellail AC, Van Meir EG | year = 2005 | title = The role of interleukin-8 and its receptors in gliomagenesis and tumoral angiogenesis | journal = Neuro-Oncology | volume = 7 | issue = 2| pages = 122–133 | doi=10.1215/s1152851704001061| pmid = 15831231 | pmc = 1871893}} In culture, a 72 amino acid peptide is the major form secreted by macrophages. [65] => [66] => There are many receptors on the surface membrane capable of binding IL-8; the most frequently studied types are the [[G protein-coupled receptor|G protein-coupled]] serpentine receptors [[interleukin 8 receptor, alpha|CXCR1]] and [[interleukin 8 receptor, beta|CXCR2]]. Expression and affinity for IL-8 differs between the two receptors (CXCR1 > CXCR2). Through a chain of biochemical reactions, IL-8 is secreted and is an important mediator of the immune reaction in the innate immune system response. [67] => [68] => === Interleukin 9 === [69] => {{main|2=Interleukin 9}} [70] => [71] => [[Interleukin 9]] (IL-9){{cite journal|vauthors=Renauld JC, Goethals A, Houssiau F, Merz H, Van Roost E, Van Snick J|date=Jun 1990|title=Human P40/IL-9. Expression in activated CD4+ T cells, genomic organization, and comparison with the mouse gene|journal=Journal of Immunology|volume=144|issue=11|pages=4235–41|doi=10.4049/jimmunol.144.11.4235 |pmid=1971295|s2cid=30151082 }} is a cytokine that supports IL-2 independent and IL-4 independent growth of helper T cells. Early studies had indicated that Interleukin 9 and 7 seem to be evolutionary related {{cite journal | vauthors = Boulay JL, Paul WE | s2cid = 42479456 | title = Hematopoietin sub-family classification based on size, gene organization and sequence homology | journal = Current Biology | volume = 3 | issue = 9 | pages = 573–81 | date = September 1993 | pmid = 15335670 | doi = 10.1016/0960-9822(93)90002-6 | bibcode = 1993CBio....3..573B }} and Pfam, InterPro and PROSITE entries exist for interleukin 7/interleukin 9 family. However, a recent study {{cite journal | vauthors = Reche PA | s2cid = 73449371 | title = The tertiary structure of γc cytokines dictates receptor sharing | journal = Cytokine | volume = 116 | pages = 161–168 | date = February 2019 | pmid = 30716660 | doi = 10.1016/j.cyto.2019.01.007 }} has shown that IL-9 is, in fact, much closer to both IL-2 and IL-15, than to IL-7. Moreover, the study showed irreconcilable structural differences between IL-7 and all the remaining cytokines signalling through the [[Common gamma chain|γc]] receptor ( IL-2, IL-4, IL-7, IL-9, IL-15 and IL-21). [72] => [73] => ===Interleukin 10=== [74] => {{main|Interleukin 10}}[[Interleukin 10]] (IL-10) is a protein that inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T cells. In structure, IL-10 is a protein of about 160 amino acids that contains four conserved cysteines involved in disulphide bonds.{{cite journal | vauthors = Zdanov A, Schalk-Hihi C, Gustchina A, Tsang M, Weatherbee J, Wlodawer A | title = Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma | journal = Structure | volume = 3 | issue = 6 | pages = 591–601 | date = Jun 1995 | pmid = 8590020 | doi = 10.1016/S0969-2126(01)00193-9 | doi-access = free }} IL-10 is highly similar to the ''[[Human herpesvirus 4]]'' (Epstein-Barr virus) BCRF1 protein, which inhibits the synthesis of gamma-interferon and to ''[[Equid herpesvirus 2]]'' (Equine herpesvirus 2) protein E7. It is also similar, but to a lesser degree, with human protein mda-7.{{cite journal | vauthors = Jiang H, Lin JJ, Su ZZ, Goldstein NI, Fisher PB | title = Subtraction hybridization identifies a novel melanoma differentiation associated gene, mda-7, modulated during human melanoma differentiation, growth and progression | journal = Oncogene | volume = 11 | issue = 12 | pages = 2477–86 | date = Dec 1995 | pmid = 8545104 }} a protein that has antiproliferative properties in human melanoma cells. Mda-7 contains only two of the four cysteines of IL-10. [75] => [76] => ===Interleukin 11=== [77] => {{main|Interleukin 11}}[[Interleukin 11]] (IL-11) is a secreted protein that stimulates megakaryocytopoiesis, initially thought to lead to an increased production of platelets (it has since been shown to be redundant to normal platelet formation), as well as activating osteoclasts, inhibiting epithelial cell proliferation and apoptosis, and inhibiting macrophage mediator production. These functions may be particularly important in mediating the hematopoietic, osseous and mucosal protective effects of interleukin 11.{{cite journal | vauthors = Leng SX, Elias JA | title = Interleukin-11 | journal = The International Journal of Biochemistry & Cell Biology | volume = 29 | issue = 8–9 | pages = 1059–62 | year = 1997 | pmid = 9416001 | doi = 10.1016/S1357-2725(97)00017-4 | doi-access = free }} [78] => [79] => ===Interleukin 12=== [80] => {{main|Interleukin 12}} [81] => [82] => [[Interleukin 12]] (IL-12) is a disulphide-bonded heterodimer consisting of a 35kDa alpha subunit and a 40kDa beta subunit. It is involved in the stimulation and maintenance of Th1 cellular immune responses, including the normal host defence against various intracellular pathogens, such as Leishmania, Toxoplasma, ''[[Measles virus]]'', and ''[[Human immunodeficiency virus 1]]'' (HIV). IL-12 also has an important role in enhancing the cytotoxic function of [[NK cell]]s{{cite book|vauthors=Abbas AK, Lichtman AH, Pillai S | title = Cellular and molecular immunology | year = 2012 | publisher = Elsevier/Saunders | location = Philadelphia | isbn = 978-1437715286 | edition = 7th }}{{cite journal | vauthors = Zhang C, Zhang J, Niu J, Zhou Z, Zhang J, Tian Z | title = Interleukin-12 improves cytotoxicity of natural killer cells via upregulated expression of NKG2D | journal = Human Immunology | volume = 69 | issue = 8 | pages = 490–500 | date = Aug 2008 | pmid = 18619507 | doi = 10.1016/j.humimm.2008.06.004 }} and role in pathological Th1 responses, such as in inflammatory bowel disease and multiple sclerosis. Suppression of IL-12 activity in such diseases may have therapeutic benefit. On the other hand, administration of recombinant IL-12 may have therapeutic benefit in conditions associated with pathological Th2 responses.{{cite journal | vauthors = Park AY, Scott P | title = Il-12: keeping cell-mediated immunity alive | journal = Scandinavian Journal of Immunology | volume = 53 | issue = 6 | pages = 529–32 | date = Jun 2001 | pmid = 11422900 | doi = 10.1046/j.1365-3083.2001.00917.x | s2cid = 32020154 }}{{cite journal | vauthors = Gately MK, Renzetti LM, Magram J, Stern AS, Adorini L, Gubler U, Presky DH | title = The interleukin-12/interleukin-12-receptor system: role in normal and pathologic immune responses | journal = Annual Review of Immunology | volume = 16 | pages = 495–521 | year = 1998 | pmid = 9597139 | doi = 10.1146/annurev.immunol.16.1.495 }} [83] => [84] => ===Interleukin 13=== [85] => {{main|Interleukin 13}} [86] => [87] => [[Interleukin 13]] (IL-13) is a pleiotropic cytokine that may be important in the regulation of the inflammatory and immune responses.{{cite journal | vauthors = Minty A, Chalon P, Derocq JM, Dumont X, Guillemot JC, Kaghad M, Labit C, Leplatois P, Liauzun P, Miloux B | s2cid = 4368915 | title = Interleukin-13 is a new human lymphokine regulating inflammatory and immune responses | journal = Nature | volume = 362 | issue = 6417 | pages = 248–50 | date = Mar 1993 | pmid = 8096327 | doi = 10.1038/362248a0 | bibcode = 1993Natur.362..248M }} It inhibits inflammatory cytokine production and synergises with IL-2 in regulating interferon-gamma synthesis. The sequences of IL-4 and IL-13 are distantly related.{{cite journal | vauthors = Seyfizadeh N, Seyfizadeh N, Gharibi T, Babaloo Z | title = Interleukin-13 as an important cytokine: A review on its roles in some human diseases | journal = Acta Microbiologica et Immunologica Hungarica | volume = 62 | issue = 4 | pages = 341–78 | date = December 2015 | pmid = 26689873 | doi = 10.1556/030.62.2015.4.2 | url = http://real.mtak.hu/36921/1/030.62.2015.4.2.pdf }} [88] => [89] => ===Interleukin 15=== [90] => {{main|Interleukin 15}} [91] => [92] => [[Interleukin 15]] (IL-15) is a cytokine that possesses a variety of biological functions, including stimulation and maintenance of cellular immune responses.{{cite journal | vauthors = Arena A, Merendino RA, Bonina L, Iannello D, Stassi G, Mastroeni P | title = Role of IL-15 on monocytic resistance to human herpesvirus 6 infection | journal = The New Microbiologica | volume = 23 | issue = 2 | pages = 105–12 | date = Apr 2000 | pmid = 10872679 }} IL-15 stimulates the proliferation of T lymphocytes, which requires interaction of IL-15 with IL-15R alpha and components of IL-2R, including IL-2R beta and IL-2R gamma (common gamma chain, γc), but not IL-2R alpha. [93] => [94] => ===Interleukin 17=== [95] => {{main|Interleukin 17}} [96] => [97] => [[Interleukin 17]] (IL-17) is a potent proinflammatory cytokine produced by activated memory T cells.{{cite journal | vauthors = Aggarwal S, Gurney AL | title = IL-17: prototype member of an emerging cytokine family | journal = Journal of Leukocyte Biology | volume = 71 | issue = 1 | pages = 1–8 | date = January 2002 | doi = 10.1189/jlb.71.1.1 | pmid = 11781375 | s2cid = 15271840 | doi-access = free }} This cytokine is characterized by its proinflammatory properties, role in recruiting neutrophils, and importance in innate and adaptive immunity. Not only does IL-17 play a key role in inflammation of many autoimmune diseases, such as RA, allergies, asthma, psoriasis, and more, but it also plays a key role in the pathogenesis of these diseases. Additionally, some studies have found that IL-17 plays a role in tumorigenesis (initial formation of a tumor) and transplant rejection.{{cite journal | vauthors = Tesmer LA, Lundy SK, Sarkar S, Fox DA | title = Th17 cells in human disease | journal = Immunological Reviews | volume = 223 | pages = 87–113 | date = June 2008 | pmid = 18613831 | pmc = 3299089 | doi = 10.1111/j.1600-065X.2008.00628.x }} The IL-17 family is thought to represent a distinct signaling system that appears to have been highly conserved across vertebrate evolution. [98] => [99] => ==In humans== [100] => [101] => {| class="wikitable" [102] => ! rowspan=2 | Name [103] => ! rowspan=2 | SourceUnless else specified in boxes, then ref is: Lippincott's Illustrated Reviews: Immunology. Paperback: 384 pages. Publisher: Lippincott Williams & Wilkins; (July 1, 2007). Language: English. {{ISBN|0-7817-9543-5}}. {{ISBN|978-0-7817-9543-2}}. Page 68 [104] => ! colspan=2 | Targets [105] => ! rowspan=2 | Function [106] => |- [107] => ! Receptors{{cite web | url = http://www.ebioscience.com/ebioscience/whatsnew/pdf/Cytokines.pdf | title = Cytokines - Master Regulators of the Immune System | access-date = 2008-02-28 | vauthors = Alaverdi N, Sehy D | date = 2007-05-01 | publisher = eBioscience | archive-url =https://web.archive.org/web/20060315211023/http://www.ebioscience.com/ebioscience/whatsnew/pdf/Cytokines.pdf| archive-date =2006-03-15| url-status = dead }} [108] => ! Cells [109] => |- [110] => |rowspan=4| [[Interleukin 1|IL-1]] [111] => |rowspan=4| [[macrophage]]s, [[B cell]]s, [[monocytes]],[http://microvet.arizona.edu/Courses/MIC419/Tutorials/cytokines.html Cytokine tutorial, The University of Arizona] {{webarchive|url=https://web.archive.org/web/20080202122645/http://microvet.arizona.edu/Courses/MIC419/Tutorials/cytokines.html |date=2008-02-02 }} [[dendritic cell]]s [112] => |rowspan=4| [[Interleukin 1 receptor, type I|CD121a/IL1R1]], [[Interleukin 1 receptor, type II|CD121b/IL1R2]] [113] => | [[T helper cell]]s || co-stimulation [114] => |- [115] => | [[B cell]]s|| maturation and proliferation [116] => |- [117] => | [[Natural killer cell|NK cells]] || activation [118] => |- [119] => | [[macrophage]]s, [[endothelium]], other || [[inflammation]], small amounts induce [[acute phase protein|acute phase reaction]], large amounts induce [[fever]] [120] => |- [121] => | [[Interleukin 2|IL-2]] || [[T helper cell|Th1-cells]] || [[IL2RA|CD25/IL2RA]], [[IL2RB|CD122/IL2RB]], [[IL2RG|CD132/IL2RG]] || activated [[T cell]]s and [[B cell]]s, [[Natural killer cell|NK cells]], [[macrophage]]s, [[oligodendrocyte]]s || stimulates growth and differentiation of T cell response. Can be used in [[immunotherapy]] to treat cancer or suppressed for transplant patients. Has also been used in clinical trials (ESPIRIT. Stalwart) to raise CD4 counts in HIV positive patients. [122] => |- [123] => |rowspan=2| [[Interleukin 3|IL-3]] ||rowspan=2| activated [[T helper cell]]s, [[mast cell]]s, [[Natural killer cell|NK cells]], [[endothelium]], [[Eosinophil granulocyte|eosinophils]] ||rowspan=2| [[IL3RA|CD123/IL3RA]], [[CSF2RB|CD131/IL3RB]] || [[hematopoietic stem cell]]s || differentiation and proliferation of myeloid progenitor cells to e.g. [[erythrocytes]], [[granulocytes]] [124] => |- [125] => | mast cells || growth and [[histamine]] release [126] => |- [127] => |rowspan=3| [[Interleukin 4|IL-4]] ||rowspan=3| [[Th2 cell]]s, just activated naive [[CD4+ cell]], [[memory CD4+ cells]], [[mast cell]]s, [[macrophage]]s ||rowspan=3| [[Interleukin-4 receptor|CD124/IL4R]], [[IL2RG|CD132/IL2RG]] || activated [[B cell]]s || proliferation and differentiation, [[IgG1]] and [[immunoglobulin E|IgE]] synthesis. Important role in [[allergic]] response ([[IgE]]) [128] => |- [129] => | [[T cell]]s || proliferation [130] => |- [131] => | [[endothelium]] || increase expression of [[vascular cell]] [[adhesion molecule]] (VCAM-1) promoting adhesion of lymphocytes.{{cite journal |vauthors=Kotowicz K, Callard RE, Friedrich K, Matthews DJ, Klein N | date = Dec 1996 | title = Biological activity of IL-4 and IL-13 on human endothelial cells: functional evidence that both cytokines act through the same receptor | journal = Int Immunol | volume = 8 | issue = 12| pages = 1915–25 | pmid = 8982776 | doi=10.1093/intimm/8.12.1915| doi-access = free }} [132] => |- [133] => |rowspan=2| [[Interleukin 5|IL-5]] ||rowspan=2| [[Th2 cell]]s, [[mast cell]]s, [[Eosinophil granulocyte|eosinophils]] ||rowspan=2| [[Interleukin 5 receptor alpha subunit|CD125/IL5RA]], [[CSF2RB|CD131/IL3RB]] || [[Eosinophil granulocyte|eosinophils]] || production [134] => |- [135] => | [[B cell]]s || differentiation, [[IgA]] production [136] => |- [137] => |rowspan=4| [[Interleukin 6|IL-6]] ||rowspan=4| [[macrophage]]s, [[Th2 cell]]s, [[B cell]]s, [[astrocytes]], [[endothelium]] ||rowspan=4| [[Interleukin-6 receptor|CD126/IL6RA]], [[Glycoprotein 130|CD130/IL6RB]] || activated [[B cell]]s || differentiation into [[plasma cell]]s [138] => |- [139] => | plasma cells || [[antibody]] secretion [140] => |- [141] => | [[hematopoietic stem cell]]s || differentiation [142] => |- [143] => | [[T cell]]s, others || induces [[acute phase protein|acute phase reaction]], [[hematopoiesis]], [[differentiation (cellular)|differentiation]], [[inflammation]] [144] => |- [145] => | [[Interleukin 7|IL-7]] || [[Bone marrow stromal cells]] and [[thymus stromal cells]] || [[Interleukin-7 receptor|CD127/IL7RA]], [[Common gamma chain|CD132/IL2RG]] || [[pre-B cell|pre]]/[[pro-B cell]], [[pre-T cell|pre]]/[[pro-T cell]], NK cells || differentiation and proliferation of lymphoid progenitor cells, involved in B, T, and NK cell survival, development, and homeostasis, ↑[[proinflammatory]] cytokines [146] => |- [147] => | [[Interleukin 8|IL-8 or CXCL8]] || macrophages, [[lymphocytes]], [[epithelial cell]]s, endothelial cells || [[Interleukin 8 receptor, alpha|CXCR1/IL8RA]], [[Interleukin 8 receptor, beta|CXCR2/IL8RB]]/CD128 || [[Neutrophil granulocyte|neutrophils]], [[Basophil granulocyte|basophils]], lymphocytes || Neutrophil [[chemotaxis]] [148] => |- [149] => | [[Interleukin 9|IL-9]] || [[Th2 cell]]s, specifically by CD4+ helper cells || [[Interleukin-9 receptor|CD129/IL9R]] || [[T cell]]s, [[B cell]]s ||Potentiates [[immunoglobulin M|IgM]], [[immunoglobulin G|IgG]], [[immunoglobulin E|IgE]], stimulates [[mast cell]]s [150] => |- [151] => |rowspan=5| [[Interleukin 10|IL-10]] ||rowspan=5| [[monocyte]]s, [[Th2 cell]]s, [[CD8+ T cells]], [[mast cell]]s, [[macrophage]]s, [[B cell]] subset ||rowspan=5| [[Interleukin 10 receptor, alpha subunit|CD210/IL10RA]], [[Interleukin 10 receptor, beta subunit|CDW210B/IL10RB]] || [[macrophage]]s || cytokine production [152] => |- [153] => | B cells || activation [154] => |- [155] => | [[mast cell]]s || [156] => |- [157] => | [[Th1 cell]]s || inhibits [[T helper cell|Th1]] cytokine production ([[IFN-γ]], [[TNF-β]], [[interleukin 2|IL-2]]) [158] => |- [159] => | [[Th2 cell]]s || Stimulation [160] => |- [161] => | [[Interleukin 11|IL-11]] || [[bone marrow stroma]] || [[Interleukin 11 receptor alpha subunit|IL11RA]] || [[bone marrow stroma]] || [[acute phase protein]] production, [[osteoclast]] formation [162] => |- [163] => |rowspan=2| [[Interleukin 12|IL-12]] ||rowspan=2| [[dendritic cell]]s, [[B cell]]s, [[T cell]]s, [[macrophage]]s ||rowspan=2| [[Interleukin 12 receptor, beta 1 subunit|CD212/IL12RB1]], [[Interleukin 12 receptor, beta 2 subunit|IR12RB2]] || activated [[T cell]]s, || differentiation into [[Cytotoxic T cell]]s with IL-2, ↑ [[IFN-γ]], [[TNF-α]], ↓ IL-10 [164] => |- [165] => | [[Natural killer cell|NK cells]] || ↑ [[IFN-γ]], [[TNF-α]] [166] => |- [167] => | [[Interleukin 13|IL-13]] || activated [[Th2 cell]]s, [[mast cell]]s, [[Natural killer cell|NK cells]] || [[Interleukin-13 receptor|IL13R]] || Th2 cells, B cells, macrophages || Stimulates growth and differentiation of [[B cell]]s ([[IgE]]), inhibits [[T helper cell|Th1 cells]] and the production of [[macrophage inflammatory cytokines]] (e.g. IL-1, IL-6), ↓ IL-8, IL-10, IL-12 [168] => |- [169] => | [[Interleukin 14|IL-14]] || T cells and certain malignant B cells || || activated B cells || controls the growth and proliferation of [[B cell]]s, inhibits Ig secretion [170] => |- [171] => | [[Interleukin 15|IL-15]] || mononuclear phagocytes (and some other cells), especially macrophages following infection by virus(es) || [[Interleukin 15 receptor, alpha subunit|IL15RA]] || T cells, activated B cells || Induces production of [[Natural killer cells]] [172] => |- [173] => | [[Interleukin 16|IL-16]] || lymphocytes, epithelial cells, eosinophils, CD8+ T cells || [[CD4]] || CD4+ T cells (Th-cells)|| [[CD4]]+ chemoattractant [174] => |- [175] => | [[Interleukin 17|IL-17]] || [[T helper 17 cell]]s (Th17) || [[IL17RA|CDw217/IL17RA]], [[IL17RB]] || epithelium, endothelium, other || [[osteoclastogenesis]], [[angiogenesis]], ↑ pro-inflammatory [[cytokines]] [176] => |- [177] => | [[Interleukin 18|IL-18]] || macrophages || [[Interleukin-18 receptor|CDw218a/IL18R1]] || Th1 cells, NK cells || Induces production of [[Interferon-gamma|IFN-γ]], ↑ NK cell activity [178] => |- [179] => | [[Interleukin 19|IL-19]] || - || [[Interleukin-20 receptor|IL20R]] || || - [180] => |- [181] => | [[Interleukin 20|IL-20]] || Activated keratinocytes and monocytes || [[Interleukin-20 receptor|IL20R]] || || regulates proliferation and differentiation of [[keratinocyte]]s [182] => |- [183] => | [[Interleukin 21|IL-21]] || activated T helper cells, NKT cells || [[Interleukin-21 receptor|IL21R]] || All lymphocytes, dendritic cells ||costimulates activation and proliferation of CD8+ T cells, augment NK cytotoxicity, augments CD40-driven B cell proliferation, differentiation and isotype switching, promotes differentiation of Th17 cells [184] => |- [185] => | [[Interleukin 22|IL-22]] || [[T helper 17 cell]]s (Th17) || [[Interleukin-22 receptor|IL22R]] || || Production of defensins from epithelial cells. Activates [[STAT1]] and [[STAT3]] and increases production of [[acute phase protein]]s such as [[serum amyloid A]], [[Alpha 1-antichymotrypsin]] and [[haptoglobin]] in [[hepatoma]] cell lines [186] => |- [187] => | [[Interleukin 23|IL-23]] || [[macrophage]]s, [[dendritic cell]]s || [[Interleukin-23 receptor|IL23R]] || || Maintenance of IL-17 producing cells, increases [[angiogenesis]] but reduces [[CD8]] T-cell infiltration [188] => |- [189] => | [[Interleukin 24|IL-24]] || [[melanocyte]]s, [[keratinocyte]]s, [[monocyte]]s, T cells || [[Interleukin-20 receptor|IL20R]] || || Plays important roles in [[tumor suppression]], wound healing and [[psoriasis]] by influencing cell survival, inflammatory cytokine expression. [190] => |- [191] => | [[Interleukin 25|IL-25]] || [[T Cell]]s, [[mast cell]]s, [[eosinophil]]s, [[macrophage]]s, mucosal epithelial cells || [[LY6E]] || || Induces the production [[Interleukin-4|IL-4]], [[Interleukin 5|IL-5]] and [[Interleukin 13|IL-13]], which stimulate [[eosinophil]] expansion [192] => |- [193] => | [[Interleukin 26|IL-26]] || [[T cell]]s, [[monocyte]]s || [[Interleukin 20 receptor, alpha subunit|IL20R1]] || || Enhances secretion of [[Interleukin 10|IL-10]] and [[Interleukin 8|IL-8]] and cell surface expression of [[CD54]] on [[epithelial cell]]s [194] => |- [195] => | [[Interleukin 27|IL-27]] || [[macrophage]]s, [[dendritic cell]]s || [[Interleukin 27 receptor, alpha subunit|IL27RA]] || || Regulates the activity of [[B lymphocyte]] and [[T lymphocyte]]s [196] => |- [197] => | [[Interleukin 28|IL-28]] || - || [[Interleukin-28 receptor|IL28R]] || || Plays a role in immune defense against [[virus]]es [198] => |- [199] => | [[Interleukin 29|IL-29]] || - || || || Plays a role in host defenses against [[microbe]]s [200] => |- [201] => | [[Interleukin 30|IL-30]] || - || || || Forms one chain of [[IL-27]] [202] => |- [203] => | [[Interleukin 31|IL-31]] || [[Th2 cell]]s || [[IL31RA]] || || May play a role in [[inflammation]] of the [[skin]] [204] => |- [205] => | [[Interleukin 32|IL-32]] || - || || || Induces monocytes and macrophages to secrete [[TNF-α]], [[Interleukin 8|IL-8]] and [[CXCL2]] [206] => |- [207] => | [[Interleukin 33|IL-33]] || [[epithelial cells]]|| || || Induces [[helper T cell]]s to produce [[type 2 cytokine]] [208] => |- [209] => | [[Interleukin 35|IL-35]] || [[regulatory T cell]]s || || || Suppression of T helper cell activation [210] => |- [211] => | [[Interleukin 36|IL-36]] || - || || || Regulates [[Dendritic cell|DC]] and [[T cell]] responses [212] => |- [213] => |} [214] => [215] => ==International nonproprietary names for analogues and derivatives== [216] => {| class="wikitable sortable" [217] => ! Endogenous form name !! Pharmaceutical form [[International Nonproprietary Name|INN]] suffix !! INNs [218] => |- [219] => | interleukin-1 (IL-1) || -nakin || [220] => |- [221] => | interleukin-1α (IL-1α) || -onakin || [[pifonakin]] [222] => |- [223] => | interleukin-1β (IL-1β) || -benakin || [[mobenakin]] [224] => |- [225] => | interleukin-2 (IL-2) || -leukin || [[adargileukin alfa]], [[aldesleukin]], [[celmoleukin]], [[denileukin diftitox]], [[pegaldesleukin]], [[teceleukin]], [[tucotuzumab celmoleukin]] [226] => |- [227] => | interleukin-3 (IL-3) || -plestim || [[daniplestim]], [[muplestim]] [228] => |- [229] => | interleukin-4 (IL-4) || -trakin || [[binetrakin]] [230] => |- [231] => | interleukin-6 (IL-6) || -exakin || [[atexakin alfa]] [232] => |- [233] => | interleukin-8 (IL-8) || -octakin || [[emoctakin]] [234] => |- [235] => | interleukin-10 (IL-10) || -decakin || [[ilodecakin]] [236] => |- [237] => | interleukin-11 (IL-11) || -elvekin || [[oprelvekin]] [238] => |- [239] => | interleukin-12 (IL-12) || -dodekin || [[edodekin alfa]] [240] => |- [241] => | interleukin-13 (IL-13) || -tredekin || [[cintredekin besudotox]] [242] => |- [243] => | interleukin-18 (IL-18) || -octadekin || [[iboctadekin]] [244] => |- [245] => |} [246] => [247] => == References == [248] => {{reflist|30em}} [249] => [250] => ==External links== [251] => *{{Commons category-inline|Interleukins}} [252] => *[http://www.cells-talk.com/ Cytokines & Cells Online Pathfinder Encyclopedia] [253] => [254] => {{Cytokines}} [255] => {{Interleukin receptor modulators}} [256] => {{InterPro content|IPR000779}} [257] => {{Authority control}} [258] => [259] => [[Category:Cytokines]] [260] => [[Category:Interleukins| ]] [] => )
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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.

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