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Interleukin Edit Wikipedia article
The function of the immune system depends in a large part 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 helper CD4 T lymphocytes, as well as through monocytes, macrophages, and endothelial cells. They promote the development and differentiation of T and B lymphocytes, and hematopoietic cells.
- 1 History and name
- 2 Common families of interleukins
- 3 List of human interleukins
- 4 References
- 5 External links
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 activating factor, mitogenic protein, T-cell replacing factor III, B-cell activating factor, B-cell differentiation factor, "Heidikine"). This decision was taken during a meeting in Interlaken (Switzerland).
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, though (the term was coined by Dr Vern Paetkau, University of Victoria); it has since been found that interleukins are produced by a wide variety of body cells.
Common families of interleukins
|Interleukin 1 / 18|
Crystallographic structure of human interleukin 1B.
Interleukin 1 alpha and interleukin 1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis. 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. 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.
Both IL-1 receptors (CD121a/IL1R1, CD121b/IL1R2) appear to be well conserved in evolution, and map to the same chromosomal location. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and IL-1RA).
The crystal structures of IL1A and IL1B 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. The beta-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel beta-barrel. Several regions, especially the loop between strands 4 and 5, have been implicated in receptor binding.
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.
Interleukin 1 also plays a role in the Central Nervous System. Research indicates that mice with a genetic deletion of the IL-1 receptor type I 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. However when mice with this genetic deletion have wild-type neural precursor cells injected into their hippocampus and these cells are allowed to mature into astrocytes containing the interleukin-1 receptor, the mice exhibit normal hippocampal-dependent memory function, and partial restoration of Long-term potentiation.
T Lymphocytes regulate the growth and differentiation of T cells and certain B cells through the release of secreted protein factors. 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, as a growth factor and antibody production stimulant. 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).
Interleukin 3 (IL3) is a cytokine that regulates blood-cell production by controlling the production, differentiation and function of granulocytes and macrophages. 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.
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.
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.
Interleukin 5 (IL5), also known as eosinophil differentiation factor (EDF), is a lineage-specific cytokine for eosinophilpoiesis. 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. The monomers are held together by 2 interchain disulphide bonds.
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. It plays an essential role in the final differentiation of B cells into IG-secreting cells, as well as inducing myeloma/plasmacytoma growth, nerve cell differentiation, and, in hepatocytes, acute-phase reactants.
A number of other cytokines may be grouped with IL6 on the basis of sequence similarity. These include granulocyte colony-stimulating factor (GCSF) and myelomonocytic growth factor (MGF). GCSF acts in hematopoiesis by affecting the production, differentiation, and function of 2 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.
Cytokines of the IL6/GCSF/MGF family are glycoproteins of about 170 to 180 amino acid residues that contains four conserved cysteine residues involved in two disulphide bonds:. They have a compact, globular fold (similar to other interleukins), stabilised by the 2 disulphide bonds. One half of the structure is dominated by a 4-alpha-helix bundle with a left-handed twist; the helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet. The fourth alpha-helix is important to the biological activity of the molecule.
Interleukins 7 and 9
|Interleukin 7/interleukin 9|
Interleukin 7 (IL-7) is a cytokine that serves as a growth factor for early lymphoid cells of both B- and T-cell lineages. Interleukin 9 (IL-9) is a cytokine that supports IL-2 independent and IL-4 independent growth of helper T cells. Interleukin 7 and 9 seems to be evolutionary related.
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. 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. a protein that has antiproliferative properties in human melanoma cells. Mda-7 contains only two of the four cysteines of IL-10.
Interleukin 11 (IL-11) is a secreted protein that stimulates megakaryocytopoiesis, resulting in increased production of platelets, 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. Family members seem to be restricted to mammals.
|Interleukin 12 alpha subunit|
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 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.
Interleukin 13 (IL-13) is a pleiotropic cytokine that may be important in the regulation of the inflammatory and immune responses. 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.
Interleukin 15 (IL-15) is a cytokine that possesses a variety of biological functions, including stimulation and maintenance of cellular immune responses. IL-15 stimulates the proliferation of T lymphocytes, which requires interaction of IL-15 with components of IL-2R, including IL-2R beta and probably IL-2R gamma, but not IL-2R alpha.
Interleukin 17 (IL-17) is a potent proinflammatory cytokine produced by activated memory T cells. The IL-17 family is thought to represent a distinct signalling system that appears to have been highly conserved across vertebrate evolution.
List of human interleukins
A list of interleukins:
|Name||Source ||Target receptors||Target cells||Function|
|IL-1||macrophages, B cells, monocytes, dendritic cells ||CD121a/IL1R1, CD121b/IL1R2||T helper cells||co-stimulation |
|B cells||maturation & proliferation |
|macrophages, endothelium, other||inflammation, small amounts induce acute phase reaction, large amounts induce fever|
|IL-2||Th1-cells||CD25/IL2RA, CD122/IL2RB, CD132/IL2RG||activated T cells and B cells, NK cells, macrophages, oligodendrocytes||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.|
|IL-3||activated T helper cells, mast cells, NK cells, endothelium, eosinophils||CD123/IL3RA, CD131/IL3RB||hematopoietic stem cells||differentiation and proliferation of myeloid progenitor cells  to e.g. erythrocytes, granulocytes|
|mast cells||growth and histamine release|
|IL-4||Th2 cells, just activated naive CD4+ cell, memory CD4+ cells, mast cells, macrophages||CD124/IL4R, CD132/IL2RG||activated B cells||proliferation and differentiation, IgG1 and IgE synthesis. Important role in allergic response (IgE)|
|IL-5||Th2 cells, mast cells, eosinophils||CD125/IL5RA, CD131/IL3RB||eosinophils||production|
|B cells||differentiation, IgA production|
|IL-6||macrophages, Th2 cells, B cells, astrocytes, endothelium||CD126/IL6RA, CD130/IR6RB||activated B cells||differentiation into plasma cells|
|plasma cells||antibody secretion|
|hematopoietic stem cells||differentiation|
|T cells, others||induces acute phase reaction, hematopoiesis, differentiation, inflammation|
|IL-7||Bone marrow stromal cells and thymus stromal cells||CD127/IL7RA, CD132/IL2RG||pre/pro-B 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|
|IL-8 or CXCL8||macrophages, lymphocytes, epithelial cells, endothelial cells||CXCR1/IL8RA, CXCR2/IL8RB/CD128||neutrophils, basophils, lymphocytes||Neutrophil chemotaxis|
|IL-9||Th2 cells, specifically by CD4+ helper cells||CD129/IL9R||T cells, B cells||Potentiates IgM, IgG, IgE, stimulates mast cells|
|IL-10||monocytes, Th2 cells, CD8+ T cells, mast cells, macrophages, B cell subset||CD210/IL10RA, CDW210B/IL10RB||macrophages||cytokine production|
|B cells||activation |
|Th1 cells||inhibits Th1 cytokine production (IFN-γ, TNF-β, IL-2)|
|IL-11||bone marrow stroma||IL11RA||bone marrow stroma||acute phase protein production, osteoclast formation|
|IL-12||dendritic cells, B cells, T cells, macrophages||CD212/IL12RB1, IR12RB2||activated  T cells,||differentiation into Cytotoxic T cells with IL-2, ↑ IFN-γ, TNF-α, ↓ IL-10|
|NK cells||↑ IFN-γ, TNF-α|
|IL-13||activated Th2 cells, mast cells, NK cells||IL13R||TH2-cells, B cells, macrophages||Stimulates growth and differentiation of B cells (IgE), inhibits TH1-cells and the production of macrophage inflammatory cytokines (e.g. IL-1, IL-6), ↓ IL-8, IL-10, IL-12|
|IL-14||T cells and certain malignant B cells||activated B cells||controls the growth and proliferation of B cells, inhibits Ig secretion|
|IL-15||mononuclear phagocytes (and some other cells), especially macrophages following infection by virus(es)||IL15RA||T cells, activated B cells||Induces production of Natural killer cells|
|IL-16||lymphocytes, epithelial cells, eosinophils, CD8+ T cells||CD4||CD4+ T cells (Th-cells)||CD4+ chemoattractant|
|IL-17||T helper 17 cells (Th17)||CDw217/IL17RA, IL17RB||epithelium, endothelium, other||osteoclastogenesis, angiogenesis, ↑ inflammatory cytokines|
|IL-18||macrophages||CDw218a/IL18R1||Th1 cells, NK cells||Induces production of IFNγ, ↑ NK cell activity|
|IL-20||Activated keratinocytes and monocytes||IL20R||regulates proliferation and differentiation of keratinocytes|
|IL-21||activated T helper cells, NKT cells||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|
|IL-22||-||IL22R||Activates STAT1 and STAT3 and increases production of acute phase proteins such as serum amyloid A, Alpha 1-antichymotrypsin and haptoglobin in hepatoma cell lines|
|IL-23||-||IL23R||Increases angiogenesis but reduces CD8 T-cell infiltration|
|IL-24||-||IL20R||Plays important roles in tumor suppression, wound healing and psoriasis by influencing cell survival.|
|IL-25||-||LY6E||Induces the production IL-4, IL-5 and IL-13, which stimulate eosinophil expansion|
|IL-26||-||IL20R1||Enhances secretion of IL-10 and IL-8 and cell surface expression of CD54 on epithelial cells|
|IL-27||-||IL27RA||Regulates the activity of B lymphocyte and T lymphocytes|
|IL-28||-||IL28R||Plays a role in immune defense against viruses|
|IL-29||-||Plays a role in host defenses against microbes|
|IL-30||-||Forms one chain of IL-27|
|IL-31||-||IL31RA||May play a role in inflammation of the skin|
|IL-32||-||Induces monocytes and macrophages to secrete TNF-α, IL-8 and CXCL2|
|IL-33||-||Induces helper T cells to produce type 2 cytokine|
|IL-35||regulatory T cells||Suppression of T helper cell activation|
|IL-36||-||Regulates DC and T cell responses|
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Interleukin-17 Provide feedback
IL-17 is a potent proinflammatory cytokine produced by activated memory T cells . The IL-17 family is thought to represent a distinct signaling system that appears to have been highly conserved across vertebrate evolution .
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR010345
Interleukins (IL) are a group of cytokines that play an important role in the immune system. They modulate inflammation and immunity by regulating growth, mobility and differentiation of lymphoid and other cells.
Interleukin-17 (IL-17) is a potent proinflammatory cytokine produced by activated memory T cells [PUBMED:11781375]. The IL-17 family (of which there are 6 known members, termed IL-17A to IL-17F) is thought to represent a distinct signalling system that appears to have been highly conserved across vertebrate evolution [PUBMED:11781375]. Family members play an active role in inflammatory diseases, autoimmune diseases and cancer [PUBMED:15485625].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Molecular function||cytokine activity (GO:0005125)|
|Biological process||inflammatory response (GO:0006954)|
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a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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- the Pfam graphic itself.
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- Pfam viewer
- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
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Note: You can also download the data file for the tree.
Curation and family details
|Seed source:||Pfam-B_9152 (release 9.0)|
|Number in seed:||20|
|Number in full:||312|
|Average length of the domain:||81.80 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||48.52 %|
|HMM build commands:||
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
Unmapped species names
Too many species/sequences
The tree shows the occurrence of this domain across different species. More...
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IL17 domain has been found. There are 10 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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