Interleukin 1 beta

IL1B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HIB, 1I1B, 1IOB, 1ITB, 1L2H, 1S0L, 1T4Q, 1TOO, 1TP0, 1TWE, 1TWM, 21BI, 2I1B, 2KH2, 2NVH, 31BI, 3O4O, 3POK, 41BI, 4DEP, 4G6J, 4G6M, 4GAI, 4I1B, 5I1B, 6I1B, 7I1B, 9ILB, 4GAF, 5BVP
Identifiers
Aliases	IL1B, IL-1, IL1-BETA, IL1F2, interleukin 1 beta, IL1beta
External IDs	OMIM: 147720; MGI: 96543; HomoloGene: 481; GeneCards: IL1B; OMA:IL1B - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q14.1 Start 112,829,751 bp End 112,836,816 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 F1|2 62.97 cM Start 129,206,490 bp End 129,213,059 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in periodontal fiber granulocyte monocyte blood bone marrow cells cartilage tissue pancreatic ductal cell gallbladder appendix decidua Top expressed in granulocyte blood tibiofemoral joint spleen embryo bone marrow islet of Langerhans right lung lumbar subsegment of spinal cord right ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein domain specific binding interleukin-1 receptor binding cytokine activity integrin binding protein binding Cellular component cytoplasm cytosol extracellular region lysosome extracellular exosome secretory granule vesicle extracellular space Biological process positive regulation of protein phosphorylation smooth muscle adaptation positive regulation of calcidiol 1-monooxygenase activity negative regulation of insulin receptor signaling pathway cellular response to mechanical stimulus positive regulation of interleukin-8 production positive regulation of mitotic nuclear division response to carbohydrate embryo implantation regulation of I-kappaB kinase/NF-kappaB signaling negative regulation of cell population proliferation apoptotic process cellular response to organic substance positive regulation of phagocytosis regulation of insulin secretion neutrophil chemotaxis positive regulation of transcription, DNA-templated positive regulation of protein export from nucleus positive regulation of prostaglandin secretion positive regulation of myosin light chain kinase activity negative regulation of MAP kinase activity positive regulation of T cell proliferation positive regulation of interleukin-6 production inflammatory response negative regulation of lipid metabolic process sequestering of triglyceride hyaluronan biosynthetic process positive regulation of heterotypic cell-cell adhesion positive regulation of lipid catabolic process cellular response to organic cyclic compound positive regulation of fever generation positive regulation of DNA-binding transcription factor activity positive regulation of angiogenesis response to lipopolysaccharide positive regulation of NF-kappaB transcription factor activity positive regulation of granulocyte macrophage colony-stimulating factor production immune response ectopic germ cell programmed cell death leukocyte migration lipopolysaccharide-mediated signaling pathway positive regulation of vascular endothelial growth factor receptor signaling pathway positive regulation of cell adhesion molecule production response to ATP monocyte aggregation protein kinase B signaling positive regulation of nitric oxide biosynthetic process cell-cell signaling positive regulation of monocyte chemotactic protein-1 production regulation of nitric-oxide synthase activity positive regulation of membrane protein ectodomain proteolysis positive regulation of interferon-gamma production MAPK cascade positive regulation of histone acetylation positive regulation of gene expression negative regulation of glucose transmembrane transport interleukin-1 beta production positive regulation of T cell mediated immunity extrinsic apoptotic signaling pathway in absence of ligand positive regulation of I-kappaB kinase/NF-kappaB signaling positive regulation of vascular endothelial growth factor production negative regulation of extrinsic apoptotic signaling pathway in absence of ligand negative regulation of lipid catabolic process negative regulation of adiponectin secretion regulation of establishment of endothelial barrier positive regulation of cell division signal transduction positive regulation of transcription by RNA polymerase II cytokine-mediated signaling pathway regulation of defense response to virus by host fever generation positive regulation of JNK cascade positive regulation of cell population proliferation regulation of signaling receptor activity positive regulation of epithelial to mesenchymal transition positive regulation of cell migration interleukin-6 production astrocyte activation regulation of neurogenesis negative regulation of neurogenesis negative regulation of synaptic transmission positive regulation of glial cell proliferation regulation of ERK1 and ERK2 cascade interleukin-1-mediated signaling pathway cellular response to lipopolysaccharide positive regulation of neuroinflammatory response positive regulation of p38MAPK cascade positive regulation of NIK/NF-kappaB signaling positive regulation of T-helper 1 cell cytokine production positive regulation of prostaglandin biosynthetic process positive regulation of complement activation positive regulation of inflammatory response response to interleukin-1 positive regulation of RNA biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3553 16176 Ensembl ENSG00000125538 ENSMUSG00000027398 UniProt P01584 P10749 RefSeq (mRNA) NM_000576 NM_008361 RefSeq (protein) NP_000567 NP_032387 Location (UCSC) Chr 2: 112.83 – 112.84 Mb Chr 2: 129.21 – 129.21 Mb PubMed search
Wikidata
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Interleukin 1 beta (IL1β) also known as '"leukocytic pyrogen"', "'leukocytic endogenous mediator'", "'mononuclear cell factor'", "'lymphocyte activating factor'" and other names, is a cytokine protein that in humans is encoded by the IL1B gene. There are two genes for Interleukin-1 (IL-1): IL-1 alpha and IL-1 beta (this gene). IL-1β precursor is cleaved by cytosolic caspase 1 (interleukin 1 beta convertase) to form mature IL-1β.

Function

The fever-producing property of human leukocytic pyrogen (Interleukin 1) was purified by Dinarello in 1977 (PNAS) with a specific activity of 10-20 nanograms/kg. In 1979, Dinarello reported that purified human leukocytic pyrogen was the same molecule that was described by Igal Gery in 1972. He named it lymphocyte-activating factor (LAF) because it was a lymphocyte mitogen. It was not until 1984 that interleukin 1 was discovered to consist of two distinct proteins, now called interleukin-1 alpha and interleukin-1 beta.

IL-1β is a member of the interleukin 1 family of cytokines. 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.

Properties

The molecular weight of the proteolytically processed IL1B is 17.5 kDa. IL1B has the following amino acid sequence:

• APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVAL GLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS

The physiological activity determined from the dose dependent proliferation of murine D10S cells is 2.5 x 10⁸ to 7.1 x 10⁸ units/mg.

Clinical significance

Increased production of IL-1B causes a number of different autoinflammatory syndromes, most notably the monogenic conditions referred to as CAPS, due to mutations in the inflammasome receptor NLRP3 which triggers processing of IL-1B.

Intestinal Dysbiosis has been observed to induce Osteomyelitis through a IL-1β dependent manner.

Therapies targeting interleukin 1 beta

Canakinumab is a human monoclonal antibody targeted at IL-1B, and approved in many countries for treatment of cryopyrin-associated periodic syndromes.

Orthographic note

Because many authors of scientific manuscripts make the minor error of using a homoglyph, sharp s (ß), instead of beta (β), mentions of "IL-1ß" [sic] often become "IL-1ss" [sic] upon automated transcoding (because ß transcodes to ss). This is why so many mentions of the latter appear in web search results.

See also

• Interleukin 1

Further reading

• Smirnova MG, Kiselev SL, Gnuchev NV, Birchall JP, Pearson JP (2003). "Role of the pro-inflammatory cytokines tumor necrosis factor-alpha, interleukin-1 beta, interleukin-6 and interleukin-8 in the pathogenesis of the otitis media with effusion". Eur. Cytokine Netw. 13 (2): 161–72. PMID 12101072.
• Griffin WS, Mrak RE (2002). "Interleukin-1 in the genesis and progression of and risk for development of neuronal degeneration in Alzheimer's disease". J. Leukoc. Biol. 72 (2): 233–8. PMID 12149413.
• Arend WP (2003). "The balance between IL-1 and IL-1Ra in disease". Cytokine Growth Factor Rev. 13 (4–5): 323–40. doi:10.1016/S1359-6101(02)00020-5. PMID 12220547.
• Chakravorty M, Ghosh A, Choudhury A, Santra A, Hembrum J, Roychoudhury S (2004). "Ethnic differences in allele distribution for the IL8 and IL1B genes in populations from eastern India". Hum. Biol. 76 (1): 153–9. doi:10.1353/hub.2004.0016. PMID 15222686.
• Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. PMID 15638726.
• Maruyama Y, Stenvinkel P, Lindholm B (2005). "Role of interleukin-1beta in the development of malnutrition in chronic renal failure patients". Blood Purif. 23 (4): 275–81. doi:10.1159/000086012. PMID 15925866.
• Roy D, Sarkar S, Felty Q (2006). "Levels of IL-1 beta control stimulatory/inhibitory growth of cancer cells". Front. Biosci. 11: 889–98. doi:10.2741/1845. PMID 16146780.
• Copeland KF (2005). "Modulation of HIV-1 transcription by cytokines and chemokines". Mini Rev Med Chem. 5 (12): 1093–101. doi:10.2174/138955705774933383. PMID 16375755.
• Prinz C, Schwendy S, Voland P (2006). "H pylori and gastric cancer: shifting the global burden". World J. Gastroenterol. 12 (34): 5458–64. PMID 17006981.
• Kamangar F, Cheng C, Abnet CC, Rabkin CS (2006). "Interleukin-1B polymorphisms and gastric cancer risk--a meta-analysis". Cancer Epidemiol. Biomarkers Prev. 15 (10): 1920–8. doi:10.1158/1055-9965.EPI-06-0267. PMID 17035400.

External links

• IL1B+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.