View source for Interleukin 1 beta

{{Short description|Mammalian protein found in Homo sapiens}}
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{{Infobox gene}}

'''Interleukin-1 beta''' ('''IL-1β''') 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]].<ref name="pmid6083565">{{cite journal | vauthors = Auron PE, Webb AC, Rosenwasser LJ, Mucci SF, Rich A, Wolff SM, Dinarello CA | title = Nucleotide sequence of human monocyte interleukin 1 precursor cDNA | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 81 | issue = 24 | pages = 7907–7911 | date = December 1984 | pmid = 6083565 | pmc = 392262 | doi = 10.1073/pnas.81.24.7907 | doi-access = free | bibcode = 1984PNAS...81.7907A }}</ref><ref name="pmid2989698">"Catabolin" is the name given by Jeremy Saklatvala for IL-1 alpha. {{cite journal | vauthors = March CJ, Mosley B, Larsen A, Cerretti DP, Braedt G, Price V, Gillis S, Henney CS, Kronheim SR, Grabstein K | display-authors = 6 | title = Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs | journal = Nature | volume = 315 | issue = 6021 | pages = 641–647 | year = 1985 | pmid = 2989698 | doi = 10.1038/315641a0 | s2cid = 4240002 | bibcode = 1985Natur.315..641M }}</ref><ref name="pmid3490654">{{cite journal | vauthors = Clark BD, Collins KL, Gandy MS, Webb AC, Auron PE | title = Genomic sequence for human prointerleukin 1 beta: possible evolution from a reverse transcribed prointerleukin 1 alpha gene | journal = Nucleic Acids Research | volume = 14 | issue = 20 | pages = 7897–7914 | date = October 1986 | pmid = 3490654 | pmc = 311823 | doi = 10.1093/nar/14.20.7897 }}</ref><ref name="pmid2954882">{{cite journal | vauthors = Bensi G, Raugei G, Palla E, Carinci V, Tornese Buonamassa D, Melli M | title = Human interleukin-1 beta gene | journal = Gene | volume = 52 | issue = 1 | pages = 95–101 | year = 1987 | pmid = 2954882 | doi = 10.1016/0378-1119(87)90398-2 }}</ref> 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 (fever)|pyrogen]] (interleukin 1) was purified by Dinarello in 1977 with a specific activity of 10–20 nanograms/kg.<ref name="pmid22079">{{cite journal | vauthors = Dinarello CA, Renfer L, Wolff SM | title = Human leukocytic pyrogen: purification and development of a radioimmunoassay | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 74 | issue = 10 | pages = 4624–4627 | date = October 1977 | pmid = 22079 | pmc = 431999 | doi = 10.1073/pnas.74.10.4624 | doi-access = free | bibcode = 1977PNAS...74.4624D }}</ref>  In 1979, Dinarello reported that purified human leukocytic pyrogen was the same molecule that was described by Igal Gery in 1972.<ref>{{cite journal | vauthors = Gery I, Gershon RK, Waksman BH | title = Potentiation of the T-lymphocyte response to mitogens. I. The responding cell | journal = The Journal of Experimental Medicine | volume = 136 | issue = 1 | pages = 128–142 | date = July 1972 | pmid = 5033417 | pmc = 2139184 | doi = 10.1084/jem.136.1.128 }}</ref><ref>{{cite journal | vauthors = Gery I, Waksman BH | title = Potentiation of the T-lymphocyte response to mitogens. II. The cellular source of potentiating mediator(s) | journal = The Journal of Experimental Medicine | volume = 136 | issue = 1 | pages = 143–155 | date = July 1972 | pmid = 5033418 | pmc = 2139186 | doi = 10.1084/jem.136.1.143 }}</ref><ref name="pmid4549027">{{cite journal | vauthors = Gery I, Handschumacher RE | title = Potentiation of the T lymphocyte response to mitogens. III. Properties of the mediator(s) from adherent cells | journal = Cellular Immunology | volume = 11 | issue = 1–3 | pages = 162–169 | date = March 1974 | pmid = 4549027 | doi = 10.1016/0008-8749(74)90016-1 }}</ref> 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.<ref name="pmid2989698"/>

IL-1β is a member of the [[interleukin 1 family]] of [[cytokine]]s. This cytokine is produced by activated [[macrophage]]s, [[monocyte]]s, and a subset of [[dendritic cell]]s known as slanDC,<ref name="Yaseen_2023" /> 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 [[PTGS2|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]].<ref>{{cite web | title = Entrez Gene: IL1B interleukin 1, beta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3553}}</ref>

IL-1β, in combination with [[Interleukin 23|IL-23]], induced expression of [[Interleukin 17|IL-17]], [[Interleukin 21|IL-21]] and [[Interleukin 22|IL-22]] by [[γδ T cell]]s. This induction of expression is in the absence of additional signals. That suggests IL-1β is involved in modulation of autoimmune inflammation <ref>{{cite journal | vauthors = Sutton CE, Lalor SJ, Sweeney CM, Brereton CF, Lavelle EC, Mills KH | title = Interleukin-1 and IL-23 induce innate IL-17 production from gammadelta T cells, amplifying Th17 responses and autoimmunity | journal = Immunity | volume = 31 | issue = 2 | pages = 331–341 | date = August 2009 | pmid = 19682929 | doi = 10.1016/j.immuni.2009.08.001 | hdl-access = free | doi-access = free | hdl = 2262/67623 }}</ref>

Different [[inflammasome]] complex &mdash; cytosolic molecular complex &mdash; have been described. Inflammasomes recognize danger signals and activate proinflammatory process and production of IL-1β and IL-18. [[NLRP3]] (contains three domain:  [[pyrin domain]], a nucleotide-binding domain and a [[leucine-rich repeat]]) type of inflammasome is activated by various stimuli and there are documented several diseases connected to NLRP3 activation like [[Diabetes mellitus, type 2|type 2 diabetes mellitus]], [[Alzheimer's disease]], [[obesity]] and [[atherosclerosis]].<ref>{{cite journal | vauthors = Abderrazak A, Syrovets T, Couchie D, El Hadri K, Friguet B, Simmet T, Rouis M | title = NLRP3 inflammasome: from a danger signal sensor to a regulatory node of oxidative stress and inflammatory diseases | journal = Redox Biology | volume = 4 | pages = 296–307 | date = April 2015 | pmid = 25625584 | pmc = 4315937 | doi = 10.1016/j.redox.2015.01.008 }}</ref>

== Properties ==

Before cleavage by caspase 1, pro-IL-1β has a molecular weight of 37 [[Dalton (unit)|kDa]].<ref name="Yaseen_2023" /> The molecular weight of the proteolytically processed IL-1β is 17.5 kDa. IL-1β has the following amino acid sequence:
* <span style="font-family: 'Courier New';">APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVAL GLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS</span>
The physiological activity determined from the dose dependent proliferation of murine D10S cells is 2.5 x 10<sup>8</sup> to 7.1 x 10<sup>8</sup> units/mg.

IL-1β is present in other species of animals, however non-mammalian sequences of IL-1β lack a conserved cascase-1 cleavage site.<ref>{{cite journal | vauthors = Pelegrín P, García-Castillo J, Mulero V, Meseguer J | title = Interleukin-1beta isolated from a marine fish reveals up-regulated expression in macrophages following activation with lipopolysaccharide and lymphokines | journal = Cytokine | volume = 16 | issue = 2 | pages = 67–72 | date = October 2001 | pmid = 11683587 | doi = 10.1006/cyto.2001.0949 }}</ref><ref>{{cite journal | vauthors = Scapigliati G, Buonocore F, Bird S, Zou J, Pelegrin P, Falasca C, Prugnoli D, Secombes CJ | display-authors = 6 | title = Phylogeny of cytokines: molecular cloning and expression analysis of sea bass Dicentrarchus labrax interleukin-1beta | journal = Fish & Shellfish Immunology | volume = 11 | issue = 8 | pages = 711–726 | date = November 2001 | pmid = 11759041 | doi = 10.1006/fsim.2001.0347 }}</ref><ref>{{cite journal | vauthors = Pelegrín P, Chaves-Pozo E, Mulero V, Meseguer J | title = Production and mechanism of secretion of interleukin-1beta from the marine fish gilthead seabream | journal = Developmental and Comparative Immunology | volume = 28 | issue = 3 | pages = 229–237 | date = March 2004 | pmid = 14642889 | doi = 10.1016/j.dci.2003.08.002 }}</ref>

== Clinical significance ==

Increased production of IL-1β causes a number of different [[autoinflammatory syndromes]], most notably the monogenic conditions referred to as [[Cryopyrin-associated periodic syndrome|Cryopyrin-Associated Periodic Syndromes (CAPS)]], due to mutations in the inflammasome receptor NLRP3 which triggers processing of IL-1β.<ref name="pmid19302049">{{cite journal | vauthors = Masters SL, Simon A, Aksentijevich I, Kastner DL | title = Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*) | journal = Annual Review of Immunology | volume = 27 | pages = 621–668 | year = 2009 | pmid = 19302049 | pmc = 2996236 | doi = 10.1146/annurev.immunol.25.022106.141627 }}</ref>

Intestinal [[dysbiosis]] has been observed to induce [[osteomyelitis]] through a IL-1β dependent manner.<ref>{{cite journal | vauthors = Lukens JR, Gurung P, Vogel P, Johnson GR, Carter RA, McGoldrick DJ, Bandi SR, Calabrese CR, Vande Walle L, Lamkanfi M, Kanneganti TD | display-authors = 6 | title = Dietary modulation of the microbiome affects autoinflammatory disease | journal = Nature | volume = 516 | issue = 7530 | pages = 246–249 | date = December 2014 | pmid = 25274309 | pmc = 4268032 | doi = 10.1038/nature13788 | bibcode = 2014Natur.516..246L }}</ref>

The presence of IL-1β has been also found in patients with [[multiple sclerosis]] (a chronic autoimmune disease of the central nervous system). However, it is not known exactly which cells produce IL-1β. Treatment of multiple sclerosis with [[glatiramer acetate]] or [[natalizumab]] has also been shown to reduce the presence of IL-1β or its receptor.<ref>{{cite journal | vauthors = Lin CC, Edelson BT | title = New Insights into the Role of IL-1β in Experimental Autoimmune Encephalomyelitis and Multiple Sclerosis | journal = Journal of Immunology | volume = 198 | issue = 12 | pages = 4553–4560 | date = June 2017 | pmid = 28583987 | pmc = 5509030 | doi = 10.4049/jimmunol.1700263 }}</ref>

=== Role in carcinogenesis ===
Several types of inflammasomes are suggested to play role in tumorgenesis due to their immunomodulatory properties, modulation of gut microbiota, differentiation and apoptosis. Over-expression of IL-1β caused by inflammasome may result in carcinogenesis. Some data suggest that [[NLRP3 inflammasome]] polymorphisms is connected to malignancies such as colon cancer and melanoma. It was reported that IL-1β secretion was elevated in the lung adenocarcinoma cell line A549. It has also been shown in another study that IL-1β, together with IL-8, plays an important role in chemoresistance of malignant pleural mesothelioma by inducing expression of transmembrane transporters.<ref name="pmid31107974">{{cite journal | vauthors = Milosevic V, Kopecka J, Salaroglio IC, Libener R, Napoli F, Izzo S, Orecchia S, Ananthanarayanan P, Bironzo P, Grosso F, Tabbò F, Comunanza V, Alexa-Stratulat T, Bussolino F, Righi L, Novello S, Scagliotti GV, Riganti C | display-authors = 6 | title = Wnt/IL-1β/IL-8 autocrine circuitries control chemoresistance in mesothelioma initiating cells by inducing ABCB5 | journal = International Journal of Cancer | volume = 146 | issue = 1 | pages = 192–207 | date = January 2020 | pmid = 31107974 | doi = 10.1002/ijc.32419 | hdl-access = free | s2cid = 160014053 | hdl = 2318/1711962 }}</ref> Another study showed that inhibition of inflammasome and IL-1β expression decreased development of cancer cells in melanoma.<ref>{{cite journal | vauthors = Moossavi M, Parsamanesh N, Bahrami A, Atkin SL, Sahebkar A | title = Role of the NLRP3 inflammasome in cancer | journal = Molecular Cancer | volume = 17 | issue = 1 | pages = 158 | date = November 2018 | pmid = 30447690 | pmc = 6240225 | doi = 10.1186/s12943-018-0900-3 | doi-access = free }}</ref>

Furthermore, it has been found that in breast cancer cells, IL-1β activates p38 and p42/22 MAPK pathways which ultimately lead to the secretion of the [[RANK]]/[[RANKL]] inhibitor [[osteoprotegerin]]. Higher osteoprotegerin and IL-1β levels are a characteristic of breast cancer cells with a higher metastatic potential.<ref>{{cite journal | vauthors = Tulotta C, Ottewell P | title = The role of IL-1B in breast cancer bone metastasis | journal = Endocrine-Related Cancer | volume = 25 | issue = 7 | pages = R421–R434 | date = July 2018 | pmid = 29760166 | pmc = 5987176 | doi = 10.1530/ERC-17-0309 }}</ref>

=== In HIV-1 infections ===
The [[HIV|human immunodeficiency virus]] (HIV) infects cells of the immune system, such as macrophages, dendritic cells, and CD4<sup>+</sup> T helper cells ([[T helper cell|T<sub>H</sub>]]). The latter can be infected by the virus in various ways with different fates depending on the state of activation of the T helper cell.<ref name="Yaseen_2023">{{cite journal | vauthors = Yaseen MM, Abuharfeil NM, Darmani H | title = The role of IL-1β during human immunodeficiency virus type 1 infection | journal = Reviews in Medical Virology | volume = 33 | issue = 1 | pages = e2400 | date = January 2023 | pmid = 36209388 | doi = 10.1002/rmv.2400 | s2cid = 252762935 }}</ref>

Firstly, T<sub>H</sub> cells can die of viral lysis due to an active infection that produces enough virions to [[Lytic cycle|kill the cell]]. Secondly, CD4<sup>+</sup> T cells can be infected by the virus but instead of producing more viral particles, the cell enters a latent phase. In this period, the T helper cells looks identical from the outside but any stressor could lead to the renewed production of HIV and its propagation to new immune cells. Lastly, the T<sub>H</sub> cell can become abortively infected, where the virus gets detected inside the cell and a programmed cell-death, known as [[pyroptosis]], kills the infected cell. Pyroptosis is mediated via caspase-1 and is characterized by cell lysis and the secretion of IL-1β causing inflammation and attraction of more immune cells. This can create a cycle of CD4<sup>+</sup> T cells getting abortively infect with HIV, dying of pyroptosis, new T helper cells arriving to the site of inflammation where they get infected again. The results is the depletion of T helper cells. Even though, levels of IL-1β in blood are not majorly different between HIV positive and negative individuals, studies have shown elevated levels of IL-1β of [[Lymphatic system|lymphatic tissue]] in HIV-infected individuals.<ref name="Yaseen_2023" />

In fact, the gut-associated lymphoid tissue ([[Gut-associated lymphoid tissue|GALT]]) has a high density of immune cells as the gut is an interface between symbiotic gut microbes that should remain with the host and pathogenic bacteria that should not gain access into the circulatory system. If HIV-infection leads to the secretion of IL-1βin monocytes and macrophages, it causes inflammation of this area. The mucosal epithelial layer responds to this by producing less or altering the tight junction proteins which makes it easier for pathogenic microbes to move into the [[lamina propria]]. Here, the pathogens can further activate local immune cells and amplify the inflammatory response.<ref name="Yaseen_2023" />

=== Retinal degeneration ===
It has been shown that IL-1 family plays important role in inflammation in many degenerative diseases, such as [[Macular degeneration|age-related macular degeneration]], [[diabetic retinopathy]] and [[retinitis pigmentosa]]. Significantly increased protein level of IL-1β has been found in the vitreous of diabetic retinopathy patient. The role of IL-1β has been investigated for potential therapeutic target for treatment of diabetic retinopathy. However, systemic using of [[canakinumab]] did not have a significant effect. The role of IL-1β in age-related macular degeneration has not been proven in patient, but in many animal models and in vitro studies it has been demonstrated the role of IL-1β in retinal pigmented epithelial cells and photoreceptor cells damage. NLRP3 inflammasome activate [[Caspase 1|caspase-1]] which catalyze cleavage of inactive cytosolic precursor pro-IL-1β to its mature form IL-1β. Retinal pigmented epithelial cells forms [[Blood–retinal barrier|blood retinal barrier]] in human retina which is important for retinal metabolic activity, integrity and inhibition of immune cells infiltration. It has been shown that human retinal pigmented epithelial cells can secrete IL-1 β in exposure to [[oxidative stress]]. The inflammatory reaction leads to damage of retinal cells and infiltration of cells of the immune system. The inflammatory process including NLRP3 upregulation is one of the causes of age-related macular degeneration and other retinal diseases that lead to vision loss.<ref>{{cite journal | vauthors = Bian ZM, Field MG, Elner SG, Kahlenberg JM, Elner VM | title = Distinct CD40L receptors mediate inflammasome activation and secretion of IL-1β and MCP-1 in cultured human retinal pigment epithelial cells | journal = Experimental Eye Research | volume = 170 | pages = 29–39 | date = May 2018 | pmid = 29454857 | pmc = 5924621 | doi = 10.1016/j.exer.2018.02.014 }}</ref><ref>{{cite journal | vauthors = Tseng WA, Thein T, Kinnunen K, Lashkari K, Gregory MS, D'Amore PA, Ksander BR | title = NLRP3 inflammasome activation in retinal pigment epithelial cells by lysosomal destabilization: implications for age-related macular degeneration | journal = Investigative Ophthalmology & Visual Science | volume = 54 | issue = 1 | pages = 110–120 | date = January 2013 | pmid = 23221073 | pmc = 3544415 | doi = 10.1167/iovs.12-10655 }}</ref><ref>{{cite journal | vauthors = Wooff Y, Man SM, Aggio-Bruce R, Natoli R, Fernando N | title = IL-1 Family Members Mediate Cell Death, Inflammation and Angiogenesis in Retinal Degenerative Diseases | journal = Frontiers in Immunology | volume = 10 | pages = 1618 | date = 2019-07-16 | pmid = 31379825 | pmc = 6646526 | doi = 10.3389/fimmu.2019.01618 | doi-access = free }}</ref> Additionally, it has been shown that caspase-1 is upregulated in the retina of diabetic patients, causing a higher production of IL-1β and subsequent death of retinal neurons.<ref name="Mendiola_2018"/>

=== Neuroinflammation ===
Studies in mice on [[experimental autoimmune encephalomyelitis]] (EAE), a model for [[multiple sclerosis]] (MS) research, have found that blocking IL-1β could make the animals resistant to EAE. IL-1β led to the production of an antigen-specific pro-inflammatory subset of T helper cells ([[T helper 17 cell|T<sub>H17</sub>]]). In combination with other cytokines, interleukin-1β can upregulate the production of the cytokine [[Granulocyte-macrophage colony-stimulating factor|GM-CSF]] which is correlated to neuroinflammation. Detailed mechanisms on this front are yet to be elucidated.<ref name="Mendiola_2018">{{cite journal | vauthors = Mendiola AS, Cardona AE | title = The IL-1β phenomena in neuroinflammatory diseases | journal = Journal of Neural Transmission | volume = 125 | issue = 5 | pages = 781–795 | date = May 2018 | pmid = 28534174 | pmc = 5699978 | doi = 10.1007/s00702-017-1732-9 }}</ref>

IL-1β has also been observed in elevated levels of the [[cerebrospinal fluid]] and brain tissues of [[Alzheimer's disease|Alzheimer]] patients. The [[Amyloid plaques|amyloid-β plaques]], that are characteristic of Alzheimer disease, are [[damage-associated molecular pattern]]s (DAMPs) that are recognized by [[pattern recognition receptor]]s (PRRs) and lead to the activation of [[microglia]]. Consequently, microglia release interleukin-1β among other cytokines. Nevertheless, the significance of IL-1β in Alzheimer disease and the onset of neuroinflammation still remains largely unknown.<ref name="Mendiola_2018" />

Lastly, ''in vitro'' studies have shown that IL-1β causes an increase in mitochondrial glutaminase activity. In response, there is excessive glutamate secretion which has a neurotoxic effect.<ref name="Mendiola_2018" />

== As a therapeutic target ==
[[Anakinra]] is a recombinant and slightly modified version of the human interleukin 1 receptor antagonist protein.  Anakinra blocks the biologic activity of IL-1 alpha and beta by competitively inhibiting IL-1 binding to the interleukin type 1 receptor (IL-1RI), which is expressed in a wide variety of tissues and organs. Anakinra is marketed as Kineret and is approved in the US for treatment of [[RA, NOMID, DIRA]].

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

[[Rilonacept]] is an IL-1 trap developed by [[Regeneron]] targeting IL-1B, and approved in the US as Arcalyst.<ref>{{cite web | title = ARCALYSTTM (rilonacept) Product Label | publisher = U.S. Food and Drug Administration | work = Regeneron Pharmaceuticals, Inc. |url=https://www.accessdata.fda.gov/drugsatfda_docs/label/2008/125249lbl.pdf |access-date=5 October 2020}}</ref>

==Orthographic note==
Because many authors of scientific manuscripts make the minor error of using a [[homoglyph]], [[ß|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.

{{Clear}}

== References ==
{{reflist|30em}}

== Further reading ==
{{refbegin|30em}}
* {{cite journal | vauthors = Smirnova MG, Kiselev SL, Gnuchev NV, Birchall JP, Pearson JP | title = 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 | journal = European Cytokine Network | volume = 13 | issue = 2 | pages = 161–172 | year = 2003 | pmid = 12101072 }}
* {{cite journal | vauthors = Griffin WS, Mrak RE | title = Interleukin-1 in the genesis and progression of and risk for development of neuronal degeneration in Alzheimer's disease | journal = Journal of Leukocyte Biology | volume = 72 | issue = 2 | pages = 233–238 | date = August 2002 | pmid = 12149413 | pmc = 3835694 | doi = 10.1189/jlb.72.2.233 }}
* {{cite journal | vauthors = Arend WP | title = The balance between IL-1 and IL-1Ra in disease | journal = Cytokine & Growth Factor Reviews | volume = 13 | issue = 4–5 | pages = 323–340 | year = 2003 | pmid = 12220547 | doi = 10.1016/S1359-6101(02)00020-5 }}
* {{cite journal | vauthors = Chakravorty M, Ghosh A, Choudhury A, Santra A, Hembrum J, Roychoudhury S | title = Ethnic differences in allele distribution for the IL8 and IL1B genes in populations from eastern India | journal = Human Biology | volume = 76 | issue = 1 | pages = 153–159 | date = February 2004 | pmid = 15222686 | doi = 10.1353/hub.2004.0016 | s2cid = 2816300 }}
* {{cite journal | vauthors = Joseph AM, Kumar M, Mitra D | title = Nef: "necessary and enforcing factor" in HIV infection | journal = Current HIV Research | volume = 3 | issue = 1 | pages = 87–94 | date = January 2005 | pmid = 15638726 | doi = 10.2174/1570162052773013 }}
* {{cite journal | vauthors = Maruyama Y, Stenvinkel P, Lindholm B | title = Role of interleukin-1beta in the development of malnutrition in chronic renal failure patients | journal = Blood Purification | volume = 23 | issue = 4 | pages = 275–281 | year = 2005 | pmid = 15925866 | doi = 10.1159/000086012 | s2cid = 72570361 }}
* {{cite journal | vauthors = Milosevic V, Kopecka J, Salaroglio IC, Libener R, Napoli F, Izzo S, Orecchia S, Ananthanarayanan P, Bironzo P, Grosso F, Tabbò F, Comunanza V, Alexa-Stratulat T, Bussolino F, Righi L, Novello S, Scagliotti GV, Riganti C | display-authors = 6 | title = Wnt/IL-1β/IL-8 autocrine circuitries control chemoresistance in mesothelioma initiating cells by inducing ABCB5 | journal = International Journal of Cancer | volume = 146 | issue = 1 | pages = 192–207 | date = January 2020 | pmid = 31107974 | doi = 10.1002/ijc.32419 | hdl-access = free | s2cid = 160014053 | hdl = 2318/1711962 }}
* {{cite journal | vauthors = Roy D, Sarkar S, Felty Q | title = Levels of IL-1 beta control stimulatory/inhibitory growth of cancer cells | journal = Frontiers in Bioscience | volume = 11 | pages = 889–898 | date = January 2006 | pmid = 16146780 | doi = 10.2741/1845 | s2cid = 23009646 | doi-access = free }}
* {{cite journal | vauthors = Copeland KF | title = Modulation of HIV-1 transcription by cytokines and chemokines | journal = Mini Reviews in Medicinal Chemistry | volume = 5 | issue = 12 | pages = 1093–1101 | date = December 2005 | pmid = 16375755 | doi = 10.2174/138955705774933383 }}
* {{cite journal | vauthors = Prinz C, Schwendy S, Voland P | title = H pylori and gastric cancer: shifting the global burden | journal = World Journal of Gastroenterology | volume = 12 | issue = 34 | pages = 5458–5464 | date = September 2006 | pmid = 17006981 | pmc = 4088226 | doi = 10.3748/wjg.v12.i34.5458 | doi-access = free }}
* {{cite journal | vauthors = Kamangar F, Cheng C, Abnet CC, Rabkin CS | title = Interleukin-1B polymorphisms and gastric cancer risk--a meta-analysis | journal = Cancer Epidemiology, Biomarkers & Prevention | volume = 15 | issue = 10 | pages = 1920–1928 | date = October 2006 | pmid = 17035400 | doi = 10.1158/1055-9965.EPI-06-0267 | s2cid = 8542733 | doi-access =  }}
{{refend}}

== External links ==
* {{MeshName|IL1B+protein,+human}}

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{{Interleukins}}
{{Interleukin receptor modulators}}

[[Category:Interleukins]]