The interleukin-1 family: back to the future
Open accessAbstract
Interleukin-1 (IL-1) is a central mediator of innate immunity and inflammation. The IL-1 family includes seven ligands with agonist activity (IL-1α and IL-1β, IL-18, IL-33, IL-36α, IL-36β, IL-36γ), three receptor antagonists (IL-1Ra, IL-36Ra, IL-38), and an anti-inflammatory cytokine (IL-37). Members of the IL-1 Receptor (IL-1R) family include six receptor chains forming four signaling receptor complexes, two decoy receptors (IL-1R2, IL-18BP), and two negative regulators (TIR8 or SIGIRR, IL-1RAcPb). A tight regulation via receptor antagonists, decoy receptors, and signaling inhibitors ensures a balance between amplification of innate immunity and uncontrolled inflammation. All cells of the innate immune system express and/or are affected by IL-1 family members. Moreover, IL-1 family members play a key role in the differentiation and function of polarized innate and adaptive lymphoid cells. Here we will review the key properties of IL-1 family members, with emphasis on pathways of negative regulation and orchestration of innate and adaptive immunity.
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Cites
Mantovani, A., Allavena, P., Sica, A., & Balkwill, F. (2008) · Nature · doi:10.1038/nature07205 · Cited by 11,399 · see citing works
Succinate is an inflammatory signal that induces IL-1β through HIF-1α
Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · cited 1× · see citing works
“Accumulation of succinate in classically Immunity 39, December 12, 2013 ª2013 Elsevier Inc. 1005 activatedM1macrophages (Tannahill et al., 2013) stabilizes hypoxia-inducible factor a (HIF-1a), which in turn induces IL-1b.”
Veldhoen, M., Hocking, R. J., Atkins, C. J., Locksley, R. M., & Stockinger, B. (2006) · Immunity · doi:10.1016/j.immuni.2006.01.001 · Cited by 3,605 · cited 1× · see citing works
“Accordingly, IL-1 is required for development of Th17 cell-sustained autoimmunity (e.g., Chung et al., 2009; Sutton et al., 2006; Veldhoen et al., 2006).”
Immunological and inflammatory functions of the interleukin-1 family
Dinarello, C. A. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132612 · Cited by 3,466 · cited 9× · see citing works
“IL-1 affects virtually all cells and organs and is a major pathogenic mediator of autoinflammatory, autoimmune, infectious, and degenerative diseases (Dinarello, 2009, 2010; Dinarello et al., 2012; Gabay et al., 2010; Sims and Smith, 2010) (Table 2).”
InfluentialSelf-citationNeutrophils in the activation and regulation of innate and adaptive immunity
Mantovani, A., Cassatella, M. A., Costantini, C., & Jaillon, S. (2011) · Nature reviews. Immunology · doi:10.1038/nri3024 · Cited by 3,044 · cited 1× · see citing works
“IL-1 markedly prolongs the lifespan and stimulates the effector function of neutrophils and macrophages (Mantovani et al., 2011).”
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530 · see citing works
Innate lymphoid cells — a proposal for uniform nomenclature
Spits, H., Artis, D., Colonna, M., Diefenbach, A., Disanto, J. D., Eberl, G., Koyasu, S., Locksley, R., McKenzie, A., Mebius, R., et al. (2013) · Nature reviews. Immunology · doi:10.1038/nri3365 · Cited by 2,380 · cited 4× · see citing works
“The discovery of innate lymphoid cells and the dissection of pathways of T cell differentiation have revealed essential functions for IL-1, IL-18, and IL-33 and have opened vistas on their functions (O’Shea and Paul, 2010; Spits et al., 2013).”
InfluentialInterleukin-1 in the pathogenesis and treatment of inflammatory diseases
Dinarello, C. A. (2011) · Blood · doi:10.1182/blood-2010-07-273417 · Cited by 2,248 · cited 4× · see citing works
“Extracellular cleavage of the inactive IL-1b precursor by neutrophil enzymes such a proteinase-3 and elastase generate active IL-1b because the cleavage site is close to that of caspase-1 (Dinarello, 2011).”
InfluentialNuocytes represent a new innate effector leukocyte that mediates type-2 immunity
Neill, D. R., Wong, S. H., Bellosi, A., Flynn, R. J., Daly, M. G., Langford, T. K. A., Bucks, C. M., Kane, C. M., Fallon, P. G., Pannell, R., et al. (2010) · Nature · doi:10.1038/nature08900 · Cited by 2,079 · cited 2× · see citing works
“IL-33 plays a protective role against parasites ranging from nematode expulsion to control of Toxoplasma gondii encephalitis (Moro et al., 2010; Neill et al., 2010).”
A Large-Scale, Consortium-Based Genomewide Association Study of Asthma
Moffatt, M. F., Gut, I. G., Démenais, F., Strachan, D. P., Bouzigon, E., Heath, S. C., von Mutius, E., Farrall, M., Lathrop, M. G., & Cookson, W. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa0906312 · Cited by 2,003 · cited 1× · see citing works
“In humans, genome-wide association studies (GWAS) have identified single nucleotide polymorphisms (SNPs) in the genes encoding ST2 and IL-33 associated with asthma (Moffatt et al., 2010).”
Innate production of TH2 cytokines by adipose tissue-associated c-Kit+Sca-1+ lymphoid cells
Moro, K., Yamada, T., Tanabe, M., Takeuchi, T., Ikawa, T., Kawamoto, H., Furusawa, J.-I., Ohtani, M., Fujii, H., & Koyasu, S. (2009) · Nature · doi:10.1038/nature08636 · Cited by 1,994 · cited 2× · see citing works
“IL-33 plays a protective role against parasites ranging from nematode expulsion to control of Toxoplasma gondii encephalitis (Moro et al., 2010; Neill et al., 2010).”
Ghiringhelli, F., Apetoh, L., Tesniere, A., Aymeric, L., Ma, Y., Ortiz, C., Vermaelen, K., Panaretakis, T., Mignot, G., Ullrich, E., et al. (2009) · Nature Medicine · doi:10.1038/nm.2028 · Cited by 1,898 · cited 1× · see citing works
“IL-1R1-deficient mice show defective capacity to generate effective CD8+ T cell responses to viruses (e.g., Joeckel et al., 2012) and tumors (Ghiringhelli et al., 2009).”
Phenotypic and functional features of human Th17 cells
Annunziato, F., Cosmi, L., Santarlasci, V., Maggi, L., Liotta, F., Mazzinghi, B., Parente, E., Filì, L., Ferri, S., Frosali, F., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070663 · Cited by 1,861 · cited 1× · see citing works
“Analysis of the differentiation of human naive T cells to Th17 cells originally revealed a key role of IL-1 (Acosta-Rodriguez et al., 2007; Annunziato et al., 2007).”
Acosta-Rodriguez, E. V., Napolitani, G., Lanzavecchia, A., & Sallusto, F. (2007) · Nature Immunology · doi:10.1038/ni1496 · Cited by 1,857 · see citing works
Treating inflammation by blocking interleukin-1 in a broad spectrum of diseases
Dinarello, C., Simon, A., & van der Meer, J. V. D. (2012) · Nature reviews. Drug discovery · doi:10.1038/nrd3800 · Cited by 1,813 · cited 6× · see citing works
“IL-1 affects virtually all cells and organs and is a major pathogenic mediator of autoinflammatory, autoimmune, infectious, and degenerative diseases (Dinarello, 2009, 2010; Dinarello et al., 2012; Gabay et al., 2010; Sims and Smith, 2010) (Table 2).”
InfluentialHoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2001) · Nature Genetics · doi:10.1038/ng756 · Cited by 1,679 · see citing works
The IL-1 family: regulators of immunity
Sims, J. E., & Smith, D. E. (2010) · Nature reviews. Immunology · doi:10.1038/nri2691 · Cited by 1,416 · cited 17× · see citing works
“IL-1 affects virtually all cells and organs and is a major pathogenic mediator of autoinflammatory, autoimmune, infectious, and degenerative diseases (Dinarello, 2009, 2010; Dinarello et al., 2012; Gabay et al., 2010; Sims and Smith, 2010) (Table 2).”
InfluentialMechanisms Underlying Lineage Commitment and Plasticity of Helper CD4 + T Cells
O’Shea, J. J., & Paul, W. E. (2010) · Science · doi:10.1126/science.1178334 · Cited by 1,338 · see citing works
Critical Regulation of Early Th17 Cell Differentiation by Interleukin-1 Signaling
Chung, Y., Chang, S. H., Martínez, G., Yang, X. O., Nurieva, R., Kang, H. S., Ma, L., Watowich, S. S., Jetten, A. M., Tian, Q., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.007 · Cited by 1,198 · cited 1× · see citing works
“Accordingly, IL-1 is required for development of Th17 cell-sustained autoimmunity (e.g., Chung et al., 2009; Sutton et al., 2006; Veldhoen et al., 2006).”
IRAK (Pelle) Family Member IRAK-2 and MyD88 as Proximal Mediators of IL-1 Signaling
Muzio, M., Ni, J., Feng, P., & Dixit, V. M. (1997) · Science · doi:10.1126/science.278.5343.1612 · Cited by 1,170 · cited 7× · see citing works
“Early on, it was realized that IL-1 was responsible for resistance against microbes (van der Meer et al., 1988), a discovery upstream of the identification of the TIR domain (originally standing for Toll-IL-1 resistance; shared by the IL-1 receptor [IL-1R] and Toll-like receptors [TLR]), and of the inflammasome.”
InfluentialAnti-inflammatory Agents: Present and Future
Dinarello, C. A. (2010) · Cell · doi:10.1016/j.cell.2010.02.043 · Cited by 1,095 · cited 18× · see citing works
“IL-1 affects virtually all cells and organs and is a major pathogenic mediator of autoinflammatory, autoimmune, infectious, and degenerative diseases (Dinarello, 2009, 2010; Dinarello et al., 2012; Gabay et al., 2010; Sims and Smith, 2010) (Table 2).”
InfluentialSelf-citationIL-33 and ST2 comprise a critical biomechanically induced and cardioprotective signaling system
Sanada, S., Hakuno, D., Higgins, L., Schreiter, E. R., McKenzie, A. N. J., & Lee, R. T. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30634 · Cited by 1,053 · cited 2× · see citing works
“In cardiovascular diseasemodels, IL-33 plays a protective role by reducing atherosclerotic plaque formation (Miller et al., 2008) or by reducing cardiac hypertrophy secondary to pressure overload (Sanada et al., 2007).”
Rodríguez-Prados, J.-C., Través, P. G., Cuenca, J., Rico, D., Aragonés, J., Martín-Sanz, P., Cascante, M., & Boscá, L. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901698 · Cited by 1,022 · cited 1× · see citing works
“IL-1 is likely to orient macrophages to aerobic glycolysis as lipopolysaccharide (LPS) does (Rodrı́guez-Prados et al., 2010) and in turn it is downstream of metabolic responses elicited by microbial sensing.”
Sutton, C. E., Brereton, C. F., Keogh, B., Mills, K. H. G., & Lavelle, E. C. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20060285 · Cited by 1,009 · cited 1× · see citing works
“Accordingly, IL-1 is required for development of Th17 cell-sustained autoimmunity (e.g., Chung et al., 2009; Sutton et al., 2006; Veldhoen et al., 2006).”
Disease-associated functions of IL-33: the new kid in the IL-1 family
Liew, F. Y., Pitman, N. I., & McInnes, I. B. (2010) · Nature reviews. Immunology · doi:10.1038/nri2692 · Cited by 1,004 · cited 2× · see citing works
“IL-33 is a driver of type 2 inflammatory conditions such as asthma, fibrosis, and response to parasites (Liew et al., 2010; McHedlidze et al., 2013; Sica et al., 2013).”
Interleukin-36–Receptor Antagonist Deficiency and Generalized Pustular Psoriasis
Marrakchi, S., Guigue, P., Renshaw, B. R., Puel, A., Pei, X.-Y., Fraitag, S., Zribi, J., Bal, É., Cluzeau, C. V. M., Chrabieh, M., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1013068 · Cited by 996 · cited 2× · see citing works
“IL36RN (IL-36Ra, human) Severe psoriasis (Marrakchi et al., 2011)”
An Autoinflammatory Disease with Deficiency of the Interleukin-1–Receptor Antagonist
Aksentijevich, I. A., Masters, S. L., Ferguson, P. J., Dancey, P., Frenkel, J., van Royen‐Kerkhof, A., Laxer, R. M., Tedgård, U., Cowen, E. W., Pham, T., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0807865 · Cited by 981 · cited 1× · see citing works
“Children bornwith a genetic deficiency of IL-1Ra or functional inactive IL-1Ra suffer from severe systemic and local inflammation, including pustular skin eruptions, vasculitis, osteolytic lesions, and sterile osteomyelitis (Aksentijevich et al., 2009; Reddy et al., 2009).”
Interleukin-1 Type II Receptor: A Decoy Target for IL-1 That Is Regulated by IL-4
Colotta, F., Re, F., Muzio, M., Bertini, R., Polentarutti, N., Sironi, M., Giri, J. G., Dower, S., Sims, J. E., & Mantovani, A. (1993) · Science · doi:10.1126/science.8332913 · Cited by 979 · cited 1× · see citing works
“It has found that a subset of Th1 clones, in particular those characterized by expression of CD161, expresses IL1R1 (Cosmi et al., 2008; Maggi et al., 2012).”
Pathogen-induced human TH17 cells produce IFN-γ or IL-10 and are regulated by IL-1β
Zielinski, C. E., Mele, F., Aschenbrenner, D., Jarrossay, D., Ronchi, F., Gattorno, M., Monticelli, S., Lanzavecchia, A., & Sallusto, F. (2012) · Nature · doi:10.1038/nature10957 · Cited by 919 · cited 1× · see citing works
“IL-1 also inhibits IL-10 production, which otherwise dampens IFN-g secretion (Zielinski et al., 2012).”
IL-1 pathways in inflammation and human diseases
Gabay, C., Lamacchia, C., & Palmer, G. (2010) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2010.4 · Cited by 897 · cited 8× · see citing works
“IL-1 affects virtually all cells and organs and is a major pathogenic mediator of autoinflammatory, autoimmune, infectious, and degenerative diseases (Dinarello, 2009, 2010; Dinarello et al., 2012; Gabay et al., 2010; Sims and Smith, 2010) (Table 2).”
InfluentialMolofsky, A. B., Nussbaum, J. C., Liang, H.-E., Dyken, S. J. V., Cheng, L. E., Mohapatra, A., Chawla, A., & Locksley, R. M. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20121964 · Cited by 879 · cited 2× · see citing works
“IL-33 is also involved in inducing ILC2-dependent in- 1008 Immunity 39, December 12, 2013 ª2013 Elsevier Inc. creases in eosinophils and M2 polarized macrophages of visceral adipose tissue, which are implicated in metabolic homeostasis (Molofsky et al., 2013).”
Chen, C.-J., Kono, H., Golenbock, D., Reed, G., Akira, S., & Rock, K. L. (2007) · Nature Medicine · doi:10.1038/nm1603 · Cited by 876 · cited 2× · see citing works
“and colitis, reduced atherosclerosis (Chen et al., 2007; Krelin et al., 2007)”
IL-37 is a fundamental inhibitor of innate immunity
Nold, M. F., Nold‐Petry, C. A., Zepp, J. A., Palmer, B. E., Bufler, P., & Dinarello, C. A. (2010) · Nature Immunology · doi:10.1038/ni.1944 · Cited by 850 · see citing works
Horai, R., Saijo, S., Tanioka, H., Nakae, S., Sudo, K., Okahara, A., Ikuse, T., Asano, M., & Iwakura, Y. (2000) · Journal of Experimental Medicine · doi:10.1084/jem.191.2.313 · Cited by 792 · cited 1× · see citing works
“Deficiency of IL-1Ra in mice results in spontaneous and lethal arteritis, destructive arthritis, and psoriatic-like skin lesions, as well as increased susceptibility to carcinogenesis (Horai et al., 2000; Nicklin et al., 2000).”
Interleukin-18 Binding Protein
Novick, D., Kim, S. H., Fantuzzi, G., Reznikov, L. L., Dinarello, C. A., & Rubinstein, M. (1999) · Immunity · doi:10.1016/s1074-7613(00)80013-8 · Cited by 781 · see citing works
Kurowska‐Stolarska, M., Stolarski, B., Kewin, P., Murphy, G., Corrigan, C. J., Ying, S., Pitman, N. I., Mirchandani, A. S., Rana, B. M. J., van Rooijen, N., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901575 · Cited by 716 · see citing works
Human interleukin 17–producing cells originate from a CD161+CD4+ T cell precursor
Cosmi, L., Palma, R. D., Santarlasci, V., Maggi, L., Capone, M., Frosali, F., Rodolico, G., Querci, V., Abbate, G., Angeli, R., et al. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20080397 · Cited by 708 · cited 1× · see citing works
“It has found that a subset of Th1 clones, in particular those characterized by expression of CD161, expresses IL1R1 (Cosmi et al., 2008; Maggi et al., 2012).”
The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1
Cayrol, C., & Girard, J.-P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812690106 · Cited by 707 · cited 1× · see citing works
“IL-33 is inactivated by caspase-1 (Cayrol and Girard, 2009), and the 30 KDa protein is one of its bioactive forms.”
IL-33 is a crucial amplifier of innate rather than acquired immunity
Oboki, K., Ohno, T., Kajiwara, N., Arae, K., Morita, H., Ishii, A., Nambu, A., Abe, T., Kiyonari, H., Matsumoto, K., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003059107 · Cited by 655 · cited 1× · see citing works
“IL-33 amplifies innate immunity and inflammatory responses, not necessarily dependent on the development of adaptive Th2 cell responses (Oboki et al., 2010).”
IL-33 reduces the development of atherosclerosis
Miller, A. M., Xu, D., Asquith, D. L., Denby, L., Li, Y., Sattar, N. A., Baker, A. H., McInnes, I. B., & Liew, F. Y. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071868 · Cited by 642 · see citing works
SIGIRR, a negative regulator of Toll-like receptor–interleukin 1 receptor signaling
Wald, D. N., Qin, J., Zhao, Z., Qian, Y., Naramura, M., Tian, L., Towne, J. E., Sims, J. E., Stark, G. R., & Li, X. (2003) · Nature Immunology · doi:10.1038/ni968 · Cited by 606 · cited 1× · see citing works
“…following stimulation of IL-1R family members or TLRs (IL-1RI, IL-18R, ST2, TLR1, TLR2, TLR3, TLR4, TLR7, and TLR9) (Bulek et al., 2009; Garlanda et al., 2004; Lech et al., 2008; Wald et al., 2003), by interfering with the recruitment of TIR-containing adaptor molecules (Wald et al., 2003).”
IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G
Lefrançais, E., Roga, S., Gautier, V., de Peredo, A. G., Monsarrat, B., Girard, J., & Cayrol, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115884109 · Cited by 598 · cited 1× · see citing works
“As for other IL-1 familymembers, calpain and the neutrophil serine proteases cathepsin G and elastase cleave human IL-33 and generate more potent mature forms (Lefrançais et al., 2012).”
The involvement of IL-1 in tumorigenesis, tumor invasiveness, metastasis and tumor-host interactions
Apte, R. N., Dotan, S., Elkabets, M., White, M. R., Reich, E., Carmi, Y., Song, X., Dvozkin, T., Krelin, Y., & Voronov, E. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-9004-4 · Cited by 593 · cited 2× · see citing works
“Early observations on augmentation of metastasis by IL-1 were subsequently extended to primary carcinogenesis in different organs (Apte et al., 2006; Salcedo et al., 2013).”
Muzio, M., Natoli, G., Saccani, S., Levrero, M., & Mantovani, A. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.12.2097 · Cited by 573 · cited 7× · see citing works
“Early on, it was realized that IL-1 was responsible for resistance against microbes (van der Meer et al., 1988), a discovery upstream of the identification of the TIR domain (originally standing for Toll-IL-1 resistance; shared by the IL-1 receptor [IL-1R] and Toll-like receptors [TLR]), and of the inflammasome.”
InfluentialIL-1α and IL-1β Recruit Different Myeloid Cells and Promote Different Stages of Sterile Inflammation
Rider, P., Carmi, Y., Guttman, O., Braiman, A., Cohen, I., Voronov, E., White, M. R., Dinarello, C. A., & Apte, R. N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1102048 · Cited by 522 · see citing works
Dehghan, A., Dupuis, J., Barbalić, M., Bis, J. C., Eiríksdóttir, G., Lu, C., Pellikka, N., Wallaschofski, H., Kettunen, J., Henneman, P., et al. (2011) · Circulation · doi:10.1161/circulationaha.110.948570 · Cited by 512 · cited 1× · see citing works
“In a GWAS of 66,185 subjects with elevated CRP, loci implicated in themetabolic syndrome include NLRP3, IL-6R, and IL-38 (Dehghan et al., 2011).”
Interleukin-33-Dependent Innate Lymphoid Cells Mediate Hepatic Fibrosis
Mchedlidze, T., Waldner, M., Zopf, S., Walker, J., Rankin, A. L., Schuchmann, M., Voehringer, D., McKenzie, A. N. J., Neurath, M. F., Pflanz, S., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.07.018 · Cited by 502 · see citing works
Interleukin-33 attenuates sepsis by enhancing neutrophil influx to the site of infection
Alves-Filho, J. C., Sônego, F., Souto, F. O., de Freitas, A., Verri, W. A., Jr., Auxiliadora‐Martins, M., Basile-Filho, A., McKenzie, A. N. J., Xu, D., Cunha, F. Q., et al. (2010) · Nature Medicine · doi:10.1038/nm.2156 · Cited by 487 · cited 1× · see citing works
“In a murine model of sepsis, IL-33 has been found to enhance neutrophil recruitment to the site of infection and bacterial clearance by preventing TLR-mediated downregulation of the CXCR2 chemokine receptor (Alves-Filho et al., 2010).”
Deficiency of interleukin-18 in mice leads to hyperphagia, obesity and insulin resistance
Netea, M. G., Joosten, L. A. B., Lewis, E., Jensen, D. R., Voshol, P. J., Kullberg, B. J., Tack, C. J., van Krieken, H., Kim, S.-H., Stalenhoef, A. F., et al. (2006) · Nature Medicine · doi:10.1038/nm1415 · Cited by 424 · cited 1× · see citing works
“IL-18 and IL-18R-deficient aged mice spontaneously develop a metabolic syndrome similar to that of humans with diabetes, insulin resistance, and atherosclerosis (Netea et al., 2006).”
Self-citationMacrophage Plasticity and Polarization in Liver Homeostasis and Pathology
Sica, A., Invernizzi, P., & Mantovani, A. (2014) · Hepatology · doi:10.1002/hep.26754 · Cited by 422 · cited 1× · see citing works
“IL-33 is a driver of type 2 inflammatory conditions such as asthma, fibrosis, and response to parasites (Liew et al., 2010; McHedlidze et al., 2013; Sica et al., 2013).”
IL-1β-converting enzyme (caspase-1) in intestinal inflammation
Siegmund, B., Lehr, H.-A., Fantuzzi, G., & Dinarello, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231473998 · Cited by 421 · cited 3× · see citing works
“Induction of IFN-g by IL-18 requires caspase-1 processing (Siegmund et al., 2001b).”
Pecaric-Petkovic, T., Didichenko, S. A., Kämpfer, S. S., Spiegl, N., & Dahinden, C. A. (2008) · Blood · doi:10.1182/blood-2008-05-157818 · Cited by 420 · cited 1× · see citing works
“By inducing IL-5 production in several cell types, ILCs in particular, and by promoting eosinophil maturation, IL-33 causes eosinophilia in vivo (Bouffi et al., 2013; Ikutani et al., 2012; Pecaric-Petkovic et al., 2009).”
Doyle, S., Campbell, M., Ozaki, E., Salomon, R. G., Mori, A., Kenna, P. F., Farrar, G. J., Kiang, A., Humphries, M. M., Lavelle, E. C., et al. (2012) · Nature Medicine · doi:10.1038/nm.2717 · Cited by 418 · cited 1× · see citing works
“In some models of disease as in age-related macular degeneration, IL-18 is protective (Doyle et al., 2012).”
IL-1 family members and STAT activators induce cytokine production by Th2, Th17, and Th1 cells
Guo, L., Wei, G., Zhu, J., Liao, W., Leonard, W. J., Zhao, K., & Paul, W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906988106 · Cited by 410 · cited 14× · see citing works
“TIR8 inhibits NF-kB and JNK activation following stimulation of IL-1R family members or TLRs (IL-1RI, IL-18R, ST2, TLR1, TLR2, TLR3, TLR4, TLR7, and TLR9) (Bulek et al., 2009; Garlanda et al., 2004; Lech et al., 2008; Wald et al., 2003), by interfering with the recruitment of TIR-containing adaptor molecules (Wald et…”
InfluentialAn Autoinflammatory Disease Due to Homozygous Deletion of the IL1RN Locus
Reddy, S. T., Jia, S., Geoffrey, R., Lorier, R., Suchi, M., Broeckel, U., Hessner, M. J., & Verbsky, J. W. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0809568 · Cited by 408 · cited 1× · see citing works
“Children bornwith a genetic deficiency of IL-1Ra or functional inactive IL-1Ra suffer from severe systemic and local inflammation, including pustular skin eruptions, vasculitis, osteolytic lesions, and sterile osteomyelitis (Aksentijevich et al., 2009; Reddy et al., 2009).”
Psoriasiform dermatitis is driven by IL-36–mediated DC-keratinocyte crosstalk
Tortola, L., Rosenwald, E., Abel, B., Blumberg, H., Schäfer, M., Coyle, A. J., Renauld, J., Werner, S., Kisielow, J., & Köpf, M. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63451 · Cited by 405 · cited 2× · see citing works
“IL-36a, IL-36b, IL-36g, and IL-36Ra do not contain caspase cleavage sites and N-terminal truncation at the level of the A-X-Asp motif conserved in all IL-1 family members dramatically increases their proinflammatory activity (Towne et al., 2011).”
ST2 as a Marker for Risk of Therapy-Resistant Graft-versus-Host Disease and Death
Lugt, M. T. V., Braun, T., Hanash, S., Ritz, J., Ho, V. T., Antin, J. H., Zhang, Q., Wong, C., Wang, H., Chin, A. P., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1213299 · Cited by 403 · see citing works
van de Veerdonk, F. L., Stoeckman, A. K., Wu, G., Boeckermann, A. N., Azam, T., Netea, M. G., Joosten, L. A. B., van der Meer, J. W. M., Hao, R., Kalabokis, V., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121534109 · Cited by 383 · cited 4× · see citing works
“IL-38 binds to the extracellular domain of recombinant IL-1Rrp2 (IL-36R) expressed as an IgG1 fusion protein (van de Veerdonk et al., 2012).”
InfluentialPuren, A. J., Fantuzzi, G., & Dinarello, C. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2256 · Cited by 379 · cited 1× · see citing works
“Similar to IL-1a, the IL-18 precursor is found in nearly all the same mesenchymal cells in health in humans and mice (Puren et al., 1999), and IL-18 is associated with the monocyte membrane, as is IL-1a (Bellora et al., 2012).”
Dinarello, C. A., Arend, W. P., Sims, J. E., Smith, D. E., Blumberg, H., O'Neill, L. A. J., Goldbach‐Mansky, R. T., Pizarro, T. T., Hoffman, H. M., Bufler, P., et al. (2010) · Nature Immunology · doi:10.1038/ni1110-973 · Cited by 351 · cited 1× · see citing works
“The IL-1 and IL-1R families have grown impressively in size, complexity, and division of labor (Dinarello et al., 2010, 2012; Dinarello, 2009, 2010;Gabay et al., 2010).”
Opposing activities of two novel members of the IL-1 ligand family regulate skin inflammation
Blumberg, H., Dinh, H., Trueblood, E. S., Pretorius, J. K., Kugler, D. G., Weng, N., Kanaly, S. T., Towne, J. E., Willis, C. R., Kuechle, M. K., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070157 · Cited by 348 · cited 2× · see citing works
“SLE, systemic lupus erythematosus; RA, rheumatoid arthritis; GvHD, graft versus host disease. inflammatory characteristics such as neutrophilia and elevated circulating concentrations of IL-1b and IL-18 and die in the neonatal period.”
Kim, S. H., Eisenstein, M., Reznikov, L. L., Fantuzzi, G., Novick, D., Rubinstein, M., & Dinarello, C. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1190 · Cited by 342 · cited 1× · see citing works
“By Immunity 39, December 12, 2013 ª2013 Elsevier Inc. 1011 preventing the binding of the agonist to IL-18R, and neutralizing IL-18 activity, IL-18BP dampens IFN-g production and consequently limits Th1 cell responses (Kim et al., 2000; Novick et al., 1999) (Figure 4).”
Inflammasome-mediated disease animal models reveal roles for innate but not adaptive immunity
Brydges, S. D., Mueller, J. L., McGeough, M. D., Pena, C. A., Misaghi, A., Gandhi, C., Putnam, C. D., Boyle, D. L., Firestein, G. S., Horner, A. A., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.05.005 · Cited by 339 · see citing works
Long-term IL-33–producing epithelial progenitor cells in chronic obstructive lung disease
Byers, D. E., Alexander-Brett, J., Patel, A. C., Agapov, E., Dang-Vu, G., Jin, X., Wu, K., You, Y., Alevy, Y., Girard, J.-P., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65570 · Cited by 337 · cited 2× · see citing works
“IL-13-dependent lung disease has been shown to depend on long-term epithelial progenitor cells programmed for excess IL-33 production (Byers et al., 2013).”
IL‐33‐activated dendritic cells are critical for allergic airway inflammation
Besnard, A., Togbe, D., Guillou, N., Erard, F., Quesniaux, V. F. J., & Ryffel, B. (2011) · European Journal of Immunology · doi:10.1002/eji.201041033 · Cited by 331 · cited 1× · see citing works
“IL-33-activated dendritic cells (DCs) favor polarization of Th2 cells (Besnard et al., 2011).”
Cohen, I., Rider, P., Carmi, Y., Braiman, A., Dotan, S., White, M. R., Voronov, E., Martin, M. U., Dinarello, C. A., & Apte, R. N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915018107 · Cited by 327 · cited 2× · see citing works
“The IL-1a precursor shuttles between the cytosol and nucleus with amazing rapidity (Cohen et al., 2010).”
Xiao, H. Q., Gulen, M. F., Qin, J., Yao, J., Bulek, K., Kish, D. D., Altuntas, C. Z., Wald, D. N., Ma, C., Zhou, H., et al. (2007) · Immunity · doi:10.1016/j.immuni.2007.02.012 · Cited by 325 · see citing works
Towne, J. E., Renshaw, B. R., Douangpanya, J., Lipsky, B. P., Shen, M., Gabel, C. A., & Sims, J. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267922 · Cited by 324 · cited 2× · see citing works
“IL-36a, IL-36b, IL-36g, and IL-36Ra do not contain caspase cleavage sites and N-terminal truncation at the level of the A-X-Asp motif conserved in all IL-1 family members dramatically increases their proinflammatory activity (Towne et al., 2011).”
Interleukin 37 expression protects mice from colitis
McNamee, E. N., Masterson, J. C., Jedlicka, P., McManus, M. C., Grenz, A., Collins, C. B., Nold, M. F., Nold‐Petry, C. A., Bufler, P., Dinarello, C. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111982108 · Cited by 320 · see citing works
Arterial Inflammation in Mice Lacking the Interleukin 1 Receptor Antagonist Gene
Nicklin, M. J. H., Hughes, D. E., Barton, J. L., Ure, J. M., & Duff, G. W. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.2.303 · Cited by 319 · cited 1× · see citing works
“Deficiency of IL-1Ra in mice results in spontaneous and lethal arteritis, destructive arthritis, and psoriatic-like skin lesions, as well as increased susceptibility to carcinogenesis (Horai et al., 2000; Nicklin et al., 2000).”
Ikutani, M., Yanagibashi, T., Ogasawara, M., Tsuneyama, K., Yamamoto, S., Hattori, Y., Kouro, T., Itakura, A., Nagai, Y., Τακακι, S., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101270 · Cited by 314 · cited 1× · see citing works
“By inducing IL-5 production in several cell types, ILCs in particular, and by promoting eosinophil maturation, IL-33 causes eosinophilia in vivo (Bouffi et al., 2013; Ikutani et al., 2012; Pecaric-Petkovic et al., 2009).”
Pomerantz, B. J., Reznikov, L. L., Harken, A. H., & Dinarello, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041611398 · Cited by 310 · cited 2× · see citing works
“Similar to IL-1a, the IL-18 precursor is found in nearly all the same mesenchymal cells in health in humans and mice (Puren et al., 1999), and IL-18 is associated with the monocyte membrane, as is IL-1a (Bellora et al.”
IL-36R ligands are potent regulators of dendritic and T cells
Vigne, S., Palmer, G., Lamacchia, C., Martin, P., Talabot‐Ayer, D., Rodriguez, E., Ronchi, F., Sallusto, F., Dinh, H., Sims, J. E., et al. (2011) · Blood · doi:10.1182/blood-2011-05-356873 · Cited by 308 · cited 1× · see citing works
“IL-36 is produced by innate immune cells and lymphocytes inducing the production of proinflammatory cytokines, chemokines, and costimulatory molecules, thus promoting Th1 and Th17 cell polarization (Vigne et al., 2011, 2012) (Figure 3B).”
Freigang, S., Ampenberger, F., Weiss, A., Kanneganti, T., Iwakura, Y., Hersberger, M., & Köpf, M. (2013) · Nature Immunology · doi:10.1038/ni.2704 · Cited by 304 · cited 1× · see citing works
“Recent results have highlighted differential induction and role of IL-1a and IL-1b in fat induced vascular responses and atherosclerosis (Freigang et al., 2013).”
Siegmund, B., Fantuzzi, G., Rieder, F., Gamboni-Robertson, F., Lehr, H.-A., Hartmann, G., Dinarello, C. A., Endres, S., & Eigler, A. (2001) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.2001.281.4.r1264 · Cited by 289 · cited 3× · see citing works
“Induction of IFN-g by IL-18 requires caspase-1 processing (Siegmund et al., 2001b).”
Bossaller, L., Chiang, P.-I., Schmidt‐Lauber, C., Ganesan, S., Kaiser, W. J., Rathinam, V. A. K., Mocarski, E. S., Subramanian, D., Green, D. R., Silverman, N. S., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202121 · Cited by 287 · cited 1× · see citing works
“By inducing IL-5 production in several cell types, ILCs in particular, and by promoting eosinophil maturation, IL-33 causes eosinophilia in vivo (Bouffi et al., 2013; Ikutani et al., 2012; Pecaric-Petkovic et al., 2009).”
Krelin, Y., Voronov, E., Dotan, S., Elkabets, M., Reich, E., Fogel, M., Huszar, M., Iwakura, Y., Segal, S., Dinarello, C. A., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2956 · Cited by 285 · cited 2× · see citing works
“and colitis, reduced atherosclerosis (Chen et al., 2007; Krelin et al., 2007)”
IL-18–induced CD83+CCR7+NK helper cells
Mailliard, R. B., Alber, S. M., Shen, H., Watkins, S. C., Kirkwood, J. M., Herberman, R. B., & Kaliński, P. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050128 · Cited by 285 · cited 1× · see citing works
“IL-18 is a keymediator in the interaction between NK cells and DC or macrophages (e.g., Bellora et al., 2012; Mailliard et al., 2005).”
Kumar, S., Hanning, C. R., Brigham-Burke, M. R., Rieman, D. J., Lehr, R. V., Khandekar, S., Kirkpatrick, R. B., Scott, G. F., Lee, J. C., Lynch, F. J., et al. (2002) · Cytokine · doi:10.1006/cyto.2002.0873 · Cited by 260 · see citing works
Intestinal inflammation in mice deficient in Tir8 , an inhibitory member of the IL-1 receptor family
Garlanda, C., Riva, F., Polentarutti, N., Buracchi, C., Sironi, M., Bortoli, M. D., Muzio, M., Bergottini, R., Scanziani, E., Vecchi, A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308680101 · Cited by 254 · cited 1× · see citing works
“…have shown that TIR8 plays nonredundant roles in regulating potentially detrimental inflammatory responses associated to infections, such as tuberculosis, candidiasis, aspergillosis, and P. aeruginosa infection (Bozza et al., 2008; Chen et al., 2011; Garlanda et al., 2007a; Huang et al., 2006).”
A complex of the IL-1 homologue IL-1F7b and IL-18-binding protein reduces IL-18 activity
Bufler, P., Azam, T., Gamboni-Robertson, F., Reznikov, L. L., Kumar, S., Dinarello, C. A., & Kim, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212519099 · Cited by 252 · cited 2× · see citing works
“Despite binding to the IL-18Ra chain, IL-37 does not act as a classical receptor antagonist (Bufler et al., 2002; Nold-Petry et al., 2009).”
Non-redundant properties of IL-1α and IL-1β during acute colon inflammation in mice
Bersudsky, M., Luski, L., Fishman, D., White, R. M., Ziv‐Sokolovskaya, N., Dotan, S., Rider, P., Kaplanov, I., Aychek, T., Dinarello, C. A., et al. (2013) · Gut · doi:10.1136/gutjnl-2012-303329 · Cited by 251 · see citing works
The meta-analysis of genome-wide association studies
Thompson, J. R., Attia, J., & Minelli, C. (2011) · Briefings in Bioinformatics · doi:10.1093/bib/bbr020 · Cited by 250 · see citing works
van der Meer, J. W., Barza, M. J., Wolff, S. M., & Dinarello, C. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.5.1620 · Cited by 243 · cited 1× · see citing works
“Early on, it was realized that IL-1 was responsible for resistance against microbes (van der Meer et al., 1988), a discovery upstream of the identification of the TIR domain (originally standing for Toll-IL-1 resistance; shared by the IL-1 receptor [IL-1R] and Toll-like receptors [TLR]), and of the…”
Ben-Sasson, S. Z., Hogg, A. E., Hu‐Li, J., Wingfield, P. T., Chen, X., Crank, M. C., Caucheteux, S. M., Ratner, M., Berzofsky, J. A., Nir‐Paz, R., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20122006 · Cited by 243 · see citing works
The IL-1 Family Member 7b Translocates to the Nucleus and Down-Regulates Proinflammatory Cytokines
Sharma, S., Kulk, N., Nold, M. F., Gräf, R., Kim, S., Reinhardt, D., Dinarello, C. A., & Bufler, P. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.8.5477 · Cited by 242 · cited 2× · see citing works
“Gene databases do not contain a murine homolog for IL-37, but human IL-37 is functional in mouse cells (Bufler et al., 2002; Sharma et al., 2008).”
Sterile inflammation of endothelial cell-derived apoptotic bodies is mediated by interleukin-1α
Berda‐Haddad, Y., Robert, S., Salers, P., Zekraoui, L., Farnarier, C., Dinarello, C. A., Dignat‐George, F., & Kaplanski, G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116848108 · Cited by 232 · cited 1× · see citing works
“However, circulating IL-1a is rarely detected even in persons with severe infections but is contained in apoptotic bodies released from endothelial cells (Berda-Haddad et al., 2011).”
Divergence of IL-1, IL-18, and cell death in NLRP3 inflammasomopathies
Brydges, S. D., Broderick, L., McGeough, M. D., Peña, C. A., Mueller, J. L., & Hoffman, H. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci71543 · Cited by 228 · see citing works
Duan, J., Chung, H., Troy, E. B., & Kasper, D. L. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.01.005 · Cited by 224 · cited 1× · see citing works
“However, Tgd17 express the IL-1R and IL-1 in concert with IL-23 drives their activation and IL-1 production, thus setting in motion an amplification circuit (Duan et al., 2010; Zeng et al., 2012).”
Vigne, S., Palmer, G., Martin, P., Lamacchia, C., Strebel, D., Rodriguez, E., Olleros, M. L., Vesin, D., Garcia, I., Ronchi, F., et al. (2012) · Blood · doi:10.1182/blood-2012-06-439026 · Cited by 218 · see citing works
Palm, N. W., Rosenstein, R. K., Yu, S., Schenten, D., Florsheim, E. B., & Medzhitov, R. M. (2013) · Immunity · doi:10.1016/j.immuni.2013.10.006 · Cited by 217 · cited 3× · see citing works
“The adaptive Th2 response against PLA2 is also IL-33 and ST2 dependent.”
Structural insights into the interaction of IL-33 with its receptors
Liu, X., Hammel, M., He, Y., Tainer, J. A., Jeng, U., Zhang, L., Wang, S., & Wang, X. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308651110 · Cited by 214 · cited 1× · see citing works
“The crystal structure of IL-33 in complex with the ectodomain of ST2 has recently been solved (Liu et al., 2013).”
The Role of IL-1β in the Early Tumor Cell–Induced Angiogenic Response
Carmi, Y., Dotan, S., Rider, P., Kaplanov, I., White, M. R., Baron, R., Abutbul, S., Huszar, M., Dinarello, C. A., Apte, R. N., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202769 · Cited by 209 · see citing works
Hughes, T. L., Becknell, B., Freud, A. G., McClory, S., Briercheck, E. L., Yu, J., Mao, C., Giovenzana, C., Nuovo, G. J., Wei, L., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.06.007 · Cited by 207 · cited 10× · see citing works
“IL-38 does not bind to IL-1R1, IL-1R3, or to IL-18Rabut only to the IL-36R.”
InfluentialZheng, Y., Humphry, M., Maguire, J. J., Bennett, M. R., & Clarke, M. C. H. (2013) · Immunity · doi:10.1016/j.immuni.2013.01.008 · Cited by 205 · cited 2× · see citing works
“Because IL-1R2 is expressed by a limited set of cells, this would represent a further mechanism of negative control of IL-1a by IL-1R2 during necrosis, restricted to specific cell types (Zheng et al., 2013).”
Zeng, X., Wei, Y.-L., Huang, J., Newell, E. W., Yu, H., Kidd, B. A., Kuhns, M. S., Waters, R., Davis, M. M., Weaver, C. T., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.06.011 · Cited by 200 · cited 1× · see citing works
“However, Tgd17 express the IL-1R and IL-1 in concert with IL-23 drives their activation and IL-1 production, thus setting in motion an amplification circuit (Duan et al., 2010; Zeng et al., 2012).”
Gulen, M. F., Kang, Z., Bulek, K., Youzhong, W., Kim, T. W., Chen, Y., Altuntas, C. Z., Bak‐Jensen, K. S., McGeachy, M. J., Do, J., et al. (2010) · Immunity · doi:10.1016/j.immuni.2009.12.003 · Cited by 197 · see citing works
Inflammation links excess fat to insulin resistance: the role of the interleukin‐1 family
Tack, C. J., Stienstra, R., Joosten, L. A. B., & Netea, M. G. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01145.x · Cited by 192 · cited 1× · see citing works
“IL-1 production can be a consequence of alterations in the homeostatic metabolic state as observed in obesity (dysbiosis) (Tack et al., 2012) (Figure 2A).”
Paget, C., Ivanov, S., Fontaine, J., Renneson, J., Blanc, F., Pichavant, M., Dumoutier, L., Ryffel, B., Renauld, J., Gosset, P., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.304758 · Cited by 185 · cited 1× · see citing works
“IL-1, together with other cytokines, has been reported to induce IL-17 production by iNKT cells and, in the context of viral infection, IL-22 (Doisne et al., 2011; Monteiro et al., 2013; Paget et al., 2012).”
Smith, D. E., Hanna, R. K., Friend, D. J., Moore, H. M., Chen, H., Farese, A. M., MacVittie, T. J., Virca, G. D., & Sims, J. E. (2003) · Immunity · doi:10.1016/s1074-7613(02)00514-9 · Cited by 182 · cited 1× · see citing works
“Finally, soluble IL-1R2 and soluble IL-1RAcP bind pro-IL-1bwith high affinity and block its processing by caspase-1 (Smith et al., 2003).”
Bulek, K., Swaidani, S., Qin, J., Lu, Y., Gulen, M. F., Herjan, T., Min, B., Kastelein, R. A., Aronica, M. A., Kosz‐Vnenchak, M., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802729 · Cited by 168 · see citing works
Garlanda, C., Anders, H., & Mantovani, A. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.06.001 · Cited by 165 · cited 1× · see citing works
“TIR8 is expressed in several tissues, particularly in the kidney, digestive tract, liver, lung, and lymphoid organs (Garlanda et al., 2009).”
Structural insights into the assembly and activation of IL-1β with its receptors
Wang, D., Zhang, S., Li, L., Liu, X., Mei, K., & Wang, X. (2010) · Nature Immunology · doi:10.1038/ni.1925 · Cited by 162 · cited 1× · see citing works
“The overall structure of the IL-1b-IL-1R2-IL-1RAcP complex is similar to that of the signaling ligand-receptor complex (Wang et al., 2010).”
Espinassous, Q., Paco, E. G. D., García-Verdugo, I., Synguélakis, M., von Aulock, S., Sallenave, J., McKenzie, A. N. J., & Kanellopoulos, J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803067 · Cited by 151 · cited 1× · see citing works
“In macrophages, IL-33 favors LPS-dependent cytokine and chemokine production, and M2 macrophage polarization (Espinassous et al., 2009; KurowskaStolarska et al., 2009).”
IL-1 and T Helper Immune Responses
Santarlasci, V., Cosmi, L., Maggi, L., Liotta, F., & Annunziato, F. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00182 · Cited by 148 · cited 1× · see citing works
“It is therefore not surprising that IL-18 has been associated with Th1 cell differentiation (Santarlasci et al., 2013).”
Croonian Lecture, 1906.—On nerve endings and on special excitable substances in cells
Langley, J. N. (1906) · Proceedings of the Royal Society of London Series B Containing Papers of a Biological Character · doi:10.1098/rspb.1906.0056 · Cited by 146 · cited 1× · see citing works
“The IL-1R2 receptor was identified as a decoy for IL-1 (Colotta et al., 1993), a paradigm shift since the original definition of ‘‘receptor’’ by Langley in the 19th century (Langley, 1906).”
Regulated Intramembrane Proteolysis of the Interleukin-1 Receptor II by α-, β-, and γ-Secretase
Kuhn, P., Marjaux, E., Imhof, A., Strooper, B. D., Haass, C., & Lichtenthaler, S. F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700356200 · Cited by 144 · cited 1× · see citing works
“It is released in a soluble form (Kuhn et al., 2007; Lorenzen et al., 2012) as a consequence of proteolytic processing or alternative splicing.”
Doisne, J., Soulard, V., Bécourt, C., Amniai, L., Henrot, P., Havenar‐Daughton, C., Blanchet, C., Zitvogel, L., Ryffel, B., Cavaillon, J., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002725 · Cited by 143 · see citing works
Zhao, J., Wei, J., Mialki, R. K., Mallampalli, D., Chen, B. B., Coon, T. A., Zou, C., Mallampalli, R. K., & Zhao, Y. (2012) · Nature Immunology · doi:10.1038/ni.2341 · Cited by 142 · see citing works
Albacker, L. A., Chaudhary, V., Chang, Y.-J., Kim, H. Y., Chuang, Y.-T., Pichavant, M., DeKruyff, R. H., Savage, P. B., & Umetsu, D. T. (2013) · Nature Medicine · doi:10.1038/nm.3321 · Cited by 140 · see citing works
Smith, D. E., Lipsky, B. P., Russell, C. B., Ketchem, R. R., Kirchner, J., Hensley, K. M., Huang, Y., Friedman, W., Boissonneault, V., Plante, M.-M., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.03.020 · Cited by 135 · cited 15× · see citing works
“Moreover, IL-1R2 forms a complex with IL-1 and the IL-1RAcP, exerting a dominant-negative effect.”
InfluentialThe natural and the inducible: interleukin (IL)-17-producing γδ T cells
Chien, Y.-H., Zeng, X., & Prinz, I. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.11.004 · Cited by 134 · cited 1× · see citing works
“Immunity 39, December 12, 2013 ª2013 Elsevier Inc. 1013 Tgdcells are themajor sourceof IL-17earlyafter infection (Chien et al., 2013).”
Myles, I. A., Fontecilla, N. M., Valdez, P. A., Vithayathil, P. J., Naik, S., Belkaid, Y., Ouyang, W., & Datta, S. K. (2013) · Nature Immunology · doi:10.1038/ni.2637 · Cited by 133 · cited 1× · see citing works
“In a mouse model of skin infection, resistance to S. aureus depends on IL-1, which promotes IL-17 production by Tgd cells (Myles et al., 2013).”
Distinctive features of classic and nonclassic ( T h17 derived) human T h1 cells
Maggi, L., Santarlasci, V., Capone, M., Rossi, M. C., Querci, V., Mazzoni, A., Cimaz, R., Palma, R. D., Liotta, F., Maggi, E., et al. (2012) · European Journal of Immunology · doi:10.1002/eji.201242648 · Cited by 132 · cited 1× · see citing works
“It has found that a subset of Th1 clones, in particular those characterized by expression of CD161, expresses IL1R1 (Cosmi et al., 2008; Maggi et al., 2012).”
Sakai, N., Sweringen, H. L. V., Belizaire, R. M., Quillin, R. C., Schuster, R. M., Blanchard, J. A., Burns, J. M., Tevar, A. D., Edwards, M. J., & Lentsch, A. B. (2012) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2012.07187.x · Cited by 132 · cited 1× · see citing works
“IL-37Tg mice are protected against inflammatory conditions involving the gut (DSS-induced colitis) (McNamee et al., 2011), the heart (ischemic heart injury) (Yousif et al., 2011), and the liver (ischemia and reperfusion) (Sakai et al., 2012).”
Association between the interleukin‐1 family gene cluster and psoriatic arthritis
Rahman, P., Sun, S., Peddle, L., Snelgrove, T., Melay, W., Greenwood, C. M. T., & Gladman, D. D. (2006) · Arthritis & Rheumatism · doi:10.1002/art.21928 · Cited by 131 · see citing works
Common genetic variation at the IL1RL1 locus regulates IL-33/ST2 signaling
Ho, J. E., Chen, W., Chen, M., Larson, M. G., McCabe, E. L., Cheng, S. C., Ghorbani, A., Coglianese, E. E., Emilsson, V., Johnson, A. D., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67119 · Cited by 124 · cited 14× · see citing works
“TIR8 inhibits NF-kB and JNK activation following stimulation of IL-1R family members or TLRs (IL-1RI, IL-18R, ST2, TLR1, TLR2, TLR3, TLR4, TLR7, and TLR9) (Bulek et al., 2009; Garlanda et al., 2004; Lech et al., 2008; Wald et al., 2003), by interfering with the recruitment of TIR-containing adaptor molecules (Wald et…”
InfluentialGarlanda, C., Riva, F., Veliz, T., Polentarutti, N., Pasqualini, F., Radaelli, E., Sironi, M., Nebuloni, M., Zorini, E. O., Scanziani, E., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0560 · Cited by 123 · cited 1× · see citing works
“TIR8 is expressed in several tissues, particularly in the kidney, digestive tract, liver, lung, and lymphoid organs (Garlanda et al., 2009).”
Lack of Toll IL-1R8 Exacerbates Th17 Cell Responses in Fungal Infection
Bozza, S., Zelante, T., Moretti, S., Bonifazi, P., DeLuca, A., D’Angelo, C., Giovannini, G., Garlanda, C., Boon, L., Bistoni, F., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.4022 · Cited by 120 · cited 2× · see citing works
“aeruginosa infection (Bozza et al., 2008; Chen et al., 2011; Garlanda et al., 2007a; Huang et al., 2006).”
Garlanda, C., Liberto, D. D., Vecchi, A., Manna, M. P. L., Buracchi, C., Caccamo, N., Salerno, A., Dieli, F., & Mantovani, A. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.5.3119 · Cited by 119 · see citing works
IL-1β suppresses innate IL-25 and IL-33 production and maintains helminth chronicity
Zaiss, M. M., Maslowski, K. M., Mosconi, I., Guenat, N., Marsland, B. J., & Harris, N. L. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003531 · Cited by 116 · cited 1× · see citing works
“Interestingly, IL-1b suppresses IL-25 and IL-33 production maintaining chronicity of helminthic infection (Zaiss et al., 2013).”
Tir8/Sigirr prevents murine lupus by suppressing the immunostimulatory effects of lupus autoantigens
Lech, M., Kulkarni, O. P., Pfeiffer, S., Savarese, E., Krug, A., Garlanda, C., Mantovani, A., & Anders, H. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20072646 · Cited by 115 · cited 4× · see citing works
“…also associated with increased susceptibility to develop allergy and autoimmunity in various models including systemic lupus erythematosus, lupus nephritis (Lech et al., 2008, 2010), arthritis (Drexler et al., 2010), experimental autoimmune encephalomyelitis, and psoriasis (Russell et al., 2013).”
InfluentialThe IL ‐36 receptor pathway regulates A spergillus fumigatus‐induced T h1 and T h17 responses
Gresnigt, M. S., Rösler, B., Jacobs, C. W. M., Becker, K. L., Joosten, L. A. B., van der Meer, J. W. M., Netea, M. G., Dinarello, C. A., & van de Veerdonk, F. L. (2012) · European Journal of Immunology · doi:10.1002/eji.201242711 · Cited by 108 · see citing works
Bouffi, C., Rochman, M., Zust, C. B., Stucke, E. M., Kartashov, A. V., Fulkerson, P. C., Barski, A., & Rothenberg, M. E. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301465 · Cited by 106 · cited 1× · see citing works
“By inducing IL-5 production in several cell types, ILCs in particular, and by promoting eosinophil maturation, IL-33 causes eosinophilia in vivo (Bouffi et al., 2013; Ikutani et al., 2012; Pecaric-Petkovic et al., 2009).”
Re, F., Sironi, M., Muzio, M., Matteucci, C., Introna, M., Orlando, S., Pentón‐Rol, G., Dower, S., Sims, J. E., Colotta, F., et al. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1841 · Cited by 102 · see citing works
Novick, D., Elbirt, D., Miller, G., Dinarello, C. A., Rubinstein, M., & Sthoeger, Z. M. (2009) · Journal of Autoimmunity · doi:10.1016/j.jaut.2009.08.002 · Cited by 95 · cited 1× · see citing works
“In several IFN-gmediated autoimmune conditions, the concentrations of free IL-18 compared to IL-18 bound to IL-18BP is important in determining the severity of the disease (Novick et al., 2010).”
MyD88 and its divergent toll in carcinogenesis
Salcedo, R., Cataisson, C., Hasan, U. A., Yuspa, S. H., & Trinchieri, G. (2013) · Trends in Immunology · doi:10.1016/j.it.2013.03.008 · Cited by 95 · cited 3× · see citing works
“Early observations on augmentation of metastasis by IL-1 were subsequently extended to primary carcinogenesis in different organs (Apte et al., 2006; Salcedo et al., 2013).”
Lech, M., Avila‐Ferrufino, A., Allam, R., Segerer, S., Khandoga, A. G., Krombach, F., Garlanda, C., Mantovani, A., & Anders, H. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900118 · Cited by 93 · cited 1× · see citing works
“TIR8 is expressed in several tissues, particularly in the kidney, digestive tract, liver, lung, and lymphoid organs (Garlanda et al., 2009).”
Bellora, F., Castriconi, R., Doni, A., Cantoni, C., Moretta, L., Mantovani, A., Moretta, A., & Bottino, C. (2012) · European Journal of Immunology · doi:10.1002/eji.201142173 · Cited by 92 · cited 2× · see citing works
“Similar to IL-1a, the IL-18 precursor is found in nearly all the same mesenchymal cells in health in humans and mice (Puren et al., 1999), and IL-18 is associated with the monocyte membrane, as is IL-1a (Bellora et al., 2012).”
Macrophage-Derived IL-33 Is a Critical Factor for Placental Growth
Fock, V., Mairhofer, M., Otti, G. R., Hiden, U., Spittler, A., Zeisler, H., Fiala, C., Knöfler, M., & Pollheimer, J. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300490 · Cited by 92 · cited 1× · see citing works
“Macrophage-derived IL-33 has been shown to be a regulator of trophoblast proliferation and placental growth during early pregnancy (Fock et al., 2013).”
IL-33–dependent induction of allergic lung inflammation by FcγRIII signaling
Tjota, M. Y., Williams, J. W., Lu, T., Clay, B. S., Byrd, T. T., Hrusch, C. L., Decker, D. C., de Araujo, C. A., Bryce, P. J., & Sperling, A. I. (2013) · Journal of Clinical Investigation · doi:10.1172/jci63802 · Cited by 84 · cited 2× · see citing works
“fumigatus-induced airway hyperreactivity (Albacker et al., 2013; Tjota et al., 2013).”
Huang, X., Hazlett, L. D., Du, W., & Barrett, R. P. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.548 · Cited by 81 · cited 1× · see citing works
“…have shown that TIR8 plays nonredundant roles in regulating potentially detrimental inflammatory responses associated to infections, such as tuberculosis, candidiasis, aspergillosis, and P. aeruginosa infection (Bozza et al., 2008; Chen et al., 2011; Garlanda et al., 2007a; Huang et al., 2006).”
Expression and Function of TNF and IL-1 Receptors on Human Regulatory T Cells
Mercer, F. K., Kozhaya, L., & Unutmaz, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008639 · Cited by 80 · cited 1× · see citing works
“…is expressed by a large variety of cell types, IL-1R2 is expressed by amore limited set of cell types, including monocytes, polarized M2 macrophages, microglial cells, neutrophils, B cells, and T regulatory (Treg) cells (Colotta et al., 1993;Martin et al., 2013;Mercer et al., 2010; Reet al., 1996).”
Induced IL-17–Producing Invariant NKT Cells Require Activation in Presence of TGF-β and IL-1β
Monteiro, M., Almeida, C. F., Agua‐Doce, A., & Graça, L. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201010 · Cited by 77 · cited 7× · see citing works
“IL-18, together with IL15, is a major stimulus for IFN-g production by group 1 ILCs; IL-33, acting in synergy with IL-25, is a potent inducer of the expansion of type 2 ILCs and of the production of extremely high amounts of Th2 cell-associated cytokines, in particular IL5 and IL-13; IL-1b and IL-23 activate group 3 I…”
InfluentialGrimsby, S., Jaensson, H., Dubrovska, A., Lomnytska, M. I., Hellman, U., & Souchelnytskyi, S. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.069 · Cited by 76 · cited 1× · see citing works
“The nuclear translocation and anti-inflammatory properties of IL-37 appear to be linked to binding to the Smad3 (Grimsby et al., 2004) transcription factor for the antiinflammatory and immunosuppressive properties of TGF-b.”
Maksymowych, W. P., Rahman, P., REEVE, J. P., Gladman, D. D., Peddle, L., & Inman, R. D. (2006) · Arthritis & Rheumatism · doi:10.1002/art.21642 · Cited by 73 · cited 1× · see citing works
“Allele combinations that include IL-38 polymorphisms are associated with psoriatic arthritis and ankylosing spondylitis (Maksymowych et al., 2006; Rahman et al., 2006), suggesting that IL-38 plays an important role in the pathogenesis of these inflammatory diseases.”
Lorenzen, I., Lokau, J., Düsterhöft, S., Trad, A., Garbers, C., Scheller, J., Rose‐John, S., & Grötzinger, J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.012 · Cited by 72 · cited 1× · see citing works
“It is released in a soluble form (Kuhn et al., 2007; Lorenzen et al., 2012) as a consequence of proteolytic processing or alternative splicing.”
Drexler, S. K., Kong, P. L., Inglis, J. J., Williams, R. O., Garlanda, C., Mantovani, A., Yazdi, A. S., Brennan, F. M., Feldmann, M., & Foxwell, B. M. J. (2010) · Arthritis & Rheumatism · doi:10.1002/art.27517 · Cited by 69 · cited 2× · see citing works
“…also associated with increased susceptibility to develop allergy and autoimmunity in various models including systemic lupus erythematosus, lupus nephritis (Lech et al., 2008, 2010), arthritis (Drexler et al., 2010), experimental autoimmune encephalomyelitis, and psoriasis (Russell et al., 2013).”
Martin, P., Palmer, G., Vigne, S., Lamacchia, C., Rodriguez, E., Talabot‐Ayer, D., Rose‐John, S., Chalaris, A., & Gabay, C. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0113035 · Cited by 67 · cited 2× · see citing works
“cell types, IL-1R2 is expressed by amore limited set of cell types, including monocytes, polarized M2 macrophages, microglial cells, neutrophils, B cells, and T regulatory (Treg) cells (Colotta et al., 1993;Martin et al., 2013;Mercer et al., 2010; Reet al., 1996).”
Xiao, H. Q., Yin, W., Ma, K., Gulen, M. F., Zhou, H., Sham, H. P., Jacobson, K., Vallance, B. A., & Li, X. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.04.043 · Cited by 60 · cited 2× · see citing works
“TIR8 can also regulate mTOR kinase activity in Th17 lymphocytes (Gulen et al., 2010) and in intestinal epithelial cells (Xiao et al., 2010).”
The Toll-IL-1R Member Tir8/SIGIRR Negatively Regulates Adaptive Immunity against Kidney Grafts
Noris, M., Cassis, P., Azzollini, N., Cavinato, R. A., Cugini, D., Casiraghi, F., Aiello, S., Solini, S., Cassis, L., Mister, M., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803549 · Cited by 56 · cited 1× · see citing works
“In kidney ischemia or transplantation, TIR8-deficiency causes increased renal injury or severe graft rejection, associated with excessive inflammation and amplified adaptive immune responses against donor antigens (Lech et al., 2009; Noris et al., 2009).”
Lack of SIGIRR/TIR8 aggravates hydrocarbon oil‐induced lupus nephritis
Lech, M., Skuginna, V., Kulkarni, O. P., Gong, J., Wei, T., Stark, R. W., Garlanda, C., Mantovani, A., & Anders, H. (2009) · The Journal of Pathology · doi:10.1002/path.2678 · Cited by 56 · cited 1× · see citing works
“…also associated with increased susceptibility to develop allergy and autoimmunity in various models including systemic lupus erythematosus, lupus nephritis (Lech et al., 2008, 2010), arthritis (Drexler et al., 2010), experimental autoimmune encephalomyelitis, and psoriasis (Russell et al., 2013).”
Lack of TIR8/SIGIRR triggers progression of chronic lymphocytic leukemia in mouse models
Bertilaccio, M. T. S., Simonetti, G., Dagklis, A., Rocchi, M., Rodríguez, T. V., Apollonio, B., Mantovani, A., Ponzoni, M., Ghia, P., Garlanda, C., et al. (2011) · Blood · doi:10.1182/blood-2011-01-329870 · Cited by 52 · see citing works
Nold‐Petry, C. A., Nold, M. F., Nielsen, J. W., Bustamante, A., Zepp, J. A., Storm, K., Hong, J., Kim, S., & Dinarello, C. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.004184 · Cited by 43 · cited 1× · see citing works
“Despite binding to the IL-18Ra chain, IL-37 does not act as a classical receptor antagonist (Bufler et al., 2002; Nold-Petry et al., 2009).”
Russell, S. E., Stefanska, A. M., Kubica, M., Horan, R. M., Mantovani, A., Garlanda, C., Fallon, P. G., & Walsh, P. T. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300828 · Cited by 40 · cited 3× · see citing works
“…also associated with increased susceptibility to develop allergy and autoimmunity in various models including systemic lupus erythematosus, lupus nephritis (Lech et al., 2008, 2010), arthritis (Drexler et al., 2010), experimental autoimmune encephalomyelitis, and psoriasis (Russell et al., 2013).”
Chen, X., Zhao, Y., Wu, X., & Qian, G. (2010) · Shock · doi:10.1097/shk.0b013e3181f226f3 · Cited by 24 · cited 1× · see citing works
“…have shown that TIR8 plays nonredundant roles in regulating potentially detrimental inflammatory responses associated to infections, such as tuberculosis, candidiasis, aspergillosis, and P. aeruginosa infection (Bozza et al., 2008; Chen et al., 2011; Garlanda et al., 2007a; Huang et al., 2006).”
Joeckel, L. T., Wallich, R., Metkar, S. S., Froelich, C. J., Simon, M. M., & Borner, C. (2012) · Journal of Virology · doi:10.1128/jvi.00682-12 · Cited by 22 · cited 1× · see citing works
“IL-1R1-deficient mice show defective capacity to generate effective CD8+ T cell responses to viruses (e.g., Joeckel et al., 2012) and tumors (Ghiringhelli et al., 2009).”
Nold, M. F., Nold‐Petry, C. A., Lo, C. Y.-W., Li, S., Rudloff, I., Zepp, J. A., Azam, T., Bufler, P., Garlanda, C., Mantovani, A., et al. (2013) · Cytokine · doi:10.1016/j.cyto.2013.06.190 · Cited by 11 · cited 2× · see citing works
“Available evidence suggests that IL-37 engages the IL-18Ra to deliver an inhibitory signal by using TIR8 (Nold et al., 2013).”
MethodLuo, Y., Cai, X., Liu, S., Wang, S., Nold‐Petry, C. A., Nold, M. F., Bufler, P., Norris, D. A., Dinarello, C. A., & Fujita, M. (2013) · Cytokine · doi:10.1016/j.cyto.2013.06.174 · Cited by 8 · cited 1× · see citing works
“In addition, there is evidence that IL-37 expressing DCs have defective capacity to activate effective T cell responses and induce T regulatory cells (Luo et al., 2013).”
Hong, D. S., Naing, A., Falchook, G. S., Piha-Paul, S. A., Wheler, J. J., Fu, S., Tsimberidou, A. M., Hui, D., Scott, R., Khan, R. S., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-11-a211 · Cited by 6 · cited 2× · see citing works
“A neutralizing monoclonal anti-IL-1a antibody has been tested in Type 2 diabetes, cancer cachexia, pustular psoriasis, occlusive vascular disease, and scarring acne vulgaris and in each condition, reduced disease severity has been observed in limited trials (Hong et al., 2011).”
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Fajgenbaum, D. C., & June, C. H. (2020) · New England Journal of Medicine · doi:10.1056/nejmra2026131 · Cited by 3,196 · see citing works
NF-κB, inflammation, immunity and cancer: coming of age
Taniguchi, K., & Karin, M. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.142 · Cited by 2,679 · see citing works
Overview of the <scp>IL</scp> ‐1 family in innate inflammation and acquired immunity
Dinarello, C. A. (2018) · Immunological Reviews · doi:10.1111/imr.12621 · Cited by 1,866 · see citing works
The Pore-Forming Protein Gasdermin D Regulates Interleukin-1 Secretion from Living Macrophages
Evavold, C. L., Ruan, J., Tan, Y., Xia, S., Wu, H., & Kagan, J. C. (2018) · Immunity · doi:10.1016/j.immuni.2017.11.013 · Cited by 1,115 · see citing works
“These pyrogens are produced as cytosolic factors that lack an N-terminal secretion signal, and are therefore not released from cells via the conventional secretory pathway (Garlanda et al., 2013).”
InfluentialCytokine release syndrome and associated neurotoxicity in cancer immunotherapy
Morris, E. C., Neelapu, S. S., Giavridis, T., & Sadelain, M. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00547-6 · Cited by 1,133 · see citing works
Pro-inflammatory cytokines: The link between obesity and osteoarthritis
Wang, T., & He, C. (2018) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2018.10.002 · Cited by 1,034 · see citing works
Interleukin-1 and Related Cytokines in the Regulation of Inflammation and Immunity
Mantovani, A., Dinarello, C. A., Molgora, M., & Garlanda, C. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.012 · Cited by 1,046 · see citing works
NLRP3 Inflammasome and the IL-1 Pathway in Atherosclerosis
Grebe, A., Hoss, F., & Latz, E. (2018) · Circulation Research · doi:10.1161/circresaha.118.311362 · Cited by 926 · see citing works
“Furthermore, IL-1β is an important constituent of the inflammatory tumor microenvironment and was attributed an important role in promoting carcinogenesis in certain tumors in which smoldering inflammation is part of the pathogenesis.(31) Interestingly, canakinumab treatment significantly reduced incident lung cancer…”
BackgroundInfluentialAkdis, M., Aab, A., Altunbulakli, C., Azkur, K., Costa, R. A., Crameri, R., Duan, S., Eiwegger, T., Eljaszewicz, A., Ferstl, R., et al. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.06.033 · Cited by 912 · see citing works
“IL-1Ra lacks the IL-1 receptor accessory protein interacting domain, so that its binding to IL-1 type I receptor inhibits IL-1 signaling.(53) Therapies under development for some inflammatory disorders involve neutralization of IL-1 activity through administration of IL-1Ra and anti–IL-1 neutralizing mAbs.”
BackgroundEdlmann, E., Giorgi-Coll, S., Whitfield, P. C., Carpenter, K. L. H., & Hutchinson, P. J. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0881-y · Cited by 740 · see citing works
IL-33: an alarmin cytokine with crucial roles in innate immunity, inflammation and allergy
Cayrol, C., & Girard, J. (2014) · Current Opinion in Immunology · doi:10.1016/j.coi.2014.09.004 · Cited by 700 · see citing works
“IL-33 is a nuclear cytokine, initially designated NF-HEV [1,2], which exhibits structural similarities with IL-1 [3 – 6].”
BackgroundInnate Immunity and the Failing Heart
Mann, D. L. (2015) · Circulation Research · doi:10.1161/circresaha.116.302317 · Cited by 690 · see citing works
The Function of Fish Cytokines
Zou, J., & Secombes, C. J. (2016) · Biology · doi:10.3390/biology5020023 · Cited by 679 · see citing works
“The IL-1β is synthesised as a precursor lacking a signal peptide and is required to be processed to release active protein [30].”
BackgroundInterleukin-33 in tissue homeostasis, injury, and inflammation
Molofsky, A. B., Savage, A. K., & Locksley, R. M. (2015) · Immunity · doi:10.1016/j.immuni.2015.06.006 · Cited by 638 · see citing works
“Whether other described inhibitors of MyD88-dependent pathways, such as A20 (TNFAIP3), IRAK-M, or SOCS family members restrict IL-33/ST2 signaling is unknown (Garlanda et al., 2013b; Tamiya et al., 2011; Turer et al., 2008).”
InfluentialThe role of IL-1β and TNF-α in intervertebral disc degeneration
Wang, Y., Che, M., Xin, J., Zheng, Z. J., Li, J., & Zhang, S. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110660 · Cited by 626 · see citing works
The role of interleukin-1 in general pathology
Kaneko, N., Kurata, M., Yamamoto, T., Morikawa, S., & Masumoto, J. (2019) · Inflammation and Regeneration · doi:10.1186/s41232-019-0101-5 · Cited by 616 · see citing works
“Currently, human sequence algorithm technologies suggest that the IL-1 family comprises a total of 11 members with similar or distinct biological effects [32, 33] .”
BackgroundNF‐κB signaling in inflammation and cancer
Zhang, T., Ma, C., Zhang, Z., Zhang, H., & Hu, H. (2021) · MedComm · doi:10.1002/mco2.104 · Cited by 615 · see citing works
Interleukin 1α and the inflammatory process
Di Paolo, N. C., & Shayakhmetov, D. M. (2016) · Nature Immunology · doi:10.1038/ni.3503 · Cited by 568 · see citing works
“Absolute amounts of IL-1 α protein vary among cell types, but barrier cells—such as endothelial and epithelial cells—express substantial amounts of this cytokine at steady state 5,12,15 .”
Role of sleep deprivation in immune-related disease risk and outcomes
Garbarino, S., Lanteri, P., Bragazzi, N. L., Magnavita, N., & Scoditti, E. (2021) · Communications Biology · doi:10.1038/s42003-021-02825-4 · Cited by 617 · see citing works
Next generation of immune checkpoint inhibitors and beyond
Marin-Acevedo, J. A., Kimbrough, E. O., & Lou, Y. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01056-8 · Cited by 560 · see citing works
“After binding to its ligand, Gas6, Axl promotes cell survival, activates phagocytosis, and induces an immunosuppressive phenotype in DCs, macrophages, and NK cells [134, 135].”
BackgroundInfluentialEmerging views of mitophagy in immunity and autoimmune diseases
Xu, Y., Shen, J., & Ran, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1603547 · Cited by 521 · see citing works
Kuswanto, W. F., Burzyn, D., Panduro, M., Wang, K. K., Jang, Y. C., Wagers, A. J., Benoist, C. O., & Mathis, D. J. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.009 · Cited by 509 · see citing works
“Although initial studies had emphasized the role of this cytokine in driving T helper 2 (Th2) cell responses, primarily through an impact on type 2 innate lymphoid cells (ILCs) and anti-inflammatory macrophages (Garlanda et al., 2013; Molofsky et al., 2013), more recent work highlighted its ability to expand Treg cell…”
NF-κB in inflammation and cancer
Mao, H., Zhao, X., & Sun, S. (2025) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01310-w · Cited by 577 · see citing works
“Paradoxically, NF-κ B also mediates early proin fl ammatory responses in TAMs via cytokines such as IL-1 β and IL-6, which fuel tumorigenesis by promoting cancer cell survival and proliferation [284, 294 – 296].”
Cytokines in rheumatoid arthritis — shaping the immunological landscape
McInnes, I. B., Buckley, C. D., & Isaacs, J. D. (2015) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2015.171 · Cited by 504 · see citing works
Proteolytic Processing of Interleukin-1 Family Cytokines: Variations on a Common Theme
Afonina, I. S., Müller, C., Martin, S. J., & Beyaert, R. (2015) · Immunity · doi:10.1016/j.immuni.2015.06.003 · Cited by 483 · see citing works
“IL-1 affects cells of the innate and adaptive immune system and exerts a wide range of biological activities including promoting fever, vasodilation, hematopoiesis, lymphocyte activation, leukocyte attraction and extravasation, angiogenesis, and antibody synthesis (Garlanda et al., 2013).”
BackgroundInfluentialNoncoding RNAs, cytokines, and inflammation-related diseases
Marques-Rocha, J. L., Samblas, M., Milagro, F. I., Bressan, J., Martínez, J. A., & Martí, A. (2015) · The FASEB Journal · doi:10.1096/fj.14-260323 · Cited by 477 · see citing works
“However, they have diverse functions: whereas IL-1a is constitutively expressed in epithelial membranes of gastrointestinal tract, lung, liver, kidney, endothelial cells, and astrocytes, IL-1b is produced by monocytes and macrophages and in response to other cytokines (89, 90).”
BackgroundInvited review: Inflammation during the transition to lactation: New adventures with an old flame
Bradford, B. J., Yuan, K., Farney, J. K., Mamedova, L. K., & Carpenter, A. J. (2015) · Journal of Dairy Science · doi:10.3168/jds.2015-9683 · Cited by 480 · see citing works
“Although immune cells are often involved in release of these signals, receptors for cytokines and eicosanoids are broadly expressed, allowing these compounds to influence nearly all tissues (Elsasser et al., 2008; Garlanda et al., 2013).”
BackgroundA 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases
Barnett, K. C., Li, S., Liang, K., & Ting, J. P.-Y. (2023) · Cell · doi:10.1016/j.cell.2023.04.025 · Cited by 458 · see citing works
The role of microglia in retinal neurodegeneration: Alzheimer’s disease, parkinson, and glaucoma.
Ramirez, A. I., de Hoz, R., Salobrar-Garcia, E., Salazar, J. J., Rojas, B., Ajoy, D., López-Cuenca, I., Rojas, P., Triviño, A., & Ramírez, J. M. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00214 · Cited by 466 · see citing works
“In addition, NLRP3 inflammasome activation reduces phagocytosis of Aβ by microglial cells, thus increasing the Aβ depositions and contributing to the pathogenesis of AD (Garlanda et al., 2013; Gold and El Khoury, 2015).”
BackgroundKaplanov, I., Carmi, Y., Kornetsky, R., Shemesh, A., Shurin, G. V., Shurin, M., Dinarello, C., Voronov, E., & Apte, R. (2018) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1812266115 · Cited by 404 · see citing works
Palomo, J., Dietrich, D., Martin, P., Palmer, G., & Gabay, C. (2015) · Cytokine · doi:10.1016/j.cyto.2015.06.017 · Cited by 447 · see citing works
Interleukin-1 Beta—A Friend or Foe in Malignancies?
Bent, R., Moll, L., Grabbe, S., & Bros, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082155 · Cited by 451 · see citing works
“In addition, in the case of chronic inflammation, sustained IL-1β may promote both tumor induction and later on also tumor propagation by different mechanisms [2].”
BackgroundInfluentialNold‐Petry, C. A., Lo, C. Y.-W., Rudloff, I., Elgass, K., Li, S., Gantier, M. P., Lotz-Havla, A. S., Gersting, S. W., Cho, S., Lao, J. C., et al. (2015) · Nature Immunology · doi:10.1038/ni.3103 · Cited by 442 · see citing works
The Role of Myeloid-Derived Suppressor Cells (MDSC) in Cancer Progression
Umansky, V., Blattner, C., Gebhardt, C., & Utikal, J. S. (2016) · Vaccines · doi:10.3390/vaccines4040036 · Cited by 440 · see citing works
“Notably, many of these inflammatory mediators (including IFN-, IL-1, IL-6, TNF-, CCL2, CCL3, CCL4, CCL5, etc.) are known be produced and secreted in the process of acute inflammation, inducing a significant activation of T cell-mediated immune reactions [1,88].”
BackgroundInfluentialQuantitative Temporal Viromics: An Approach to Investigate Host-Pathogen Interaction
Weekes, M. P., Tomašec, P., Huttlin, E. L., Fielding, C. A., Nusinow, D. P., Stanton, R. J., Wang, E. C. Y., Aicheler, R., Murrell, I., Wilkinson, G. W. G., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.028 · Cited by 427 · see citing works
Microbe-host interplay in atopic dermatitis and psoriasis
Fyhrquist, N., Muirhead, G., Prast‐Nielsen, S., Jeanmougin, M., Oláh, P., Skoog, T., Jules-Clément, G., Feld, M., Barrientos‐Somarribas, M., Sinkko, H., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12253-y · Cited by 416 · see citing works
Interleukin 33 is a guardian of barriers and a local alarmin
Martin, N., & Martin, M. (2016) · Nature Immunology · doi:10.1038/ni.3370 · Cited by 393 · see citing works
Neuromodulation by the immune system: a focus on cytokines
Salvador, A. F., de Lima, K. A., & Kipnis, J. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00508-z · Cited by 389 · see citing works
Keratoconus: an inflammatory disorder?
Galvis, V., Sherwin, T., Tello, A., Merayo, J., Barrera, R., & Acera, A. (2015) · Eye · doi:10.1038/eye.2015.63 · Cited by 398 · see citing works
Chen, X., Liu, G., Yuan, Y., Wu, G., Wang, S., & Yuan, L. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2157-1 · Cited by 394 · see citing works
Interleukin-1β signaling in osteoarthritis – chondrocytes in focus
Jenei‐Lanzl, Z., Meurer, A., & Zaucke, F. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.10.005 · Cited by 392 · see citing works
The family of the interleukin‐1 receptors
Boraschi, D., Italiani, P., Weil, S., & Martin, M. U. (2017) · Immunological Reviews · doi:10.1111/imr.12606 · Cited by 384 · see citing works
Lefrançais, E., Duval, A., Mirey, E., Roga, S., Espinosa, É., Cayrol, C., & Girard, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410700111 · Cited by 385 · see citing works
Koushki, K., Shahbaz, S. K., Mashayekhi, K., Sadeghi, M., Zayeri, Z. D., Taba, M. Y., Banach, M., Al-Rasadi, K., Johnston, T. P., & Sahebkar, A. (2021) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-020-08791-9 · Cited by 382 · see citing works
InflammasomesPreprint
de Zoete, M. R., Palm, N. W., Zhu, S., & Flavell, R. A. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016287 · Cited by 382 · see citing works
“IL-1b and IL-18 are critical for the initiation and control of the adaptive immune response; for example, IL-1b is intimately involved in the instruction of Th17 responses, which are implicated in many autoimmune disorders, and IL-18 supports Th1 responses (Garlanda et al. 2013).”
BackgroundThe Gasdermin‐D pore acts as a conduit for IL‐1β secretion in mice
Heilig, R., Dick, M. S., Sborgi, L., Meunier, É., Hiller, S., & Brož, P. (2017) · European Journal of Immunology · doi:10.1002/eji.201747404 · Cited by 377 · see citing works
NLRP3 inflammasome-driven pathways in depression: clinical and preclinical findings
Kaufmann, F. N., Costa, A. P., Ghisleni, G., Diaz, A. P., Rodrigues, A. L. S., Peluffo, H., & Kaster, M. P. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2017.03.002 · Cited by 370 · see citing works
“Caspase-1 is an inflammatory caspase produced as a pro-enzyme (pro-caspase-1) that requires cleavage by the NLRP3 inflammasome (Garlanda et al., 2013; Hoffman et al., 2001).”
<scp>IL</scp>‐1 and <scp>IL</scp>‐1 regulatory pathways in cancer progression and therapy
Mantovani, A., Barajon, I., & Garlanda, C. (2018) · Immunological Reviews · doi:10.1111/imr.12614 · Cited by 376 · see citing works
Kolodin, D., van Panhuys, N., Li, C., Magnuson, A. M., Cipolletta, D., Miller, C. M., Wagers, A., Germain, R. N., Benoist, C., & Mathis, D. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.03.005 · Cited by 365 · see citing works
“IL-33, amember of the IL-1 family of cytokines, is garneringmore and more attention (Garlanda et al., 2013).”
BackgroundInflammasome signaling and regulation of interleukin-1 family cytokines
Chan, A. H., & Schroder, K. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20190314 · Cited by 374 · see citing works
The IL-1 family of cytokines and receptors in rheumatic diseases
Dinarello, C. A. (2019) · Nature Reviews Rheumatology · doi:10.1038/s41584-019-0277-8 · Cited by 368 · see citing works
The microbiota–gut–brain axis and neurodevelopmental disorders
Wang, Q., Yang, Q., & Liu, X. (2023) · Protein & Cell · doi:10.1093/procel/pwad026 · Cited by 407 · see citing works
Interleukin-17 and innate immunity in infections and chronic inflammation
Isailovic, N., Daigo, K., Mantovani, A., & Selmi, C. F. (2015) · Journal of Autoimmunity · doi:10.1016/j.jaut.2015.04.006 · Cited by 364 · see citing works
Viganò, E., Diamond, C. E., Spreafico, R., Balachander, A., Sobota, R. M., & Mortellaro, A. (2015) · Nature Communications · doi:10.1038/ncomms9761 · Cited by 353 · see citing works
Wang, J., Li, D., Cang, H., & Guo, B. (2019) · Cancer Medicine · doi:10.1002/cam4.2327 · Cited by 353 · see citing works
Cytokinocytes: the diverse contribution of keratinocytes to immune responses in skin
Jiang, Y., Tsoi, L. C., Billi, A. C., Ward, N. L., Harms, P. W., Zeng, C., Maverakis, E. M., Kahlenberg, J. M., & Gudjonsson, J. E. (2020) · JCI Insight · doi:10.1172/jci.insight.142067 · Cited by 350 · see citing works
Cavalli, G., Colafrancesco, S., Emmi, G., Imazio, M., Lopalco, G., Maggio, M. C., Sota, J., & Dinarello, C. A. (2021) · Autoimmunity Reviews · doi:10.1016/j.autrev.2021.102763 · Cited by 356 · see citing works
IL-1 is a critical regulator of group 2 innate lymphoid cell function and plasticity
Ohne, Y., Silver, J. S., Thompson-Snipes, L., Collet, M. A., Blanck, J. P., Cantarel, B. L., Copenhaver, A. M., Humbles, A. A., & Liu, Y. (2016) · Nature Immunology · doi:10.1038/ni.3447 · Cited by 347 · see citing works
Martínez, G. J., Celermajer, D. S., & Patel, S. (2017) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2017.12.027 · Cited by 346 · see citing works
Rébé, C., & Ghiringhelli, F. (2020) · Cancers · doi:10.3390/cancers12071791 · Cited by 342 · see citing works
“IL-1α, IL-1β, and IL-33 are cytokine activators, while IL-1RA is an inhibitory cytokine [1].”
BackgroundBeyond adiponectin and leptin: adipose tissue-derived mediators of inter-organ communication
Funcke, J., & Scherer, P. E. (2019) · Journal of Lipid Research · doi:10.1194/jlr.r094060 · Cited by 337 · see citing works
Function and regulation of IL ‐1α in inflammatory diseases and cancer
Malik, A., & Kanneganti, T. (2017) · Immunological Reviews · doi:10.1111/imr.12615 · Cited by 325 · see citing works
Inflammasome-independent regulation of IL-1-family cytokines
Netea, M. G., van de Veerdonk, F. L., van der Meer, J. W. M., Dinarello, C. A., & Joosten, L. A. B. (2015) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112306 · Cited by 326 · see citing works
Self-citationTilg, H., Moschen, A. R., & Szabó, G. (2016) · Hepatology · doi:10.1002/hep.28456 · Cited by 319 · see citing works
“These mediators are mainly proinflammatory but can also be anti-inflammatory and are important in almost all inflammatory conditions, exerting their specific effects through IL-1Rs 1-10.((6)) They are also involved in the differentiation and function of many innate and lymphoid cells, direct many complex inflammatory…”
BackgroundInfluentialHematopoietic progenitor cells as integrative hubs for adaptation to and fine-tuning of inflammation
Chavakis, T., Mitroulis, I., & Hajishengallis, G. (2019) · Nature Immunology · doi:10.1038/s41590-019-0402-5 · Cited by 318 · see citing works
IL-18 cleavage triggers cardiac inflammation and fibrosis upon &bgr;-adrenergic insult
Xiao, H., Li, H., Wang, J., Zhang, J., Shen, J., An, X., Zhang, C., Wu, J.-M., Song, Y., Wang, X.-Y., et al. (2018) · European Heart Journal · doi:10.1093/eurheartj/ehx261 · Cited by 279 · see citing works
“We next examined IL-1b and IL-18, both are known to enhance expression of chemokines and adhesion molecules.(9) Pro-IL-1b and pro-IL-18 need to be converted to the mature and active form by inflammasomedependent cleavage.”
BackgroundSelected cytokine pathways in rheumatoid arthritis
Noack, M., & Miossec, P. (2017) · Seminars in Immunopathology · doi:10.1007/s00281-017-0619-z · Cited by 307 · see citing works
“IL-1, secreted mainly by macrophages, monocytes, and dendritic cells, was the first interleukin to be identified; it was described as a protein-inducing fever with two major proteins, IL-1α and IL-1β encoded by two distinct genes [64, 85, 90].”
BackgroundStructural Basis of IL-1 Family Cytokine Signaling
Fields, J. K., Günther, S., & Sundberg, E. J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01412 · Cited by 302 · see citing works
Vascular Endothelial Cells and Innate Immunity
Shao, Y., Saredy, J., Yang, W. Y., Sun, Y., Lu, Y., Saaoud, F., Drummer, C., Johnson, C., Xu, K., Jiang, X., et al. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.120.314330 · Cited by 302 · see citing works
The IL-1 cytokine family and its role in inflammation and fibrosis in the lung
Borthwick, L. A. (2016) · Seminars in Immunopathology · doi:10.1007/s00281-016-0559-z · Cited by 294 · see citing works
The dual roles of cytokines in Alzheimer’s disease: update on interleukins, TNF-α, TGF-β and IFN-γ
Zheng, C., Zhou, X.-W., & Wang, J.-Z. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0054-4 · Cited by 292 · see citing works
“IL-1 family [144] IL-1α = \ = or ↓ \ -889 C/T (rs1800587) T: ↑ * ↑ in EOAD Meta-analysis [145]”
IL-1 Family Members in Cancer; Two Sides to Every Story
Baker, K. J., Houston, A. M., & Brint, E. K. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01197 · Cited by 285 · see citing works
Interleukin-1 function and role in rheumatic disease
Schett, G. A., Dayer, J., & Manger, B. (2015) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2016.166 · Cited by 278 · see citing works
Inflammasome-dependent IL-1β release depends upon membrane permeabilisation
Martín‐Sánchez, F., Diamond, C. E., Zeitler, M., Gomez, A. I., Baroja‐Mazo, A., Bagnall, J., Spiller, D. G., White, M. H., Daniels, M. J. D., Mortellaro, A., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2015.176 · Cited by 279 · see citing works
“Interleukin-1β (IL-1β) is a proinflammatory cytokine that is central for host responses to infection.(1) IL-1β is produced as an inactive precursor called pro-IL-1β mainly by inflammatory cells of myeloid lineage.”
BackgroundIL-1 Family Cytokine Regulation of Vascular Permeability and Angiogenesis
Fahey, E., & Doyle, S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01426 · Cited by 276 · see citing works
Boutet, M., Bart, G., Penhoat, M. G., Amiaud, J., Brulin, B., Charrier, C., Morel, F., Lecron, J., Rolli‐Derkinderen, M., Bourreille, A., et al. (2015) · Clinical & Experimental Immunology · doi:10.1111/cei.12761 · Cited by 275 · see citing works
Colchicine in Cardiovascular Disease: In-Depth Review.
Deftereos, S. G., Beerkens, F., Shah, B., Γιαννόπουλος, Γ., Vrachatis, D. A., Giotaki, S. G., Siasos, G., Nicolas, J., Arnott, C. G., Patel, S. V., et al. (2022) · PubMed · doi:10.1161/circulationaha.121.056171 · Cited by 137 · see citing works
“The study demonstrated a higher number of patients with left ventricle thrombus in the colchicine group (18) than in the placebo group (6) at 5 days, a difference that was no longer observed at 3 months.”
Inflammation in epileptogenesis after traumatic brain injury
Webster, K. M., Sun, M., Crack, P. J., O'Brien, T. J., Shultz, S. R., & Semple, B. D. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0786-1 · Cited by 273 · see citing works
“, IL-1α and β) and 3 receptor antagonists [110], and amongst these the IL-1β isoform has been the most commonly studied in the brain injury and epilepsy settings.”
BackgroundOxidation of the alarmin IL-33 regulates ST2-dependent inflammation
Cohen, E. S., Scott, I. C., Majithiya, J. B., Rapley, L., Kemp, B., England, E., Rees, D. G., Overed-Sayer, C. L., Woods, J., Bond, N. J., et al. (2015) · Nature Communications · doi:10.1038/ncomms9327 · Cited by 271 · see citing works
Role of the NLRP3 inflammasome in autoimmune diseases
Li, Z., Guo, J., & Bi, L. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110542 · Cited by 268 · see citing works
Immune Mechanisms in Heart Failure
Zhang, Y., Bauersachs, J. K., & Langer, H. F. (2017) · European Journal of Heart Failure · doi:10.1002/ejhf.942 · Cited by 260 · see citing works
Inflammasomes in Tissue Damages and Immune Disorders After Trauma
Bortolotti, P., Faure, E., & Kipnis, É. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01900 · Cited by 259 · see citing works
Ballak, D. B., Stienstra, R., Tack, C. J., Dinarello, C. A., & van Diepen, J. A. (2015) · Cytokine · doi:10.1016/j.cyto.2015.05.005 · Cited by 256 · see citing works
“The role of IL-38, also ascribed with receptor antagonizing properties, appears to have anti-inflammatory properties largely unknown [21, 22].”
BackgroundModulation of learning and memory by cytokines: Signaling mechanisms and long term consequences
Donzis, E. J., & Tronson, N. C. (2014) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2014.08.008 · Cited by 254 · see citing works
“Interactions between IL-1b and other IL-1 family members (Garlanda et al., 2013) likely contribute the effects on memory.”
Targeting Interleukin-1β Reduces Leukocyte Production After Acute Myocardial Infarction
Sager, H. B., Heidt, T., Hulsmans, M., Dutta, P., Courties, G., Sebas, M., Wojtkiewicz, G. R., Tricot, B., Iwamoto, Y., Sun, Y., et al. (2015) · Circulation · doi:10.1161/circulationaha.115.016160 · Cited by 250 · see citing works
Schappe, M. S., Szteyn, K., Stremska, M. E., Mendu, S. K., Downs, T. K., Seegren, P. V., Mahoney, M. A., Dixit, S., Krupa, J. K., Stipes, E. J., et al. (2018) · Immunity · doi:10.1016/j.immuni.2017.11.026 · Cited by 251 · see citing works
“The secretion of potent inflammatory cytokines IL-1b and IL-18, however, also requires additional regulatory inputs from the inflammasomemachinery (Garlanda et al., 2013).”
BackgroundOf Inflammasomes and Alarmins: IL-1β and IL-1α in Kidney Disease
Anders, H. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016020177 · Cited by 251 · see citing works
P2X7 receptor and the NLRP3 inflammasome: Partners in crime
Pelegrı́n, P. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114385 · Cited by 241 · see citing works
Apoptosis and Necroptosis as Host Defense Strategies to Prevent Viral Infection
Orzalli, M. H., & Kagan, J. C. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.05.007 · Cited by 238 · see citing works
“In addition, expression of cytokines and the activation of inflammatory cell death pathways contribute to the recruitment of immune cells to the site of infection and promote adaptive immunity [4].”
BackgroundThe NLRP3 and Pyrin Inflammasomes: Implications in the Pathophysiology of Autoinflammatory Diseases
de Torre‐Minguela, C., Mesa-del-Castillo, P., & Pelegrı́n, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00043 · Cited by 239 · see citing works
NLRP3 inflammasome priming: A riddle wrapped in a mystery inside an enigma
McKee, C. M., & Coll, R. C. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr0720-513r · Cited by 236 · see citing works
The Role of Mitochondria in Inflammation: From Cancer to Neurodegenerative Disorders
Missiroli, S., Genovese, I., Perrone, M., Vezzani, B., Vitto, V. A. M., & Giorgi, C. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9030740 · Cited by 231 · see citing works
“cascades, such as the activation of nuclear factor NF-kB (nuclear factor kappa-light-chain-enhancer of activated B cells) or the cellular kinase c-Jun amino-terminal kinase (JNK) [12], and the release of proinflammatory cytokines, chemokines and adhesion molecules, thereby accelerating the inflammatory response [13].”
BackgroundSystematic assessment of long-read RNA-seq methods for transcript identification and quantification
Pardo-Palacios, F. J., Wang, D., Reese, F., Diekhans, M., Sala, S. C., Williams, B. A., Loveland, J. E., María, M. D., Adams, M. S., Balderrama-Gutierrez, G., et al. (2024) · Nature Methods · doi:10.1038/s41592-024-02298-3 · Cited by 252 · see citing works
“IL1B is an inflammatory cytokine, an amplifier of an immune response, involved in cell proliferation, differentiation and apoptosis 51 .”
Nakamura, K., Kassem, S., Cleynen, A., Chrétien, M., Guillerey, C., Putz, E. M., Bald, T., Förster, I., Vučković, S., Hill, G. R., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.02.007 · Cited by 232 · see citing works
IL-1R8 is a checkpoint in NK cells regulating anti-tumour and anti-viral activity
Molgora, M., Bonavita, E., Ponzetta, A., Riva, F., Barbagallo, M., Jaillon, S., Popović, B., Bernardini, G., Magrini, E. I., Gianni, F., et al. (2017) · Nature · doi:10.1038/nature24293 · Cited by 228 · see citing works
Fleischmann, R., Bliddal, H., Blanco, F., Schnitzer, T., Peterfy, C., Chen, S., Wang, L., Feng, S., Conaghan, P., Berenbaum, F., et al. (2019) · Arthritis & Rheumatology · doi:10.1002/art.40840 · Cited by 222 · see citing works
Harris, J., Lang, T., Thomas, J., Sukkar, M. B., Nabar, N. R., & Kehrl, J. H. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.02.013 · Cited by 224 · see citing works
Targeting innate immune pathways for cancer immunotherapy
Cao, L. L., & Kagan, J. C. (2023) · Immunity · doi:10.1016/j.immuni.2023.07.018 · Cited by 224 · see citing works
Zeinali, M., Rezaee, S. A., & Hosseinzadeh, H. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.06.003 · Cited by 219 · see citing works
ST2/IL-33-Dependent Microglial Response Limits Acute Ischemic Brain Injury
Yang, Y.-Y., Liu, H., Zhang, H., Ye, Q., Wang, J.-Y., Yang, B.-Y., Mao, L.-L., Zhu, W., Leak, R., Xiao, B., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3233-16.2017 · Cited by 188 · see citing works
“The expression of ST2 on T lymphocytes has been shown to drive the production of type-2 cytokines and is responsible for protective type-2 inflammatory responses during infections and tissue repair (Garlanda et al., 2013).”
Background
- Authors
- Garlanda, C., Dinarello, C. A., & Mantovani, A.
- Affiliations
- Radboud University Medical Center (NL)
- University of Milan (IT)
- Corresponding author
- Mantovani, Alberto
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 39
- Issue
- 6
- Pages
- 1003-1018
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC3933951
- OpenAlex
- W2145866317
- Cited by
- 1,945
- References
- 151
- Citations by year
- 2026: 80 · 2025: 118 · 2024: 136 · 2023: 122 · 2022: 168 · 2021: 172 · 2020: 202 · 2019: 165 · 2018: 194 · 2017: 192 · 2016: 171 · 2015: 156 · 2014: 66 · 2013: 1
- FWCI
- 11.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Radboud Repository (Radboud University) (submittedVersion)
- Funders
- European Research Council
- Associazione Italiana per la Ricerca sul Cancro
- National Institutes of Health (A115614, AR-45584)
- European Commission (FP7-HEALTH-2011- ADITEC 280873)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › IL-33, ST2, and ILC Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- interleukin-1 family, innate immunity, inflammation, IL-1 receptor family, interleukin-1 receptor antagonist, decoy receptor, IL-18, IL-33, IL-36, IL-37, IL-38, IL1RAP, SIGIRR, negative regulation of cytokine signaling, lymphocyte differentiation, innate and adaptive immunity
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Immunity, Innate, Interleukin-1, Interleukins, Ligands, Receptors, Interleukin-1, Adaptive Immunity
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