Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

IL-1 Family

  • Diana Boraschi
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101688

Synonyms

Historical Background

The family of IL-1 cytokines (IL-1F) encompasses eleven proteins that share similar structure and signaling mode (similar receptors, similar signaling pathways) (Dinarello 2013). IL-1F cytokines are involved in initiation as well as regulation of inflammation and are central players of innate immunity.

Studies started in the 1940s with the first identification of factors able to induce fever (pyrexin, endogenous pyrogen, leukocytic pyrogen) and developed until the cloning of the first cytokines of the family (IL-1α and IL-1β) in the 1980s. After that, studies bloomed and at present eleven members of the family have been identified, and the function of several of them clarified.

Several IL-1F cytokines are synthesized as long precursors, of which the C-terminal domain is the active secreted cytokine. Secretion takes place by nonconventional mechanisms that are still partly unknown.

In many cases, the procytokine forms have an...

This is a preview of subscription content, log in to check access.

References

  1. Arend WP, Guthridge CJ. Biological role of interleukin-1 receptor antagonist isoforms. Ann Rheum Dis. 2000;59(s1):i60–4.PubMedPubMedCentralCrossRefGoogle Scholar
  2. Baldari CT, Telford JL. The intracellular precursor of IL-1β is associated with microtubules in activated U937 cells. J Immunol. 1989;142:785–91.PubMedGoogle Scholar
  3. Boraschi D, Dinarello CA. IL-18 and autoimmunity. Eur Cytokine Netw. 2006;17:224–52.PubMedGoogle Scholar
  4. Boraschi D, Tagliabue A. The Interleukin-1 receptor family. Sem. Immunol. 2013;25:394–407.CrossRefGoogle Scholar
  5. Boraschi D, Lucchesi D, Hainzl S, Leitner M, Maier E, Mangelberger D, et al. IL- 37: a new anti-inflammatory cytokine of the IL-1 family. Eur Cytokine Netw. 2011;22:127–47.PubMedGoogle Scholar
  6. Boraschi D, Nencioni L, Villa L, Censini S, Bossù P, Ghiara P, et al. In vivo stimulation and restoration of the immune response by the noninflammatory fragment 163.171 of human IL-1β. J Exp Med. 1988;168:675–86.CrossRefPubMedGoogle Scholar
  7. Costelloe C, Watson M, Murphy A, McQuillan K, Loscher C, Armstrong ME, et al. IL-1F5 mediates anti-inflammatory activity in the brain through induction of IL-4 following interaction with SIGIRR/TIR8. J Neurochem. 2008;105:1960–9.CrossRefPubMedGoogle Scholar
  8. Dinarello CA. Overview of the IL-1 family of ligands and receptors. Semin Immunol. 2013;25:389–93.CrossRefPubMedGoogle Scholar
  9. Dinarello CA, Arend W, Sims J, Smith D, Blumberg H, O’Neill L, et al. IL-1 family nomenclature. Nat Immunol. 2010;11:973.PubMedPubMedCentralCrossRefGoogle Scholar
  10. Dinarello CA, Bufler P. Interleukin-37. Semin Immunol. 2013;25:466–8.CrossRefPubMedGoogle Scholar
  11. Dinarello CA, van der Meer JWM. Treating inflammation by blocking interleukin-1 in humans. Semin Immunol. 2013;25:469–84.PubMedPubMedCentralCrossRefGoogle Scholar
  12. Gresnigt MS, van de Veerdonk FL. Biology of IL-36 cytokines and their role in disease. Semin Immunol. 2013;25:458–65.CrossRefPubMedGoogle Scholar
  13. Joosten LAB, Netea MG, Dinarello CA. Inteleukin-1β in innate inflammation, autophagy and immunity. Semin Immunol. 2013;25:416–24.CrossRefPubMedGoogle Scholar
  14. Lin H et al. Cloning and characterization of IL-1HY2, a novel interleukin-1 family member. J Biol Chem. 2001;276:20, 597–602PubMedCrossRefGoogle Scholar
  15. Martin MU. IL-33 and the IL-33 receptor complex. Semin Immunol. 2013;25:449–57.CrossRefPubMedGoogle Scholar
  16. Martin NT, Martin MU. Interleukin 33 is a guardian of barriers and a local alarmin. Nat Immunol. 2016;17:122–31.CrossRefPubMedGoogle Scholar
  17. Mora J, Schlemmer A, Wittig I, Richter F, Putyrski M, Frank A-C, et al. Interleukin-38 is released from apoptotic cells to limit inflammatory macrophage responses. J Mol Cell Biol. 2016;8:426–38.CrossRefGoogle Scholar
  18. Lang D, Knop J, Wesche H, Rafftseder U, Kurrle R, Boraschi D, Martin MU. The type II interleukin-1 receptor interacts with the interleukin-1 accessory protein: a novel mechanism of regulation of the interleukin-1 responsiveness. J Immunol. 1998;161:6871–7.PubMedGoogle Scholar
  19. Nold-Petry CA, Lo CY, Rudloff I, Elgass KD, Li S, Gantier MP, et al. IL-37 requires the receptors IL-18Rα and IL-1R8 (SIGIRR) to carry out its multifaceted anti-inflammatory program upon innate signal transduction. Nat Immunol. 2015;16:354–65.CrossRefPubMedGoogle Scholar
  20. Novick D, Kim S, Kaplanski G, Dinarello CA. Interleukin-18, more than a Th1 cytokine. Semin Immunol. 2013;25:439–48.CrossRefPubMedGoogle Scholar
  21. Rider P, Carmi Y, Voronov E, Apte RN. Interleukin-1α. Semin Immunol. 2013;25:430–8.CrossRefPubMedGoogle Scholar
  22. Towne JE, Garka KE, Renshaw BR, Virca GD, Sims JE. Interleukin (IL)-1F6, IL-1F8, and IL-1F9 signal through IL-1Rrp2 and IL-1RAcP to activate the pathway leading to NF-κB and MAPKs. J Biol Chem. 2004;279:13677–88.CrossRefPubMedGoogle Scholar
  23. Towne JE, Renshaw BR, Douangpanya J, Lipsky BP, Shen M, Gabel CA, et al. Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36alpha, IL- 36beta, and IL-36gamma) or antagonist (IL-36Ra) activity. J Biol Chem. 2011;286:42594–602.PubMedPubMedCentralCrossRefGoogle Scholar
  24. van de Veerdonk FL, Stoeckman AK, Wu G, Boeckermann AN, Azam T, Netea MG, et al. IL-38 binds to the IL-36 receptor and has biological effects on immune cells similar to IL-36 receptor antagonist. Proc Natl Acad Sci USA. 2012;109:3001–5.PubMedPubMedCentralCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Institute of Protein BiochemistryNational Research CouncilNaplesItaly