The interleukin (IL)-1 cytokine family - Balance between agonists and antagonists in inflammatory diseases

Cytokine

Volumn 76, Issue 1, 2015, Pages 25-37

  Palomo, Jennifer ^a   Dietrich, Damien ^a   Martin, Praxedis ^a   Palmer, Gaby ^a   Gabay, Cem ^a  

^a UNIVERSITY OF GENEVA MEDICAL SCHOOL   (Switzerland)

Author keywords

Autoinflammatory disorders; Cytokine antagonists; Inflammasome; Interleukin 1

Indexed keywords

IMMUNOGLOBULIN; INTERLEUKIN 1; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 1 RECEPTOR BLOCKING AGENT; INTERLEUKIN 1 RECEPTOR TYPE II; INTERLEUKIN 18; INTERLEUKIN 18 BINDING PROTEIN; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; INTERLEUKIN 33; INTERLEUKIN 36 RECEPTOR BLOCKING AGENT; INTERLEUKIN 36ALPHA; INTERLEUKIN 36BETA; INTERLEUKIN 36GAMMA; INTERLEUKIN 37; INTERLEUKIN 38; SINGLE IMMUNOGLOBULIN INTERLEUKIN 1 RECEPTOR RELATED MOLECULE; UNCLASSIFIED DRUG; INTERLEUKIN DERIVATIVE;

ADULT RESPIRATORY DISTRESS SYNDROME; AMYLOIDOSIS; ATHEROSCLEROSIS; ATOPIC DERMATITIS; CLINICAL TRIAL (TOPIC); CONJUNCTIVITIS; CROHN DISEASE; CYTOKINE PRODUCTION; DNA MODIFICATION; ENDOTOXEMIA; FAMILIAL MEDITERRANEAN FEVER; GENE MUTATION; HEPATITIS; HUMAN; INFLAMMATION; INFLAMMATORY DISEASE; INTRACELLULAR SIGNALING; LISTERIOSIS; MENINGITIS; NEUTROPHILIA; NONHUMAN; OSTEITIS; PATHOGENESIS; PERIODONTITIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PSORIASIS; RECEPTOR BINDING; RESPIRATORY TRACT INFLAMMATION; REVIEW; RHEUMATOID ARTHRITIS; SEPSIS; SPLENOMEGALY; THROMBOCYTOPENIA; ULCERATIVE COLITIS; AGONISTS; ANIMAL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; IMMUNOLOGY; METABOLISM; MOUSE; SIGNAL TRANSDUCTION;

ANIMALS; CASPASE 1; HUMANS; INFLAMMATION; INTERLEUKIN-1; INTERLEUKIN-18; INTERLEUKIN-1BETA; INTERLEUKIN-33; INTERLEUKINS; MICE; RECEPTORS, INTERLEUKIN-1; SIGNAL TRANSDUCTION;

EID: 84941742533     PISSN: 10434666     EISSN: 10960023     Source Type: Journal    
DOI: 10.1016/j.cyto.2015.06.017     Document Type: Review

References (206)

1. Garlanda C., Dinarello C.A., Mantovani A. The interleukin-1 family: back to the future. Immunity 2013, 39:1003-1018.
2. Gabay C., Lamacchia C., Palmer G. IL-1 pathways in inflammation and human diseases. Nat. Rev. Rheumatol. 2010, 6:232-241.
3. Guma M., Ronacher L., Liu-Bryan R., Takai S., Karin M., Corr M. Caspase 1-independent activation of interleukin-1beta in neutrophil-predominant inflammation. Arthritis. Rheum. 2009, 60:3642-3650.
4. Joosten L.A., Netea M.G., Fantuzzi G., Koenders M.I., Helsen M.M., Sparrer H., et al. Inflammatory arthritis in caspase 1 gene-deficient mice. contribution of proteinase 3 to caspase 1-independent production of bioactive interleukin-1beta. Arthritis. Rheum. 2009, 60:3651-3662.
5. Towne J.E., Renshaw B.R., Douangpanya J., Lipsky B.P., Shen M., Gabel C.A., 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, 286:42594-42602.
6. Afonina I.S., Tynan G.A., Logue S.E., Cullen S.P., Bots M., Luthi A.U., et al. Granzyme B-dependent proteolysis acts as a switch to enhance the proinflammatory activity of IL-1alpha. Mol. Cell. 2011, 44:265-278.
7. Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., Monsarrat B., Girard J.P., et al. IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G. Proc. Natl. Acad. Sci. U S A. 2012, 109:1673-1678.
8. Lefrancais E., Duval A., Mirey E., Roga S., Espinosa E., Cayrol C., et al. Central domain of IL-33 is cleaved by mast cell proteases for potent activation of group-2 innate lymphoid cells. Proc. Natl. Acad. Sci. U S A. 2014, 111:15502-15507.
9. Born T.L., Smith D.E., Garka K.E., Renshaw B.R., Bertles J.S., Sims J.E. Identification and characterization of two members of a novel class of the interleukin-1 receptor (IL-1R) family. Delineation of a new class of IL-1R-related proteins based on signaling. J. Biol. Chem. 2000, 275:41528.
10. Carrie A., Jun L., Bienvenu T., Vinet M.C., McDonell N., Couvert P., et al. A new member of the IL-1 receptor family highly expressed in hippocampus and involved in X-linked mental retardation. Nat. Genet. 1999, 23:25-31.
11. Eisenberg S.P., Brewer M.T., Verderber E., Heimdal P., Brandhuber B.J., Thompson R.C. Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanism. Proc. Natl. Acad. Sci. U S A. 1991, 88:5232-5236.
12. Dripps D.J., Brandhuber B.J., Thompson R.C., Eisenberg S.P. Interleukin-1 (IL-1) receptor antagonist binds to the 80-kDa IL-1 receptor but does not initiate IL-1 signal transduction. J. Biol. Chem. 1991, 266:10331-10336.
13. Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E., Akeson A., et al. A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. Nature 1997, 386:194-200.
14. Wang D., Zhang S., Li L., Liu X., Mei K., Wang X. Structural insights into the assembly and activation of IL-1beta with its receptors. Nat. Immunol. 2010, 11:905-911.
15. Arend W.P., Welgus H.G., Thompson R.C., Eisenberg S.P. Biological properties of recombinant human monocyte-derived interleukin 1 receptor antagonist. J. Clin. Invest. 1990, 85:1694-1697.
16. La E., Rundhaug J.E., Fischer S.M. Role of intracellular interleukin-1 receptor antagonist in skin carcinogenesis. Mol. Carcinog. 2001, 30:218-223.
17. Garat C., Arend W.P. Intracellular IL-1Ra type 1 inhibits IL-1-induced IL-6 and IL-8 production in Caco-2 intestinal epithelial cells through inhibition of p38 mitogen-activated protein kinase and NF-kappaB pathways. Cytokine 2003, 23:31-40.
18. Merhi-Soussi F., Berti M., Wehrle-Haller B., Gabay C. Intracellular interleukin-1 receptor antagonist type 1 antagonizes the stimulatory effect of interleukin-1 alpha precursor on cell motility. Cytokine 2005, 32:163-170.
19. Vecile E., Dobrina A., Salloum F.N., Van Tassell B.W., Falcione A., Gustini E., et al. Intracellular function of interleukin-1 receptor antagonist in ischemic cardiomyocytes. PLoS ONE 2013, 8:e53265.
20. Parsons P.E., Moss M., Vannice J.L., Moore E.E., Moore F.A., Repine J.E. Circulating IL-1ra and IL-10 levels are increased but do not predict the development of acute respiratory distress syndrome in at-risk patients. Am. J. Respir. Crit. Care Med. 1997, 155:1469-1473.
21. Rogy M.A., Coyle S.M., Oldenburg H.S., Rock C.S., Barie P.S., Van Zee K.J., et al. Persistently elevated soluble tumor necrosis factor receptor and interleukin-1 receptor antagonist levels in critically ill patients. J. Am. Coll. Surg. 1994, 178:132-138.
22. Jouvenne P., Vannier E., Dinarello C.A., Miossec P. Elevated levels of soluble interleukin-1 receptor type II and interleukin-1 receptor antagonist in patients with chronic arthritis: correlations with markers of inflammation and joint destruction. Arthritis. Rheum. 1998, 41:1083-1089.
23. Hyams J.S., Fitzgerald J.E., Wyzga N., Treem W.R., Justinich C.J., Kreutzer D.L. Characterization of circulating interleukin-1 receptor antagonist expression in children with inflammatory bowel disease. Dig. Dis. Sci. 1994, 39:1893-1899.
24. Propst A., Propst T., Herold M., Vogel W., Judmaier G. Interleukin-1 receptor antagonist in differential diagnosis of inflammatory bowel diseases. Eur. J. Gastroenterol. Hepatol. 1995, 7:1031-1036.
25. Firestein G.S., Berger A.E., Tracey D.E., Chosay J.G., Chapman D.L., Paine M.M., et al. IL-1 receptor antagonist protein production and gene expression in rheumatoid arthritis and osteoarthritis synovium. J. Immunol. 1992, 149:1054-1062.
26. McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D., Brunton L.L., et al. A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types. EMBO J. 1991, 10:2821-2832.
27. Groves R.W., Giri J., Sims J., Dower S.K., Kupper T.S. Inducible expression of type 2 IL-1 receptors by cultured human keratinocytes. Implications for IL-1-mediated processes in epidermis. J. Immunol. 1995, 154:4065-4072.
28. Tran D.Q., Andersson J., Hardwick D., Bebris L., Illei G.G., Shevach E.M. Selective expression of latency-associated peptide (LAP) and IL-1 receptor type I/II (CD121a/CD121b) on activated human FOXP3+ regulatory T cells allows for their purification from expansion cultures. Blood 2009, 113:5125-5133.
29. Mercer F., Kozhaya L., Unutmaz D. Expression and function of TNF and IL-1 receptors on human regulatory T cells. PLoS ONE 2010, 5:e8639.
30. Spriggs M.K., Nevens P.J., Grabstein K., Dower S.K., Cosman D., Armitage R.J., et al. Molecular characterization of the interleukin-1 receptor (IL-1R) on monocytes and polymorphonuclear cells. Cytokine 1992, 4:90-95.
31. Agis H., Fureder W., Bankl H.C., Kundi M., Sperr W.R., Willheim M., et al. Comparative immunophenotypic analysis of human mast cells, blood basophils and monocytes. Immunology 1996, 87:535-543.
32. Rhyne J.A., Mizel S.B., Taylor R.G., Chedid M., McCall C.E. Characterization of the human interleukin 1 receptor on human polymorphonuclear leukocytes. Clin. Immunol. Immunopathol. 1988, 48:354-361.
33. Colotta F., Re F., Muzio M., Bertini R., Polentarutti N., Sironi M., et al. Interleukin-1 type II receptor: a decoy target for IL-1 that is regulated by IL-4. Science 1993, 261:472-475.
34. Re F., Muzio M., De Rossi M., Polentarutti N., Giri J.G., Mantovani A., et al. The type II "receptor" as a decoy target for interleukin 1 in polymorphonuclear leukocytes: characterization of induction by dexamethasone and ligand binding properties of the released decoy receptor. J. Exp. Med. 1994, 179:739-743.
35. Gabellec M.M., Griffais R., Fillion G., Haour F. Interleukin-1 receptors type I and type II in the mouse brain: kinetics of mRNA expressions after peripheral administration of bacterial lipopolysaccharide. J. Neuroimmunol. 1996, 66:65-70.
36. Bellehumeur C., Blanchet J., Fontaine J.Y., Bourcier N., Akoum A. Interleukin 1 regulates its own receptors in human endometrial cells via distinct mechanisms. Hum. Reprod. 2009, 24:2193-2204.
37. Zhang X.H., Tian Z., Lei W., Zhao Z.A., Wang T.S., Yang Z.M. Differential expression of interleukin 1 receptor type II during mouse decidualization. Reprod. Sci. 2012, 19:923-931.
38. Martin P., Palmer G., Vigne S., Lamacchia C., Rodriguez E., Talabot-Ayer D., et al. Mouse neutrophils express the decoy type 2 interleukin-1 receptor (IL-1R2) constitutively and in acute inflammatory conditions. J. Leukoc. Biol. 2013, 94:791-802.
39. Shimizu K., Nakajima A., Sudo K., Liu Y., Mizoroki A., Ikarashi T., et al. IL-1 receptor type 2 suppresses collagen-induced arthritis by inhibiting IL-1 signal on macrophages. J. Immunol. 2015, 194:3156-3168.
40. Symons J.A., Young P.R., Duff G.W. Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist. Proc. Natl. Acad. Sci. U S A. 1995, 92:1714-1718.
41. Burger D., Chicheportiche R., Giri J.G., Dayer J.M. The inhibitory activity of human interleukin-1 receptor antagonist is enhanced by type II interleukin-1 soluble receptor and hindered by type I interleukin-1 soluble receptor. J. Clin. Invest. 1995, 96:38-41.
42. Colotta F., Dower S.K., Sims J.E., Mantovani A. The type II 'decoy' receptor: a novel regulatory pathway for interleukin 1. Immunol. Today. 1994, 15:562-566.
43. Zheng Y., Humphry M., Maguire J.J., Bennett M.R., Clarke M.C. Intracellular interleukin-1 receptor 2 binding prevents cleavage and activity of interleukin-1alpha, controlling necrosis-induced sterile inflammation. Immunity 2013, 38:285-295.
44. Reddy P., Slack J.L., Davis R., Cerretti D.P., Kozlosky C.J., Blanton R.A., et al. Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme. J. Biol. Chem. 2000, 275:14608-14614.
45. Lorenzen I., Lokau J., Dusterhoft S., Trad A., Garbers C., Scheller J., et al. The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II. FEBS Lett. 2012, 586:1093-1100.
46. Cui X., Rouhani F.N., Hawari F., Levine S.J. Shedding of the type II IL-1 decoy receptor requires a multifunctional aminopeptidase, aminopeptidase regulator of TNF receptor type 1 shedding. J. Immunol. 2003, 171:6814-6819.
47. Kuhn P.H., Marjaux E., Imhof A., De Strooper B., Haass C., Lichtenthaler S.F. Regulated intramembrane proteolysis of the interleukin-1 receptor II by alpha-, beta-, and gamma-secretase. J. Biol. Chem. 2007, 282:11982-11995.
48. Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., De Souza E.B. Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA. J. Biol. Chem. 1996, 271:20965-20972.
49. Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G. Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex. J. Biol. Chem. 1995, 270:13757-13765.
50. Jensen L.E., Muzio M., Mantovani A., Whitehead A.S. IL-1 signaling cascade in liver cells and the involvement of a soluble form of the IL-1 receptor accessory protein. J. Immunol. 2000, 164:5277-5286.
51. Smith D.E., Hanna R., Della F., Moore H., Chen H., Farese A.M., et al. The soluble form of IL-1 receptor accessory protein enhances the ability of soluble type II IL-1 receptor to inhibit IL-1 action. Immunity 2003, 18:87-96.
52. Colotta F., Saccani S., Giri J.G., Dower S.K., Sims J.E., Introna M., et al. Regulated expression and release of the IL-1 decoy receptor in human mononuclear phagocytes. J. Immunol. 1996, 156:2534-2541.
53. Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J., et al. Elevated levels of shed type II IL-1 receptor in sepsis. Potential role for type II receptor in regulation of IL-1 responses. J. Immunol. 1994, 153:5802-5809.
54. Colotta F., Orlando S., Fadlon E.J., Sozzani S., Matteucci C., Mantovani A. Chemoattractants induce rapid release of the interleukin 1 type II decoy receptor in human polymorphonuclear cells. J. Exp. Med. 1995, 181:2181-2186.
55. Orlando S., Matteucci C., Fadlon E.J., Buurman W.A., Bardella M.T., Colotta F., et al. TNF-alpha, unlike other pro- and anti-inflammatory cytokines, induces rapid release of the IL-1 type II decoy receptor in human myelomonocytic cells. J. Immunol. 1997, 158:3861-3868.
56. Daun J.M., Ball R.W., Burger H.R., Cannon J.G. Aspirin-induced increases in soluble IL-1 receptor type II concentrations in vitro and in vivo. J. Leukoc. Biol. 1999, 65:863-866.
57. Penton-Rol G., Orlando S., Polentarutti N., Bernasconi S., Muzio M., Introna M., et al. Bacterial lipopolysaccharide causes rapid shedding, followed by inhibition of mRNA expression, of the IL-1 type II receptor, with concomitant up-regulation of the type I receptor and induction of incompletely spliced transcripts. J. Immunol. 1999, 162:2931-2938.
58. Kovach M.A., Stringer K.A., Bunting R., Wu X., San Mateo L., Newstead M.W., et al. Microarray analysis identifies IL-1 receptor type 2 as a novel candidate biomarker in patients with acute respiratory distress syndrome. Respir. Res. 2015, 16:29.
59. Pruitt J.H., Welborn M.B., Edwards P.D., Harward T.R., Seeger J.W., Martin T.D., et al. Increased soluble interleukin-1 type II receptor concentrations in postoperative patients and in patients with sepsis syndrome. Blood 1996, 87:3282-3288.
60. Arend W.P., Malyak M., Smith M.F., Whisenand T.D., Slack J.L., Sims J.E., et al. Binding of IL-1 alpha, IL-1 beta, and IL-1 receptor antagonist by soluble IL-1 receptors and levels of soluble IL-1 receptors in synovial fluids. J. Immunol. 1994, 153:4766-4774.
61. Pietruczuk A., Swierzbinska R., Pancewicz S., Pietruczuk M., Hermanowska-Szpakowicz T. Serum levels of interleukin-18 (IL-18), interleukin-1beta (IL-1beta), its soluble receptor sIL-1RII and C-reactive protein (CRP) in patients with Lyme arthritis. Infection 2006, 34:158-162.
62. Muller B., Peri G., Doni A., Perruchoud A.P., Landmann R., Pasqualini F., et al. High circulating levels of the IL-1 type II decoy receptor in critically ill patients with sepsis: association of high decoy receptor levels with glucocorticoid administration. J. Leukoc. Biol. 2002, 72:643-649.
63. Pou J., Martinez-Gonzalez J., Rebollo A., Rodriguez C., Rodriguez-Calvo R., Martin-Fuentes P., et al. Type II interleukin-1 receptor expression is reduced in monocytes/macrophages and atherosclerotic lesions. Biochim. Biophys. Acta 2011, 1811:556-563.
64. Akoum A., Lawson C., McColl S., Villeneuve M. Ectopic endometrial cells express high concentrations of interleukin (IL)-8 in vivo regardless of the menstrual cycle phase and respond to oestradiol by up-regulating IL-1-induced IL-8 expression in vitro. Mol. Hum. Reprod. 2001, 7:859-866.
65. Kharfi A., Boucher A., Akoum A. Abnormal interleukin-1 receptor type II gene expression in the endometrium of women with endometriosis. Biol. Reprod. 2002, 66:401-406.
66. Bossu P., Visconti U., Ruggiero P., Macchia G., Muda M., Bertini R., et al. Transfected type II interleukin-1 receptor impairs responsiveness of human keratinocytes to interleukin-1. Am. J. Pathol. 1995, 147:1852-1861.
67. Dawson J., Engelhardt P., Kastelic T., Cheneval D., MacKenzie A., Ramage P. Effects of soluble interleukin-1 type II receptor on rabbit antigen-induced arthritis: clinical, biochemical and histological assessment. Rheumatology 1999, 38:401-406.
68. Bessis N., Guery L., Mantovani A., Vecchi A., Sims J.E., Fradelizi D., et al. The type II decoy receptor of IL-1 inhibits murine collagen-induced arthritis. Eur. J. Immunol. 2000, 30:867-875.
69. Rauschmayr T., Groves R.W., Kupper T.S. Keratinocyte expression of the type 2 interleukin 1 receptor mediates local and specific inhibition of interleukin 1-mediated inflammation. Proc. Natl. Acad. Sci. U S A. 1997, 94:5814-5819.
70. Simeoni E., Dudler J., Fleury S., Li J., Pagnotta M., Pascual M., et al. Gene transfer of a soluble IL-1 type 2 receptor-Ig fusion protein improves cardiac allograft survival in rats. Euro. J. Cardio-thoracic Surg.: Official J. Euro. Assoc. Cardio-thoracic Surg. 2007, 31:222-228.
71. Jea Calwell, Results of a phase 1 safety and pharmacokinetic study of interleukin-1 receptor in rheumatoid arthritis, in: Proc Eur League against Rheum Abstract FR10098, 2002.
72. Dinarello C.A., Simon A., van der Meer J.W. Treating inflammation by blocking interleukin-1 in a broad spectrum of diseases. Nat. Rev. Drug Discov. 2012, 11:633-652.
73. Novick D., Kim S.H., Fantuzzi G., Reznikov L.L., Dinarello C.A., Rubinstein M. Interleukin-18 binding protein: a novel modulator of the Th1 cytokine response. Immunity 1999, 10:127-136.
74. Kim S.H., Eisenstein M., Reznikov L., Fantuzzi G., Novick D., Rubinstein M., et al. Structural requirements of six naturally occurring isoforms of the IL-18 binding protein to inhibit IL-18. Proc. Natl. Acad. Sci. U S A. 2000, 97:1190-1195.
75. Muhl H., Kampfer H., Bosmann M., Frank S., Radeke H., Pfeilschifter J. Interferon-gamma mediates gene expression of IL-18 binding protein in nonleukocytic cells. Biochem. Biophys. Res. Commun. 2000, 267:960-963.
76. Paulukat J., Bosmann M., Nold M., Garkisch S., Kampfer H., Frank S., et al. Expression and release of IL-18 binding protein in response to IFN-gamma. J. Immunol. 2001, 167:7038-7043.
77. Wittmann M., Doble R., Bachmann M., Pfeilschifter J., Werfel T., Muhl H. IL-27 Regulates IL-18 binding protein in skin resident cells. PLoS ONE 2012, 7:e38751.
78. Corbaz A., ten Hove T., Herren S., Graber P., Schwartsburd B., Belzer I., et al. IL-18-binding protein expression by endothelial cells and macrophages is up-regulated during active Crohn's disease. J. Immunol. 2002, 168:3608-3616.
79. Bergers G., Reikerstorfer A., Braselmann S., Graninger P., Busslinger M. Alternative promoter usage of the Fos-responsive gene Fit-1 generates mRNA isoforms coding for either secreted or membrane-bound proteins related to the IL-1 receptor. EMBO J. 1994, 13:1176-1188.
80. Hayakawa H., Hayakawa M., Kume A., Tominaga S. Soluble ST2 blocks interleukin-33 signaling in allergic airway inflammation. J. Biol. Chem. 2007, 282:26369-26380.
81. Palmer G., Lipsky B.P., Smithgall M.D., Meininger D., Siu S., Talabot-Ayer D., et al. The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33. Cytokine 2008, 42:358-364.
82. Iwahana H., Yanagisawa K., Ito-Kosaka A., Kuroiwa K., Tago K., Komatsu N., et al. Different promoter usage and multiple transcription initiation sites of the interleukin-1 receptor-related human ST2 gene in UT-7 and TM12 cells. Eur. J. Biochem. 1999, 264:397-406.
83. Lipsky B.P., Toy D.Y., Swart D.A., Smithgall M.D., Smith D. Deletion of the ST2 proximal promoter disrupts fibroblast-specific expression but does not reduce the amount of soluble ST2 in circulation. Eur. J. Immunol. 2012, 42:1863-1869.
84. Shah R.V., Januzzi J.L. ST2: a novel remodeling biomarker in acute and chronic heart failure. Curr. Heart Fail. Rep. 2010, 7:9-14.
85. Ishikawa S., Shimizu M., Ueno K., Sugimoto N., Yachie A. Soluble ST2 as a marker of disease activity in systemic juvenile idiopathic arthritis. Cytokine 2013, 62:272-277.
86. Carrier Y., Ma H.L., Ramon H.E., Napierata L., Small C., O'Toole M., et al. Inter-regulation of Th17 cytokines and the IL-36 cytokines in vitro and in vivo: implications in psoriasis pathogenesis. J. Invest. Dermatol. 2011, 131:2428-2437.
87. Lian L.H., Milora K.A., Manupipatpong K.K., Jensen L.E. The double-stranded RNA analogue polyinosinic-polycytidylic acid induces keratinocyte pyroptosis and release of IL-36gamma. J. Invest. Dermatol. 2012, 132:1346-1353.
88. Debets R., Timans J.C., Homey B., Zurawski S., Sana T.R., Lo S., et al. Two novel IL-1 family members, IL-1 delta and IL-1 epsilon, function as an antagonist and agonist of NF-kappa B activation through the orphan IL-1 receptor-related protein 2. J. Immunol. 2001, 167:1440-1446.
89. Gunther S., Sundberg E.J. Molecular determinants of agonist and antagonist signaling through the IL-36 receptor. J. Immunol. 2014, 193:921-930.
90. Thomassen E., Renshaw B.R., Sims J.E. IDENTIFICATION AND CHARACTERIZATION OF SIGIRR, A MOLECULE REPRESENTING A NOVEL SUBTYPE OF THE IL-1R SUPERFAMILY. Cytokine 1999, 11:389-399.
91. Polentarutti N., Rol G.P., Muzio M., Bosisio D., Camnasio M., Riva F., et al. Unique pattern of expression and inhibition of IL-1 signaling by the IL-1 receptor family member TIR8/SIGIRR. Eur. Cytokine Netw. 2003, 14:211-218.
92. Wald D., Qin J., Zhao Z., Qian Y., Naramura M., Tian L., et al. SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling. Nat. Immunol. 2003, 4:920-927.
93. Garlanda C., Riva F., Polentarutti N., Buracchi C., Sironi M., De Bortoli M., et al. Intestinal inflammation in mice deficient in Tir8, an inhibitory member of the IL-1 receptor family. Proc. Natl. Acad. Sci. U S A. 2004, 101:3522-3526.
94. Kadota C., Ishihara S., Aziz M.M., Rumi M.A., Oshima N., Mishima Y., et al. Down-regulation of single immunoglobulin interleukin-1R-related molecule (SIGIRR)/TIR8 expression in intestinal epithelial cells during inflammation. Clin. Exp. Immunol. 2010, 162:348-361.
95. Ueno-Shuto K., Kato K., Tasaki Y., Sato M., Sato K., Uchida Y., et al. Lipopolysaccharide decreases single immunoglobulin interleukin-1 receptor-related molecule (SIGIRR) expression by suppressing specificity protein 1 (Sp1) via the Toll-like receptor 4 (TLR4)-p38 pathway in monocytes and neutrophils. J. Biol. Chem. 2014, 289:18097-18109.
96. Costelloe C., Watson M., Murphy A., McQuillan K., Loscher C., Armstrong M.E., et al. IL-1F5 mediates anti-inflammatory activity in the brain through induction of IL-4 following interaction with SIGIRR/TIR8. J. Neurochem. 2008, 105:1960-1969.
97. Bulek K., Swaidani S., Qin J., Lu Y., Gulen M.F., Herjan T., et al. The essential role of single Ig IL-1 receptor-related molecule/Toll IL-1R8 in regulation of Th2 immune response. J. Immunol. 2009, 182:2601-2609.
98. Li S., Neff C.P., Barber K., Hong J., Luo Y., Azam T., et al. Extracellular forms of IL-37 inhibit innate inflammation in vitro and in vivo but require the IL-1 family decoy receptor IL-1R8. Proc. Natl. Acad. Sci. U S A. 2015, 112:2497-2502.
99. Nold-Petry C.A., Lo C.Y., Rudloff I., Elgass K.D., Li S., Gantier M.P., et al. IL-37 requires the receptors IL-18Ralpha and IL-1R8 (SIGIRR) to carry out its multifaceted anti-inflammatory program upon innate signal transduction. Nat. Immunol. 2015, 16:354-365.
100. Lunding L., Webering S., Vock C., Schroder A., Raedler D., Schaub B., et al. IL-37 requires IL-18Ralpha and SIGIRR/IL-1R8 to diminish allergic airway inflammation in mice. Allergy 2015, 70:366-373.
101. Qin J., Qian Y., Yao J., Grace C., Li X. SIGIRR inhibits interleukin-1 receptor- and toll-like receptor 4-mediated signaling through different mechanisms. J. Biol. Chem. 2005, 280:25233-25241.
102. Gong J., Wei T., Stark R.W., Jamitzky F., Heckl W.M., Anders H.J., et al. Inhibition of Toll-like receptors TLR4 and 7 signaling pathways by SIGIRR: a computational approach. J. Struct. Biol. 2010, 169:323-330.
103. Lech M., Garlanda C., Mantovani A., Kirschning C.J., Schlondorff D., Anders H.J. Different roles of TiR8/Sigirr on toll-like receptor signaling in intrarenal antigen-presenting cells and tubular epithelial cells. Kidney Int. 2007, 72:182-192.
104. Watson M.B., Costello D.A., Carney D.G., McQuillan K., Lynch M.A. SIGIRR modulates the inflammatory response in the brain. Brain. Behav. Immun. 2010, 24:985-995.
105. Lech M., Avila-Ferrufino A., Allam R., Segerer S., Khandoga A., Krombach F., et al. Resident dendritic cells prevent postischemic acute renal failure by help of single Ig IL-1 receptor-related protein. J. Immunol. 2009, 183:4109-4118.
106. Noris M., Cassis P., Azzollini N., Cavinato R., Cugini D., Casiraghi F., et al. The Toll-IL-1R member Tir8/SIGIRR negatively regulates adaptive immunity against kidney grafts. J. Immunol. 2009, 183:4249-4260.
107. Leemans J.C., Butter L.M., Teske G.J., Stroo I., Pulskens W.P., Florquin S. The toll interleukin-1 receptor (IL-1R) 8/single Ig domain IL-1R-related molecule modulates the renal response to bacterial infection. Infect. Immun. 2012, 80:3812-3820.
108. Garlanda C., Di Liberto D., Vecchi A., La Manna M.P., Buracchi C., Caccamo N., et al. Damping excessive inflammation and tissue damage in Mycobacterium tuberculosis infection by Toll IL-1 receptor 8/single Ig IL-1-related receptor, a negative regulator of IL-1/TLR signaling. J. Immunol. 2007, 179:3119-3125.
109. Veliz Rodriguez T., Moalli F., Polentarutti N., Paroni M., Bonavita E., Anselmo A., et al. Role of Toll interleukin-1 receptor (IL-1R) 8, a negative regulator of IL-1R/Toll-like receptor signaling, in resistance to acute Pseudomonas aeruginosa lung infection. Infect. Immun. 2012, 80:100-109.
110. Barry J., Loh Z., Collison A., Mazzone S., Lalwani A., Zhang V., et al. Absence of Toll-IL-1 receptor 8/single immunoglobulin IL-1 receptor-related molecule reduces house dust mite-induced allergic airway inflammation in mice. Am. J. Respir. Cell Mol. Biol. 2013, 49:481-490.
111. Horne D.J., Randhawa A.K., Chau T.T., Bang N.D., Yen N.T., Farrar J.J., et al. Common polymorphisms in the PKP3-SIGIRR-TMEM16J gene region are associated with susceptibility to tuberculosis. J. Infect. Dis. 2012, 205:586-594.
112. Xiao H., Gulen M.F., Qin J., Yao J., Bulek K., Kish D., et al. The Toll-interleukin-1 receptor member SIGIRR regulates colonic epithelial homeostasis, inflammation, and tumorigenesis. Immunity 2007, 26:461-475.
113. Sham H.P., Yu E.Y., Gulen M.F., Bhinder G., Stahl M., Chan J.M., et al. SIGIRR, a negative regulator of TLR/IL-1R signalling promotes Microbiota dependent resistance to colonization by enteric bacterial pathogens. PLoS Pathog. 2013, 9:e1003539.
114. Smith D.E., Renshaw B.R., Ketchem R.R., Kubin M., Garka K.E., Sims J.E. Four new members expand the interleukin-1 superfamily. J. Biol. Chem. 2000, 275:1169-1175.
115. Busfield S.J., Comrack C.A., Yu G., Chickering T.W., Smutko J.S., Zhou H., et al. Identification and gene organization of three novel members of the IL-1 family on human chromosome 2. Genomics 2000, 66:213-216.
116. Kumar S., McDonnell P.C., Lehr R., Tierney L., Tzimas M.N., Griswold D.E., et al. Identification and initial characterization of four novel members of the interleukin-1 family. J. Biol. Chem. 2000, 275:10308-10314.
117. Pan G., Risser P., Mao W., Baldwin D.T., Zhong A.W., Filvaroff E., et al. IL-1H, an interleukin 1-related protein that binds IL-18 receptor/IL-1Rrp. Cytokine 2001, 13:1-7.
118. 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, 22:127-147.
119. Kumar S., Hanning C.R., Brigham-Burke M.R., Rieman D.J., Lehr R., Khandekar S., et al. Interleukin-1F7B (IL-1H4/IL-1F7) is processed by caspase-1 and mature IL-1F7B binds to the IL-18 receptor but does not induce IFN-gamma production. Cytokine 2002, 18:61-71.
120. Bulau A.M., Nold M.F., Li S., Nold-Petry C.A., Fink M., Mansell A., et al. Role of caspase-1 in nuclear translocation of IL-37, release of the cytokine, and IL-37 inhibition of innate immune responses. Proc. Natl. Acad. Sci. U S A. 2014, 111:2650-2655.
121. Sharma S., Kulk N., Nold M.F., Graf R., Kim S.H., Reinhardt D., et al. The IL-1 family member 7b translocates to the nucleus and down-regulates proinflammatory cytokines. J. Immunol. 2008, 180:5477-5482.
122. Ross R., Grimmel J., Goedicke S., Mobus A.M., Bulau A.M., Bufler P., et al. Analysis of nuclear localization of interleukin-1 family cytokines by flow cytometry. J. Immunol. Meth. 2013, 387:219-227.
123. Nold M.F., Nold-Petry C.A., Zepp J.A., Palmer B.E., Bufler P., Dinarello C.A. IL-37 is a fundamental inhibitor of innate immunity. Nat. Immunol. 2010, 11:1014-1022.
124. McNamee E.N., Masterson J.C., Jedlicka P., McManus M., Grenz A., Collins C.B., et al. Interleukin 37 expression protects mice from colitis. Proc. Natl. Acad. Sci. U S A. 2011, 108:16711-16716.
125. Patel F.J., Volkmann D.T., Taylor G.W., Hansson M.A., Anderson J.F., Zhou Y., et al. IL-37 reduces inflammatory response after cerebral ischemia and reperfusion injury through down-regulation of pro-inflammatory cytokines. Cytokine 2014, 69:234-239.
126. Ballak D.B., van Diepen J.A., Moschen A.R., Jansen H.J., Hijmans A., Groenhof G.J., et al. IL-37 protects against obesity-induced inflammation and insulin resistance. Nat. Commun. 2014, 5:4711.
127. Yang Y., Zhang Z.X., Lian D., Haig A., Bhattacharjee R.N., Jevnikar A.M. IL-37 inhibits IL-18-induced tubular epithelial cell expression of pro-inflammatory cytokines and renal ischemia-reperfusion injury. Kidney Int. 2015, 87:396-408.
128. Luo Y., Cai X., Liu S., Wang S., Nold-Petry C.A., Nold M.F., et al. Suppression of antigen-specific adaptive immunity by IL-37 via induction of tolerogenic dendritic cells. Proc. Natl. Acad. Sci. U S A. 2014, 111:15178-15183.
129. Teng X., Hu Z., Wei X., Wang Z., Guan T., Liu N., et al. IL-37 ameliorates the inflammatory process in psoriasis by suppressing proinflammatory cytokine production. J. Immunol. 2014, 192:1815-1823.
130. Sakai N., Van Sweringen H.L., Belizaire R.M., Quillin R.C., Schuster R., Blanchard J., et al. Interleukin-37 reduces liver inflammatory injury via effects on hepatocytes and non-parenchymal cells. J. Gastroenterol. Hepatol. 2012, 27:1609-1616.
131. Wu B., Meng K., Ji Q., Cheng M., Yu K., Zhao X., et al. Interleukin-37 ameliorates myocardial ischaemia/reperfusion injury in mice. Clin. Exp. Immunol. 2014, 176:438-451.
132. Chai M., Ji Q., Zhang H., Zhou Y., Yang Q., Zhou Y., et al. The Protective Effect of Interleukin-37 on Vascular Calcification and Atherosclerosis in Apolipoprotein E-Deficient Mice with Diabetes. J Interferon Cytokine Res. 2015.
133. Ye L., Jiang B., Deng J., Du J., Xiong W., Guan Y., et al. IL-37 Alleviates Rheumatoid Arthritis by Suppressing IL-17 and IL-17-Triggering Cytokine Production and Limiting Th17 Cell Proliferation. J. Immunol. 2015, 194:5110-5119.
134. van de Veerdonk F.L., Gresnigt M.S., Oosting M., van der Meer J.W., Joosten L.A., Netea M.G., et al. Protective host defense against disseminated candidiasis is impaired in mice expressing human interleukin-37. Front Microbiol. 2014, 5:762.
135. Bufler P., Azam T., Gamboni-Robertson F., Reznikov L.L., Kumar S., Dinarello C.A., et al. A complex of the IL-1 homologue IL-1F7b and IL-18-binding protein reduces IL-18 activity. Proc. Natl. Acad. Sci. U S A. 2002, 99:13723-13728.
136. Lin H., Ho A.S., Haley-Vicente D., Zhang J., Bernal-Fussell J., Pace A.M., et al. Cloning and characterization of IL-1HY2, a novel interleukin-1 family member. J. Biol. Chem. 2001, 276:20597-20602.
137. Bensen J.T., Dawson P.A., Mychaleckyj J.C., Bowden D.W. Identification of a novel human cytokine gene in the interleukin gene cluster on chromosome 2q12-14. J. Interferon. Cytokine Res. 2001, 21:899-904.
138. Ciccia F., Accardo-Palumbo A., Alessandro R., Alessandri C., Priori R., Guggino G., et al. IL-36alpha axis is modulated in patients with primary Sjogren's Syndrome. Clin. Exp. Immunol. 2015.
139. van de Veerdonk F.L., Stoeckman A.K., Wu G., Boeckermann A.N., Azam T., Netea M.G., 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. U S A. 2012, 109:3001-3005.
140. Monnet D., Kadi A., Izac B., Lebrun N., Letourneur F., Zinovieva E., et al. Association between the IL-1 family gene cluster and spondyloarthritis. Ann. Rheum. Dis. 2012, 71:885-890.
141. Lea W.I., Lee Y.H. The associations between interleukin-1 polymorphisms and susceptibility to ankylosing spondylitis: a meta-analysis. Joint Bone Spine. 2012, 79:370-374.
142. Broderick L., De Nardo D., Franklin B.S., Hoffman H.M., Latz E. The inflammasomes and autoinflammatory syndromes. Annu. Rev. Pathol. 2015, 10:395-424.
143. Vance R.E. The NAIP/NLRC4 inflammasomes. Curr. Opin. Immunol. 2015, 32:84-89.
144. Brydges S.D., Mueller J.L., McGeough M.D., Pena C.A., Misaghi A., Gandhi C., et al. Inflammasome-mediated disease animal models reveal roles for innate but not adaptive immunity. Immunity 2009, 30:875-887.
145. Brydges S.D., Broderick L., McGeough M.D., Pena C.A., Mueller J.L., Hoffman H.M. Divergence of IL-1, IL-18, and cell death in NLRP3 inflammasomopathies. J. Clin. Invest. 2013, 123:4695-4705.
146. Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., Hong A., et al. Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin. Exp. Biol. Med. (Maywood). 2009, 234:40-52.
147. Chae J.J., Komarow H.D., Cheng J., Wood G., Raben N., Liu P.P., et al. Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis. Mol. Cell. 2003, 11:591-604.
148. Hesker P.R., Nguyen M., Kovarova M., Ting J.P., Koller B.H. Genetic loss of murine pyrin, the Familial Mediterranean Fever protein, increases interleukin-1beta levels. PLoS ONE 2012, 7:e51105.
149. Kim M.L., Chae J.J., Park Y.H., De Nardo D., Stirzaker R.A., Ko H.J., et al. Aberrant actin depolymerization triggers the pyrin inflammasome and autoinflammatory disease that is dependent on IL-18, not IL-1beta. J. Exp. Med. 2015, 212:927-938.
150. Sellin M.E., Muller A.A., Felmy B., Dolowschiak T., Diard M., Tardivel A., et al. Epithelium-intrinsic NAIP/NLRC4 inflammasome drives infected enterocyte expulsion to restrict Salmonella replication in the intestinal mucosa. Cell Host Microbe. 2014, 16:237-248.
151. Nordlander S., Pott J., Maloy K.J. NLRC4 expression in intestinal epithelial cells mediates protection against an enteric pathogen. Mucosal. Immunol. 2014, 7:775-785.
152. Kitamura A., Sasaki Y., Abe T., Kano H., Yasutomo K. An inherited mutation in NLRC4 causes autoinflammation in human and mice. J. Exp. Med. 2014, 211:2385-2396.
153. Irikura V.M., Lagraoui M., Hirsh D. The epistatic interrelationships of IL-1, IL-1 receptor antagonist, and the type I IL-1 receptor. J. Immunol. 2002, 169:393-398.
154. Palmer G., Talabot-Ayer D., Kaya G., Gabay C. Type I IL-1 receptor mediates IL-1 and intracellular IL-1 receptor antagonist effects in skin inflammation. J. Invest. Dermatol. 2007, 127:1938-1946.
155. Zhou F., He X., Iwakura Y., Horai R., Stuart J.M. Arthritis in mice that are deficient in interleukin-1 receptor antagonist is dependent on genetic background. Arthritis. Rheum. 2005, 52:3731-3738.
156. Nicklin M.J., Hughes D.E., Barton J.L., Ure J.M., Duff G.W. Arterial inflammation in mice lacking the interleukin 1 receptor antagonist gene. J. Exp. Med. 2000, 191:303-312.
157. Hirsch E., Irikura V.M., Paul S.M., Hirsh D. Functions of interleukin 1 receptor antagonist in gene knockout and overproducing mice. Proc. Natl. Acad. Sci. U S A. 1996, 93:11008-11013.
158. Lamacchia C., Palmer G., Bischoff L., Rodriguez E., Talabot-Ayer D., Gabay C. Distinct roles of hepatocyte- and myeloid cell-derived IL-1 receptor antagonist during endotoxemia and sterile inflammation in mice. J. Immunol. 2010, 185:2516-2524.
159. Izawa A., Ishihara Y., Mizutani H., Kobayashi S., Goto H., Okabe E., et al. Inflammatory bone loss in experimental periodontitis induced by Aggregatibacter actinomycetemcomitans in interleukin-1 receptor antagonist knockout mice. Infect Immun. 2014, 82:1904-1913.
160. Krelin Y., Voronov E., Dotan S., Elkabets M., Reich E., Fogel M., et al. Interleukin-1beta-driven inflammation promotes the development and invasiveness of chemical carcinogen-induced tumors. Cancer Res. 2007, 67:1062-1071.
161. Gabay C., Smith M.F., Eidlen D., Arend W.P. Interleukin 1 receptor antagonist (IL-1Ra) is an acute-phase protein. J. Clin. Invest. 1997, 99:2930-2940.
162. Gabay C., Porter B., Guenette D., Billir B., Arend W.P. Interleukin-4 (IL-4) and IL-13 enhance the effect of IL-1beta on production of IL-1 receptor antagonist by human primary hepatocytes and hepatoma HepG2 cells: differential effect on C-reactive protein production. Blood 1999, 93:1299-1307.
163. Gabay C., Gigley J., Sipe J., Arend W.P., Fantuzzi G. Production of IL-1 receptor antagonist by hepatocytes is regulated as an acute-phase protein in vivo. Eur. J. Immunol. 2001, 31:490-499.
164. Lamacchia C., Rodriguez E., Palmer G., Vesin C., Seemayer C.A., Rubbia-Brandt L., et al. Mice deficient in hepatocyte-specific IL-1Ra show delayed resolution of concanavalin A-induced hepatitis. Eur. J. Immunol. 2012, 42:1294-1303.
165. Ma Y., Thornton S., Boivin G.P., Hirsh D., Hirsch R., Hirsch E. Altered susceptibility to collagen-induced arthritis in transgenic mice with aberrant expression of interleukin-1 receptor antagonist. Arthritis. Rheum. 1998, 41:1798-1805.
166. Lamacchia C., Palmer G., Seemayer C.A., Talabot-Ayer D., Gabay C. Enhanced Th1 and Th17 responses and arthritis severity in mice with a deficiency of myeloid cell-specific interleukin-1 receptor antagonist. Arthritis. Rheum. 2010, 62:452-462.
167. Lamacchia C., Rodriguez E., Palmer G., Vigne S., Martin P., Talabot-Ayer D., et al. Articular inflammation is controlled by myeloid cell-derived interleukin 1 receptor antagonist during the acute phase of arthritis in mice. Ann. Rheum. Dis. 2012, 71:281-287.
168. Devlin C.M., Kuriakose G., Hirsch E., Tabas I. Genetic alterations of IL-1 receptor antagonist in mice affect plasma cholesterol level and foam cell lesion size. Proc. Natl. Acad. Sci. U S A. 2002, 99:6280-6285.
169. Merhi-Soussi F., Kwak B.R., Magne D., Chadjichristos C., Berti M., Pelli G., et al. Interleukin-1 plays a major role in vascular inflammation and atherosclerosis in male apolipoprotein E-knockout mice. Cardiovasc. Res. 2005, 66:583-593.
170. Zhiguang X., Wei C., Steven R., Wei D., Wei Z., Rong M., et al. Over-expression of IL-33 leads to spontaneous pulmonary inflammation in mIL-33 transgenic mice. Immunol. Lett. 2010, 131:159-165.
171. Imai Y., Yasuda K., Sakaguchi Y., Haneda T., Mizutani H., Yoshimoto T., et al. Skin-specific expression of IL-33 activates group 2 innate lymphoid cells and elicits atopic dermatitis-like inflammation in mice. Proc. Natl. Acad. Sci. U S A. 2013, 110:13921-13926.
172. Talabot-Ayer D., Martin P., Vesin C., Seemayer C.A., Vigne S., Gabay C., et al. Severe neutrophil-dominated inflammation and enhanced myelopoiesis in IL-33-overexpressing CMV/IL33 mice. J. Immunol. 2015, 194:750-760.
173. Keller J., Catala-Lehnen P., Wintges K., Schulze J., Bickert T., Ito W., et al. Transgenic over-expression of interleukin-33 in osteoblasts results in decreased osteoclastogenesis. Biochem. Biophys. Res. Commun. 2012, 417:217-222.
174. Bessa J., Meyer C.A., de Vera Mudry M.C., Schlicht S., Smith S.H., Iglesias A., et al. Altered subcellular localization of IL-33 leads to non-resolving lethal inflammation. J. Autoimmun. 2014, 55:33-41.
175. Blumberg H., Dinh H., Trueblood E.S., Pretorius J., Kugler D., Weng N., et al. Opposing activities of two novel members of the IL-1 ligand family regulate skin inflammation. J. Exp. Med. 2007, 204:2603-2614.
176. Tortola L., Rosenwald E., Abel B., Blumberg H., Schafer M., Coyle A.J., et al. Psoriasiform dermatitis is driven by IL-36-mediated DC-keratinocyte crosstalk. J. Clin. Invest. 2012, 122:3965-3976.
177. Hoffman H.M., Mueller J.L., Broide D.H., Wanderer A.A., Kolodner R.D. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 2001, 29:301-305.
178. Feldmann J., Prieur A.M., Quartier P., Berquin P., Certain S., Cortis E., et al. Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am. J. Hum. Genet. 2002, 71:198-203.
179. Aksentijevich I., D.Putnam C., Remmers E.F., Mueller J.L., Le J., Kolodner R.D., Moak Z., Chuang M., Austin F., Goldbach-Mansky R., Hoffman H.M., Kastner D.L. The clinical continuum of cryopyrinopathies: novel CIAS1 mutations in North American patients and a new cryopyrin model. Arthritis Rheum 2007, 56:1273-1285.
180. Dowds T.A., Masumoto J., Zhu L., Inohara N., Nunez G. Cryopyrin-induced interleukin 1beta secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC. J. Biol. Chem. 2004, 279:21924-21928.
181. Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J. NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 2004, 20:319-325.
182. Miyamae T. Cryopyrin-associated periodic syndromes: diagnosis and management. Paediatr. Drugs 2012, 14:109-117.
183. Leslie K.S., Lachmann H.J., Bruning E., McGrath J.A., Bybee A., Gallimore J.R., et al. Phenotype, genotype, and sustained response to anakinra in 22 patients with autoinflammatory disease associated with CIAS-1/NALP3 mutations. Arch. Dermatol. 2006, 142:1591-1597.
184. Mirault T., Launay D., Cuisset L., Hachulla E., Lambert M., Queyrel V., et al. Recovery from deafness in a patient with Muckle-Wells syndrome treated with anakinra. Arthritis. Rheum. 2006, 54:1697-1700.
185. Granel B., Serratrice J., Disdier P., Weiller P.J. Dramatic improvement with anakinra in a case of chronic infantile neurological cutaneous and articular (CINCA) syndrome. Rheumatology 2005, 44:689-690.
186. Goldbach-Mansky R., Dailey N.J., Canna S.W., Gelabert A., Jones J., Rubin B.I., et al. Neonatal-onset multisystem inflammatory disease responsive to interleukin-1beta inhibition. New England J. Med. 2006, 355:581-592.
187. Goldbach-Mansky R., Shroff S.D., Wilson M., Snyder C., Plehn S., Barham B., et al. A pilot study to evaluate the safety and efficacy of the long-acting interleukin-1 inhibitor rilonacept (interleukin-1 Trap) in patients with familial cold autoinflammatory syndrome. Arthritis. Rheum. 2008, 58:2432-2442.
188. Hoffman H.M., Throne M.L., Amar N.J., Sebai M., Kivitz A.J., Kavanaugh A., et al. Efficacy and safety of rilonacept (interleukin-1 Trap) in patients with cryopyrin-associated periodic syndromes: results from two sequential placebo-controlled studies. Arthritis. Rheum. 2008, 58:2443-2452.
189. Lachmann H.J., Kone-Paut I., Kuemmerle-Deschner J.B., Leslie K.S., Hachulla E., Quartier P., et al. Use of canakinumab in the cryopyrin-associated periodic syndrome. New England J. Med. 2009, 360:2416-2425.
190. Romberg N., Al Moussawi K., Nelson-Williams C., Stiegler A.L., Loring E., Choi M., et al. Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation. Nat. Genet. 2014, 46:1135-1139.
191. Canna S.W., de Jesus A.A., Gouni S., Brooks S.R., Marrero B., Liu Y., et al. An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome. Nat. Genet. 2014, 46:1140-1146.
192. Shohat M., Halpern G.J. Familial Mediterranean fever-a review. Genet. Med.: Official J. Am. College Med. Genet. 2011, 13:487-498.
193. Tennent G.A., Lovat L.B., Pepys M.B. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc. Natl. Acad. Sci. U S A. 1995, 92:4299-4303.
194. S. Goldfinger, Management of familial mediterranean fever, UpToDate, T.W. Post (Ed.), UpToDate, Waltham, MA, 2015.
195. Eroglu F.K., Besbas N., Topaloglu R., Ozen S. Treatment of colchicine-resistant Familial Mediterranean fever in children and adolescents. Rheumatol. Int. 2015.
196. Aksentijevich I., Masters S.L., Ferguson P.J., Dancey P., Frenkel J., van Royen-Kerkhoff A., et al. An autoinflammatory disease with deficiency of the interleukin-1-receptor antagonist. New England J. Med. 2009, 360:2426-2437.
197. Reddy S., Jia S., Geoffrey R., Lorier R., Suchi M., Broeckel U., et al. An autoinflammatory disease due to homozygous deletion of the IL1RN locus. The New England J. Med. 2009, 360:2438-2444.
198. Marrakchi S., Guigue P., Renshaw B.R., Puel A., Pei X.Y., Fraitag S., et al. Interleukin-36-receptor antagonist deficiency and generalized pustular psoriasis. The New England J. Med. 2011, 365:620-628.
199. Onoufriadis A., Simpson M.A., Pink A.E., Di Meglio P., Smith C.H., Pullabhatla V., et al. Mutations in IL36RN/IL1F5 are associated with the severe episodic inflammatory skin disease known as generalized pustular psoriasis. Am. J. Hum. Genet. 2011, 89:432-437.
200. Farooq M., Nakai H., Fujimoto A., Fujikawa H., Matsuyama A., Kariya N., et al. Mutation analysis of the IL36RN gene in 14 Japanese patients with generalized pustular psoriasis. Hum. Mutat. 2013, 34:176-183.
201. Sugiura K., Takemoto A., Yamaguchi M., Takahashi H., Shoda Y., Mitsuma T., et al. The majority of generalized pustular psoriasis without psoriasis vulgaris is caused by deficiency of interleukin-36 receptor antagonist. J. Invest. Dermatol. 2013, 133:2514-2521.
202. Rossi-Semerano L., Piram M., Chiaverini C., De Ricaud D., Smahi A., Kone-Paut I. First clinical description of an infant with interleukin-36-receptor antagonist deficiency successfully treated with anakinra. Pediatrics 2013, 132:e1043-e1047.
203. Dierselhuis M.P., Frenkel J., Wulffraat N.M., Boelens J.J. Anakinra for flares of pyogenic arthritis in PAPA syndrome. Rheumatology 2005, 44:406-408.
204. Gattorno M., Pelagatti M.A., Meini A., Obici L., Barcellona R., Federici S., et al. Persistent efficacy of anakinra in patients with tumor necrosis factor receptor-associated periodic syndrome. Arthritis. Rheum. 2008, 58:1516-1520.
205. Gul A., Tugal-Tutkun I., Dinarello C.A., Reznikov L., Esen B.A., Mirza A., et al. Interleukin-1beta-regulating antibody XOMA 052 (gevokizumab) in the treatment of acute exacerbations of resistant uveitis of Behcet's disease: an open-label pilot study. Ann. Rheum. Dis. 2012, 71:563-566.
206. Ruperto N., Brunner H.I., Quartier P., Constantin T., Wulffraat N., Horneff G., et al. Two randomized trials of canakinumab in systemic juvenile idiopathic arthritis. New England J. Med. 2012, 367:2396-2406.