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• W2069066505 abstract "IL-33 contributes to disease processes in association with Th1 and Th2 phenotypes. IL-33 mRNA is rapidly regulated, but the fate of synthesized IL-33 protein is unknown. To understand the interplay among IL-33, IFN-γ, and IL-4 proteins, recombinant replication-deficient adenoviruses were produced and used for dual expression of IL-33 and IFN-γ or IL-33 and IL-4. The effects of such dual gene delivery were compared with the effects of similar expression of each of these cytokines alone. In lung fibroblast culture, co-expression of IL-33 and IFN-γ resulted in suppression of the levels of both proteins, whereas co-expression of IL-33 and IL-4 led to mutual elevation. In vivo, co-expression of IL-33 and IFN-γ in the lungs led to attenuation of IL-33 protein levels. Purified IFN-γ also attenuated IL-33 protein in fibroblast culture, suggesting that IFN-γ controls IL-33 protein degradation. Specific inhibition of caspase-1, -3, and -8 had minimal effect on IFN-γ-driven IL-33 protein down-regulation. Pharmacological inhibition, siRNA-mediated silencing, or gene deficiency of STAT1 potently up-regulated IL-33 protein expression levels and attenuated the down-regulating effect of IFN-γ on IL-33. Stimulation with IFN-γ strongly elevated the levels of the LMP2 proteasome subunit, known for its role in IFN-γ-regulated antigen processing. siRNA-mediated silencing of LMP2 expression abrogated the effect of IFN-γ on IL-33. Thus, IFN-γ, IL-4, and IL-33 are engaged in a complex interplay. The down-regulation of IL-33 protein levels by IFN-γ in pulmonary fibroblasts and in the lungs in vivo occurs through STAT1 and non-canonical use of the LMP2 proteasome subunit in a caspase-independent fashion. IL-33 contributes to disease processes in association with Th1 and Th2 phenotypes. IL-33 mRNA is rapidly regulated, but the fate of synthesized IL-33 protein is unknown. To understand the interplay among IL-33, IFN-γ, and IL-4 proteins, recombinant replication-deficient adenoviruses were produced and used for dual expression of IL-33 and IFN-γ or IL-33 and IL-4. The effects of such dual gene delivery were compared with the effects of similar expression of each of these cytokines alone. In lung fibroblast culture, co-expression of IL-33 and IFN-γ resulted in suppression of the levels of both proteins, whereas co-expression of IL-33 and IL-4 led to mutual elevation. In vivo, co-expression of IL-33 and IFN-γ in the lungs led to attenuation of IL-33 protein levels. Purified IFN-γ also attenuated IL-33 protein in fibroblast culture, suggesting that IFN-γ controls IL-33 protein degradation. Specific inhibition of caspase-1, -3, and -8 had minimal effect on IFN-γ-driven IL-33 protein down-regulation. Pharmacological inhibition, siRNA-mediated silencing, or gene deficiency of STAT1 potently up-regulated IL-33 protein expression levels and attenuated the down-regulating effect of IFN-γ on IL-33. Stimulation with IFN-γ strongly elevated the levels of the LMP2 proteasome subunit, known for its role in IFN-γ-regulated antigen processing. siRNA-mediated silencing of LMP2 expression abrogated the effect of IFN-γ on IL-33. Thus, IFN-γ, IL-4, and IL-33 are engaged in a complex interplay. The down-regulation of IL-33 protein levels by IFN-γ in pulmonary fibroblasts and in the lungs in vivo occurs through STAT1 and non-canonical use of the LMP2 proteasome subunit in a caspase-independent fashion. Interleukin (IL)-33 is a member of the IL-1 family (1.Arend W.P. Palmer G. Gabay C. IL-1, IL-18, and IL-33 families of cytokines.Immunol. Rev. 2008; 223: 20-38Crossref PubMed Scopus (650) Google Scholar, 2.Sims J.E. Smith D.E. The IL-1 family: regulators of immunity.Nat. Rev. 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McInnes I.B. Liew F.Y. IL-33 exacerbates antigen-induced arthritis by activating mast cells.Proc. Natl. Acad. Sci. U.S.A. 2008; 105: 10913-10918Crossref PubMed Scopus (401) Google Scholar, 16.Palmer G. Talabot-Ayer D. Lamacchia C. Toy D. Seemayer C.A. Viatte S. Finckh A. Smith D.E. Gabay C. Inhibition of interleukin-33 signaling attenuates the severity of experimental arthritis.Arthritis Rheum. 2009; 60: 738-749Crossref PubMed Scopus (261) Google Scholar, 17.Hueber A.J. Alves-Filho J.C. Asquith D.L. Michels C. Millar N.L. Reilly J.H. Graham G.J. Liew F.Y. Miller A.M. McInnes I.B. IL-33 induces skin inflammation with mast cell and neutrophil activation.Eur. J. Immunol. 2011; 41: 2229-2237Crossref PubMed Scopus (135) Google Scholar, 18.Sponheim J. Pollheimer J. Olsen T. Balogh J. Hammarström C. Loos T. Kasprzycka M. Sørensen D.R. Nilsen H.R. Küchler A.M. Vatn M.H. Haraldsen G. Inflammatory bowel disease-associated interleukin-33 is preferentially expressed in ulceration-associated myofibroblasts.Am. J. Pathol. 2010; 177: 2804-2815Abstract Full Text Full Text PDF PubMed Scopus (127) Google Scholar, 19.Seidelin J.B. Bjerrum J.T. Coskun M. Widjaya B. Vainer B. Nielsen O.H. IL-33 is up-regulated in colonocytes of ulcerative colitis.Immunol. Lett. 2010; 128: 80-85Crossref PubMed Scopus (118) Google Scholar, 20.Yanaba K. Yoshizaki A. Asano Y. Kadono T. Sato S. Serum IL-33 levels are raised in patients with systemic sclerosis: association with extent of skin sclerosis and severity of pulmonary fibrosis.Clin. Rheumatol. 2011; 30: 825-830Crossref PubMed Scopus (101) Google Scholar, 21.McHedlidze T. Waldner M. Zopf S. Walker J. Rankin A.L. Schuchmann M. Voehringer D. McKenzie A.N. Neurath M.F. Pflanz S. Wirtz S. Interleukin-33-dependent innate lymphoid cells mediate hepatic fibrosis.Immunity. 2013; 39: 357-371Abstract Full Text Full Text PDF PubMed Scopus (366) Google Scholar, 22.Liang Y. Jie Z. Hou L. Aguilar-Valenzuela R. Vu D. Soong L. Sun J. IL-33 induces nuocytes and modulates liver injury in viral hepatitis.J. Immunol. 2013; 190: 5666-5675Crossref PubMed Scopus (60) Google Scholar). Full-length IL-33 precursor is synthesized as a ∼30-kDa precursor consisting of 270 amino acid residues for human IL-33 and 266 amino acid residues for mouse (m) 3The abbreviations used are: mmouse (e.g. mIL-33)AdVadenoviralNMLFnormal mouse lung fibroblastqPCRquantitative PCRfmkfluoromethyl ketoneRSVRous sarcoma virusBALbronchoalveolar lavage. IL-33. This form is almost entirely intracellular and, moreover, intranuclear (3.Baekkevold E.S. Roussigné M. Yamanaka T. Johansen F.E. Jahnsen F.L. Amalric F. Brandtzaeg P. Erard M. Haraldsen G. Girard J.P. Molecular characterization of NF-HEV, a nuclear factor preferentially expressed in human high endothelial venules.Am. J. Pathol. 2003; 163: 69-79Abstract Full Text Full Text PDF PubMed Scopus (379) Google Scholar, 4.Luzina I.G. Kopach P. Lockatell V. Kang P.H. Nagarsekar A. Burke A.P. Hasday J.D. Todd N.W. Atamas S.P. Interleukin-33 potentiates bleomycin-induced lung injury.Am. J. Respir. Cell Mol. Biol. 2013; 49: 999-1008Crossref PubMed Scopus (95) Google Scholar, 5.Luzina I.G. Pickering E.M. Kopach P. Kang P.H. Lockatell V. Todd N.W. Papadimitriou J.C. McKenzie A.N. Atamas S.P. Full-length IL-33 promotes inflammation but not Th2 response in vivo in an ST2-independent fashion.J. Immunol. 2012; 189: 403-410Crossref PubMed Scopus (88) Google Scholar, 23.Carriere V. Roussel L. Ortega N. Lacorre D.A. Americh L. Aguilar L. Bouche G. Girard J.P. IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a chromatin-associated nuclear factor in vivo.Proc. Natl. Acad. Sci. U.S.A. 2007; 104: 282-287Crossref PubMed Scopus (783) Google Scholar). Partial proteolysis of the IL-33 precursor produces a shorter mature form (24.Schmitz J. Owyang A. Oldham E. Song Y. Murphy E. McClanahan T.K. Zurawski G. Moshrefi M. Qin J. Li X. Gorman D.M. Bazan J.F. Kastelein R.A. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines.Immunity. 2005; 23: 479-490Abstract Full Text Full Text PDF PubMed Scopus (2829) Google Scholar, 25.Lefrançais E. Roga S. Gautier V. Gonzalez-de-Peredo A. Monsarrat B. Girard J.P. Cayrol C. IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G.Proc. Natl. Acad. Sci. U.S.A. 2012; 109: 1673-1678Crossref PubMed Scopus (408) Google Scholar), which acts as the IL-33 cytokine when released into the extracellular space and bound to the specific cell surface receptor, a heterodimer of the IL-1RAP and T1/ST2 chains (24.Schmitz J. Owyang A. Oldham E. Song Y. Murphy E. McClanahan T.K. Zurawski G. Moshrefi M. Qin J. Li X. Gorman D.M. Bazan J.F. Kastelein R.A. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines.Immunity. 2005; 23: 479-490Abstract Full Text Full Text PDF PubMed Scopus (2829) Google Scholar, 26.Chackerian A.A. Oldham E.R. Murphy E.E. Schmitz J. Pflanz S. Kastelein R.A. IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor complex.J. Immunol. 2007; 179: 2551-2555Crossref PubMed Scopus (436) Google Scholar). Other proteases, specifically caspases, cleave IL-33, inactivating its function (27.Lüthi A.U. Cullen S.P. McNeela E.A. Duriez P.J. Afonina I.S. Sheridan C. Brumatti G. Taylor R.C. Kersse K. Vandenabeele P. Lavelle E.C. Martin S.J. Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases.Immunity. 2009; 31: 84-98Abstract Full Text Full Text PDF PubMed Scopus (543) Google Scholar, 28.Cayrol C. Girard J.P. The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1.Proc. Natl. Acad. Sci. U.S.A. 2009; 106: 9021-9026Crossref PubMed Scopus (541) Google Scholar). The IL-33-T1/ST2 pathway is centrally involved in Th2-driven processes, including allergies, asthma, anaphylaxis, and parasite expulsion, whereas the intracellular form binds DNA and functions as a regulator of gene expression (3.Baekkevold E.S. Roussigné M. Yamanaka T. Johansen F.E. Jahnsen F.L. Amalric F. Brandtzaeg P. Erard M. Haraldsen G. Girard J.P. Molecular characterization of NF-HEV, a nuclear factor preferentially expressed in human high endothelial venules.Am. J. Pathol. 2003; 163: 69-79Abstract Full Text Full Text PDF PubMed Scopus (379) Google Scholar, 4.Luzina I.G. Kopach P. Lockatell V. Kang P.H. Nagarsekar A. Burke A.P. Hasday J.D. Todd N.W. Atamas S.P. Interleukin-33 potentiates bleomycin-induced lung injury.Am. J. Respir. Cell Mol. Biol. 2013; 49: 999-1008Crossref PubMed Scopus (95) Google Scholar, 5.Luzina I.G. Pickering E.M. Kopach P. Kang P.H. Lockatell V. Todd N.W. Papadimitriou J.C. McKenzie A.N. Atamas S.P. Full-length IL-33 promotes inflammation but not Th2 response in vivo in an ST2-independent fashion.J. Immunol. 2012; 189: 403-410Crossref PubMed Scopus (88) Google Scholar, 23.Carriere V. Roussel L. Ortega N. Lacorre D.A. Americh L. Aguilar L. Bouche G. Girard J.P. IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a chromatin-associated nuclear factor in vivo.Proc. Natl. Acad. Sci. U.S.A. 2007; 104: 282-287Crossref PubMed Scopus (783) Google Scholar, 24.Schmitz J. Owyang A. Oldham E. Song Y. Murphy E. McClanahan T.K. Zurawski G. Moshrefi M. Qin J. Li X. Gorman D.M. Bazan J.F. Kastelein R.A. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines.Immunity. 2005; 23: 479-490Abstract Full Text Full Text PDF PubMed Scopus (2829) Google Scholar, 25.Lefrançais E. Roga S. Gautier V. Gonzalez-de-Peredo A. Monsarrat B. Girard J.P. Cayrol C. IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G.Proc. Natl. Acad. Sci. U.S.A. 2012; 109: 1673-1678Crossref PubMed Scopus (408) Google Scholar, 26.Chackerian A.A. Oldham E.R. Murphy E.E. Schmitz J. Pflanz S. Kastelein R.A. IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor complex.J. Immunol. 2007; 179: 2551-2555Crossref PubMed Scopus (436) Google Scholar, 27.Lüthi A.U. Cullen S.P. McNeela E.A. Duriez P.J. Afonina I.S. Sheridan C. Brumatti G. Taylor R.C. Kersse K. Vandenabeele P. Lavelle E.C. Martin S.J. Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases.Immunity. 2009; 31: 84-98Abstract Full Text Full Text PDF PubMed Scopus (543) Google Scholar, 29.Liew F.Y. IL-33: a Janus cytokine.Ann. Rheum. Dis. 2012; 71: i101-i104Crossref PubMed Scopus (81) Google Scholar, 30.Polumuri S.K. Jayakar G.G. Shirey K.A. Roberts Z.J. Perkins D.J. Pitha P.M. Vogel S.N. Transcriptional regulation of murine IL-33 by TLR and non-TLR agonists.J. Immunol. 2012; 189: 50-60Crossref PubMed Scopus (91) Google Scholar, 31.Ali S. Mohs A. Thomas M. Klare J. Ross R. Schmitz M.L. Martin M.U. The dual function cytokine IL-33 interacts with the transcription factor NF-κB to dampen NF-κB-stimulated gene transcription.J. Immunol. 2011; 187: 1609-1616Crossref PubMed Scopus (258) Google Scholar). mouse (e.g. mIL-33) adenoviral normal mouse lung fibroblast quantitative PCR fluoromethyl ketone Rous sarcoma virus bronchoalveolar lavage. IL-33 mRNA is regulated rapidly, within hours (30.Polumuri S.K. Jayakar G.G. Shirey K.A. Roberts Z.J. Perkins D.J. Pitha P.M. Vogel S.N. Transcriptional regulation of murine IL-33 by TLR and non-TLR agonists.J. Immunol. 2012; 189: 50-60Crossref PubMed Scopus (91) Google Scholar, 32.Seltmann J. Werfel T. Wittmann M. Evidence for a regulatory loop between IFN-γ and IL-33 in skin inflammation.Exp. Dermatol. 2013; 22: 102-107Crossref PubMed Scopus (52) Google Scholar, 33.Meephansan J. Tsuda H. Komine M. Tominaga S. Ohtsuki M. Regulation of IL-33 expression by IFN-γ and tumor necrosis factor-α in normal human epidermal keratinocytes.J. Invest. Dermatol. 2012; 132: 2593-2600Abstract Full Text Full Text PDF PubMed Scopus (87) Google Scholar), whereas the fate of synthesized IL-33 protein is unknown. Abundant evidence suggests that IL-33 is a potent pro-Th2 cytokine (5.Luzina I.G. Pickering E.M. Kopach P. Kang P.H. Lockatell V. Todd N.W. Papadimitriou J.C. McKenzie A.N. Atamas S.P. Full-length IL-33 promotes inflammation but not Th2 response in vivo in an ST2-independent fashion.J. Immunol. 2012; 189: 403-410Crossref PubMed Scopus (88) Google Scholar, 8.Walzl G. Matthews S. Kendall S. Gutierrez-Ramos J.C. Coyle A.J. Openshaw P.J. Hussell T. Inhibition of T1/ST2 during respiratory syncytial virus infection prevents T helper cell type 2 (Th2)- but not Th1-driven immunopathology.J. Exp. Med. 2001; 193: 785-792Crossref PubMed Scopus (106) Google Scholar, 24.Schmitz J. Owyang A. Oldham E. Song Y. Murphy E. McClanahan T.K. Zurawski G. Moshrefi M. Qin J. Li X. Gorman D.M. Bazan J.F. Kastelein R.A. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines.Immunity. 2005; 23: 479-490Abstract Full Text Full Text PDF PubMed Scopus (2829) Google Scholar, 34.Komai-Koma M. Xu D. Li Y. McKenzie A.N. McInnes I.B. Liew F.Y. IL-33 is a chemoattractant for human Th2 cells.Eur. J. 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T1/ST2-deficient mice demonstrate the importance of T1/ST2 in developing primary T helper cell type 2 responses.J. Exp. Med. 2000; 191: 1069-1076Crossref PubMed Scopus (413) Google Scholar), whereas data on the regulation of IL-33 expression at the mRNA and/or protein levels by IL-4 are limited (41.Zhao W.H. Hu Z.Q. Up-regulation of IL-33 expression in various types of murine cells by IL-3 and IL-4.Cytokine. 2012; 58: 267-273Crossref PubMed Scopus (17) Google Scholar). The interplay between IL-33 and IFN-γ remains a matter of controversy. Various studies have reported a down-regulating (5.Luzina I.G. Pickering E.M. Kopach P. Kang P.H. Lockatell V. Todd N.W. Papadimitriou J.C. McKenzie A.N. Atamas S.P. Full-length IL-33 promotes inflammation but not Th2 response in vivo in an ST2-independent fashion.J. Immunol. 2012; 189: 403-410Crossref PubMed Scopus (88) Google Scholar, 42.Jiang H.R. Milovanovi M. Allan D. Niedbala W. Besnard A.G. Fukada S.Y. Alves-Filho J.C. Togbe D. Goodyear C.S. Linington C. Xu D. Lukic M.L. Liew F.Y. IL-33 attenuates EAE by suppressing IL-17 and IFN-γ production and inducing alternatively activated macrophages.Eur. J. Immunol. 2012; 42: 1804-1814Crossref PubMed Scopus (238) Google Scholar, 43.Groβ P. Doser K. Falk W. Obermeier F. Hofmann C. IL-33 attenuates development and perpetuation of chronic intestinal inflammation.Inflamm. Bowel Dis. 2012; 18: 1900-1909Crossref PubMed Scopus (91) Google Scholar), a null (44.Imai Y. Yasuda K. Sakaguchi Y. Haneda T. Mizutani H. Yoshimoto T. Nakanishi K. Yamanishi K. 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: 13921-13926Crossref PubMed Scopus (326) Google Scholar), or an up-regulating (45.Bourgeois E. Van L.P. Samson M. Diem S. Barra A. Roga S. Gombert J.M. Schneider E. Dy M. Gourdy P. Girard J.P. Herbelin A. The pro-Th2 cytokine IL-33 directly interacts with invariant NKT and NK cells to induce IFN-γ production.Eur. J. Immunol. 2009; 39: 1046-1055Crossref PubMed Scopus (271) Google Scholar, 46.Smithgall M.D. Comeau M.R. Yoon B.R. Kaufman D. Armitage R. Smith D.E. IL-33 amplifies both Th1- and Th2-type responses through its activity on human basophils, allergen-reactive Th2 cells, iNKT and NK cells.Int. Immunol. 2008; 20: 1019-1030Crossref PubMed Scopus (494) Google Scholar) effect of IL-33 on IFN-γ levels. Furthermore, there is a dearth of information about the effects of IFN-γ on IL-33. Some evidence suggests an IFN-γ-driven increase in IL-33 mRNA transcription in human skin keratinocytes (32.Seltmann J. Werfel T. Wittmann M. Evidence for a regulatory loop between IFN-γ and IL-33 in skin inflammation.Exp. Dermatol. 2013; 22: 102-107Crossref PubMed Scopus (52) Google Scholar, 33.Meephansan J. Tsuda H. Komine M. Tominaga S. Ohtsuki M. Regulation of IL-33 expression by IFN-γ and tumor necrosis factor-α in normal human epidermal keratinocytes.J. Invest. Dermatol. 2012; 132: 2593-2600Abstract Full Text Full Text PDF PubMed Scopus (87) Google Scholar), cardiac myocytes, and fibroblasts (47.Demyanets S. Kaun C. Pentz R. Krychtiuk K.A. Rauscher S. Pfaffenberger S. Zuckermann A. Aliabadi A. Gröger M. Maurer G. Huber K. Wojta J. Components of the interleukin-33/ST2 system are differentially expressed and regulated in human cardiac cells and in cells of the cardiac vasculature.J. Mol. Cell. Cardiol. 2013; 60: 16-26Abstract Full Text Full Text PDF PubMed Scopus (119) Google Scholar) but not dermal fibroblasts (32.Seltmann J. Werfel T. Wittmann M. Evidence for a regulatory loop between IFN-γ and IL-33 in skin inflammation.Exp. Dermatol. 2013; 22: 102-107Crossref PubMed Scopus (52) Google Scholar, 33.Meephansan J. Tsuda H. Komine M. Tominaga S. Ohtsuki M. 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• W2069066505 date "2014-04-01" @default.
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• W2069066505 title "IFN-γ Directly Controls IL-33 Protein Level through a STAT1- and LMP2-dependent Mechanism" @default.
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