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Volumn 37, Issue 4, 2015, Pages 419-427

Caspase-1: An integral regulator of innate immunity

Author keywords

Anti inflammatory; Autoinflammation; Defective; Procaspase 1; Variant

Indexed keywords

ENZYME PRECURSOR; INFLAMMASOME; INTERLEUKIN 1BETA CONVERTING ENZYME; PROCASPASE 1; UNCLASSIFIED DRUG;

EID: 84943580934     PISSN: 18632297     EISSN: 18632300     Source Type: Journal    
DOI: 10.1007/s00281-015-0494-4     Document Type: Review
Times cited : (72)

References (80)
  • 2
    • 66749174867 scopus 로고    scopus 로고
    • The inflammasomes: Guardians of the body
    • Martinon F, Mayor A, Tschopp J (2009) The inflammasomes: guardians of the body. Annu Rev Immunol 27:229-265. doi:10.1146/annurev.immunol.021908.132715
    • (2009) Annu Rev Immunol , vol.27 , pp. 229-265
    • Martinon, F.1    Mayor, A.2    Tschopp, J.3
  • 4
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases
    • Martinon F, Tschopp J (2004) Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117:561-574. doi:10.1016/j.cell.2004.05.004
    • (2004) Cell , vol.117 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 6
    • 0002928890 scopus 로고
    • Identification of a monocyte specific pre-interleukin 1 beta convertase activity
    • Kostura MJ, Tocci MJ, Limjuco G et al (1989) Identification of a monocyte specific pre-interleukin 1 beta convertase activity. Proc Natl Acad Sci U S A 86:5227-5231
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 5227-5231
    • Kostura, M.J.1    Tocci, M.J.2    Limjuco, G.3
  • 7
    • 0024551325 scopus 로고
    • A pre-aspartatespecific protease from human leukocytes that cleaves prointerleukin- 1 beta
    • Black RA, Kronheim SR, Merriam JE et al (1989) A pre-aspartatespecific protease from human leukocytes that cleaves prointerleukin- 1 beta. J Biol Chem 264:5323-5326
    • (1989) J Biol Chem , vol.264 , pp. 5323-5326
    • Black, R.A.1    Kronheim, S.R.2    Merriam, J.E.3
  • 8
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry NA, Bull HG, Calaycay JR et al (1992) A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356:768-774. doi:10.1038/356768a0
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3
  • 9
    • 0026517239 scopus 로고
    • Molecular cloning of the interleukin-1 beta converting enzyme
    • Cerretti DP, Kozlosky CJ, Mosley B et al (1992) Molecular cloning of the interleukin-1 beta converting enzyme. Science 256:97-100
    • (1992) Science , vol.256 , pp. 97-100
    • Cerretti, D.P.1    Kozlosky, C.J.2    Mosley, B.3
  • 10
    • 0028107827 scopus 로고
    • Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: A (p20/p10)2 homodimer
    • Walker NP, Talanian RV, Brady KD et al (1994) Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer. Cell 78:343-352
    • (1994) Cell , vol.78 , pp. 343-352
    • Walker, N.P.1    Talanian, R.V.2    Brady, K.D.3
  • 11
    • 4143096903 scopus 로고    scopus 로고
    • Crystal structures of a ligand-free and malonate-bound human caspase- 1: Implications for the mechanism of substrate binding
    • Romanowski MJ, Scheer JM, O’Brien T, McDowell RS (2004) Crystal structures of a ligand-free and malonate-bound human caspase- 1: implications for the mechanism of substrate binding. Structure 12:1361-1371. doi:10.1016/j.str.2004.05.010
    • (2004) Structure , vol.12 , pp. 1361-1371
    • Romanowski, M.J.1    Scheer, J.M.2    O’Brien, T.3    McDowell, R.S.4
  • 12
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J (2002) The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 10:417-426
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 13
    • 84869504451 scopus 로고    scopus 로고
    • Inflammasomes and their roles in health and disease
    • Lamkanfi M, Dixit VM (2012) Inflammasomes and their roles in health and disease. Annu Rev Cell Dev Biol 28:137-161. doi:10.1146/annurev-cellbio-101011-155745
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 137-161
    • Lamkanfi, M.1    Dixit, V.M.2
  • 14
    • 33847376042 scopus 로고    scopus 로고
    • Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation
    • Faustin B, Lartigue L, Bruey J-M et al (2007) Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell 25:713-724. doi:10.1016/j.molcel.2007.01. 032
    • (2007) Mol Cell , vol.25 , pp. 713-724
    • Faustin, B.1    Lartigue, L.2    Bruey, J.-M.3
  • 15
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden ED, Dietrich WF (2006) Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 38:240-244. doi:10.1038/ng1724
    • (2006) Nat Genet , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 16
    • 34250835251 scopus 로고    scopus 로고
    • The inflammasome mediates UVB-induced activation and secretion of interleukin- 1beta by keratinocytes
    • Feldmeyer L, Keller M, Niklaus G et al (2007) The inflammasome mediates UVB-induced activation and secretion of interleukin- 1beta by keratinocytes. Curr Biol 17:1140-1145. doi:10.1016/j. cub.2007.05.074
    • (2007) Curr Biol , vol.17 , pp. 1140-1145
    • Feldmeyer, L.1    Keller, M.2    Niklaus, G.3
  • 17
    • 84921909014 scopus 로고    scopus 로고
    • The inflammasome and autoinflammatory syndromes
    • 141125121526004
    • Broderick L, De Nardo D, Franklin BS et al (2014) The inflammasome and autoinflammatory syndromes. Annu Rev Pathol 10:141125121526004. doi:10.1146/annurev-pathol- 012414-040431
    • (2014) Annu Rev Pathol , vol.10
    • Broderick, L.1    De Nardo, D.2    Franklin, B.S.3
  • 18
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • Latz E, Xiao TS, Stutz A (2013) Activation and regulation of the inflammasomes. Nat Publ Group 13:397-411. doi:10.1038/nri3452
    • (2013) Nat Publ Group , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 19
    • 84861474688 scopus 로고    scopus 로고
    • Signaling in innate immunity and inflammation
    • pii: a006049
    • Newton, K, & Dixit, VM (2012) Signaling in innate immunity and inflammation. Cold Spring Harbor Perspectives in Biology, 4(3), pii: a006049. doi:10.1101/cshperspect.a006049
    • (2012) Cold Spring Harbor Perspectives in Biology , vol.4 , Issue.3
    • Newton, K.1    Dixit, V.M.2
  • 20
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF- κB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulatingNLRP3 expression
    • Bauernfeind FG, Horvath G, Stutz A et al (2009) Cutting edge: NF- κB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulatingNLRP3 expression. J Immunol 183:787-791. doi:10.4049/jimmunol.0901363
    • (2009) J Immunol , vol.183 , pp. 787-791
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3
  • 21
    • 84885459019 scopus 로고    scopus 로고
    • Cutting edge: TLR signaling licenses IRAK1 for rapid activation of the NLRP3 inflammasome
    • Fernandes-Alnemri T, Kang S, Anderson C et al (2013) Cutting edge: TLR signaling licenses IRAK1 for rapid activation of the NLRP3 inflammasome. J Immunol 191:3995-3999. doi:10.4049/jimmunol.1301681
    • (2013) J Immunol , vol.191 , pp. 3995-3999
    • Fernandes-Alnemri, T.1    Kang, S.2    Erson, C.3
  • 22
    • 84869088114 scopus 로고    scopus 로고
    • Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction
    • Schroder K, Sagulenko V, Zamoshnikova A et al (2012) Acute lipopolysaccharide priming boosts inflammasome activation independently of inflammasome sensor induction. Immunobiology. doi: 10.1016/j.imbio.2012.07.020
    • (2012) Immunobiology
    • Schroder, K.1    Sagulenko, V.2    Zamoshnikova, A.3
  • 23
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py BF, Kim M-S, Vakifahmetoglu-Norberg H, Yuan J (2013) Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol Cell 49:331-338. doi:10.1016/j. molcel.2012.11.009
    • (2013) Mol Cell , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.-S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 24
    • 84867770402 scopus 로고    scopus 로고
    • Nontranscriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Juliana C, Fernandes-Alnemri T, Kang S et al (2012) Nontranscriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem 287:36617-36622. doi: 10.1074/jbc.M112.407130
    • (2012) J Biol Chem , vol.287 , pp. 36617-36622
    • Juliana, C.1    Fernandes-Alnemri, T.2    Kang, S.3
  • 25
    • 84855989829 scopus 로고    scopus 로고
    • Inflammasomes in health and disease
    • Strowig T, Henao-Mejia J, Elinav E, Flavell R (2012) Inflammasomes in health and disease. Nature 481:278-286. doi: 10.1038/nature10759
    • (2012) Nature , vol.481 , pp. 278-286
    • Strowig, T.1    Henao-Mejia, J.2    Elinav, E.3    Flavell, R.4
  • 26
    • 0033515520 scopus 로고    scopus 로고
    • Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes
    • McDermott MF, Aksentijevich I, Galon J et al (1999) Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 97:133-144
    • (1999) Cell , vol.97 , pp. 133-144
    • McDermott, M.F.1    Aksentijevich, I.2    Galon, J.3
  • 27
    • 84882284037 scopus 로고    scopus 로고
    • Monogenic autoinflammatory diseases: Concept and clinical manifestations
    • Almeida de Jesus A, Goldbach-Mansky R (2013) Monogenic autoinflammatory diseases: concept and clinical manifestations. Clin Immunol 147:155-174. doi:10.1016/j.clim.2013.03.016
    • (2013) Clin Immunol , vol.147 , pp. 155-174
    • De Almeida Jesus, A.1    Goldbach-Mansky, R.2
  • 28
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a newgene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman HM, Mueller JL, Broide DH et al (2001) Mutation of a newgene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat Genet 29:301-305. doi:10.1038/ng756
    • (2001) Nat Genet , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3
  • 29
    • 0036899758 scopus 로고    scopus 로고
    • De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal-onset multisystem inflammatory disease (NOMID): A new member of the expanding family of pyrinassociated autoinflammatory diseases
    • Aksentijevich I, Nowak M, Mallah M et al (2002) De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal-onset multisystem inflammatory disease (NOMID): a new member of the expanding family of pyrinassociated autoinflammatory diseases. Arthritis Rheum 46:3340- 3348. doi:10.1002/art.10688
    • (2002) Arthritis Rheum , vol.46
    • Aksentijevich, I.1    Nowak, M.2    Mallah, M.3
  • 30
    • 0036302235 scopus 로고    scopus 로고
    • Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes
    • Feldmann J, Prieur A-M, Quartier P et al (2002) 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 71:198-203
    • (2002) Am J Hum Genet , vol.71 , pp. 198-203
    • Feldmann, J.1    Prieur, A.-M.2    Quartier, P.3
  • 31
    • 67650736238 scopus 로고    scopus 로고
    • Horror autoinflammaticus: The Molecular pathophysiology of autoinflammatory disease
    • Masters SL, Simon A, Aksentijevich I, Kastner DL (2009) Horror autoinflammaticus: the Molecular pathophysiology of autoinflammatory disease. Annu Rev Immunol 27:621-668. doi: 10.1146/annurev.immunol.25.022106.141627
    • (2009) Annu Rev Immunol , vol.27 , pp. 621-668
    • Masters, S.L.1    Simon, A.2    Aksentijevich, I.3    Kastner, D.L.4
  • 32
    • 77950363011 scopus 로고    scopus 로고
    • Autoinflammatory disease reloaded: A clinical perspective
    • Kastner DL, Aksentijevich I, Goldbach-Mansky R (2010) Autoinflammatory disease reloaded: a clinical perspective. Cell 140:784-790. doi:10.1016/j.cell.2010.03.002
    • (2010) Cell , vol.140 , pp. 784-790
    • Kastner, D.L.1    Aksentijevich, I.2    Goldbach-Mansky, R.3
  • 33
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller M, Rüegg A, Werner S, Beer H-D (2008) Active caspase-1 is a regulator of unconventional protein secretion. Cell 132:818-831. doi:10.1016/j.cell.2007.12.040
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Rüegg, A.2    Werner, S.3    Beer, H.-D.4
  • 34
    • 84894344719 scopus 로고    scopus 로고
    • Role of caspase-1 in nuclear translocation of IL-37, release of the cytokine, and IL-37 inhibition of innate immune responses
    • Bulau A-M, Nold MF, Li S et al (2014) 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. doi:10.1073/pnas.1324140111
    • (2014) Proc Natl Acad Sci U S A
    • Bulau, A.-M.1    Nold, M.F.2    Li, S.3
  • 35
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L, Abrami L, Girardin S et al (2006) Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126:1135-1145. doi:10.1016/j. cell.2006.07.033
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3
  • 36
    • 84893947749 scopus 로고    scopus 로고
    • Caspase-1 cleavage of the TLR adaptor TRIF inhibits autophagy and β-interferon production during Pseudomonas aeruginosa infection
    • Jabir MS, Ritchie ND, Li D et al (2014) Caspase-1 cleavage of the TLR adaptor TRIF inhibits autophagy and β-interferon production during Pseudomonas aeruginosa infection. Cell Host Microbe 15: 214-227. doi:10.1016/j.chom.2014.01.010
    • (2014) Cell Host Microbe , vol.15 , pp. 214-227
    • Jabir, M.S.1    Ritchie, N.D.2    Li, D.3
  • 37
    • 84939631887 scopus 로고    scopus 로고
    • Caspase-1 activation by NLRP3 inflammasome dampens IL-33-dependent house dust mite-induced allergic lung inflammation
    • Madouri F, Guillou N, Fauconnier L et al (2015) Caspase-1 activation by NLRP3 inflammasome dampens IL-33-dependent house dust mite-induced allergic lung inflammation. J Mol Cell Biol. doi:10.1093/jmcb/mjv012
    • (2015) J Mol Cell Biol
    • Madouri, F.1    Guillou, N.2    Fauconnier, L.3
  • 38
    • 83655191976 scopus 로고    scopus 로고
    • A protective role for inflammasome activation following injury
    • Osuka A, Hanschen M, Stoecklein V, Lederer JA (2012) A protective role for inflammasome activation following injury. Shock 37: 47-55. doi:10.1097/SHK.0b013e318234f7ff
    • (2012) Shock , vol.37 , pp. 47-55
    • Osuka, A.1    Hanschen, M.2    Stoecklein, V.3    Lederer, J.A.4
  • 39
    • 84858786676 scopus 로고    scopus 로고
    • Caspase-1 is hepatoprotective during trauma and hemorrhagic shock by reducing liver injury and inflammation
    • Menzel CL, Sun Q, Loughran PA et al (2011) Caspase-1 is hepatoprotective during trauma and hemorrhagic shock by reducing liver injury and inflammation. Mol Med 17:1031-1038. doi:10.2119/molmed.2011.00015
    • (2011) Mol Med , vol.17 , pp. 1031-1038
    • Menzel, C.L.1    Sun, Q.2    Loughran, P.A.3
  • 40
    • 84871608014 scopus 로고    scopus 로고
    • Naturally occurring genetic variants of human caspase-1 differ considerably in structure and the ability to activate interleukin-1β
    • Luksch H, Romanowski MJ, Chara O et al (2013) Naturally occurring genetic variants of human caspase-1 differ considerably in structure and the ability to activate interleukin-1β. Hum Mutat 34: 122-131. doi:10.1002/humu.22169
    • (2013) Hum Mutat , vol.34 , pp. 122-131
    • Luksch, H.1    Romanowski, M.J.2    Chara, O.3
  • 41
    • 84899560815 scopus 로고    scopus 로고
    • Human procaspase-1 variants with decreased enzymatic activity are associated with febrile episodes and may contribute to inflammation via RIP2 and NF-κB signaling
    • Heymann MC, Winkler S, Luksch H et al (2014) Human procaspase-1 variants with decreased enzymatic activity are associated with febrile episodes and may contribute to inflammation via RIP2 and NF-κB signaling. J Immunol 192:4379-4385. doi:10.4049/jimmunol.1203524
    • (2014) J Immunol , vol.192 , pp. 4379-4385
    • Heymann, M.C.1    Winkler, S.2    Luksch, H.3
  • 42
    • 0028984948 scopus 로고
    • Mice deficient in IL-1b-converting enzyme are defective in production of mature IL-1b and resistant to endotoxic shock
    • Li P (1995) Mice deficient in IL-1b-converting enzyme are defective in production of mature IL-1b and resistant to endotoxic shock. Cell 80:401-411. doi:10.1016/0092-8674(95)90490-5
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1
  • 43
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis inmice deficient in interleukin-1 beta converting enzyme
    • Kuida K, Lippke JA, Ku G et al (1995) Altered cytokine export and apoptosis inmice deficient in interleukin-1 beta converting enzyme. Science 267:2000-2003
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3
  • 44
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky A, Prevost MC, Sansonetti PJ (1992) Shigella flexneri induces apoptosis in infected macrophages. Nature 358:167-169. doi:10.1038/358167a0
    • (1992) Nature , vol.358 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 45
    • 80052179138 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptotic cell death
    • Miao EA, Rajan JV, Aderem A (2011) Caspase-1-induced pyroptotic cell death. Immunol Rev 243:206-214. doi:10.1111/j. 1600-065X.2011.01044.x
    • (2011) Immunol Rev , vol.243 , pp. 206-214
    • Miao, E.A.1    Rajan, J.V.2    Aderem, A.3
  • 46
    • 58449083290 scopus 로고    scopus 로고
    • Pyroptosis: Host cell death and inflammation
    • Bergsbaken T, Fink SL, Cookson BT (2009) Pyroptosis: host cell death and inflammation. Nat Rev Microbiol 7:99-109. doi:10.1038/nrmicro2070
    • (2009) Nat Rev Microbiol , vol.7 , pp. 99-109
    • Bergsbaken, T.1    Fink, S.L.2    Cookson, B.T.3
  • 47
    • 62649139025 scopus 로고    scopus 로고
    • Immunological and inflammatory functions of the interleukin-1 family
    • Dinarello CA (2009) Immunological and inflammatory functions of the interleukin-1 family. Annu Rev Immunol 27:519-550. doi:10.1146/annurev.immunol.021908.132612
    • (2009) Annu Rev Immunol , vol.27 , pp. 519-550
    • Dinarello, C.A.1
  • 48
    • 33847672241 scopus 로고    scopus 로고
    • NF-κB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
    • Miggin SM, Palsson-McDermott E, Dunne A et al (2007) NF-κB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1. Proc Natl Acad Sci U S A 104:3372-3377. doi:10.1073/pnas.0608100104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3372-3377
    • Miggin, S.M.1    Palsson-McDermott, E.2    Dunne, A.3
  • 49
    • 84860325913 scopus 로고    scopus 로고
    • Inflammasomeactivated caspase 7 cleaves PARP1 to enhance the expression of a subset of NF-κB target genes
    • Erener S, Pétrilli V, Kassner I et al (2012) Inflammasomeactivated caspase 7 cleaves PARP1 to enhance the expression of a subset of NF-κB target genes. Mol Cell. doi:10.1016/j. molcel.2012.02.016
    • (2012) Mol Cell
    • Erener, S.1    Pétrilli, V.2    Kassner, I.3
  • 50
    • 2642517305 scopus 로고    scopus 로고
    • Caspase-1 activates nuclear factor of the kappa-enhancer in B cells independently of its enzymatic activity
    • Lamkanfi M, Kalai M, Saelens X et al (2004) Caspase-1 activates nuclear factor of the kappa-enhancer in B cells independently of its enzymatic activity. J Biol Chem 279:24785-24793. doi:10.1074/jbc.M400985200
    • (2004) J Biol Chem , vol.279 , pp. 24785-24793
    • Lamkanfi, M.1    Kalai, M.2    Saelens, X.3
  • 51
    • 80053894653 scopus 로고    scopus 로고
    • Interaction patches of procaspase-1 caspase recruitment domains (CARDs) Are differently involved in procaspase-1 activation and receptorinteracting protein 2 (RIP2)-dependent nuclear factor B signaling
    • Kersse K, Lamkanfi M, Bertrand MJM et al (2011) Interaction patches of procaspase-1 caspase recruitment domains (CARDs) Are differently involved in procaspase-1 activation and receptorinteracting protein 2 (RIP2)-dependent nuclear factor B signaling. J Biol Chem 286:35874-35882. doi:10.1074/jbc.M111.242321
    • (2011) J Biol Chem , vol.286 , pp. 35874-35882
    • Kersse, K.1    Lamkanfi, M.2    Bertrand, M.3
  • 52
    • 33645757512 scopus 로고    scopus 로고
    • ASC directs NF-kappaB activation by regulating receptor interacting protein-2 (RIP2) caspase-1 interactions
    • Sarkar A, Duncan M, Hart J et al (2006) ASC directs NF-kappaB activation by regulating receptor interacting protein-2 (RIP2) caspase-1 interactions. J Immunol 176:4979-4986
    • (2006) J Immunol , vol.176 , pp. 4979-4986
    • Sarkar, A.1    Duncan, M.2    Hart, J.3
  • 53
    • 0024369393 scopus 로고
    • Monospecific antibodies implicate basic fibroblast growth factor in normal wound repair
    • Broadley KN, Aquino AM, Woodward SC et al (1989) Monospecific antibodies implicate basic fibroblast growth factor in normal wound repair. Lab Investig 61:571-575
    • (1989) Lab Investig , vol.61 , pp. 571-575
    • Broadley, K.N.1    Aquino, A.M.2    Woodward, S.C.3
  • 54
    • 0036020218 scopus 로고    scopus 로고
    • 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
    • Kumar S, Hanning CR, Brigham-Burke MR et al (2002) 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 18:61-71. doi:10.1006/cyto. 2002.0873
    • (2002) Cytokine , vol.18 , pp. 61-71
    • Kumar, S.1    Hanning, C.R.2    Brigham-Burke, M.R.3
  • 55
    • 45949111754 scopus 로고    scopus 로고
    • The IL-1 family member 7b translocates to the nucleus and down-regulates proinflammatory cytokines
    • Sharma S, Kulk N, Nold MF et al (2008) The IL-1 family member 7b translocates to the nucleus and down-regulates proinflammatory cytokines. J Immunol 180:5477-5482
    • (2008) J Immunol , vol.180 , pp. 5477-5482
    • Sharma, S.1    Kulk, N.2    Nold, M.F.3
  • 56
    • 77958149102 scopus 로고    scopus 로고
    • IL-37 is a fundamental inhibitor of innate immunity
    • Nold MF, Nold-Petry CA, Zepp JA et al (2010) IL-37 is a fundamental inhibitor of innate immunity. Nat Immunol 11:1014-1022. doi:10.1038/ni.1944
    • (2010) Nat Immunol , vol.11 , pp. 1014-1022
    • Nold, M.F.1    Nold-Petry, C.A.2    Zepp, J.A.3
  • 57
    • 84912106429 scopus 로고    scopus 로고
    • IL-37 inhibits inflammasome activation and disease severity in murine aspergillosis
    • Moretti S, Bozza S, Oikonomou V et al (2014) IL-37 inhibits inflammasome activation and disease severity in murine aspergillosis. PLoS Pathog 10:e1004462. doi:10.1371/journal.ppat. 1004462
    • (2014) Plos Pathog , vol.10
    • Moretti, S.1    Bozza, S.2    Oikonomou, V.3
  • 58
    • 84873710963 scopus 로고    scopus 로고
    • Nitric oxide suppresses NLRP3 inflammasome activation and protects against LPSinduced septic shock
    • Mao K, Chen S, Chen M et al (2013) Nitric oxide suppresses NLRP3 inflammasome activation and protects against LPSinduced septic shock. Cell Res 23:201-212. doi:10.1038/cr. 2013.6
    • (2013) Cell Res , vol.23 , pp. 201-212
    • Mao, K.1    Chen, S.2    Chen, M.3
  • 59
    • 84856024206 scopus 로고    scopus 로고
    • Inflammasome activation via intracellular NLRs triggered by bacterial infection
    • Koizumi Y, Toma C, Higa N et al (2011) Inflammasome activation via intracellular NLRs triggered by bacterial infection. Cell Microbiol 14:149-154. doi:10.1111/j.1462-5822.2011.01707.x
    • (2011) Cell Microbiol , vol.14 , pp. 149-154
    • Koizumi, Y.1    Toma, C.2    Higa, N.3
  • 60
    • 30344473341 scopus 로고    scopus 로고
    • Brown MS(2006) Protein sensors for membrane sterols
    • Goldstein JL, DeBose-Boyd RA, Brown MS(2006) Protein sensors for membrane sterols. Cell 124:35-46. doi:10.1016/j.cell.2005.12. 022
    • Cell , vol.124 , pp. 35-46
    • Goldstein, J.L.1    Debose-Boyd, R.A.2
  • 61
    • 84927922772 scopus 로고    scopus 로고
    • Caspase-1 cleavage of transcription factor GATA4 and regulation of cardiac cell fate
    • Aries A, Whitcomb J, Shao Wet al (2014) Caspase-1 cleavage of transcription factor GATA4 and regulation of cardiac cell fate. Cell Death Dis 5:e1566. doi:10.1038/cddis.2014.524
    • (2014) Cell Death Dis , vol.5
    • Aries, A.1    Whitcomb, J.2    Al, S.W.3
  • 62
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic V, Levine B (2009) Autophagy, immunity, and microbial adaptations. Cell Host Microbe 5:527-549. doi:10.1016/j.chom. 2009.05.016
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 63
    • 20344387475 scopus 로고    scopus 로고
    • Autophagy: Dual roles in life and death?
    • Baehrecke EH (2005) Autophagy: dual roles in life and death? Nat Rev Mol Cell Biol 6:505. doi:10.1038/nrm1666
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 505
    • Baehrecke, E.H.1
  • 64
    • 54049126870 scopus 로고    scopus 로고
    • The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases
    • Rebsamen M, Meylan E, Curran J, Tschopp J (2008) The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases. Cell Death Differ 15:1804-1811. doi:10.1038/cdd.2008. 119
    • (2008) Cell Death Differ , vol.15 , pp. 1804-1811
    • Rebsamen, M.1    Meylan, E.2    Curran, J.3    Tschopp, J.4
  • 65
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki N, Warming S, Lamkanfi M et al (2011) Non-canonical inflammasome activation targets caspase-11. Nature 479:117-121. doi:10.1038/nature10558
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3
  • 66
    • 84864600268 scopus 로고    scopus 로고
    • TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gramnegative bacteria
    • Rathinam VAK, Vanaja SK, Waggoner L et al (2012) TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gramnegative bacteria. Cell 150:606-619. doi:10.1016/j.cell.2012.07. 007
    • (2012) Cell , vol.150 , pp. 606-619
    • Rathinam, V.1    Vanaja, S.K.2    Waggoner, L.3
  • 67
    • 84867241369 scopus 로고    scopus 로고
    • Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-β (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein- and Nlrp3 inflammasome-mediated host defense against enteropathogens
    • Gurung P, Malireddi RKS, Anand PK et al (2012) Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-β (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein- and Nlrp3 inflammasome-mediated host defense against enteropathogens. J Biol Chem 287:34474-34483. doi:10.1074/jbc.M112.401406
    • (2012) J Biol Chem , vol.287 , pp. 34474-34483
    • Gurung, P.1    Malireddi, R.2    Anand, P.K.3
  • 68
    • 34249044447 scopus 로고    scopus 로고
    • Type I interferon signaling is required for activation of the inflammasome during Francisella infection
    • Henry T, Brotcke A, Weiss DS et al (2007) Type I interferon signaling is required for activation of the inflammasome during Francisella infection. J Exp Med 204:987-994. doi:10.1084/jem. 20062665
    • (2007) J Exp Med , vol.204 , pp. 987-994
    • Henry, T.1    Brotcke, A.2    Weiss, D.S.3
  • 69
    • 84895807942 scopus 로고    scopus 로고
    • Role of interleukin 33 in respiratory allergy and asthma
    • Makrinioti H, Toussaint M, Jackson DJ et al (2014) Role of interleukin 33 in respiratory allergy and asthma. Lancet Respir Med 2: 226-237. doi:10.1016/S2213-2600(13)70261-3
    • (2014) Lancet Respir Med , vol.2 , pp. 226-237
    • Makrinioti, H.1    Toussaint, M.2    Jackson, D.J.3
  • 70
    • 84889653647 scopus 로고    scopus 로고
    • Emerging role of interleukin-33 in autoimmune diseases
    • Pei C, Barbour M, Fairlie-Clarke KJ et al (2013) Emerging role of interleukin-33 in autoimmune diseases. Immunology 141:9-17. doi:10.1111/imm.12174
    • (2013) Immunology , vol.141 , pp. 9-17
    • Pei, C.1    Barbour, M.2    Fairlie-Clarke, K.J.3
  • 71
    • 53249113212 scopus 로고    scopus 로고
    • The IL-33/ST2 pathway: Therapeutic target and novel biomarker
    • Kakkar R, Lee RT (2008) The IL-33/ST2 pathway: therapeutic target and novel biomarker. Nat Rev Drug Discov 7:827-840. doi:10.1038/nrd2660
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 827-840
    • Kakkar, R.1    Lee, R.T.2
  • 72
    • 67049158193 scopus 로고    scopus 로고
    • The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1
    • Cayrol C, Girard J-P (2009) The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1. Proc Natl Acad Sci U S A 106:9021-9026. doi:10.1073/pnas.0812690106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9021-9026
    • Cayrol, C.1    Girard, J.-P.2
  • 73
    • 79954597670 scopus 로고    scopus 로고
    • An unexpected role for uric acid as an inducer of T helper 2 cell immunity to inhaled antigens and inflammatory mediator of allergic asthma
    • Kool M, Willart MAM, van Nimwegen M et al (2011) An unexpected role for uric acid as an inducer of T helper 2 cell immunity to inhaled antigens and inflammatory mediator of allergic asthma. Immunity 34:527-540. doi:10.1016/j.immuni.2011.03.015
    • (2011) Immunity , vol.34 , pp. 527-540
    • Kool, M.1    Willart, M.2    Van Nimwegen, M.3
  • 74
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor kappaB signaling
    • Hoffmann A, Baltimore D (2006) Circuitry of nuclear factor kappaB signaling. Immunol Rev 210:171-186. doi:10.1111/j. 0105-2896.2006.00375.x
    • (2006) Immunol Rev , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 75
    • 0035895992 scopus 로고    scopus 로고
    • Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NFkappaB
    • Ogura Y, Inohara N, Benito A et al (2001) Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NFkappaB. J Biol Chem 276:4812-4818. doi:10.1074/jbc. M008072200
    • (2001) J Biol Chem , vol.276 , pp. 4812-4818
    • Ogura, Y.1    Inohara, N.2    Benito, A.3
  • 76
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S, Newton K, Monack DM et al (2004) Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430:213-218. doi:10.1038/nature02664
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.M.3
  • 77
    • 84858761335 scopus 로고    scopus 로고
    • Inflammasome activators induce interleukin-1α secretion via distinct pathways with differential requirement for the protease function of caspase-1
    • Groß O, Yazdi AS, Thomas CJ et al (2012) Inflammasome activators induce interleukin-1α secretion via distinct pathways with differential requirement for the protease function of caspase-1. Immunity 36:388-400. doi:10.1016/j.immuni.2012.01.018
    • (2012) Immunity , vol.36 , pp. 388-400
    • Groß, O.1    Yazdi, A.S.2    Thomas, C.J.3
  • 78
    • 78650210802 scopus 로고    scopus 로고
    • Differential requirement for Caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing
    • Broz P, von Moltke J, Jones JW et al (2010) Differential requirement for Caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing. Cell Host Microbe 8:471-483. doi:10.1016/j.chom.2010.11.007
    • (2010) Cell Host Microbe , vol.8 , pp. 471-483
    • Broz, P.1    Von Moltke, J.2    Jones, J.W.3
  • 79
    • 84914132432 scopus 로고    scopus 로고
    • Caspase-1 autoproteolysis is differentially required for NLRP1b and NLRP3 inflammasome function
    • Guey B, Bodnar M, Manié SN et al (2014) Caspase-1 autoproteolysis is differentially required for NLRP1b and NLRP3 inflammasome function. Proc Natl Acad Sci U S A 111:17254- 17259. doi:10.1073/pnas.1415756111
    • (2014) Proc Natl Acad Sci U S a 111:17254- , pp. 17259
    • Guey, B.1    Bodnar, M.2    Manié, S.N.3
  • 80
    • 84893835896 scopus 로고    scopus 로고
    • Activation of the NLRP1b inflammasome independently of ASCmediated caspase-1 autoproteolysis and speck formation
    • Van Opdenbosch N, Gurung P, Vande Walle L et al (2014) Activation of the NLRP1b inflammasome independently of ASCmediated caspase-1 autoproteolysis and speck formation. Nat Commun 5:3209. doi:10.1038/ncomms4209
    • (2014) Nat Commun , vol.5 , pp. 3209
    • Van Opdenbosch, N.1    Gurung, P.2    Vande Walle, L.3


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