메뉴 건너뛰기




Volumn 10, Issue 9, 2014, Pages

Reactive Oxygen Species Regulate Caspase-11 Expression and Activation of the Non-canonical NLRP3 Inflammasome during Enteric Pathogen Infection

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 11; CRYOPYRIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 18; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; CARD15 PROTEIN, MOUSE; CARRIER PROTEIN; CASP11 PROTEIN, MOUSE; CASPASE; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CIAS1 PROTEIN, MOUSE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK2 PROTEIN, MOUSE;

EID: 84907584408     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004410     Document Type: Article
Times cited : (84)

References (64)
  • 2
    • 36549048075 scopus 로고    scopus 로고
    • Utility of the Citrobacter rodentium infection model in laboratory mice
    • Borenshtein D, McBee ME, Schauer DB, (2008) Utility of the Citrobacter rodentium infection model in laboratory mice. Curr Opin Gastroenterol 24: 32–37.
    • (2008) Curr Opin Gastroenterol , vol.24 , pp. 32-37
    • Borenshtein, D.1    McBee, M.E.2    Schauer, D.B.3
  • 4
    • 84861972274 scopus 로고    scopus 로고
    • Regulated virulence controls the ability of a pathogen to compete with the gut microbiota
    • Kamada N, Kim YG, Sham HP, Vallance BA, Puente JL, et al. (2012) Regulated virulence controls the ability of a pathogen to compete with the gut microbiota. Science 336: 1325–1329.
    • (2012) Science , vol.336 , pp. 1325-1329
    • Kamada, N.1    Kim, Y.G.2    Sham, H.P.3    Vallance, B.A.4    Puente, J.L.5
  • 5
    • 0041322730 scopus 로고    scopus 로고
    • Central role for B lymphocytes and CD4+ T cells in immunity to infection by the attaching and effacing pathogen Citrobacter rodentium
    • Simmons CP, Clare S, Ghaem-Maghami M, Uren TK, Rankin J, et al. (2003) Central role for B lymphocytes and CD4+ T cells in immunity to infection by the attaching and effacing pathogen Citrobacter rodentium. Infect Immun 71: 5077–5086.
    • (2003) Infect Immun , vol.71 , pp. 5077-5086
    • Simmons, C.P.1    Clare, S.2    Ghaem-Maghami, M.3    Uren, T.K.4    Rankin, J.5
  • 6
    • 0347364688 scopus 로고    scopus 로고
    • Critical role of T cell-dependent serum antibody, but not the gut-associated lymphoid tissue, for surviving acute mucosal infection with Citrobacter rodentium, an attaching and effacing pathogen
    • Bry L, Brenner MB, (2004) Critical role of T cell-dependent serum antibody, but not the gut-associated lymphoid tissue, for surviving acute mucosal infection with Citrobacter rodentium, an attaching and effacing pathogen. J Immunol 172: 433–441.
    • (2004) J Immunol , vol.172 , pp. 433-441
    • Bry, L.1    Brenner, M.B.2
  • 7
    • 38849189905 scopus 로고    scopus 로고
    • MyD88 signalling plays a critical role in host defence by controlling pathogen burden and promoting epithelial cell homeostasis during Citrobacter rodentium-induced colitis
    • Gibson DL, Ma C, Bergstrom KS, Huang JT, Man C, et al. (2008) MyD88 signalling plays a critical role in host defence by controlling pathogen burden and promoting epithelial cell homeostasis during Citrobacter rodentium-induced colitis. Cell Microbiol 10: 618–631.
    • (2008) Cell Microbiol , vol.10 , pp. 618-631
    • Gibson, D.L.1    Ma, C.2    Bergstrom, K.S.3    Huang, J.T.4    Man, C.5
  • 8
    • 38049174332 scopus 로고    scopus 로고
    • Toll-like receptor 2 plays a critical role in maintaining mucosal integrity during Citrobacter rodentium-induced colitis
    • Gibson DL, Ma C, Rosenberger CM, Bergstrom KS, Valdez Y, et al. (2008) Toll-like receptor 2 plays a critical role in maintaining mucosal integrity during Citrobacter rodentium-induced colitis. Cell Microbiol 10: 388–403.
    • (2008) Cell Microbiol , vol.10 , pp. 388-403
    • Gibson, D.L.1    Ma, C.2    Rosenberger, C.M.3    Bergstrom, K.S.4    Valdez, Y.5
  • 9
    • 79956319462 scopus 로고    scopus 로고
    • The Nod2 sensor promotes intestinal pathogen eradication via the chemokine CCL2-dependent recruitment of inflammatory monocytes
    • Kim YG, Kamada N, Shaw MH, Warner N, Chen GY, et al. (2011) The Nod2 sensor promotes intestinal pathogen eradication via the chemokine CCL2-dependent recruitment of inflammatory monocytes. Immunity 34: 769–780.
    • (2011) Immunity , vol.34 , pp. 769-780
    • Kim, Y.G.1    Kamada, N.2    Shaw, M.H.3    Warner, N.4    Chen, G.Y.5
  • 10
    • 79960131814 scopus 로고    scopus 로고
    • Identification of an innate T helper type 17 response to intestinal bacterial pathogens
    • Geddes K, Rubino SJ, Magalhaes JG, Streutker C, Le Bourhis L, et al. (2011) Identification of an innate T helper type 17 response to intestinal bacterial pathogens. Nat Med 17: 837–844.
    • (2011) Nat Med , vol.17 , pp. 837-844
    • Geddes, K.1    Rubino, S.J.2    Magalhaes, J.G.3    Streutker, C.4    Le Bourhis, L.5
  • 11
    • 17944380130 scopus 로고    scopus 로고
    • CARD4/Nod1 mediates NF-kappaB and JNK activation by invasive Shigella flexneri
    • Girardin SE, Tournebize R, Mavris M, Page AL, Li X, et al. (2001) CARD4/Nod1 mediates NF-kappaB and JNK activation by invasive Shigella flexneri. EMBO Rep 2: 736–742.
    • (2001) EMBO Rep , vol.2 , pp. 736-742
    • Girardin, S.E.1    Tournebize, R.2    Mavris, M.3    Page, A.L.4    Li, X.5
  • 12
    • 0033532091 scopus 로고    scopus 로고
    • Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kappaB
    • Bertin J, Nir WJ, Fischer CM, Tayber OV, Errada PR, et al. (1999) Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kappaB. J Biol Chem 274: 12955–12958.
    • (1999) J Biol Chem , vol.274 , pp. 12955-12958
    • Bertin, J.1    Nir, W.J.2    Fischer, C.M.3    Tayber, O.V.4    Errada, P.R.5
  • 13
    • 33846936219 scopus 로고    scopus 로고
    • RICK/RIP2 mediates innate immune responses induced through Nod1 and Nod2 but not TLRs
    • Park JH, Kim YG, McDonald C, Kanneganti TD, Hasegawa M, et al. (2007) RICK/RIP2 mediates innate immune responses induced through Nod1 and Nod2 but not TLRs. J Immunol 178: 2380–2386.
    • (2007) J Immunol , vol.178 , pp. 2380-2386
    • Park, J.H.1    Kim, Y.G.2    McDonald, C.3    Kanneganti, T.D.4    Hasegawa, M.5
  • 14
    • 84879596906 scopus 로고    scopus 로고
    • K(+) Efflux Is the Common Trigger of NLRP3 Inflammasome Activation by Bacterial Toxins and Particulate Matter
    • Munoz-Planillo R, Kuffa P, Martinez-Colon G, Smith BL, Rajendiran TM, et al. (2013) K(+) Efflux Is the Common Trigger of NLRP3 Inflammasome Activation by Bacterial Toxins and Particulate Matter. Immunity 38: 1142–1153.
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Munoz-Planillo, R.1    Kuffa, P.2    Martinez-Colon, G.3    Smith, B.L.4    Rajendiran, T.M.5
  • 15
    • 76249108958 scopus 로고    scopus 로고
    • Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1beta, depending on listeriolysin O and NLRP3
    • Meixenberger K, Pache F, Eitel J, Schmeck B, Hippenstiel S, et al. (2010) Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1beta, depending on listeriolysin O and NLRP3. J Immunol 184: 922–930.
    • (2010) J Immunol , vol.184 , pp. 922-930
    • Meixenberger, K.1    Pache, F.2    Eitel, J.3    Schmeck, B.4    Hippenstiel, S.5
  • 16
    • 79960408020 scopus 로고    scopus 로고
    • The NLRP3 inflammasome is differentially activated by pneumolysin variants and contributes to host defense in pneumococcal pneumonia
    • Witzenrath M, Pache F, Lorenz D, Koppe U, Gutbier B, et al. (2011) The NLRP3 inflammasome is differentially activated by pneumolysin variants and contributes to host defense in pneumococcal pneumonia. J Immunol 187: 434–440.
    • (2011) J Immunol , vol.187 , pp. 434-440
    • Witzenrath, M.1    Pache, F.2    Lorenz, D.3    Koppe, U.4    Gutbier, B.5
  • 17
    • 84879527408 scopus 로고    scopus 로고
    • Caspase-11 activation in response to bacterial secretion systems that access the host cytosol
    • Casson CN, Copenhaver AM, Zwack EE, Nguyen HT, Strowig T, et al. (2013) Caspase-11 activation in response to bacterial secretion systems that access the host cytosol. PLoS Pathog 9: e1003400.
    • (2013) PLoS Pathog , vol.9 , pp. e1003400
    • Casson, C.N.1    Copenhaver, A.M.2    Zwack, E.E.3    Nguyen, H.T.4    Strowig, T.5
  • 18
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression
    • Bauernfeind FG, Horvath G, Stutz A, Alnemri ES, MacDonald K, et al. (2009) Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol 183: 787–791.
    • (2009) J Immunol , vol.183 , pp. 787-791
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3    Alnemri, E.S.4    Macdonald, K.5
  • 19
    • 77953464026 scopus 로고    scopus 로고
    • Nlrp3: an immune sensor of cellular stress and infection
    • Lamkanfi M, Kanneganti TD, (2010) Nlrp3: an immune sensor of cellular stress and infection. Int J Biochem Cell Biol 42: 792–795.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 792-795
    • Lamkanfi, M.1    Kanneganti, T.D.2
  • 20
    • 77649179433 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production?
    • Tschopp J, Schroder K, (2010) NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production? Nat Rev Immunol 10: 210–215.
    • (2010) Nat Rev Immunol , vol.10 , pp. 210-215
    • Tschopp, J.1    Schroder, K.2
  • 21
    • 35348932070 scopus 로고    scopus 로고
    • Intracellular NOD-like receptors in host defense and disease
    • Kanneganti TD, Lamkanfi M, Nunez G, (2007) Intracellular NOD-like receptors in host defense and disease. Immunity 27: 549–559.
    • (2007) Immunity , vol.27 , pp. 549-559
    • Kanneganti, T.D.1    Lamkanfi, M.2    Nunez, G.3
  • 22
    • 32944462834 scopus 로고    scopus 로고
    • Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
    • Kanneganti TD, Ozoren N, Body-Malapel M, Amer A, Park JH, et al. (2006) Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440: 233–236.
    • (2006) Nature , vol.440 , pp. 233-236
    • Kanneganti, T.D.1    Ozoren, N.2    Body-Malapel, M.3    Amer, A.4    Park, J.H.5
  • 23
    • 0037192793 scopus 로고    scopus 로고
    • PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B
    • Manji GA, Wang L, Geddes BJ, Brown M, Merriam S, et al. (2002) PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B. J Biol Chem 277: 11570–11575.
    • (2002) J Biol Chem , vol.277 , pp. 11570-11575
    • Manji, G.A.1    Wang, L.2    Geddes, B.J.3    Brown, M.4    Merriam, S.5
  • 24
    • 16244362671 scopus 로고    scopus 로고
    • Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells
    • Fink SL, Cookson BT, (2005) Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect Immun 73: 1907–1916.
    • (2005) Infect Immun , vol.73 , pp. 1907-1916
    • Fink, S.L.1    Cookson, B.T.2
  • 25
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • Miao EA, Leaf IA, Treuting PM, Mao DP, Dors M, et al. (2010) Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol 11: 1136–1142.
    • (2010) Nat Immunol , vol.11 , pp. 1136-1142
    • Miao, E.A.1    Leaf, I.A.2    Treuting, P.M.3    Mao, D.P.4    Dors, M.5
  • 26
  • 27
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • Wang S, Miura M, Jung YK, Zhu H, Li E, et al. (1998) Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92: 501–509.
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.1    Miura, M.2    Jung, Y.K.3    Zhu, H.4    Li, E.5
  • 28
    • 84873202976 scopus 로고    scopus 로고
    • Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila
    • Case CL, Kohler LJ, Lima JB, Strowig T, de Zoete MR, et al. (2013) Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila. Proc Natl Acad Sci U S A 110: 1851–1856.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1851-1856
    • Case, C.L.1    Kohler, L.J.2    Lima, J.B.3    Strowig, T.4    De Zoete, M.R.5
  • 29
    • 84867333450 scopus 로고    scopus 로고
    • Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
    • Broz P, Ruby T, Belhocine K, Bouley DM, Kayagaki N, et al. (2012) Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1. Nature 490: 288–291.
    • (2012) Nature , vol.490 , pp. 288-291
    • Broz, P.1    Ruby, T.2    Belhocine, K.3    Bouley, D.M.4    Kayagaki, N.5
  • 30
    • 84867241369 scopus 로고    scopus 로고
    • Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-beta (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein- and Nlrp3 inflammasome-mediated host defense against enteropathogens
    • Gurung P, Malireddi RK, Anand PK, Demon D, Walle LV, et al. (2012) Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-beta (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.
    • (2012) J Biol Chem , vol.287 , pp. 34474-34483
    • Gurung, P.1    Malireddi, R.K.2    Anand, P.K.3    Demon, D.4    Walle, L.V.5
  • 31
    • 84864600268 scopus 로고    scopus 로고
    • TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria
    • Rathinam VA, Vanaja SK, Waggoner L, Sokolovska A, Becker C, et al. (2012) TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria. Cell 150: 606–619.
    • (2012) Cell , vol.150 , pp. 606-619
    • Rathinam, V.A.1    Vanaja, S.K.2    Waggoner, L.3    Sokolovska, A.4    Becker, C.5
  • 32
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S, Newton K, Monack DM, Vucic D, French DM, et al. (2004) Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430: 213–218.
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.M.3    Vucic, D.4    French, D.M.5
  • 33
    • 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
  • 34
    • 33744464740 scopus 로고    scopus 로고
    • Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages
    • Franchi L, Amer A, Body-Malapel M, Kanneganti TD, Ozoren N, et al. (2006) Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages. Nat Immunol 7: 576–582.
    • (2006) Nat Immunol , vol.7 , pp. 576-582
    • Franchi, L.1    Amer, A.2    Body-Malapel, M.3    Kanneganti, T.D.4    Ozoren, N.5
  • 35
    • 33744493091 scopus 로고    scopus 로고
    • Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
    • Miao EA, Alpuche-Aranda CM, Dors M, Clark AE, Bader MW, et al. (2006) Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf. Nat Immunol 7: 569–575.
    • (2006) Nat Immunol , vol.7 , pp. 569-575
    • Miao, E.A.1    Alpuche-Aranda, C.M.2    Dors, M.3    Clark, A.E.4    Bader, M.W.5
  • 37
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • Nakahira K, Haspel JA, Rathinam VA, Lee SJ, Dolinay T, et al. (2011) Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol 12: 222–230.
    • (2011) Nat Immunol , vol.12 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.3    Lee, S.J.4    Dolinay, T.5
  • 38
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R, Yazdi AS, Menu P, Tschopp J, (2011) A role for mitochondria in NLRP3 inflammasome activation. Nature 469: 221–225.
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 39
    • 84876685141 scopus 로고    scopus 로고
    • Receptor interacting protein kinase 2-mediated mitophagy regulates inflammasome activation during virus infection
    • Lupfer C, Thomas PG, Anand PK, Vogel P, Milasta S, et al. (2013) Receptor interacting protein kinase 2-mediated mitophagy regulates inflammasome activation during virus infection. Nat Immunol 14: 480–488.
    • (2013) Nat Immunol , vol.14 , pp. 480-488
    • Lupfer, C.1    Thomas, P.G.2    Anand, P.K.3    Vogel, P.4    Milasta, S.5
  • 40
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, et al. (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19: 5720–5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5
  • 41
    • 0029955623 scopus 로고    scopus 로고
    • Reactive oxygen species mediate cytokine activation of c-Jun NH2-terminal kinases
    • Lo YY, Wong JM, Cruz TF, (1996) Reactive oxygen species mediate cytokine activation of c-Jun NH2-terminal kinases. J Biol Chem 271: 15703–15707.
    • (1996) J Biol Chem , vol.271 , pp. 15703-15707
    • Lo, Y.Y.1    Wong, J.M.2    Cruz, T.F.3
  • 42
    • 84883196771 scopus 로고    scopus 로고
    • Pellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis
    • Yang S, Wang B, Humphries F, Jackson R, Healy ME, et al. (2013) Pellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis. Nat Immunol 14: 927–936.
    • (2013) Nat Immunol , vol.14 , pp. 927-936
    • Yang, S.1    Wang, B.2    Humphries, F.3    Jackson, R.4    Healy, M.E.5
  • 43
    • 84900564237 scopus 로고    scopus 로고
    • Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
    • Meunier E, Dick MS, Dreier RF, Schurmann N, Kenzelmann Broz D, et al. (2014) Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases. Nature 509: 366–370.
    • (2014) Nature , vol.509 , pp. 366-370
    • Meunier, E.1    Dick, M.S.2    Dreier, R.F.3    Schurmann, N.4    Kenzelmann Broz, D.5
  • 44
    • 84874189388 scopus 로고    scopus 로고
    • Caspase-11 protects against bacteria that escape the vacuole
    • Aachoui Y, Leaf IA, Hagar JA, Fontana MF, Campos CG, et al. (2013) Caspase-11 protects against bacteria that escape the vacuole. Science 339: 975–978.
    • (2013) Science , vol.339 , pp. 975-978
    • Aachoui, Y.1    Leaf, I.A.2    Hagar, J.A.3    Fontana, M.F.4    Campos, C.G.5
  • 45
    • 84899098318 scopus 로고    scopus 로고
    • Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS
    • Pilla DM, Hagar JA, Haldar AK, Mason AK, Degrandi D, et al. (2014) Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS. Proc Natl Acad Sci U S A 111: 6046–6051.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 6046-6051
    • Pilla, D.M.1    Hagar, J.A.2    Haldar, A.K.3    Mason, A.K.4    Degrandi, D.5
  • 46
    • 84883775365 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation by intracellular LPS independent of TLR4
    • Kayagaki N, Wong MT, Stowe IB, Ramani SR, Gonzalez LC, et al. (2013) Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 341: 1246–1249.
    • (2013) Science , vol.341 , pp. 1246-1249
    • Kayagaki, N.1    Wong, M.T.2    Stowe, I.B.3    Ramani, S.R.4    Gonzalez, L.C.5
  • 47
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock
    • Hagar JA, Powell DA, Aachoui Y, Ernst RK, Miao EA, (2013) Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science 341: 1250–1253.
    • (2013) Science , vol.341 , pp. 1250-1253
    • Hagar, J.A.1    Powell, D.A.2    Aachoui, Y.3    Ernst, R.K.4    Miao, E.A.5
  • 48
    • 84860859210 scopus 로고    scopus 로고
    • Role of inflammasomes in host defense against Citrobacter rodentium infection
    • Liu Z, Zaki MH, Vogel P, Gurung P, Finlay BB, et al. (2012) Role of inflammasomes in host defense against Citrobacter rodentium infection. J Biol Chem 287: 16955–16964.
    • (2012) J Biol Chem , vol.287 , pp. 16955-16964
    • Liu, Z.1    Zaki, M.H.2    Vogel, P.3    Gurung, P.4    Finlay, B.B.5
  • 49
    • 84864292536 scopus 로고    scopus 로고
    • Caspase-11 promotes the fusion of phagosomes harboring pathogenic bacteria with lysosomes by modulating actin polymerization
    • Akhter A, Caution K, Abu Khweek A, Tazi M, Abdulrahman BA, et al. (2012) Caspase-11 promotes the fusion of phagosomes harboring pathogenic bacteria with lysosomes by modulating actin polymerization. Immunity 37: 35–47.
    • (2012) Immunity , vol.37 , pp. 35-47
    • Akhter, A.1    Caution, K.2    Abu Khweek, A.3    Tazi, M.4    Abdulrahman, B.A.5
  • 50
    • 0034679578 scopus 로고    scopus 로고
    • Salmonella exploits caspase-1 to colonize Peyer's patches in a murine typhoid model
    • Monack DM, Hersh D, Ghori N, Bouley D, Zychlinsky A, et al. (2000) Salmonella exploits caspase-1 to colonize Peyer's patches in a murine typhoid model. J Exp Med 192: 249–258.
    • (2000) J Exp Med , vol.192 , pp. 249-258
    • Monack, D.M.1    Hersh, D.2    Ghori, N.3    Bouley, D.4    Zychlinsky, A.5
  • 51
    • 84864812784 scopus 로고    scopus 로고
    • NLRP1-dependent pyroptosis leads to acute lung injury and morbidity in mice
    • Kovarova M, Hesker PR, Jania L, Nguyen M, Snouwaert JN, et al. (2012) NLRP1-dependent pyroptosis leads to acute lung injury and morbidity in mice. J Immunol 189: 2006–2016.
    • (2012) J Immunol , vol.189 , pp. 2006-2016
    • Kovarova, M.1    Hesker, P.R.2    Jania, L.3    Nguyen, M.4    Snouwaert, J.N.5
  • 52
    • 68149100523 scopus 로고    scopus 로고
    • NLRP3 (NALP3, Cryopyrin) facilitates in vivo caspase-1 activation, necrosis, and HMGB1 release via inflammasome-dependent and -independent pathways
    • Willingham SB, Allen IC, Bergstralh DT, Brickey WJ, Huang MT, et al. (2009) NLRP3 (NALP3, Cryopyrin) facilitates in vivo caspase-1 activation, necrosis, and HMGB1 release via inflammasome-dependent and -independent pathways. J Immunol 183: 2008–2015.
    • (2009) J Immunol , vol.183 , pp. 2008-2015
    • Willingham, S.B.1    Allen, I.C.2    Bergstralh, D.T.3    Brickey, W.J.4    Huang, M.T.5
  • 53
    • 83355163381 scopus 로고    scopus 로고
    • TLR2 and RIP2 pathways mediate autophagy of Listeria monocytogenes via extracellular signal-regulated kinase (ERK) activation
    • Anand PK, Tait SW, Lamkanfi M, Amer AO, Nunez G, et al. (2011) TLR2 and RIP2 pathways mediate autophagy of Listeria monocytogenes via extracellular signal-regulated kinase (ERK) activation. J Biol Chem 286: 42981–42991.
    • (2011) J Biol Chem , vol.286 , pp. 42981-42991
    • Anand, P.K.1    Tait, S.W.2    Lamkanfi, M.3    Amer, A.O.4    Nunez, G.5
  • 54
    • 66949138341 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2
    • Bertrand MJ, Doiron K, Labbe K, Korneluk RG, Barker PA, et al. (2009) Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2. Immunity 30: 789–801.
    • (2009) Immunity , vol.30 , pp. 789-801
    • Bertrand, M.J.1    Doiron, K.2    Labbe, K.3    Korneluk, R.G.4    Barker, P.A.5
  • 55
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • Mariathasan S, Weiss DS, Newton K, McBride J, O'Rourke K, et al. (2006) Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440: 228–232.
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1    Weiss, D.S.2    Newton, K.3    McBride, J.4    O'Rourke, K.5
  • 56
    • 77954958602 scopus 로고    scopus 로고
    • Aspergillus fumigatus stimulates the NLRP3 inflammasome through a pathway requiring ROS production and the Syk tyrosine kinase
    • Said-Sadier N, Padilla E, Langsley G, Ojcius DM, (2010) Aspergillus fumigatus stimulates the NLRP3 inflammasome through a pathway requiring ROS production and the Syk tyrosine kinase. PLoS One 5: e10008.
    • (2010) PLoS One , vol.5 , pp. e10008
    • Said-Sadier, N.1    Padilla, E.2    Langsley, G.3    Ojcius, D.M.4
  • 57
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • Hugot JP, Chamaillard M, Zouali H, Lesage S, Cezard JP, et al. (2001) Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature 411: 599–603.
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.P.1    Chamaillard, M.2    Zouali, H.3    Lesage, S.4    Cezard, J.P.5
  • 58
    • 84879212560 scopus 로고    scopus 로고
    • Development of a peptidoglycan-polysaccharide murine model of Crohn's disease: effect of genetic background
    • Reingold L, Rahal K, Schmiedlin-Ren P, Rittershaus AC, Bender D, et al. (2013) Development of a peptidoglycan-polysaccharide murine model of Crohn's disease: effect of genetic background. Inflamm Bowel Dis 19: 1238–1244.
    • (2013) Inflamm Bowel Dis , vol.19 , pp. 1238-1244
    • Reingold, L.1    Rahal, K.2    Schmiedlin-Ren, P.3    Rittershaus, A.C.4    Bender, D.5
  • 59
    • 84874896525 scopus 로고    scopus 로고
    • Nucleotide-binding oligomerization domain 2 signaling promotes hyperresponsive macrophages and colitis in IL-10-deficient mice
    • Jamontt J, Petit S, Clark N, Parkinson SJ, Smith P, (2013) Nucleotide-binding oligomerization domain 2 signaling promotes hyperresponsive macrophages and colitis in IL-10-deficient mice. J Immunol 190: 2948–2958.
    • (2013) J Immunol , vol.190 , pp. 2948-2958
    • Jamontt, J.1    Petit, S.2    Clark, N.3    Parkinson, S.J.4    Smith, P.5
  • 60
    • 84873372079 scopus 로고    scopus 로고
    • NOD2-mediated dysbiosis predisposes mice to transmissible colitis and colorectal cancer
    • Couturier-Maillard A, Secher T, Rehman A, Normand S, De Arcangelis A, et al. (2013) NOD2-mediated dysbiosis predisposes mice to transmissible colitis and colorectal cancer. J Clin Invest 123: 700–711.
    • (2013) J Clin Invest , vol.123 , pp. 700-711
    • Couturier-Maillard, A.1    Secher, T.2    Rehman, A.3    Normand, S.4    De Arcangelis, A.5
  • 61
    • 33748493563 scopus 로고    scopus 로고
    • Nucleotide binding oligomerization domain 2 deficiency leads to dysregulated TLR2 signaling and induction of antigen-specific colitis
    • Watanabe T, Kitani A, Murray PJ, Wakatsuki Y, Fuss IJ, et al. (2006) Nucleotide binding oligomerization domain 2 deficiency leads to dysregulated TLR2 signaling and induction of antigen-specific colitis. Immunity 25: 473–485.
    • (2006) Immunity , vol.25 , pp. 473-485
    • Watanabe, T.1    Kitani, A.2    Murray, P.J.3    Wakatsuki, Y.4    Fuss, I.J.5
  • 62
    • 84895098842 scopus 로고    scopus 로고
    • Nod2 deficiency is associated with an increased mucosal immunoregulatory response to commensal microorganisms
    • Amendola A, Butera A, Sanchez M, Strober W, Boirivant M, (2013) Nod2 deficiency is associated with an increased mucosal immunoregulatory response to commensal microorganisms. Mucosal Immunol 7: 391–404.
    • (2013) Mucosal Immunol , vol.7 , pp. 391-404
    • Amendola, A.1    Butera, A.2    Sanchez, M.3    Strober, W.4    Boirivant, M.5
  • 63
    • 0037075551 scopus 로고    scopus 로고
    • RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems
    • Kobayashi K, Inohara N, Hernandez LD, Galan JE, Nunez G, et al. (2002) RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature 416: 194–199.
    • (2002) Nature , vol.416 , pp. 194-199
    • Kobayashi, K.1    Inohara, N.2    Hernandez, L.D.3    Galan, J.E.4    Nunez, G.5
  • 64
    • 13244292161 scopus 로고    scopus 로고
    • Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract
    • Kobayashi KS, Chamaillard M, Ogura Y, Henegariu O, Inohara N, et al. (2005) Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307: 731–734.
    • (2005) Science , vol.307 , pp. 731-734
    • Kobayashi, K.S.1    Chamaillard, M.2    Ogura, Y.3    Henegariu, O.4    Inohara, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.