메뉴 건너뛰기




Volumn 185, Issue 1, 2015, Pages 17-25

Novel Roles for Caspase-8 in IL-1β and Inflammasome Regulation

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 8; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 1BETA; CASP8 PROTEIN, HUMAN; CASP8 PROTEIN, MOUSE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK3 PROTEIN, MOUSE;

EID: 84918802996     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2014.08.025     Document Type: Short Survey
Times cited : (137)

References (82)
  • 1
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • M.P. Boldin, T.M. Goncharov, Y.V. Goltsev, and D. Wallach Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death Cell 85 1996 803 815
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 4
  • 5
    • 14044252160 scopus 로고    scopus 로고
    • Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis
    • D. Sohn, K. Schulze-Osthoff, and R.U. Jänicke Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis J Biol Chem 280 2005 5267 5273
    • (2005) J Biol Chem , vol.280 , pp. 5267-5273
    • Sohn, D.1    Schulze-Osthoff, K.2    Jänicke, R.U.3
  • 6
    • 0036790423 scopus 로고    scopus 로고
    • Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: Absolute requirement for removal of caspase-6 prodomain
    • V. Cowling, and J. Downward Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain Cell Death Differ 9 2002 1046 1056
    • (2002) Cell Death Differ , vol.9 , pp. 1046-1056
    • Cowling, V.1    Downward, J.2
  • 8
    • 84862285729 scopus 로고    scopus 로고
    • Cathepsin D primes caspase-8 activation by multiple intra-chain proteolysis
    • S. Conus, C. Pop, S.J. Snipas, G.S. Salvesen, and H.U. Simon Cathepsin D primes caspase-8 activation by multiple intra-chain proteolysis J Biol Chem 287 2012 21142 21151
    • (2012) J Biol Chem , vol.287 , pp. 21142-21151
    • Conus, S.1    Pop, C.2    Snipas, S.J.3    Salvesen, G.S.4    Simon, H.U.5
  • 12
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • F. Martinon, K. Burns, and J. Tschopp The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta Mol Cell 10 2002 417 426
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 13
    • 1642285783 scopus 로고    scopus 로고
    • NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder
    • L. Agostini, F. Martinon, K. Burns, M.F. McDermott, P.N. Hawkins, and J. Tschopp NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder Immunity 20 2004 319 325
    • (2004) Immunity , vol.20 , pp. 319-325
    • Agostini, L.1    Martinon, F.2    Burns, K.3    McDermott, M.F.4    Hawkins, P.N.5    Tschopp, J.6
  • 22
    • 84893835896 scopus 로고    scopus 로고
    • Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation
    • N. Van Opdenbosch, P. Gurung, L. Vande Walle, A. Fossoul, T.D. Kanneganti, and M. Lamkanfi Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation Nat Commun 5 2014 3209
    • (2014) Nat Commun , vol.5 , pp. 3209
    • Van Opdenbosch, N.1    Gurung, P.2    Vande Walle, L.3    Fossoul, A.4    Kanneganti, T.D.5    Lamkanfi, M.6
  • 23
    • 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
    • P. Gurung, R.K. Malireddi, P.K. Anand, D. Demon, L. Vande Walle, Z. Liu, P. Vogel, M. Lamkanfi, and T.D. Kanneganti 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 2012 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    Vande Walle, L.5    Liu, Z.6    Vogel, P.7    Lamkanfi, M.8    Kanneganti, T.D.9
  • 26
    • 0024592109 scopus 로고
    • Purification and characterization of human recombinant precursor interleukin 1 beta
    • D. Hazuda, R.L. Webb, P. Simon, and P. Young Purification and characterization of human recombinant precursor interleukin 1 beta J Biol Chem 264 1989 1689 1693
    • (1989) J Biol Chem , vol.264 , pp. 1689-1693
    • Hazuda, D.1    Webb, R.L.2    Simon, P.3    Young, P.4
  • 28
    • 84866552287 scopus 로고    scopus 로고
    • The IL-1-dependent sterile inflammatory response has a substantial caspase-1-independent component that requires cathepsin C
    • H. Kono, G.M. Orlowski, Z. Patel, and K.L. Rock The IL-1-dependent sterile inflammatory response has a substantial caspase-1-independent component that requires cathepsin C J Immunol 189 2012 3734 3740
    • (2012) J Immunol , vol.189 , pp. 3734-3740
    • Kono, H.1    Orlowski, G.M.2    Patel, Z.3    Rock, K.L.4
  • 29
    • 84867903731 scopus 로고    scopus 로고
    • Cutting edge: IL-1beta processing during Pseudomonas aeruginosa infection is mediated by neutrophil serine proteases and is independent of NLRC4 and caspase-1
    • M. Karmakar, Y. Sun, A.G. Hise, A. Rietsch, and E. Pearlman Cutting edge: IL-1beta processing during Pseudomonas aeruginosa infection is mediated by neutrophil serine proteases and is independent of NLRC4 and caspase-1 J Immunol 189 2012 4231 4235
    • (2012) J Immunol , vol.189 , pp. 4231-4235
    • Karmakar, M.1    Sun, Y.2    Hise, A.G.3    Rietsch, A.4    Pearlman, E.5
  • 30
    • 84886928516 scopus 로고    scopus 로고
    • Acidosis drives damage-associated molecular pattern (DAMP)-induced interleukin-1 secretion via a caspase-1-independent pathway
    • M.E. Edye, G. Lopez-Castejon, S.M. Allan, and D. Brough Acidosis drives damage-associated molecular pattern (DAMP)-induced interleukin-1 secretion via a caspase-1-independent pathway J Biol Chem 288 2013 30485 30494
    • (2013) J Biol Chem , vol.288 , pp. 30485-30494
    • Edye, M.E.1    Lopez-Castejon, G.2    Allan, S.M.3    Brough, D.4
  • 33
  • 35
    • 84885966098 scopus 로고    scopus 로고
    • Proapoptotic chemotherapeutic drugs induce noncanonical processing and release of IL-1beta via caspase-8 in dendritic cells
    • C. Antonopoulos, C. El Sanadi, W.J. Kaiser, E.S. Mocarski, and G.R. Dubyak Proapoptotic chemotherapeutic drugs induce noncanonical processing and release of IL-1beta via caspase-8 in dendritic cells J Immunol 191 2013 4789 4803
    • (2013) J Immunol , vol.191 , pp. 4789-4803
    • Antonopoulos, C.1    El Sanadi, C.2    Kaiser, W.J.3    Mocarski, E.S.4    Dubyak, G.R.5
  • 37
    • 52149095957 scopus 로고    scopus 로고
    • Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome-transgenic mice
    • T.B. Kang, G.S. Oh, E. Scandella, B. Bolinger, B. Ludewig, A. Kovalenko, and D. Wallach Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome-transgenic mice J Immunol 181 2008 2522 2532
    • (2008) J Immunol , vol.181 , pp. 2522-2532
    • Kang, T.B.1    Oh, G.S.2    Scandella, E.3    Bolinger, B.4    Ludewig, B.5    Kovalenko, A.6    Wallach, D.7
  • 38
    • 0034648529 scopus 로고    scopus 로고
    • Activation of the NF-kappaB pathway by caspase 8 and its homologs
    • P.M. Chaudhary, M.T. Eby, A. Jasmin, A. Kumar, L. Liu, and L. Hood Activation of the NF-kappaB pathway by caspase 8 and its homologs Oncogene 19 2000 4451 4460
    • (2000) Oncogene , vol.19 , pp. 4451-4460
    • Chaudhary, P.M.1    Eby, M.T.2    Jasmin, A.3    Kumar, A.4    Liu, L.5    Hood, L.6
  • 39
    • 0034646478 scopus 로고    scopus 로고
    • Activation of NF-kappaB by FADD, Casper, and caspase-8
    • W.H. Hu, H. Johnson, and H.B. Shu Activation of NF-kappaB by FADD, Casper, and caspase-8 J Biol Chem 275 2000 10838 10844
    • (2000) J Biol Chem , vol.275 , pp. 10838-10844
    • Hu, W.H.1    Johnson, H.2    Shu, H.B.3
  • 41
    • 33645786318 scopus 로고    scopus 로고
    • Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA
    • K. Takahashi, T. Kawai, H. Kumar, S. Sato, S. Yonehara, and S. Akira Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA J Immunol 176 2006 4520 4524
    • (2006) J Immunol , vol.176 , pp. 4520-4524
    • Takahashi, K.1    Kawai, T.2    Kumar, H.3    Sato, S.4    Yonehara, S.5    Akira, S.6
  • 42
    • 79952770123 scopus 로고    scopus 로고
    • RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein
    • A. Rajput, A. Kovalenko, K. Bogdanov, S.H. Yang, T.B. Kang, J.C. Kim, J. Du, and D. Wallach RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein Immunity 34 2011 340 351
    • (2011) Immunity , vol.34 , pp. 340-351
    • Rajput, A.1    Kovalenko, A.2    Bogdanov, K.3    Yang, S.H.4    Kang, T.B.5    Kim, J.C.6    Du, J.7    Wallach, D.8
  • 45
    • 84887439544 scopus 로고    scopus 로고
    • Salmonella infection induces recruitment of caspase-8 to the inflammasome to modulate IL-1β production
    • S.M. Man, P. Tourlomousis, L. Hopkins, T.P. Monie, K.A. Fitzgerald, and C.E. Bryant Salmonella infection induces recruitment of caspase-8 to the inflammasome to modulate IL-1β production J Immunol 191 2013 5239 5246
    • (2013) J Immunol , vol.191 , pp. 5239-5246
    • Man, S.M.1    Tourlomousis, P.2    Hopkins, L.3    Monie, T.P.4    Fitzgerald, K.A.5    Bryant, C.E.6
  • 46
    • 17144413785 scopus 로고    scopus 로고
    • Apoptosis induced by the Toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif
    • W.J. Kaiser, and M.K. Offermann Apoptosis induced by the Toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif J Immunol 174 2005 4942 4952
    • (2005) J Immunol , vol.174 , pp. 4942-4952
    • Kaiser, W.J.1    Offermann, M.K.2
  • 47
    • 77952241062 scopus 로고    scopus 로고
    • Proapoptotic signalling through Toll-like receptor-3 involves TRIF-dependent activation of caspase-8 and is under the control of inhibitor of apoptosis proteins in melanoma cells
    • A. Weber, Z. Kirejczyk, R. Besch, S. Potthoff, M. Leverkus, and G. Häcker Proapoptotic signalling through Toll-like receptor-3 involves TRIF-dependent activation of caspase-8 and is under the control of inhibitor of apoptosis proteins in melanoma cells Cell Death Differ 17 2010 942 951
    • (2010) Cell Death Differ , vol.17 , pp. 942-951
    • Weber, A.1    Kirejczyk, Z.2    Besch, R.3    Potthoff, S.4    Leverkus, M.5    Häcker, G.6
  • 48
    • 84857175933 scopus 로고    scopus 로고
    • Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1beta via a noncanonical caspase-8 inflammasome
    • S.I. Gringhuis, T.M. Kaptein, B.A. Wevers, B. Theelen, M. van der Vlist, T. Boekhout, and T.B. Geijtenbeek Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1beta via a noncanonical caspase-8 inflammasome Nat Immunol 13 2012 246 254
    • (2012) Nat Immunol , vol.13 , pp. 246-254
    • Gringhuis, S.I.1    Kaptein, T.M.2    Wevers, B.A.3    Theelen, B.4    Van Der Vlist, M.5    Boekhout, T.6    Geijtenbeek, T.B.7
  • 49
    • 51049100571 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 3 and 4 induces interleukin-1beta maturation by caspase-8
    • J. Maelfait, E. Vercammen, S. Janssens, P. Schotte, M. Haegman, S. Magez, and R. Beyaert Stimulation of Toll-like receptor 3 and 4 induces interleukin-1beta maturation by caspase-8 J Exp Med 205 2008 1967 1973
    • (2008) J Exp Med , vol.205 , pp. 1967-1973
    • Maelfait, J.1    Vercammen, E.2    Janssens, S.3    Schotte, P.4    Haegman, M.5    Magez, S.6    Beyaert, R.7
  • 50
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • R.J. Kaufman Orchestrating the unfolded protein response in health and disease J Clin Invest 110 2002 1389 1398
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 51
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: Multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • J. Li, B. Lee, and A.S. Lee Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53 J Biol Chem 281 2006 7260 7270
    • (2006) J Biol Chem , vol.281 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 54
    • 84879596906 scopus 로고    scopus 로고
    • K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • R. Muñoz-Planillo, P. Kuffa, G. Martínez-Colón, B.L. Smith, T.M. Rajendiran, and G. Núñez K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter Immunity 38 2013 1142 1153
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Muñoz-Planillo, R.1    Kuffa, P.2    Martínez-Colón, G.3    Smith, B.L.4    Rajendiran, T.M.5    Núñez, G.6
  • 56
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • H.M. Hoffman, J.L. Mueller, D.H. Broide, A.A. Wanderer, and R.D. Kolodner Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome Nat Genet 29 2001 301 305
    • (2001) Nat Genet , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 57
    • 0037216780 scopus 로고    scopus 로고
    • The expanding spectrum of systemic autoinflammatory disorders and their rheumatic manifestations
    • K.M. Hull, N. Shoham, J.J. Chae, I. Aksentijevich, and D.L. Kastner The expanding spectrum of systemic autoinflammatory disorders and their rheumatic manifestations Curr Opin Rheumatol 15 2003 61 69
    • (2003) Curr Opin Rheumatol , vol.15 , pp. 61-69
    • Hull, K.M.1    Shoham, N.2    Chae, J.J.3    Aksentijevich, I.4    Kastner, D.L.5
  • 58
    • 0036892403 scopus 로고    scopus 로고
    • Genetic clues to understanding periodic fevers, and possible therapies
    • M.F. McDermott Genetic clues to understanding periodic fevers, and possible therapies Trends Mol Med 8 2002 550 554
    • (2002) Trends Mol Med , vol.8 , pp. 550-554
    • McDermott, M.F.1
  • 63
    • 84875970670 scopus 로고    scopus 로고
    • Fas-mediated inflammatory response in Listeria monocytogenes infection
    • R. Uchiyama, S. Yonehara, and H. Tsutsui Fas-mediated inflammatory response in Listeria monocytogenes infection J Immunol 190 2013 4245 4254
    • (2013) J Immunol , vol.190 , pp. 4245-4254
    • Uchiyama, R.1    Yonehara, S.2    Tsutsui, H.3
  • 64
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • T.B. Kang, S.H. Yang, B. Toth, A. Kovalenko, and D. Wallach Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome Immunity 38 2013 27 40
    • (2013) Immunity , vol.38 , pp. 27-40
    • Kang, T.B.1    Yang, S.H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 70
    • 12444281807 scopus 로고    scopus 로고
    • Caspase-8 gene is frequently inactivated by the frameshift somatic mutation 1225-1226delTG in hepatocellular carcinomas
    • Y.H. Soung, J.W. Lee, S.Y. Kim, Y.J. Sung, W.S. Park, S.W. Nam, S.H. Kim, J.Y. Lee, N.J. Yoo, and S.H. Lee Caspase-8 gene is frequently inactivated by the frameshift somatic mutation 1225-1226delTG in hepatocellular carcinomas Oncogene 24 2005 141 147
    • (2005) Oncogene , vol.24 , pp. 141-147
    • Soung, Y.H.1    Lee, J.W.2    Kim, S.Y.3    Sung, Y.J.4    Park, W.S.5    Nam, S.W.6    Kim, S.H.7    Lee, J.Y.8    Yoo, N.J.9    Lee, S.H.10
  • 74
    • 77952315915 scopus 로고    scopus 로고
    • CASP8 polymorphisms contribute to cancer susceptibility: Evidence from a meta-analysis of 23 publications with 55 individual studies
    • M. Yin, J. Yan, S. Wei, and Q. Wei CASP8 polymorphisms contribute to cancer susceptibility: evidence from a meta-analysis of 23 publications with 55 individual studies Carcinogenesis 31 2010 850 857
    • (2010) Carcinogenesis , vol.31 , pp. 850-857
    • Yin, M.1    Yan, J.2    Wei, S.3    Wei, Q.4
  • 77
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • C.A. Dinarello Biologic basis for interleukin-1 in disease Blood 87 1996 2095 2147
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 78
    • 77749304035 scopus 로고    scopus 로고
    • IL-1: Discoveries, controversies and future directions
    • C.A. Dinarello IL-1: discoveries, controversies and future directions Eur J Immunol 40 2010 599 606
    • (2010) Eur J Immunol , vol.40 , pp. 599-606
    • Dinarello, C.A.1
  • 79
    • 77952296338 scopus 로고    scopus 로고
    • Interleukin-1beta (IL-1beta) processing pathway
    • A. Weber, P. Wasiliew, and M. Kracht Interleukin-1beta (IL-1beta) processing pathway Sci Signal 3 2010 cm2
    • (2010) Sci Signal , vol.3 , pp. 2
    • Weber, A.1    Wasiliew, P.2    Kracht, M.3
  • 81
    • 0026056197 scopus 로고
    • Blocking IL-1: Interleukin 1 receptor antagonist in vivo and in vitro
    • C.A. Dinarello, and R.C. Thompson Blocking IL-1: interleukin 1 receptor antagonist in vivo and in vitro Immunol Today 12 1991 404 410
    • (1991) Immunol Today , vol.12 , pp. 404-410
    • Dinarello, C.A.1    Thompson, R.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.