메뉴 건너뛰기




Volumn 17, Issue 1, 2015, Pages

Conditional deletion of caspase-8 in macrophages alters macrophage activation in a RIPK-dependent manner

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; CASPASE 8; IMIQUIMOD; IMMUNOGLOBULIN; INTERLEUKIN 1BETA; METRONIDAZOLE; NEOMYCIN; PROTEIN SERINE THREONINE KINASE; RECEPTOR INTERACTING SERINE THREONINE KINASE; UNCLASSIFIED DRUG; VANCOMYCIN; CD11B ANTIGEN; CD86 ANTIGEN; DIFFERENTIATION ANTIGEN; LY ANTIGEN; LY-6C ANTIGEN, MOUSE; LYSOZYME; LYSOZYME M, MOUSE; MONOCYTE-MACROPHAGE DIFFERENTIATION ANTIGEN; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK3 PROTEIN, MOUSE; TOLL LIKE RECEPTOR;

EID: 84944877351     PISSN: 14786354     EISSN: 14786362     Source Type: Journal    
DOI: 10.1186/s13075-015-0794-z     Document Type: Article
Times cited : (34)

References (26)
  • 1
    • 68149139457 scopus 로고    scopus 로고
    • BH3-only proteins in rheumatoid arthritis: potential targets for therapeutic intervention
    • Hutcheson J, Perlman H. BH3-only proteins in rheumatoid arthritis: potential targets for therapeutic intervention. Oncogene. 2008;27 Suppl 1:S168-75.
    • (2008) Oncogene. , vol.27 , Issue.SUPPL 1 , pp. S168-S175
    • Hutcheson, J.1    Perlman, H.2
  • 3
    • 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
    • Rajput A, Kovalenko A, Bogdanov K, Yang SH, Kang TB, Kim JC, et al. RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein. Immunity. 2011;34:340-51.
    • (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
  • 4
    • 80052989433 scopus 로고    scopus 로고
    • Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation
    • Sears N, Sen GC, Stark GR, Chattopadhyay S. Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation. J Biol Chem. 2011;286:33037-33044.
    • (2011) J Biol Chem. , vol.286 , pp. 33037-33044
    • Sears, N.1    Sen, G.C.2    Stark, G.R.3    Chattopadhyay, S.4
  • 5
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • Kang TB, Yang SH, Toth B, Kovalenko A, Wallach D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity. 2013;38:27-40.
    • (2013) Immunity. , vol.38 , pp. 27-40
    • Kang, T.B.1    Yang, S.H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 6
    • 84857404572 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation
    • Vince JE, Wong WW, Gentle I, Lawlor KE, Allam R, O'Reilly L, et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity. 2012;36:215-27.
    • (2012) Immunity. , vol.36 , pp. 215-227
    • Vince, J.E.1    Wong, W.W.2    Gentle, I.3    Lawlor, K.E.4    Allam, R.5    O'Reilly, L.6
  • 7
    • 84894271641 scopus 로고    scopus 로고
    • FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes
    • Gurung P, Anand PK, Malireddi RK, Vande Walle L, Van Opdenbosch N, Dillon CP, et al. FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes. J Immunol. 2014;192:1835-46.
    • (2014) J Immunol. , vol.192 , pp. 1835-1846
    • Gurung, P.1    Anand, P.K.2    Malireddi, R.K.3    Vande Walle, L.4    Opdenbosch, N.5    Dillon, C.P.6
  • 8
    • 79960922705 scopus 로고    scopus 로고
    • cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova M, Geserick P, Kellert B, Dimitrova DP, Langlais C, Hupe M, et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell. 2011;43:449-63.
    • (2011) Mol Cell. , vol.43 , pp. 449-463
    • Feoktistova, M.1    Geserick, P.2    Kellert, B.3    Dimitrova, D.P.4    Langlais, C.5    Hupe, M.6
  • 9
    • 84857733516 scopus 로고    scopus 로고
    • Requirement of myeloid cell-specific Fas expression for prevention of systemic autoimmunity in mice
    • Cuda CM, Agrawal H, Misharin AV, Haines 3rd GK, Hutcheson J, Weber E, et al. Requirement of myeloid cell-specific Fas expression for prevention of systemic autoimmunity in mice. Arthritis Rheum. 2012;64:808-20.
    • (2012) Arthritis Rheum. , vol.64 , pp. 808-820
    • Cuda, C.M.1    Agrawal, H.2    Misharin, A.V.3    Haines, G.K.4    Hutcheson, J.5    Weber, E.6
  • 10
    • 84902127968 scopus 로고    scopus 로고
    • Caspase-8 acts as a molecular rheostat to limit RIPK1- and MyD88-mediated dendritic cell activation
    • Cuda CM, Misharin AV, Gierut AK, Saber R, Haines 3rd GK, Hutcheson J, et al. Caspase-8 acts as a molecular rheostat to limit RIPK1- and MyD88-mediated dendritic cell activation. J Immunol. 2014;192:5548-60.
    • (2014) J Immunol. , vol.192 , pp. 5548-5560
    • Cuda, C.M.1    Misharin, A.V.2    Gierut, A.K.3    Saber, R.4    Haines, G.K.5    Hutcheson, J.6
  • 11
    • 24744459035 scopus 로고    scopus 로고
    • Cutting edge: innate immunity conferred by B cells is regulated by caspase-8
    • Beisner DR, Ch'en IL, Kolla RV, Hoffmann A, Hedrick SM. Cutting edge: innate immunity conferred by B cells is regulated by caspase-8. J Immunol. 2005;175:3469-73.
    • (2005) J Immunol. , vol.175 , pp. 3469-3473
    • Beisner, D.R.1    Ch'en, I.L.2    Kolla, R.V.3    Hoffmann, A.4    Hedrick, S.M.5
  • 12
    • 38949209522 scopus 로고    scopus 로고
    • Combined deficiency of proapoptotic regulators Bim and Fas results in the early onset of systemic autoimmunity
    • Hutcheson J, Scatizzi JC, Siddiqui AM, Haines 3rd GK, Wu T, Li QZ, et al. Combined deficiency of proapoptotic regulators Bim and Fas results in the early onset of systemic autoimmunity. Immunity. 2008;28:206-17.
    • (2008) Immunity. , vol.28 , pp. 206-217
    • Hutcheson, J.1    Scatizzi, J.C.2    Siddiqui, A.M.3    Haines, G.K.4    Wu, T.5    Li, Q.Z.6
  • 13
    • 84858794257 scopus 로고    scopus 로고
    • A novel Ly6C/Ly6G-based strategy to analyze the mouse splenic myeloid compartment
    • Rose S, Misharin A, Perlman H. A novel Ly6C/Ly6G-based strategy to analyze the mouse splenic myeloid compartment. Cytometry A. 2011;81:343-50.
    • (2011) Cytometry A. , vol.81 , pp. 343-350
    • Rose, S.1    Misharin, A.2    Perlman, H.3
  • 15
    • 0025875259 scopus 로고
    • lpr and gld: single gene models of systemic autoimmunity and lymphoproliferative disease
    • Cohen PL, Eisenberg RA. lpr and gld: single gene models of systemic autoimmunity and lymphoproliferative disease. Annu Rev Immunol. 1991;9:243-69.
    • (1991) Annu Rev Immunol , vol.9 , pp. 243-269
    • Cohen, P.L.1    Eisenberg, R.A.2
  • 16
    • 34249915031 scopus 로고    scopus 로고
    • Inhibition of Toll-like receptor-7 (TLR-7) or TLR-7 plus TLR-9 attenuates glomerulonephritis and lung injury in experimental lupus
    • Pawar RD, Ramanjaneyulu A, Kulkarni OP, Lech M, Segerer S, Anders HJ. Inhibition of Toll-like receptor-7 (TLR-7) or TLR-7 plus TLR-9 attenuates glomerulonephritis and lung injury in experimental lupus. J Am Soc Nephrol. 2007;18:1721-31.
    • (2007) J Am Soc Nephrol. , vol.18 , pp. 1721-1731
    • Pawar, R.D.1    Ramanjaneyulu, A.2    Kulkarni, O.P.3    Lech, M.4    Segerer, S.5    Anders, H.J.6
  • 17
    • 0029132698 scopus 로고
    • Defective signal-transduction pathways in T-cells from autoimmune MRL-lpr/lpr mice are associated with increased polyamine concentrations
    • Thomas TJ, Gunnia UB, Seibold JR, Thomas T. Defective signal-transduction pathways in T-cells from autoimmune MRL-lpr/lpr mice are associated with increased polyamine concentrations. Biochem J. 1995;311:175-82.
    • (1995) Biochem J. , vol.311 , pp. 175-182
    • Thomas, T.J.1    Gunnia, U.B.2    Seibold, J.R.3    Thomas, T.4
  • 18
    • 80054944901 scopus 로고    scopus 로고
    • Role of the commensal microbiota in normal and pathogenic host immune responses
    • Littman DR, Pamer EG. Role of the commensal microbiota in normal and pathogenic host immune responses. Cell Host Microbe. 2011;10:311-23.
    • (2011) Cell Host Microbe. , vol.10 , pp. 311-323
    • Littman, D.R.1    Pamer, E.G.2
  • 19
    • 80054927213 scopus 로고    scopus 로고
    • Microbiota and autoimmune disease: the hosted self
    • Mathis D, Benoist C. Microbiota and autoimmune disease: the hosted self. Cell Host Microbe. 2011;10:297-301.
    • (2011) Cell Host Microbe. , vol.10 , pp. 297-301
    • Mathis, D.1    Benoist, C.2
  • 22
    • 84879799191 scopus 로고    scopus 로고
    • Commensal microbiota are required for systemic inflammation triggered by necrotic dendritic cells
    • Young JA, He TH, Reizis B, Winoto A. Commensal microbiota are required for systemic inflammation triggered by necrotic dendritic cells. Cell Rep. 2013;3:1932-44.
    • (2013) Cell Rep. , vol.3 , pp. 1932-1944
    • Young, J.A.1    He, T.H.2    Reizis, B.3    Winoto, A.4
  • 23
    • 0036715377 scopus 로고    scopus 로고
    • Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA
    • Kalai M, Van Loo G, Vanden Berghe T, Meeus A, Burm W, Saelens X, et al. Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA. Cell Death Differ. 2002;9:981-94.
    • (2002) Cell Death Differ. , vol.9 , pp. 981-994
    • Kalai, M.1    Loo, G.2    Vanden Berghe, T.3    Meeus, A.4    Burm, W.5    Saelens, X.6
  • 24
    • 84929485512 scopus 로고    scopus 로고
    • Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88-dependent systemic inflammation
    • Schock SN, Young JA, He TH, Sun Y, Winoto A. Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88-dependent systemic inflammation. PLoS One. 2015;10:e0124391.
    • (2015) PLoS One. , vol.10 , pp. e0124391
    • Schock, S.N.1    Young, J.A.2    He, T.H.3    Sun, Y.4    Winoto, A.5
  • 25
    • 33846922252 scopus 로고    scopus 로고
    • Caspase-8 prevents sustained activation of NF-κB in monocytes undergoing macrophagic differentiation
    • Rébé C, Cathelin S, Launay S, Filomenko R, Prévotat L, L'Ollivier C, et al. Caspase-8 prevents sustained activation of NF-κB in monocytes undergoing macrophagic differentiation. Blood. 2007;109:1442-50.
    • (2007) Blood. , vol.109 , pp. 1442-1450
    • Rébé, C.1    Cathelin, S.2    Launay, S.3    Filomenko, R.4    Prévotat, L.5    L'Ollivier, C.6
  • 26
    • 0037114624 scopus 로고    scopus 로고
    • Specific involvement of caspases in the differentiation of monocytes into macrophages
    • Sordet O, Rébé C, Plenchette S, Zermati Y, Hermine O, Vainchenker W, et al. Specific involvement of caspases in the differentiation of monocytes into macrophages. Blood. 2002;100:4446-53.
    • (2002) Blood. , vol.100 , pp. 4446-4453
    • Sordet, O.1    Rébé, C.2    Plenchette, S.3    Zermati, Y.4    Hermine, O.5    Vainchenker, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.