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Volumn 82, Issue 1, 2014, Pages 62-71

In vitro infection of bovine monocytes with Mycoplasma bovis delays apoptosis and suppresses production of gamma interferon and tumor necrosis factor alpha but not interleukin-10

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 9; GAMMA INTERFERON; INTERLEUKIN 10; SUPPRESSOR OF CYTOKINE SIGNALING 1; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA;

EID: 84890960140     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00961-13     Document Type: Article
Times cited : (60)

References (83)
  • 1
    • 44449106058 scopus 로고    scopus 로고
    • The role of Mycoplasma bovis in bovine respiratory disease outbreaks in veal calf feedlots
    • Arcangioli MA, Duet A, Meyer G, Dernburg A, Bezille P, Poumarat F, Le Grand D. 2008. The role of Mycoplasma bovis in bovine respiratory disease outbreaks in veal calf feedlots. Vet. J. 177:89-93. http://dx.doi.org/10.1016/j.tvjl.2007.03.008.
    • (2008) Vet. J. , vol.177 , pp. 89-93
    • Arcangioli, M.A.1    Duet, A.2    Meyer, G.3    Dernburg, A.4    Bezille, P.5    Poumarat, F.6    Le Grand, D.7
  • 2
    • 0037381753 scopus 로고    scopus 로고
    • Mycoplasma bovis: disease, diagnosis, and control
    • Nicholas RA, Ayling RD. 2003. Mycoplasma bovis: disease, diagnosis, and control. Res. Vet. Sci. 74:105-112. http://dx.doi.org/10.1016/S0034-5288(02)00155-8.
    • (2003) Res. Vet. Sci. , vol.74 , pp. 105-112
    • Nicholas, R.A.1    Ayling, R.D.2
  • 3
    • 33748416721 scopus 로고    scopus 로고
    • Bovine respiratory disease in feedlot cattle: environmental, genetic, and economic factors
    • Snowder GD, Van Vleck LD, Cundiff LV, Bennett GL. 2006. Bovine respiratory disease in feedlot cattle: environmental, genetic, and economic factors. J. Anim. Sci. 84:1999-2008. http://dx.doi.org/10.2527/jas.2006-046.
    • (2006) J. Anim. Sci. , vol.84 , pp. 1999-2008
    • Snowder, G.D.1    Van Vleck, L.D.2    Cundiff, L.V.3    Bennett, G.L.4
  • 5
    • 0023578531 scopus 로고
    • Immune response of cattle to respiratory mycoplasmas
    • Howard CJ, Thomas LH, Parsons KR. 1987. Immune response of cattle to respiratory mycoplasmas. Vet. Immunol. Immunopathol. 17:401-412. http://dx.doi.org/10.1016/0165-2427(87)90157-7.
    • (1987) Vet. Immunol. Immunopathol. , vol.17 , pp. 401-412
    • Howard, C.J.1    Thomas, L.H.2    Parsons, K.R.3
  • 6
    • 0038384091 scopus 로고    scopus 로고
    • Characterization of the immune response to Mycoplasma bovis lung infection
    • Vanden Bush TJ, Rosenbusch RF. 2003. Characterization of the immune response to Mycoplasma bovis lung infection. Vet. Immunol. Immunopathol. 94:23-33. http://dx.doi.org/10.1016/S0165-2427(03)00056-4.
    • (2003) Vet. Immunol. Immunopathol. , vol.94 , pp. 23-33
    • Vanden Bush, T.J.1    Rosenbusch, R.F.2
  • 7
    • 84856442296 scopus 로고    scopus 로고
    • Chronic pneumonia in calves after experimental infection with Mycoplasma bovis strain 1067: characterization of lung pathology, persistence of variable surface protein antigens and local immune response
    • Hermeyer K, Buchenau I, Thomasmeyer A, Baum B, Spergser J, Rosengarten R, Hewicker-Trautwein M. 2012. Chronic pneumonia in calves after experimental infection with Mycoplasma bovis strain 1067: characterization of lung pathology, persistence of variable surface protein antigens and local immune response. Acta Vet. Scand. 54:9. http://dx.doi.org/10.1186/1751-0147-54-9.
    • (2012) Acta Vet. Scand. , vol.54 , pp. 9
    • Hermeyer, K.1    Buchenau, I.2    Thomasmeyer, A.3    Baum, B.4    Spergser, J.5    Rosengarten, R.6    Hewicker-Trautwein, M.7
  • 8
    • 0041412648 scopus 로고    scopus 로고
    • Mycoplasma bovis-associated suppurative otitis media and pneumonia in bull calves
    • Maeda T, Shibahara T, Kimura K, Wada Y, Sato K, Imada Y, Ishikawa Y, Kadota K. 2003. Mycoplasma bovis-associated suppurative otitis media and pneumonia in bull calves. J. Comp. Pathol. 129:100-110. http://dx.doi.org/10.1016/S0021-9975(03)00009-4.
    • (2003) J. Comp. Pathol. , vol.129 , pp. 100-110
    • Maeda, T.1    Shibahara, T.2    Kimura, K.3    Wada, Y.4    Sato, K.5    Imada, Y.6    Ishikawa, Y.7    Kadota, K.8
  • 9
    • 0035202137 scopus 로고    scopus 로고
    • The immunohistochemical detection of Mycoplasma bovis and bovine viral diarrhea virus in tissues of feedlot cattle with chronic, unresponsive respiratory disease and/or arthritis
    • Haines DM, Martin KM, Clark EG, Jim GK, Janzen ED. 2001. The immunohistochemical detection of Mycoplasma bovis and bovine viral diarrhea virus in tissues of feedlot cattle with chronic, unresponsive respiratory disease and/or arthritis. Can. Vet. J. 42:857-860. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1476660/.
    • (2001) Can. Vet. J. , vol.42 , pp. 857-860
    • Haines, D.M.1    Martin, K.M.2    Clark, E.G.3    Jim, G.K.4    Janzen, E.D.5
  • 11
    • 78049450066 scopus 로고    scopus 로고
    • Invasion of bovine peripheral blood mononuclear cells and erythrocytes by Mycoplasma bovis
    • van der Merwe J, Prysliak T, Perez-Casal J. 2010. Invasion of bovine peripheral blood mononuclear cells and erythrocytes by Mycoplasma bovis. Infect. Immun. 78:4570-4578. http://dx.doi.org/10.1128/IAI.00707-10.
    • (2010) Infect. Immun. , vol.78 , pp. 4570-4578
    • van der Merwe, J.1    Prysliak, T.2    Perez-Casal, J.3
  • 12
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. 2002. The protein kinase complement of the human genome. Science 298:1912-1934. http://dx.doi.org/10.1126/science.1075762.
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 13
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twentyfirst century? Nat
    • Cohen P. 2002. Protein kinases-the major drug targets of the twentyfirst century? Nat. Rev. Drug Discov. 1:309-315. http://dx.doi.org/10.1038/nrd773.
    • (2002) Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 14
    • 0017638132 scopus 로고
    • Role of multiple basic residues in determining the substrate specificity of cyclic AMPdependent protein kinase
    • Kemp BE, Graves DJ, Benjamini E, Krebs EG. 1977. Role of multiple basic residues in determining the substrate specificity of cyclic AMPdependent protein kinase. J. Biol. Chem. 252:4888-4894.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4888-4894
    • Kemp, B.E.1    Graves, D.J.2    Benjamini, E.3    Krebs, E.G.4
  • 15
    • 0017078844 scopus 로고
    • The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver
    • Zetterqvist O, Ragnarsson U, Humble E, Berglund L, Engstrom L. 1976. The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver. Biochem. Biophys. Res. Commun. 70:696-703. http://dx.doi.org/10.1016/0006-291X(76)90648-3.
    • (1976) Biochem. Biophys. Res. Commun. , vol.70 , pp. 696-703
    • Zetterqvist, O.1    Ragnarsson, U.2    Humble, E.3    Berglund, L.4    Engstrom, L.5
  • 16
    • 10344223002 scopus 로고    scopus 로고
    • Kinome profiling for studying lipopolysaccharide signal transduction in human peripheral blood mononuclear cells
    • Diks SH, Kok K, O'Toole T, Hommes DW, van Dijken P, Joore J, Peppelenbosch MP. 2004. Kinome profiling for studying lipopolysaccharide signal transduction in human peripheral blood mononuclear cells. J. Biol. Chem. 279:49206-49213. http://dx.doi.org/10.1074/jbc.M405028200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49206-49213
    • Diks, S.H.1    Kok, K.2    O'Toole, T.3    Hommes, D.W.4    van Dijken, P.5    Joore, J.6    Peppelenbosch, M.P.7
  • 21
    • 84867599547 scopus 로고    scopus 로고
    • Mycobacterium avium subsp. paratuberculosis inhibits gamma interferon-induced signaling in bovine monocytes: insights into the cellular mechanisms of Johne's disease
    • Arsenault RJ, Li Y, Bell K, Doig K, Potter A, Griebel PJ, Kusalik A, Napper S. 2012. Mycobacterium avium subsp. paratuberculosis inhibits gamma interferon-induced signaling in bovine monocytes: insights into the cellular mechanisms of Johne's disease. Infect. Immun. 80:3039-3048. http://dx.doi.org/10.1128/IAI.00406-12.
    • (2012) Infect. Immun. , vol.80 , pp. 3039-3048
    • Arsenault, R.J.1    Li, Y.2    Bell, K.3    Doig, K.4    Potter, A.5    Griebel, P.J.6    Kusalik, A.7    Napper, S.8
  • 22
    • 84871886189 scopus 로고    scopus 로고
    • Altered Toll-like receptor 9 signaling in Mycobacterium avium subsp. paratuberculosis-infected bovine monocytes reveals potential therapeutic targets
    • Arsenault RJ, Li Y, Maattanen P, Scruten E, Doig K, Potter A, Griebel P, Kusalik A, Napper S. 2013. Altered Toll-like receptor 9 signaling in Mycobacterium avium subsp. paratuberculosis-infected bovine monocytes reveals potential therapeutic targets. Infect. Immun. 81:226-237. http://dx.doi.org/10.1128/IAI.00785-12.
    • (2013) Infect. Immun. , vol.81 , pp. 226-237
    • Arsenault, R.J.1    Li, Y.2    Maattanen, P.3    Scruten, E.4    Doig, K.5    Potter, A.6    Griebel, P.7    Kusalik, A.8    Napper, S.9
  • 23
    • 67649404131 scopus 로고    scopus 로고
    • Blood monocytes: development, heterogeneity, and relationship with dendritic cells
    • Auffray C, Sieweke MH, Geissmann F. 2009. Blood monocytes: development, heterogeneity, and relationship with dendritic cells. Annu. Rev. Immunol. 27:669-692. http://dx.doi.org/10.1146/annurev.immunol.021908.132557.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 669-692
    • Auffray, C.1    Sieweke, M.H.2    Geissmann, F.3
  • 24
    • 33747358360 scopus 로고    scopus 로고
    • Migratory fate and differentiation of blood monocyte subsets
    • Tacke F, Randolph GJ. 2006. Migratory fate and differentiation of blood monocyte subsets. Immunobiology 211:609-618. http://dx.doi.org/10.1016/j.imbio.2006.05.025.
    • (2006) Immunobiology , vol.211 , pp. 609-618
    • Tacke, F.1    Randolph, G.J.2
  • 25
    • 34548617845 scopus 로고    scopus 로고
    • Detection of antibodies against the Mycoplasma bovis glyceraldehyde-3-phosphate dehydrogenase protein in beef cattle
    • Perez-Casal J, Prysliak T. 2007. Detection of antibodies against the Mycoplasma bovis glyceraldehyde-3-phosphate dehydrogenase protein in beef cattle. Microb. Pathog. 43:189-197. http://dx.doi.org/10.1016/j.micpath.2007.05.009.
    • (2007) Microb. Pathog. , vol.43 , pp. 189-197
    • Perez-Casal, J.1    Prysliak, T.2
  • 27
    • 84880694838 scopus 로고    scopus 로고
    • Divergent immune responses to Mycobacterium avium subsp. paratuberculosis infection correlate with kinome responses at the site of intestinal infection
    • Maattanen P, Trost B, Scruten E, Potter A, Kusalik A, Griebel P, Napper S. 2013. Divergent immune responses to Mycobacterium avium subsp. paratuberculosis infection correlate with kinome responses at the site of intestinal infection. Infect. Immun. 81:2861-2872. http://dx.doi.org/10.1128/IAI.00339-13.
    • (2013) Infect. Immun. , vol.81 , pp. 2861-2872
    • Maattanen, P.1    Trost, B.2    Scruten, E.3    Potter, A.4    Kusalik, A.5    Griebel, P.6    Napper, S.7
  • 30
    • 0027459291 scopus 로고
    • Capture immunoassay for ruminant tumor necrosis factor-alpha: comparison with bioassay
    • Ellis JA, Godson D, Campos M, Sileghem M, Babiuk LA. 1993. Capture immunoassay for ruminant tumor necrosis factor-alpha: comparison with bioassay. Vet. Immunol. Immunopathol. 35:289-300. http://dx.doi.org/10.1016/0165-2427(93)90040-B.
    • (1993) Vet. Immunol. Immunopathol. , vol.35 , pp. 289-300
    • Ellis, J.A.1    Godson, D.2    Campos, M.3    Sileghem, M.4    Babiuk, L.A.5
  • 32
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin M, Lin A. 2002. NF-kappaB at the crossroads of life and death. Nat. Immunol. 3:221-227. http://dx.doi.org/10.1038/ni0302-221.
    • (2002) Nat. Immunol. , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 34
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. 2002. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9:459-470. http://dx.doi.org/10.1016/S1097-2765(02)00482-3.
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 35
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry NA, Lazebnik Y. 1998. Caspases: enemies within. Science 281:1312-1316. http://dx.doi.org/10.1126/science.281.5381.1312.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 36
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl SJ, Shi Y. 2004. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5:897-907. http://dx.doi.org/10.1038/nrm1496.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 37
    • 0033614347 scopus 로고    scopus 로고
    • The CED-4-homologous protein FLASH is involved in Fasmediated activation of caspase-8 during apoptosis
    • Imai Y, Kimura T, Murakami A, Yajima N, Sakamaki K, Yonehara S. 1999. The CED-4-homologous protein FLASH is involved in Fasmediated activation of caspase-8 during apoptosis. Nature 398:777-785. http://dx.doi.org/10.1038/19709.
    • (1999) Nature , vol.398 , pp. 777-785
    • Imai, Y.1    Kimura, T.2    Murakami, A.3    Yajima, N.4    Sakamaki, K.5    Yonehara, S.6
  • 38
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang L, Du F, Wang X. 2008. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133:693-703. http://dx.doi.org/10.1016/j.cell.2008.03.036.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 39
    • 0034801684 scopus 로고    scopus 로고
    • SOCS proteins: negative regulators of cytokine signaling
    • Krebs DL, Hilton DJ. 2001. SOCS proteins: negative regulators of cytokine signaling. Stem Cells 19:378-387. http://dx.doi.org/10.1634/stemcells.19-5-378.
    • (2001) Stem Cells , vol.19 , pp. 378-387
    • Krebs, D.L.1    Hilton, D.J.2
  • 40
    • 0032567353 scopus 로고    scopus 로고
    • The suppressor of cytokine signaling (SOCS) 1 and SOCS3 but not SOCS2 proteins inhibit interferon-mediated antiviral and antiproliferative activities
    • Song MM, Shuai K. 1998. The suppressor of cytokine signaling (SOCS) 1 and SOCS3 but not SOCS2 proteins inhibit interferon-mediated antiviral and antiproliferative activities. J. Biol. Chem. 273:35056-35062. http://dx.doi.org/10.1074/jbc.273.52.35056.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35056-35062
    • Song, M.M.1    Shuai, K.2
  • 41
    • 0034624986 scopus 로고    scopus 로고
    • Signals transducers and activators of transcription (STAT)-induced STAT inhibitor-1 (SSI-1)/suppressor of cytokine signaling-1 (SOCS-1) suppresses tumor necrosis factor alpha-induced cell death in fibroblasts
    • Morita Y, Naka T, Kawazoe Y, Fujimoto M, Narazaki M, Nakagawa R, Fukuyama H, Nagata S, Kishimoto T. 2000. Signals transducers and activators of transcription (STAT)-induced STAT inhibitor-1 (SSI-1)/suppressor of cytokine signaling-1 (SOCS-1) suppresses tumor necrosis factor alpha-induced cell death in fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 97:5405-5410. http://dx.doi.org/10.1073/pnas.090084797.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5405-5410
    • Morita, Y.1    Naka, T.2    Kawazoe, Y.3    Fujimoto, M.4    Narazaki, M.5    Nakagawa, R.6    Fukuyama, H.7    Nagata, S.8    Kishimoto, T.9
  • 42
    • 0037310860 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 inhibits IL-10-mediated immune responses
    • Ding Y, Chen D, Tarcsafalvi A, Su R, Qin L, Bromberg JS. 2003. Suppressor of cytokine signaling 1 inhibits IL-10-mediated immune responses. J. Immunol. 170:1383-1391.
    • (2003) J. Immunol. , vol.170 , pp. 1383-1391
    • Ding, Y.1    Chen, D.2    Tarcsafalvi, A.3    Su, R.4    Qin, L.5    Bromberg, J.S.6
  • 43
    • 82955226309 scopus 로고    scopus 로고
    • Respiratory disease caused by Mycoplasma bovis is enhanced by exposure to bovine herpes virus 1 (BHV-1) and not to bovine viral diarrhoea virus (BVDV) type 2
    • Prysliak T, Van der Merwe J, Lawman Z, Wilson D, Townsend H, van Drunen Littel-van den Hurk S, Perez-Casal J. 2011. Respiratory disease caused by Mycoplasma bovis is enhanced by exposure to bovine herpes virus 1 (BHV-1) and not to bovine viral diarrhoea virus (BVDV) type 2. Can. Vet. J. 52:1195-1202. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3196011/.
    • (2011) Can. Vet. J. , vol.52 , pp. 1195-1202
    • Prysliak, T.1    Van der Merwe, J.2    Lawman, Z.3    Wilson, D.4    Townsend, H.5    van Drunen Littel-van den Hurk, S.6    Perez-Casal, J.7
  • 44
    • 0017687659 scopus 로고
    • Nasal prevalence of Mycoplasma bovis and IHA titers in young dairy animals
    • Bennett RH, Jasper DE. 1977. Nasal prevalence of Mycoplasma bovis and IHA titers in young dairy animals. Cornell Vet. 67:361-373.
    • (1977) Cornell Vet. , vol.67 , pp. 361-373
    • Bennett, R.H.1    Jasper, D.E.2
  • 45
    • 73449118544 scopus 로고    scopus 로고
    • Association between an outbreak strain causing Mycoplasma bovis mastitis and its asymptomatic carriage in the herd: a case study from Idaho, USA
    • Punyapornwithaya V, Fox LK, Hancock DD, Gay JM, Alldredge JR. 2010. Association between an outbreak strain causing Mycoplasma bovis mastitis and its asymptomatic carriage in the herd: a case study from Idaho, USA. Prev. Vet. Med. 93:66-70. http://dx.doi.org/10.1016/j.prevetmed.2009.08.008.
    • (2010) Prev. Vet. Med. , vol.93 , pp. 66-70
    • Punyapornwithaya, V.1    Fox, L.K.2    Hancock, D.D.3    Gay, J.M.4    Alldredge, J.R.5
  • 46
    • 41549098597 scopus 로고    scopus 로고
    • Staying alive: bacterial inhibition of apoptosis during infection
    • Faherty CS, Maurelli AT. 2008. Staying alive: bacterial inhibition of apoptosis during infection. Trends Microbiol. 16:173-180. http://dx.doi.org/10.1016/j.tim.2008.02.001.
    • (2008) Trends Microbiol. , vol.16 , pp. 173-180
    • Faherty, C.S.1    Maurelli, A.T.2
  • 47
    • 5444245799 scopus 로고    scopus 로고
    • Chlamydia inhibit host cell apoptosis by degradation of proapoptotic BH3-only proteins
    • Fischer SF, Vier J, Kirschnek S, Klos A, Hess S, Ying S, Hacker G. 2004. Chlamydia inhibit host cell apoptosis by degradation of proapoptotic BH3-only proteins. J. Exp. Med. 200:905-916. http://dx.doi.org/10.1084/jem.20040402.
    • (2004) J. Exp. Med. , vol.200 , pp. 905-916
    • Fischer, S.F.1    Vier, J.2    Kirschnek, S.3    Klos, A.4    Hess, S.5    Ying, S.6    Hacker, G.7
  • 48
    • 33845992928 scopus 로고    scopus 로고
    • The secreted protease factor CPAF is responsible for degrading pro-apoptotic BH3-only proteins in Chlamydia trachomatis-infected cells
    • Pirbhai M, Dong F, Zhong Y, Pan KZ, Zhong G. 2006. The secreted protease factor CPAF is responsible for degrading pro-apoptotic BH3-only proteins in Chlamydia trachomatis-infected cells. J. Biol. Chem. 281: 31495-31501. http://dx.doi.org/10.1074/jbc.M602796200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31495-31501
    • Pirbhai, M.1    Dong, F.2    Zhong, Y.3    Pan, K.Z.4    Zhong, G.5
  • 49
    • 4544363784 scopus 로고    scopus 로고
    • Chlamydia trachomatis infection inhibits both Bax and Bak activation induced by staurosporine
    • Xiao Y, Zhong Y, Greene W, Dong F, Zhong G. 2004. Chlamydia trachomatis infection inhibits both Bax and Bak activation induced by staurosporine. Infect. Immun. 72:5470-5474. http://dx.doi.org/10.1128/IAI.72.9.5470-5474.2004.
    • (2004) Infect. Immun. , vol.72 , pp. 5470-5474
    • Xiao, Y.1    Zhong, Y.2    Greene, W.3    Dong, F.4    Zhong, G.5
  • 50
    • 34248348720 scopus 로고    scopus 로고
    • Shigella flexneri inhibits staurosporineinduced apoptosis in epithelial cells
    • Clark CS, Maurelli AT. 2007. Shigella flexneri inhibits staurosporineinduced apoptosis in epithelial cells. Infect. Immun. 75:2531-2539. http://dx.doi.org/10.1128/IAI.01866-06.
    • (2007) Infect. Immun. , vol.75 , pp. 2531-2539
    • Clark, C.S.1    Maurelli, A.T.2
  • 52
    • 33845511552 scopus 로고    scopus 로고
    • A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death
    • Laguna RK, Creasey EA, Li Z, Valtz N, Isberg RR. 2006. A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death. Proc. Natl. Acad. Sci. U.S.A. 103:18745-18750. http://dx.doi.org/10.1073/pnas.0609012103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18745-18750
    • Laguna, R.K.1    Creasey, E.A.2    Li, Z.3    Valtz, N.4    Isberg, R.R.5
  • 53
    • 0031822941 scopus 로고    scopus 로고
    • Mycoplasma nucleases able to induce internucleosomal DNA degradation in cultured cells possess many characteristics of eukaryotic apoptotic nucleases
    • Paddenberg R, Weber A, Wulf S, Mannherz HG. 1998. Mycoplasma nucleases able to induce internucleosomal DNA degradation in cultured cells possess many characteristics of eukaryotic apoptotic nucleases. Cell Death Differ. 5:517-528. http://dx.doi.org/10.1038/sj.cdd.4400380.
    • (1998) Cell Death Differ. , vol.5 , pp. 517-528
    • Paddenberg, R.1    Weber, A.2    Wulf, S.3    Mannherz, H.G.4
  • 54
    • 0031038691 scopus 로고    scopus 로고
    • Mycoplasma fermentans enhances concanavalin A-induced apoptosis of mouse splenic T cells
    • Shibata K, Watanabe T. 1997. Mycoplasma fermentans enhances concanavalin A-induced apoptosis of mouse splenic T cells. FEMS Immunol. Med. Microbiol. 17:103-109. http://dx.doi.org/10.1111/j.1574-695X.1997.tb01002.x.
    • (1997) FEMS Immunol. Med. Microbiol. , vol.17 , pp. 103-109
    • Shibata, K.1    Watanabe, T.2
  • 55
    • 0032408808 scopus 로고    scopus 로고
    • Mycoplasma infection can sensitize host cells to apoptosis through contribution of apoptotic-like endonuclease(s)
    • Sokolova IA, Vaughan AT, Khodarev NN. 1998. Mycoplasma infection can sensitize host cells to apoptosis through contribution of apoptotic-like endonuclease(s). Immunol. Cell Biol. 76:526-534. http://dx.doi.org/10.1046/j.1440-1711.1998.00781.x.
    • (1998) Immunol. Cell Biol. , vol.76 , pp. 526-534
    • Sokolova, I.A.1    Vaughan, A.T.2    Khodarev, N.N.3
  • 56
    • 0037074515 scopus 로고    scopus 로고
    • Mycoplasma bovis induces apoptosis of bovine lymphocytes
    • Vanden Bush TJ, Rosenbusch RF. 2002. Mycoplasma bovis induces apoptosis of bovine lymphocytes. FEMS Immunol. Med. Microbiol. 32:97-103. http://dx.doi.org/10.1111/j.1574-695X.2002.tb00540.x.
    • (2002) FEMS Immunol. Med. Microbiol. , vol.32 , pp. 97-103
    • Vanden Bush, T.J.1    Rosenbusch, R.F.2
  • 58
    • 0038648686 scopus 로고    scopus 로고
    • Nuclear factor kappa B protects against host cell apoptosis during Rickettsia rickettsii infection by inhibiting activation of apical and effector caspases and maintaining mitochondrial integrity
    • Joshi SG, Francis CW, Silverman DJ, Sahni SK. 2003. Nuclear factor kappa B protects against host cell apoptosis during Rickettsia rickettsii infection by inhibiting activation of apical and effector caspases and maintaining mitochondrial integrity. Infect. Immun. 71:4127-4136. http://dx.doi.org/10.1128/IAI.71.7.4127-4136.2003.
    • (2003) Infect. Immun. , vol.71 , pp. 4127-4136
    • Joshi, S.G.1    Francis, C.W.2    Silverman, D.J.3    Sahni, S.K.4
  • 59
    • 0036081269 scopus 로고    scopus 로고
    • Host-pathogen interactions: subversion and utilization of the NF-kappa B pathway during infection
    • Tato CM, Hunter CA. 2002. Host-pathogen interactions: subversion and utilization of the NF-kappa B pathway during infection. Infect. Immun. 70:3311-3317. http://dx.doi.org/10.1128/IAI.70.7.3311-3317.2002.
    • (2002) Infect. Immun. , vol.70 , pp. 3311-3317
    • Tato, C.M.1    Hunter, C.A.2
  • 60
    • 0035042056 scopus 로고    scopus 로고
    • Differential activation of NF-kappa B subunits in dendritic cells in response to Gram-negative bacteria and to lipopolysaccharide
    • Hofer S, Rescigno M, Granucci F, Citterio S, Francolini M, Ricciardi-Castagnoli P. 2001. Differential activation of NF-kappa B subunits in dendritic cells in response to Gram-negative bacteria and to lipopolysaccharide. Microbes Infect. 3:259-265. http://dx.doi.org/10.1016/S1286-4579(01)01378-8.
    • (2001) Microbes Infect. , vol.3 , pp. 259-265
    • Hofer, S.1    Rescigno, M.2    Granucci, F.3    Citterio, S.4    Francolini, M.5    Ricciardi-Castagnoli, P.6
  • 61
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li Q, Verma IM. 2002. NF-kappaB regulation in the immune system. Nat. Rev. Immunol. 2:725-734. http://dx.doi.org/10.1038/nri910.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 62
    • 0038605236 scopus 로고    scopus 로고
    • NF-kappaB and virus infection: who controls whom
    • Santoro MG, Rossi A, Amici C. 2003. NF-kappaB and virus infection: who controls whom. EMBO J. 22:2552-2560. http://dx.doi.org/10.1093/emboj/cdg267.
    • (2003) EMBO J. , vol.22 , pp. 2552-2560
    • Santoro, M.G.1    Rossi, A.2    Amici, C.3
  • 63
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-kappaB: players, pathways, perspectives
    • Gilmore TD. 2006. Introduction to NF-kappaB: players, pathways, perspectives. Oncogene 25:6680-6684. http://dx.doi.org/10.1038/sj.onc.1209954.
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 64
    • 0033996762 scopus 로고    scopus 로고
    • The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling
    • Karin M, Delhase M. 2000. The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling. Semin. Immunol. 12:85-98. http://dx.doi.org/10.1006/smim.2000.0210.
    • (2000) Semin. Immunol. , vol.12 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 65
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-kappaB activity
    • Karin M, Ben-Neriah Y. 2000. Phosphorylation meets ubiquitination: the control of NF-kappaB activity. Annu. Rev. Immunol. 18:621-663. http://dx.doi.org/10.1146/annurev.immunol.18.1.621.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 66
    • 1642513702 scopus 로고    scopus 로고
    • Stimulation of human Toll-like receptor (TLR) 2 and TLR6 with membrane lipoproteins of Mycoplasma fermentans induces apoptotic cell death after NF-kappa B activation
    • Into T, Kiura K, Yasuda M, Kataoka H, Inoue N, Hasebe A, Takeda K, Akira S, Shibata K. 2004. Stimulation of human Toll-like receptor (TLR) 2 and TLR6 with membrane lipoproteins of Mycoplasma fermentans induces apoptotic cell death after NF-kappa B activation. Cell. Microbiol. 6:187-199. http://dx.doi.org/10.1046/j.1462-5822.2003.00356.x.
    • (2004) Cell. Microbiol. , vol.6 , pp. 187-199
    • Into, T.1    Kiura, K.2    Yasuda, M.3    Kataoka, H.4    Inoue, N.5    Hasebe, A.6    Takeda, K.7    Akira, S.8    Shibata, K.9
  • 67
    • 62449312200 scopus 로고    scopus 로고
    • Mycoplasma genitalium-encoded MG309 activates NF-kappaB via Toll-like receptors 2 and 6 to elicit proinflammatory cytokine secretion from human genital epithelial cells
    • McGowin CL, Ma L, Martin DH, Pyles RB. 2009. Mycoplasma genitalium-encoded MG309 activates NF-kappaB via Toll-like receptors 2 and 6 to elicit proinflammatory cytokine secretion from human genital epithelial cells. Infect. Immun. 77:1175-1181. http://dx.doi.org/10.1128/IAI.00845-08.
    • (2009) Infect. Immun. , vol.77 , pp. 1175-1181
    • McGowin, C.L.1    Ma, L.2    Martin, D.H.3    Pyles, R.B.4
  • 68
    • 25444505635 scopus 로고    scopus 로고
    • A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-kappa B through TLR1, TLR2, and TLR6
    • Shimizu T, Kida Y, Kuwano K. 2005. A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-kappa B through TLR1, TLR2, and TLR6. J. Immunol. 175:4641-4646.
    • (2005) J. Immunol. , vol.175 , pp. 4641-4646
    • Shimizu, T.1    Kida, Y.2    Kuwano, K.3
  • 69
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • Beg AA, Baltimore D. 1996. An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 274:782-784. http://dx.doi.org/10.1126/science.274.5288.782.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 70
    • 0029992609 scopus 로고    scopus 로고
    • Suppression of TNF-alpha-induced apoptosis by NF-kappaB
    • Van Antwerp DJ, Martin SJ, Kafri T, Green DR, Verma IM. 1996. Suppression of TNF-alpha-induced apoptosis by NF-kappaB. Science 274:787-789. http://dx.doi.org/10.1126/science.274.5288.787.
    • (1996) Science , vol.274 , pp. 787-789
    • Van Antwerp, D.J.1    Martin, S.J.2    Kafri, T.3    Green, D.R.4    Verma, I.M.5
  • 71
    • 0029858387 scopus 로고    scopus 로고
    • TNF-and cancer therapyinduced apoptosis: potentiation by inhibition of NF-kappaB
    • Wang CY, Mayo MW, Baldwin AS, Jr. 1996. TNF-and cancer therapyinduced apoptosis: potentiation by inhibition of NF-kappaB. Science 274: 784-787. http://dx.doi.org/10.1126/science.274.5288.784.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin Jr., A.S.3
  • 73
    • 0344142396 scopus 로고    scopus 로고
    • Emerging roles of caspase-3 in apoptosis
    • Porter AG, Janicke RU. 1999. Emerging roles of caspase-3 in apoptosis. Cell Death Differ. 6:99-104. http://dx.doi.org/10.1038/sj.cdd.4400476.
    • (1999) Cell Death Differ. , vol.6 , pp. 99-104
    • Porter, A.G.1    Janicke, R.U.2
  • 75
    • 0030896618 scopus 로고    scopus 로고
    • Differential induction of apoptosis by Fas-Fas ligand interactions in human monocytes and macrophages
    • Kiener PA, Davis PM, Starling GC, Mehlin C, Klebanoff SJ, Ledbetter JA, Liles WC. 1997. Differential induction of apoptosis by Fas-Fas ligand interactions in human monocytes and macrophages. J. Exp. Med. 185: 1511-1516. http://dx.doi.org/10.1084/jem.185.8.1511.
    • (1997) J. Exp. Med. , vol.185 , pp. 1511-1516
    • Kiener, P.A.1    Davis, P.M.2    Starling, G.C.3    Mehlin, C.4    Klebanoff, S.J.5    Ledbetter, J.A.6    Liles, W.C.7
  • 76
    • 0034845246 scopus 로고    scopus 로고
    • The Fas-FasL death receptor and PI3K pathways independently regulate monocyte homeostasis
    • Perlman H, Pagliari LJ, Nguyen N, Bradley K, Liu H, Pope RM. 2001. The Fas-FasL death receptor and PI3K pathways independently regulate monocyte homeostasis. Eur. J. Immunol. 31:2421-2430. http://dx.doi.org/10.1002/1521-4141(200108)31:8<2421::AID-IMMU2421>3.0.C O;2-W.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 2421-2430
    • Perlman, H.1    Pagliari, L.J.2    Nguyen, N.3    Bradley, K.4    Liu, H.5    Pope, R.M.6
  • 77
    • 0035821647 scopus 로고    scopus 로고
    • Staurosporine induces apoptosis through both caspase-dependent and caspaseindependent mechanisms
    • Belmokhtar CA, Hillion J, Segal-Bendirdjian E. 2001. Staurosporine induces apoptosis through both caspase-dependent and caspaseindependent mechanisms. Oncogene 20:3354-3362. http://dx.doi.org/10.1038/sj.onc.1204436.
    • (2001) Oncogene , vol.20 , pp. 3354-3362
    • Belmokhtar, C.A.1    Hillion, J.2    Segal-Bendirdjian, E.3
  • 79
    • 44449096726 scopus 로고    scopus 로고
    • IL-10: the master regulator of immunity to infection
    • Couper KN, Blount DG, Riley EM. 2008. IL-10: the master regulator of immunity to infection. J. Immunol. 180:5771-5777.
    • (2008) J. Immunol. , vol.180 , pp. 5771-5777
    • Couper, K.N.1    Blount, D.G.2    Riley, E.M.3
  • 80
    • 0031974687 scopus 로고    scopus 로고
    • IL-10 prevents the differentiation of monocytes to dendritic cells but promotes their maturation to macrophages
    • Allavena P, Piemonti L, Longoni D, Bernasconi S, Stoppacciaro A, Ruco L, Mantovani A. 1998. IL-10 prevents the differentiation of monocytes to dendritic cells but promotes their maturation to macrophages. Eur. J. Immunol. 28:359-369. http://dx.doi.org/10.1002/(SICI)1521-4141(199801)28:01<359::AID-IMMU359> 3.0.CO;2-4.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 359-369
    • Allavena, P.1    Piemonti, L.2    Longoni, D.3    Bernasconi, S.4    Stoppacciaro, A.5    Ruco, L.6    Mantovani, A.7
  • 83
    • 0842332227 scopus 로고    scopus 로고
    • Characterization of a lymphoinhibitory peptide produced by Mycoplasma bovis
    • Vanden Bush TJ, Rosenbusch RF. 2004. Characterization of a lymphoinhibitory peptide produced by Mycoplasma bovis. Biochem. Biophys. Res. Commun. 315:336-341. http://dx.doi.org/10.1016/j.bbrc.2004.01.063.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 336-341
    • Vanden Bush, T.J.1    Rosenbusch, R.F.2


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