메뉴 건너뛰기




Volumn 41, Issue 6, 2006, Pages 226-240

Intracellular replication of Edwardsiella tarda in murine macrophage is dependent on the type III secretion system and induces an up-regulation of anti-apoptotic NF-κB target genes protecting the macrophage from staurosporine-induced apoptosis

Author keywords

Anti apoptosis; Edwardsiella tarda; Intracellular replication; Macrophage; NF B; The type III secretion system

Indexed keywords

CYTOKINE; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KAMEBAKAURIN; MESSENGER RNA; STAUROSPORINE; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 1; UNCLASSIFIED DRUG;

EID: 33750394163     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2006.08.002     Document Type: Article
Times cited : (67)

References (84)
  • 2
    • 0027420345 scopus 로고
    • Infections associated with the genus Edwardsiella: the role of Edwardsiella tarda in human disease
    • Janda J.M., and Abbott S.L. Infections associated with the genus Edwardsiella: the role of Edwardsiella tarda in human disease. Clin Infect Dis 17 (1993) 742-748
    • (1993) Clin Infect Dis , vol.17 , pp. 742-748
    • Janda, J.M.1    Abbott, S.L.2
  • 3
    • 0014471557 scopus 로고
    • Human infection with Edwardsiella tarda
    • Jordan G.W., and Hadley W.K. Human infection with Edwardsiella tarda. Ann Int Med 70 (1969) 283-288
    • (1969) Ann Int Med , vol.70 , pp. 283-288
    • Jordan, G.W.1    Hadley, W.K.2
  • 4
    • 0038282867 scopus 로고    scopus 로고
    • Maternal colonization and neonatal sepsis caused by Edwardsiella tarda
    • Mowbray E.E., Buck G., Humbaugh K.E., and Marshall G.S. Maternal colonization and neonatal sepsis caused by Edwardsiella tarda. Pediatrics 111 (2003) 296-298
    • (2003) Pediatrics , vol.111 , pp. 296-298
    • Mowbray, E.E.1    Buck, G.2    Humbaugh, K.E.3    Marshall, G.S.4
  • 5
    • 0024579210 scopus 로고
    • Serious infections with Edwardsiella tarda. A case report and review of the literature
    • Wilson J., and Waterer R. Serious infections with Edwardsiella tarda. A case report and review of the literature. Arch Intern Med 149 (1989) 208-210
    • (1989) Arch Intern Med , vol.149 , pp. 208-210
    • Wilson, J.1    Waterer, R.2
  • 6
    • 0015546499 scopus 로고
    • Edwardsiella tarda, a new pathogen of catfish (Ictalurus punctatus)
    • Meyer F.P., and Bullock G.L. Edwardsiella tarda, a new pathogen of catfish (Ictalurus punctatus). Appl Microbiol 25 (1973) 155-156
    • (1973) Appl Microbiol , vol.25 , pp. 155-156
    • Meyer, F.P.1    Bullock, G.L.2
  • 7
    • 0035914044 scopus 로고    scopus 로고
    • Viral and bacterial diseases of marine fish and shellfish in Japanese hatcheries
    • Muroga K. Viral and bacterial diseases of marine fish and shellfish in Japanese hatcheries. Aquaculture 202 (2001) 23-44
    • (2001) Aquaculture , vol.202 , pp. 23-44
    • Muroga, K.1
  • 8
    • 11144286294 scopus 로고    scopus 로고
    • Edwardsiella septicaemias
    • Woo P.T.K., and Bruno D.W. (Eds), CABI Publishing, London
    • Plumb J.A. Edwardsiella septicaemias. In: Woo P.T.K., and Bruno D.W. (Eds). Fish diseases and disorders, (1999), CABI Publishing, London 479-521
    • (1999) Fish diseases and disorders , pp. 479-521
    • Plumb, J.A.1
  • 9
    • 85008035966 scopus 로고
    • Edwardsiella tarda (Paracolobactrum anguillimortiferum) associated with pond-cultured eel disease
    • Wakabayashi H., and Egusa S. Edwardsiella tarda (Paracolobactrum anguillimortiferum) associated with pond-cultured eel disease. Bull Jpn Soc Sci Fish 39 (1973) 931-936
    • (1973) Bull Jpn Soc Sci Fish , vol.39 , pp. 931-936
    • Wakabayashi, H.1    Egusa, S.2
  • 10
    • 0017570312 scopus 로고
    • Edwardsiellosis in man and animals in Panama: clinical and epidemiological characteristics
    • Kourany M., Vasquez M.A., and Saenz R. Edwardsiellosis in man and animals in Panama: clinical and epidemiological characteristics. Am J Trop Med Hyg 26 (1977) 1183-1190
    • (1977) Am J Trop Med Hyg , vol.26 , pp. 1183-1190
    • Kourany, M.1    Vasquez, M.A.2    Saenz, R.3
  • 12
    • 0019449134 scopus 로고
    • Aerobic bacterial oral flora of garter snakes: development of normal flora and pathogenic potential for snakes and humans
    • Goldstein E.J.C., Agyare E.O., Vagvolgi A.E., and Halpern M. Aerobic bacterial oral flora of garter snakes: development of normal flora and pathogenic potential for snakes and humans. J Clin Microbiol 13 (1981) 954-956
    • (1981) J Clin Microbiol , vol.13 , pp. 954-956
    • Goldstein, E.J.C.1    Agyare, E.O.2    Vagvolgi, A.E.3    Halpern, M.4
  • 13
    • 0015550786 scopus 로고
    • The occurrence of Salmonellae and Edwardsiella in the turtles of the New York Zoological park
    • Otis V.S., and Behler J.L. The occurrence of Salmonellae and Edwardsiella in the turtles of the New York Zoological park. J Wildl Dis 9 (1973) 4-6
    • (1973) J Wildl Dis , vol.9 , pp. 4-6
    • Otis, V.S.1    Behler, J.L.2
  • 14
    • 0022196833 scopus 로고
    • Chronic enteritis associated with Edwardsiella tarda infection in Rockhopper penguins
    • Cook R.A., and Tappe J.P. Chronic enteritis associated with Edwardsiella tarda infection in Rockhopper penguins. J Am Vet Med Assoc 187 (1985) 1219-1220
    • (1985) J Am Vet Med Assoc , vol.187 , pp. 1219-1220
    • Cook, R.A.1    Tappe, J.P.2
  • 15
    • 0019854345 scopus 로고
    • Gram-negative, aerobic, enteric pathogens among intestinal microflora of wild turkey vultures (Cathartes aura) in west central Texas
    • Winsor D.K., Bloebaum A.P., and Mathewson J.J. Gram-negative, aerobic, enteric pathogens among intestinal microflora of wild turkey vultures (Cathartes aura) in west central Texas. Appl Environ Microbiol 42 (1981) 1123-1124
    • (1981) Appl Environ Microbiol , vol.42 , pp. 1123-1124
    • Winsor, D.K.1    Bloebaum, A.P.2    Mathewson, J.J.3
  • 16
    • 0026430568 scopus 로고
    • Edwardsiella tarda infection in a puppy with possible parvovirus infection
    • Van Assche J. Edwardsiella tarda infection in a puppy with possible parvovirus infection. Vet Rec 129 (1991) 475-476
    • (1991) Vet Rec , vol.129 , pp. 475-476
    • Van Assche, J.1
  • 17
    • 0040965485 scopus 로고
    • On a new bacterium, Paracolobactrum anguillimortiferum
    • Hoshina T. On a new bacterium, Paracolobactrum anguillimortiferum. Bull Jpn Soc Sci Fish 28 (1962) 162-164
    • (1962) Bull Jpn Soc Sci Fish , vol.28 , pp. 162-164
    • Hoshina, T.1
  • 18
  • 19
    • 0037009857 scopus 로고    scopus 로고
    • Microbiological comparative study of isolates of Edwardsiella tarda isolated in different countries from fish and humans
    • Nucci C., da Silveira W.D., da Silva Corrêa S., Nakazato G., Bando S.Y., Ribeiro M.A., et al. Microbiological comparative study of isolates of Edwardsiella tarda isolated in different countries from fish and humans. Vet Microbiol 89 (2002) 29-39
    • (2002) Vet Microbiol , vol.89 , pp. 29-39
    • Nucci, C.1    da Silveira, W.D.2    da Silva Corrêa, S.3    Nakazato, G.4    Bando, S.Y.5    Ribeiro, M.A.6
  • 21
    • 0037369747 scopus 로고    scopus 로고
    • Functional genomics approach to the identification of virulence genes involved in Edwardsiella tarda pathogenesis
    • Srinivasa Rao P.S., Lim T.M., and Leung K.Y. Functional genomics approach to the identification of virulence genes involved in Edwardsiella tarda pathogenesis. Infect Immun 71 (2003) 1343-1351
    • (2003) Infect Immun , vol.71 , pp. 1343-1351
    • Srinivasa Rao, P.S.1    Lim, T.M.2    Leung, K.Y.3
  • 22
    • 0036840350 scopus 로고    scopus 로고
    • Comparative proteomic analysis of extracellular proteins of Edwardsiella tarda
    • Tan Y.P., Lin Q., Wang X.H., Joshi S., Hew C.L., and Leung K.Y. Comparative proteomic analysis of extracellular proteins of Edwardsiella tarda. Infect Immun 70 (2002) 6475-6480
    • (2002) Infect Immun , vol.70 , pp. 6475-6480
    • Tan, Y.P.1    Lin, Q.2    Wang, X.H.3    Joshi, S.4    Hew, C.L.5    Leung, K.Y.6
  • 23
    • 22144483385 scopus 로고    scopus 로고
    • Role of type III secretion in Edwardsiella tarda virulence
    • Tan Y.P., Zheng J., Tung S.L., Rosenshine I., and Leung K.Y. Role of type III secretion in Edwardsiella tarda virulence. Microbiology 151 (2005) 2301-2313
    • (2005) Microbiology , vol.151 , pp. 2301-2313
    • Tan, Y.P.1    Zheng, J.2    Tung, S.L.3    Rosenshine, I.4    Leung, K.Y.5
  • 24
    • 8844275498 scopus 로고    scopus 로고
    • Type III protein secretion mechanism in mammalian and plant pathogens
    • He S.Y., Nomura K., and Whittam T.S. Type III protein secretion mechanism in mammalian and plant pathogens. Biochim Biophys Acta 1694 (2004) 181-206
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 181-206
    • He, S.Y.1    Nomura, K.2    Whittam, T.S.3
  • 25
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses
    • Ghosh S., May M.J., and Kopp E.B. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16 (1998) 225-260
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 26
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • Baeuerle P.A., and Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol 12 (1994) 141-179
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 27
    • 0026699666 scopus 로고
    • Transcriptional activation of the tumor necrosis factor alpha-inducible zinc finger protein, A20, is mediated by kappa B elements
    • Krikos A., Laherty C.D., and Dixit V.M. Transcriptional activation of the tumor necrosis factor alpha-inducible zinc finger protein, A20, is mediated by kappa B elements. J Biol Chem 267 (1992) 17971-17976
    • (1992) J Biol Chem , vol.267 , pp. 17971-17976
    • Krikos, A.1    Laherty, C.D.2    Dixit, V.M.3
  • 28
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang C.Y., Mayo M.W., Korneluk R.G., Goeddel D.V., and Baldwin A.S. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281 (1998) 1680-1683
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin, A.S.5
  • 29
    • 0032516651 scopus 로고    scopus 로고
    • IEX-1L, an apoptosis inhibitor involved in NF-kappaB-mediated cell survival
    • Wu M.X., Ao Z., Prasad K.V.S., Wu R., and Schlossman S.F. IEX-1L, an apoptosis inhibitor involved in NF-kappaB-mediated cell survival. Science 281 (1998) 998-1001
    • (1998) Science , vol.281 , pp. 998-1001
    • Wu, M.X.1    Ao, Z.2    Prasad, K.V.S.3    Wu, R.4    Schlossman, S.F.5
  • 30
    • 0033558215 scopus 로고    scopus 로고
    • The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis
    • Zong W.X., Edelstein L.C., Chen C., Bash J., and Gélinas C. The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis. Genes Dev 13 (1999) 382-387
    • (1999) Genes Dev , vol.13 , pp. 382-387
    • Zong, W.X.1    Edelstein, L.C.2    Chen, C.3    Bash, J.4    Gélinas, C.5
  • 32
    • 0344766146 scopus 로고    scopus 로고
    • Apoptosis in macrophages and alveolar epithelial cells during early stages of infection by Legionella pneumophila and its role in cytopathogenicity
    • Gao L., and Kwaik Y.A. Apoptosis in macrophages and alveolar epithelial cells during early stages of infection by Legionella pneumophila and its role in cytopathogenicity. Infect Immun 67 (1999) 862-870
    • (1999) Infect Immun , vol.67 , pp. 862-870
    • Gao, L.1    Kwaik, Y.A.2
  • 33
    • 0030780833 scopus 로고    scopus 로고
    • Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis
    • Ruckdeschel K., Roggenkamp A., Lafont V., Mangeat P., Heesemann J., and Rouot B. Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis. Infect Immun 65 (1997) 4813-4821
    • (1997) Infect Immun , vol.65 , pp. 4813-4821
    • Ruckdeschel, K.1    Roggenkamp, A.2    Lafont, V.3    Mangeat, P.4    Heesemann, J.5    Rouot, B.6
  • 34
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky A., Prevost M.C., and Sansonetti P.J. Shigella flexneri induces apoptosis in infected macrophages. Nature 9 (1992) 167-169
    • (1992) Nature , vol.9 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 35
    • 0034011205 scopus 로고    scopus 로고
    • Modulation of host immune responses, induction of apoptosis and inhibition of NF-kappaB activation by the Bordetella type III secretion system
    • Yuk M.H., Harvill E.T., Cotter P.A., and Miller J.F. Modulation of host immune responses, induction of apoptosis and inhibition of NF-kappaB activation by the Bordetella type III secretion system. Mol Microbiol 35 (2000) 991-1004
    • (2000) Mol Microbiol , vol.35 , pp. 991-1004
    • Yuk, M.H.1    Harvill, E.T.2    Cotter, P.A.3    Miller, J.F.4
  • 36
    • 0032536526 scopus 로고    scopus 로고
    • Inhibition of apoptosis in chlamydia-infected cells: blockade of mitochondrial cytochrome c release and caspase activation
    • Fan T., Lu H., Hu H., Shi L., McClarty G.A., Nance D.M., et al. Inhibition of apoptosis in chlamydia-infected cells: blockade of mitochondrial cytochrome c release and caspase activation. J Exp Med 187 (1998) 487-496
    • (1998) J Exp Med , vol.187 , pp. 487-496
    • Fan, T.1    Lu, H.2    Hu, H.3    Shi, L.4    McClarty, G.A.5    Nance, D.M.6
  • 37
    • 0034773537 scopus 로고    scopus 로고
    • Characterization of antiapoptotic activities of Chlamydia pneumoniae in human cells
    • Fischer S.F., Schwarz C., Vier J., and Hacker G. Characterization of antiapoptotic activities of Chlamydia pneumoniae in human cells. Infect Immun 69 (2001) 7121-7129
    • (2001) Infect Immun , vol.69 , pp. 7121-7129
    • Fischer, S.F.1    Schwarz, C.2    Vier, J.3    Hacker, G.4
  • 38
    • 0031760359 scopus 로고    scopus 로고
    • Re-evaluation of the culture condition of polymorphonuclear cells for the study of apoptosis induction
    • Hiroi M., Shimojima T., Kashimata M., Miyata T., Takano H., Takahama M., et al. Re-evaluation of the culture condition of polymorphonuclear cells for the study of apoptosis induction. Anticancer Res 18 (1998) 3475-3479
    • (1998) Anticancer Res , vol.18 , pp. 3475-3479
    • Hiroi, M.1    Shimojima, T.2    Kashimata, M.3    Miyata, T.4    Takano, H.5    Takahama, M.6
  • 40
    • 0042697098 scopus 로고    scopus 로고
    • Infection of human urethral epithelium with Neisseria gonorrhoeae elicits an upregulation of host anti-apoptotic factors and protects cells from staurosporine-induced apoptosis
    • Binnicker M.J., Williams R.D., and Apicella M.A. Infection of human urethral epithelium with Neisseria gonorrhoeae elicits an upregulation of host anti-apoptotic factors and protects cells from staurosporine-induced apoptosis. Cell Microbiol 5 (2003) 549-560
    • (2003) Cell Microbiol , vol.5 , pp. 549-560
    • Binnicker, M.J.1    Williams, R.D.2    Apicella, M.A.3
  • 41
    • 12444338487 scopus 로고    scopus 로고
    • NF-kappa B activation is not required for Chlamydia trachomatis inhibition of host epithelial cell apoptosis
    • Xiao Y., Zhong Y., Su H., Zhou Z., Paul C., and Zhong G. NF-kappa B activation is not required for Chlamydia trachomatis inhibition of host epithelial cell apoptosis. J Immunol 174 (2005) 1701-1708
    • (2005) J Immunol , vol.174 , pp. 1701-1708
    • Xiao, Y.1    Zhong, Y.2    Su, H.3    Zhou, Z.4    Paul, C.5    Zhong, G.6
  • 42
    • 0032516101 scopus 로고    scopus 로고
    • NF-kappa B-dependent inhibition of apoptosis is essential for host cellsurvival during Rickettsia rickettsii infection
    • Clifton D.R., Goss R.A., Sahni S.K., Van Antwerp D., Baggs R.B., Marder V.J., et al. NF-kappa B-dependent inhibition of apoptosis is essential for host cellsurvival during Rickettsia rickettsii infection. Proc Natl Acad Sci USA 95 (1998) 4646-4651
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4646-4651
    • Clifton, D.R.1    Goss, R.A.2    Sahni, S.K.3    Van Antwerp, D.4    Baggs, R.B.5    Marder, V.J.6
  • 43
    • 2342489869 scopus 로고    scopus 로고
    • Sahni SKNF-kappaB activation suppresses host cell apoptosis during Rickettsia rickettsii infection via regulatory effects on intracellular localization or levels of apoptogenic and anti-apoptotic proteins
    • Joshi S.G., Francis C.W., and Silverman D.J. Sahni SKNF-kappaB activation suppresses host cell apoptosis during Rickettsia rickettsii infection via regulatory effects on intracellular localization or levels of apoptogenic and anti-apoptotic proteins. FEMS Microbiol Lett 234 (2004) 333-341
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 333-341
    • Joshi, S.G.1    Francis, C.W.2    Silverman, D.J.3
  • 44
    • 0346256758 scopus 로고    scopus 로고
    • Helicobacter pylori induces antiapoptosis through nuclear factor-kappaB activation
    • Yanai A., Hirata Y., Mitsuno Y., Maeda S., Shibata W., Akanuma M., et al. Helicobacter pylori induces antiapoptosis through nuclear factor-kappaB activation. J Infect Dis 188 (2003) 1741-1751
    • (2003) J Infect Dis , vol.188 , pp. 1741-1751
    • Yanai, A.1    Hirata, Y.2    Mitsuno, Y.3    Maeda, S.4    Shibata, W.5    Akanuma, M.6
  • 45
    • 10844242078 scopus 로고    scopus 로고
    • Hemozoin induces macrophage chemokine expression through oxidative stress-dependent and -independent mechanisms
    • Jaramillo M., Godbout M., and Olivier M. Hemozoin induces macrophage chemokine expression through oxidative stress-dependent and -independent mechanisms. J Immunol 174 (2005) 475-484
    • (2005) J Immunol , vol.174 , pp. 475-484
    • Jaramillo, M.1    Godbout, M.2    Olivier, M.3
  • 46
    • 0037159513 scopus 로고    scopus 로고
    • IKKalpha, IKKbeta, and NEMO/IKKgamma are each required for the NF-kappa B-mediated inflammatory response program
    • Li X., Massa P.E., Hanidu A., Peet G.W., Aro P., Savitt A., et al. IKKalpha, IKKbeta, and NEMO/IKKgamma are each required for the NF-kappa B-mediated inflammatory response program. J Biol Chem 277 (2002) 45129-45140
    • (2002) J Biol Chem , vol.277 , pp. 45129-45140
    • Li, X.1    Massa, P.E.2    Hanidu, A.3    Peet, G.W.4    Aro, P.5    Savitt, A.6
  • 47
  • 49
    • 0344428149 scopus 로고    scopus 로고
    • Regulation and functional involvement of macrophage scavenger receptor MARCO in clearance of bacteria in vivo
    • Van der Laan L.J.W., Döpp E.A., Haworth R., Pikkarainen T., Kangas M., Elomaa O., et al. Regulation and functional involvement of macrophage scavenger receptor MARCO in clearance of bacteria in vivo. J Immunol 162 (1999) 939-947
    • (1999) J Immunol , vol.162 , pp. 939-947
    • Van der Laan, L.J.W.1    Döpp, E.A.2    Haworth, R.3    Pikkarainen, T.4    Kangas, M.5    Elomaa, O.6
  • 50
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E., Newmeyer D.D., and Green D.R. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 17 (1998) 37-49
    • (1998) EMBO J , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 52
    • 0029906431 scopus 로고    scopus 로고
    • BCL-2 and MCL-1 expression in Chinese hamster ovary cells inhibits intracellular acidification and apoptosis induced by staurosporine
    • Reynolds J.E., Li J., Craig R.W., and Eastman A. BCL-2 and MCL-1 expression in Chinese hamster ovary cells inhibits intracellular acidification and apoptosis induced by staurosporine. Exp Cell Res 225 (1996) 430-436
    • (1996) Exp Cell Res , vol.225 , pp. 430-436
    • Reynolds, J.E.1    Li, J.2    Craig, R.W.3    Eastman, A.4
  • 53
    • 0034908490 scopus 로고    scopus 로고
    • Transient expression of the Bcl-2 family member, A1-a, results in nuclear localization and resistance to staurosporine-induced apoptosis
    • Somogyi R.D., Wu Y., Orlofsky A., and Prystowsky M.B. Transient expression of the Bcl-2 family member, A1-a, results in nuclear localization and resistance to staurosporine-induced apoptosis. Cell Death Differ 8 (2001) 785-793
    • (2001) Cell Death Differ , vol.8 , pp. 785-793
    • Somogyi, R.D.1    Wu, Y.2    Orlofsky, A.3    Prystowsky, M.B.4
  • 55
    • 0242662781 scopus 로고    scopus 로고
    • Alveolar macrophage apoptosis contributes to pneumococcal clearance in a resolving model of pulmonary infection
    • Dockrell D.H., Marriott H.M., Prince L.R., Ridger V.C., Ince P.G., Hellewell P.G., et al. Alveolar macrophage apoptosis contributes to pneumococcal clearance in a resolving model of pulmonary infection. J Immunol 171 (2003) 5380-5388
    • (2003) J Immunol , vol.171 , pp. 5380-5388
    • Dockrell, D.H.1    Marriott, H.M.2    Prince, L.R.3    Ridger, V.C.4    Ince, P.G.5    Hellewell, P.G.6
  • 56
    • 0034641931 scopus 로고    scopus 로고
    • Corpse clearance defines the meaning of cell death
    • Savill J., and Fadok V. Corpse clearance defines the meaning of cell death. Nature 407 (2000) 784-788
    • (2000) Nature , vol.407 , pp. 784-788
    • Savill, J.1    Fadok, V.2
  • 57
    • 0027326012 scopus 로고
    • Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2
    • Lin E.Y., Orlofsky A., Berger M.S., and Prystowsky M.B. Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2. J Immunol 151 (1993) 1979-1988
    • (1993) J Immunol , vol.151 , pp. 1979-1988
    • Lin, E.Y.1    Orlofsky, A.2    Berger, M.S.3    Prystowsky, M.B.4
  • 58
    • 0030053684 scopus 로고    scopus 로고
    • A1, a Bcl-2 family member, prolongs cell survival and permits myeloid differentiation
    • Lin E.Y., Orlofsky A., Wang H.G., Reed J.C., and Prystowsky M.B. A1, a Bcl-2 family member, prolongs cell survival and permits myeloid differentiation. Blood 87 (1996) 983-992
    • (1996) Blood , vol.87 , pp. 983-992
    • Lin, E.Y.1    Orlofsky, A.2    Wang, H.G.3    Reed, J.C.4    Prystowsky, M.B.5
  • 59
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 60
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 61
    • 0037174864 scopus 로고    scopus 로고
    • TRAIL receptor and CD95 signal to mitochondria via FADD, caspase-8/10, Bid, and Bax but differentially regulate events downstream from truncated Bid
    • Werner A.B., de Vries E., Tait S.W., Bontjer I., and Borst J. TRAIL receptor and CD95 signal to mitochondria via FADD, caspase-8/10, Bid, and Bax but differentially regulate events downstream from truncated Bid. J Biol Chem 277 (2002) 40760-40767
    • (2002) J Biol Chem , vol.277 , pp. 40760-40767
    • Werner, A.B.1    de Vries, E.2    Tait, S.W.3    Bontjer, I.4    Borst, J.5
  • 62
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B., Montessuit S., Sanchez B., and Martinou J.C. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J Biol Chem 276 (2001) 11615-11623
    • (2001) J Biol Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 63
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death
    • Wei M.C., Zong W.X., Cheng E.H., Lindsten T., Panoutsakopoulou V., Ross A.J., et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292 (2001) 727-730
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3    Lindsten, T.4    Panoutsakopoulou, V.5    Ross, A.J.6
  • 65
    • 0035297708 scopus 로고    scopus 로고
    • Requirement of A1-a for bacillus Calmette-Guerin-mediated protection of macrophages against nitric oxide-induced apoptosis
    • Kausalya S., Somogyi R., Orlofsky A., and Prystowsky M.B. Requirement of A1-a for bacillus Calmette-Guerin-mediated protection of macrophages against nitric oxide-induced apoptosis. J Immunol 166 (2001) 4721-4727
    • (2001) J Immunol , vol.166 , pp. 4721-4727
    • Kausalya, S.1    Somogyi, R.2    Orlofsky, A.3    Prystowsky, M.B.4
  • 66
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Deveraux Q.L., and Reed J.C. IAP family proteins-suppressors of apoptosis. Genes Dev 13 (1999) 239-252
    • (1999) Genes Dev , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 68
    • 0037108761 scopus 로고    scopus 로고
    • Innate recognition of bacteria by a macrophage cytosolic surveillance pathway
    • O'Riordan M., Yi C.H., Gonzales R., Lee K.D., and Portnoy D.A. Innate recognition of bacteria by a macrophage cytosolic surveillance pathway. Proc Natl Acad Sci USA 99 (2002) 13861-13866
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13861-13866
    • O'Riordan, M.1    Yi, C.H.2    Gonzales, R.3    Lee, K.D.4    Portnoy, D.A.5
  • 69
    • 0038624558 scopus 로고    scopus 로고
    • NODs: intracellular proteins involved in inflammation and apoptosis
    • Inohara N., and Nuñez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat Rev Immunol 3 (2003) 371-382
    • (2003) Nat Rev Immunol , vol.3 , pp. 371-382
    • Inohara, N.1    Nuñez, G.2
  • 70
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • Girardin S.E., Boneca I.G., Viala J., Chamaillard M., Labigne A., Thomas G., et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem 278 (2003) 8869-8872
    • (2003) J Biol Chem , vol.278 , pp. 8869-8872
    • Girardin, S.E.1    Boneca, I.G.2    Viala, J.3    Chamaillard, M.4    Labigne, A.5    Thomas, G.6
  • 71
    • 0037458665 scopus 로고    scopus 로고
    • Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease
    • Inohara N., Ogura Y., Fontalba A., Gutierrez O., Pons F., Crespo J., et al. Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease. J Biol Chem 278 (2003) 5509-5512
    • (2003) J Biol Chem , vol.278 , pp. 5509-5512
    • Inohara, N.1    Ogura, Y.2    Fontalba, A.3    Gutierrez, O.4    Pons, F.5    Crespo, J.6
  • 72
    • 0032573408 scopus 로고    scopus 로고
    • Prostaglandins prevent inducible nitric oxide synthase protein expression by inhibiting nuclear factor-κB activation in J774 macrophages
    • D'Acquisto F., Sautebin L., Iuvone T., Di Rosa M., and Carnuccio R. Prostaglandins prevent inducible nitric oxide synthase protein expression by inhibiting nuclear factor-κB activation in J774 macrophages. FEBS Lett 440 (1998) 76-80
    • (1998) FEBS Lett , vol.440 , pp. 76-80
    • D'Acquisto, F.1    Sautebin, L.2    Iuvone, T.3    Di Rosa, M.4    Carnuccio, R.5
  • 74
    • 0027268399 scopus 로고
    • Influence of 3′ half-site sequence of NF-κB motifs on the binding of lipopolysaccharide-activatable macrophage NF-κB proteins
    • Muroi M., Muroi Y., Yamamoto K., and Suzuki T. Influence of 3′ half-site sequence of NF-κB motifs on the binding of lipopolysaccharide-activatable macrophage NF-κB proteins. J Biol Chem 268 (1993) 19534-19539
    • (1993) J Biol Chem , vol.268 , pp. 19534-19539
    • Muroi, M.1    Muroi, Y.2    Yamamoto, K.3    Suzuki, T.4
  • 75
    • 0037166268 scopus 로고    scopus 로고
    • Kaurane diterpene, kamebakaurin, inhibits NF-kappa B by directly targeting the DNA-binding activity of p50 and blocks the expression of antiapoptotic NF-kappa B target genes
    • Lee J., Koo T.H., Hwang B.Y., and Lee J.J. Kaurane diterpene, kamebakaurin, inhibits NF-kappa B by directly targeting the DNA-binding activity of p50 and blocks the expression of antiapoptotic NF-kappa B target genes. J Biol Chem 277 (2002) 18411-18420
    • (2002) J Biol Chem , vol.277 , pp. 18411-18420
    • Lee, J.1    Koo, T.H.2    Hwang, B.Y.3    Lee, J.J.4
  • 76
    • 0026623426 scopus 로고
    • mxiA of Shigella flexneri 2a, which facilitates export of invasion plasmid antigens, encodes a homolog of the low-calcium-response protein, LcrD, of Yersinia pestis
    • Andrews G.P., and Maurelli A.T. mxiA of Shigella flexneri 2a, which facilitates export of invasion plasmid antigens, encodes a homolog of the low-calcium-response protein, LcrD, of Yersinia pestis. Infect Immun 60 (1992) 3287-3295
    • (1992) Infect Immun , vol.60 , pp. 3287-3295
    • Andrews, G.P.1    Maurelli, A.T.2
  • 77
    • 0036837752 scopus 로고    scopus 로고
    • Evidence for a type III secretion system in Aeromonas salmonicida subsp. salmonicida
    • Burr S.E., Stuber K., Wahli T., and Frey J. Evidence for a type III secretion system in Aeromonas salmonicida subsp. salmonicida. J Bacteriol 184 (2002) 5966-5970
    • (2002) J Bacteriol , vol.184 , pp. 5966-5970
    • Burr, S.E.1    Stuber, K.2    Wahli, T.3    Frey, J.4
  • 78
    • 0026921856 scopus 로고
    • Determinants of pathogenicity in Xanthomonas campestris pv. vesicatoria are related to proteins involved in secretion in bacterial pathogens of animals
    • Fenselau S., Balbo I., and Bonas U. Determinants of pathogenicity in Xanthomonas campestris pv. vesicatoria are related to proteins involved in secretion in bacterial pathogens of animals. Mol Plant-Microbe Interact 5 (1992) 390-396
    • (1992) Mol Plant-Microbe Interact , vol.5 , pp. 390-396
    • Fenselau, S.1    Balbo, I.2    Bonas, U.3
  • 79
    • 0026720513 scopus 로고
    • Molecular and functional characterization of the Salmonella invasion gene invA: homology of InvA to members of a new protein family
    • Galan J.E., Ginocchio C., and Costeas P. Molecular and functional characterization of the Salmonella invasion gene invA: homology of InvA to members of a new protein family. J Bacteriol 17 (1992) 4338-4349
    • (1992) J Bacteriol , vol.17 , pp. 4338-4349
    • Galan, J.E.1    Ginocchio, C.2    Costeas, P.3
  • 80
    • 0021829611 scopus 로고
    • The DNA sequence of the gene for the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites
    • Steinmetz M., Le Coq D., Aymerich S., Gonzy-Treboul G., and Gay P. The DNA sequence of the gene for the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites. Mol Gen Genet 200 (1985) 220-228
    • (1985) Mol Gen Genet , vol.200 , pp. 220-228
    • Steinmetz, M.1    Le Coq, D.2    Aymerich, S.3    Gonzy-Treboul, G.4    Gay, P.5
  • 82
    • 27644590078 scopus 로고    scopus 로고
    • Polyglutamine tract-binding protein-1 dysfunction induces cell death of neurons through mitochondrial stress
    • Marubuchi S., Wada Y., Okuda T., Hara Y., Qi M., Hoshino M., et al. Polyglutamine tract-binding protein-1 dysfunction induces cell death of neurons through mitochondrial stress. J Neurochem 95 (2005) 858-870
    • (2005) J Neurochem , vol.95 , pp. 858-870
    • Marubuchi, S.1    Wada, Y.2    Okuda, T.3    Hara, Y.4    Qi, M.5    Hoshino, M.6
  • 83
    • 0034724689 scopus 로고    scopus 로고
    • PDZ domain-dependent suppression of NF-κB/p65-induced Aβ42 production by a neuron-specific X11-like protein
    • Tomita S., Fujita T., Kirino Y., and Suzuki T. PDZ domain-dependent suppression of NF-κB/p65-induced Aβ42 production by a neuron-specific X11-like protein. J Biol Chem 275 (2000) 13056-13060
    • (2000) J Biol Chem , vol.275 , pp. 13056-13060
    • Tomita, S.1    Fujita, T.2    Kirino, Y.3    Suzuki, T.4
  • 84
    • 21244477221 scopus 로고    scopus 로고
    • Identification of Trichomonas vaginalis cysteine proteases that induce apoptosis in human vaginal epithelial cells
    • Sommer U., Costello C.E., Hayes G.R., Beach D.H., Gilbert R.O., Lucas J.J., et al. Identification of Trichomonas vaginalis cysteine proteases that induce apoptosis in human vaginal epithelial cells. J Biol Chem 280 (2005) 23853-23860
    • (2005) J Biol Chem , vol.280 , pp. 23853-23860
    • Sommer, U.1    Costello, C.E.2    Hayes, G.R.3    Beach, D.H.4    Gilbert, R.O.5    Lucas, J.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.