메뉴 건너뛰기




Volumn 47, Issue 3, 2009, Pages 143-150

Induction of apoptosis in human neutrophils by Mycobacterium tuberculosis is dependent on mature bacterial lipoproteins

Author keywords

Apoptotic signaling; Innate immunity; Phagocytosis; Virulence

Indexed keywords

BACTERIAL PROTEIN; LIPOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 68149099858     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2009.05.006     Document Type: Article
Times cited : (17)

References (47)
  • 1
    • 0025121957 scopus 로고
    • Macrophages and polymorphonuclear neutrophils in lung defense and injury
    • Sibille Y., and Reynolds H.Y. Macrophages and polymorphonuclear neutrophils in lung defense and injury. Am Rev Respir Dis 141 (1990) 471-501
    • (1990) Am Rev Respir Dis , vol.141 , pp. 471-501
    • Sibille, Y.1    Reynolds, H.Y.2
  • 2
    • 0016742008 scopus 로고
    • Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival
    • Armstrong J.A., and Hart P.D. Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival. J Exp Med 142 (1975) 1-16
    • (1975) J Exp Med , vol.142 , pp. 1-16
    • Armstrong, J.A.1    Hart, P.D.2
  • 3
    • 25444486695 scopus 로고    scopus 로고
    • Survival of virulent Mycobacterium tuberculosis involves preventing apoptosis induced by Bcl-2 upregulation and release resulting from necrosis in J774 macrophages
    • Zhang J., Jiang R., Takayama H., and Tanaka Y. Survival of virulent Mycobacterium tuberculosis involves preventing apoptosis induced by Bcl-2 upregulation and release resulting from necrosis in J774 macrophages. Microbiol Immunol 49 (2005) 845-852
    • (2005) Microbiol Immunol , vol.49 , pp. 845-852
    • Zhang, J.1    Jiang, R.2    Takayama, H.3    Tanaka, Y.4
  • 4
    • 33644837680 scopus 로고    scopus 로고
    • A mechanism of virulence: virulent Mycobacterium tuberculosis strain H37Rv, but not attenuated H37Ra, causes significant mitochondrial inner membrane disruption in macrophages leading to necrosis
    • Chen M., Gan H., and Remold H.G. A mechanism of virulence: virulent Mycobacterium tuberculosis strain H37Rv, but not attenuated H37Ra, causes significant mitochondrial inner membrane disruption in macrophages leading to necrosis. J Immunol 176 (2006) 3707-3716
    • (2006) J Immunol , vol.176 , pp. 3707-3716
    • Chen, M.1    Gan, H.2    Remold, H.G.3
  • 5
    • 0033214553 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis inhibits IFN-gamma transcriptional responses without inhibiting activation of STAT1
    • Ting L.M., Kim A.C., Cattamanchi A., and Ernst J.D. Mycobacterium tuberculosis inhibits IFN-gamma transcriptional responses without inhibiting activation of STAT1. J Immunol 163 (1999) 3898-3906
    • (1999) J Immunol , vol.163 , pp. 3898-3906
    • Ting, L.M.1    Kim, A.C.2    Cattamanchi, A.3    Ernst, J.D.4
  • 6
    • 0023550258 scopus 로고
    • Capacity of human neutrophils to kill Mycobacterium tuberculosis
    • Brown A.E., Holzer T.J., and Andersen B.R. Capacity of human neutrophils to kill Mycobacterium tuberculosis. J Infect Dis 156 (1987) 985-989
    • (1987) J Infect Dis , vol.156 , pp. 985-989
    • Brown, A.E.1    Holzer, T.J.2    Andersen, B.R.3
  • 7
    • 0031845345 scopus 로고    scopus 로고
    • Expression of chemokines and induction of rapid cell death in human blood neutrophils by Mycobacterium tuberculosis
    • Kasahara K., Sato I., Ogura K., Takeuchi H., Kobayashi K., and Adachi M. Expression of chemokines and induction of rapid cell death in human blood neutrophils by Mycobacterium tuberculosis. J Infect Dis 178 (1998) 127-137
    • (1998) J Infect Dis , vol.178 , pp. 127-137
    • Kasahara, K.1    Sato, I.2    Ogura, K.3    Takeuchi, H.4    Kobayashi, K.5    Adachi, M.6
  • 8
    • 0032519925 scopus 로고    scopus 로고
    • Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF
    • Fadok V.A., Bratton D.L., Konowal A., Freed P.W., Westcott J.Y., and Henson P.M. Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF. J Clin Invest 101 (1998) 890-898
    • (1998) J Clin Invest , vol.101 , pp. 890-898
    • Fadok, V.A.1    Bratton, D.L.2    Konowal, A.3    Freed, P.W.4    Westcott, J.Y.5    Henson, P.M.6
  • 9
    • 0030777041 scopus 로고    scopus 로고
    • Chemokine secretion by human polymorphonuclear granulocytes after stimulation with Mycobacterium tuberculosis and lipoarabinomannan
    • Riedel D.D., and Kaufmann S.H. Chemokine secretion by human polymorphonuclear granulocytes after stimulation with Mycobacterium tuberculosis and lipoarabinomannan. Infect Immun 65 (1997) 4620-4623
    • (1997) Infect Immun , vol.65 , pp. 4620-4623
    • Riedel, D.D.1    Kaufmann, S.H.2
  • 10
    • 0034759331 scopus 로고    scopus 로고
    • Priming of human neutrophils by mycobacterial lipoarabinomannans: role of granule mobilisation
    • Faldt J., Dahlgren C., Ridell M., and Karlsson A. Priming of human neutrophils by mycobacterial lipoarabinomannans: role of granule mobilisation. Microbes Infect 3 (2001) 1101-1109
    • (2001) Microbes Infect , vol.3 , pp. 1101-1109
    • Faldt, J.1    Dahlgren, C.2    Ridell, M.3    Karlsson, A.4
  • 11
    • 40949164333 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis-induced apoptotic neutrophils trigger a pro-inflammatory response in macrophages through release of heat shock protein 72, acting in synergy with the bacteria
    • Persson Y.A., Blomgran-Julinder R., Rahman S., Zheng L., and Stendahl O. Mycobacterium tuberculosis-induced apoptotic neutrophils trigger a pro-inflammatory response in macrophages through release of heat shock protein 72, acting in synergy with the bacteria. Microbes Infect 10 (2008) 233-240
    • (2008) Microbes Infect , vol.10 , pp. 233-240
    • Persson, Y.A.1    Blomgran-Julinder, R.2    Rahman, S.3    Zheng, L.4    Stendahl, O.5
  • 12
    • 34247849157 scopus 로고    scopus 로고
    • Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization
    • Blomgran R., Zheng L., and Stendahl O. Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization. J Leukoc Biol 81 (2007) 1213-1223
    • (2007) J Leukoc Biol , vol.81 , pp. 1213-1223
    • Blomgran, R.1    Zheng, L.2    Stendahl, O.3
  • 13
    • 0032212160 scopus 로고    scopus 로고
    • Fusion of azurophil granules with phagosomes and activation of the tyrosine kinase Hck are specifically inhibited during phagocytosis of mycobacteria by human neutrophils
    • N'Diaye E.N., Darzacq X., Astarie-Dequeker C., Daffe M., Calafat J., and Maridonneau-Parini I. Fusion of azurophil granules with phagosomes and activation of the tyrosine kinase Hck are specifically inhibited during phagocytosis of mycobacteria by human neutrophils. J Immunol 161 (1998) 4983-4991
    • (1998) J Immunol , vol.161 , pp. 4983-4991
    • N'Diaye, E.N.1    Darzacq, X.2    Astarie-Dequeker, C.3    Daffe, M.4    Calafat, J.5    Maridonneau-Parini, I.6
  • 14
    • 0037087512 scopus 로고    scopus 로고
    • Rab5a GTPase regulates fusion between pathogen-containing phagosomes and cytoplasmic organelles in human neutrophils
    • Perskvist N., Roberg K., Kulyte A., and Stendahl O. Rab5a GTPase regulates fusion between pathogen-containing phagosomes and cytoplasmic organelles in human neutrophils. J Cell Sci 115 (2002) 1321-1330
    • (2002) J Cell Sci , vol.115 , pp. 1321-1330
    • Perskvist, N.1    Roberg, K.2    Kulyte, A.3    Stendahl, O.4
  • 15
    • 0029793103 scopus 로고    scopus 로고
    • Salmonella typhimurium invasion induces apoptosis in infected macrophages
    • Monack D.M., Raupach B., Hromockyj A.E., and Falkow S. Salmonella typhimurium invasion induces apoptosis in infected macrophages. Proc Natl Acad Sci U S A 93 (1996) 9833-9838
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9833-9838
    • Monack, D.M.1    Raupach, B.2    Hromockyj, A.E.3    Falkow, S.4
  • 16
    • 0346100665 scopus 로고    scopus 로고
    • Differential effects of invasion by and phagocytosis of Salmonella typhimurium on apoptosis in human macrophages: potential role of Rho-GTPases and Akt
    • Forsberg M., Blomgran R., Lerm M., Sarndahl E., Sebti S.M., Hamilton A., et al. Differential effects of invasion by and phagocytosis of Salmonella typhimurium on apoptosis in human macrophages: potential role of Rho-GTPases and Akt. J Leukoc Biol 74 (2003) 620-629
    • (2003) J Leukoc Biol , vol.74 , pp. 620-629
    • Forsberg, M.1    Blomgran, R.2    Lerm, M.3    Sarndahl, E.4    Sebti, S.M.5    Hamilton, A.6
  • 17
    • 0037097677 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis promotes apoptosis in human neutrophils by activating caspase-3 and altering expression of Bax/Bcl-xL via an oxygen-dependent pathway
    • Perskvist N., Long M., Stendahl O., and Zheng L. Mycobacterium tuberculosis promotes apoptosis in human neutrophils by activating caspase-3 and altering expression of Bax/Bcl-xL via an oxygen-dependent pathway. J Immunol 168 (2002) 6358-6365
    • (2002) J Immunol , vol.168 , pp. 6358-6365
    • Perskvist, N.1    Long, M.2    Stendahl, O.3    Zheng, L.4
  • 18
    • 0035423453 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 19-kDa lipoprotein promotes neutrophil activation
    • Neufert C., Pai R.K., Noss E.H., Berger M., Boom W.H., and Harding C.V. Mycobacterium tuberculosis 19-kDa lipoprotein promotes neutrophil activation. J Immunol 167 (2001) 1542-1549
    • (2001) J Immunol , vol.167 , pp. 1542-1549
    • Neufert, C.1    Pai, R.K.2    Noss, E.H.3    Berger, M.4    Boom, W.H.5    Harding, C.V.6
  • 19
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.G., et al. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 130 (2007) 1071-1082
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5    Paik, S.G.6
  • 20
    • 0032478798 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent and -independent intracellular signal transduction pathways leading to apoptosis in human neutrophils
    • Frasch S.C., Nick J.A., Fadok V.A., Bratton D.L., Worthen G.S., and Henson P.M. p38 mitogen-activated protein kinase-dependent and -independent intracellular signal transduction pathways leading to apoptosis in human neutrophils. J Biol Chem 273 (1998) 8389-8397
    • (1998) J Biol Chem , vol.273 , pp. 8389-8397
    • Frasch, S.C.1    Nick, J.A.2    Fadok, V.A.3    Bratton, D.L.4    Worthen, G.S.5    Henson, P.M.6
  • 21
    • 0034468736 scopus 로고    scopus 로고
    • Role of reactive oxygen species (ROS) in apoptosis induction
    • Simon H.U., Haj-Yehia A., and Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis 5 (2000) 415-418
    • (2000) Apoptosis , vol.5 , pp. 415-418
    • Simon, H.U.1    Haj-Yehia, A.2    Levi-Schaffer, F.3
  • 23
    • 0033436344 scopus 로고    scopus 로고
    • Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative stress
    • Roberg K., Johansson U., and Ollinger K. Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative stress. Free Radic Biol Med 27 (1999) 1228-1237
    • (1999) Free Radic Biol Med , vol.27 , pp. 1228-1237
    • Roberg, K.1    Johansson, U.2    Ollinger, K.3
  • 24
    • 0034090797 scopus 로고    scopus 로고
    • Rapid neutrophil response controls fast-replicating intracellular bacteria but not slow-replicating Mycobacterium tuberculosis
    • Seiler P., Aichele P., Raupach B., Odermatt B., Steinhoff U., and Kaufmann S.H. Rapid neutrophil response controls fast-replicating intracellular bacteria but not slow-replicating Mycobacterium tuberculosis. J Infect Dis 181 (2000) 671-680
    • (2000) J Infect Dis , vol.181 , pp. 671-680
    • Seiler, P.1    Aichele, P.2    Raupach, B.3    Odermatt, B.4    Steinhoff, U.5    Kaufmann, S.H.6
  • 25
    • 0031803096 scopus 로고    scopus 로고
    • Roles of calcium and annexins in phagocytosis and elimination of an attenuated strain of Mycobacterium tuberculosis in human neutrophils
    • Majeed M., Perskvist N., Ernst J.D., Orselius K., and Stendahl O. Roles of calcium and annexins in phagocytosis and elimination of an attenuated strain of Mycobacterium tuberculosis in human neutrophils. Microb Pathog 24 (1998) 309-320
    • (1998) Microb Pathog , vol.24 , pp. 309-320
    • Majeed, M.1    Perskvist, N.2    Ernst, J.D.3    Orselius, K.4    Stendahl, O.5
  • 26
    • 0023191983 scopus 로고
    • Evidence for activation of a respiratory burst in the interaction of human neutrophils with Mycobacterium tuberculosis
    • May M.E., and Spagnuolo P.J. Evidence for activation of a respiratory burst in the interaction of human neutrophils with Mycobacterium tuberculosis. Infect Immun 55 (1987) 2304-2307
    • (1987) Infect Immun , vol.55 , pp. 2304-2307
    • May, M.E.1    Spagnuolo, P.J.2
  • 27
    • 0034650439 scopus 로고    scopus 로고
    • Activation of human neutrophils by Mycobacterium tuberculosis H37Ra involves phospholipase C gamma 2, Shc adapter protein, and p38 mitogen-activated protein kinase
    • Perskvist N., Zheng L., and Stendahl O. Activation of human neutrophils by Mycobacterium tuberculosis H37Ra involves phospholipase C gamma 2, Shc adapter protein, and p38 mitogen-activated protein kinase. J Immunol 164 (2000) 959-965
    • (2000) J Immunol , vol.164 , pp. 959-965
    • Perskvist, N.1    Zheng, L.2    Stendahl, O.3
  • 28
    • 0036070607 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha stimulates killing of Mycobacterium tuberculosis by human neutrophils
    • Kisich K.O., Higgins M., Diamond G., and Heifets L. Tumor necrosis factor alpha stimulates killing of Mycobacterium tuberculosis by human neutrophils. Infect Immun 70 (2002) 4591-4599
    • (2002) Infect Immun , vol.70 , pp. 4591-4599
    • Kisich, K.O.1    Higgins, M.2    Diamond, G.3    Heifets, L.4
  • 29
    • 0025118297 scopus 로고
    • Killing of Mycobacterium tuberculosis by neutrophils: a nonoxidative process
    • Jones G.S., Amirault H.J., and Andersen B.R. Killing of Mycobacterium tuberculosis by neutrophils: a nonoxidative process. J Infect Dis 162 (1990) 700-704
    • (1990) J Infect Dis , vol.162 , pp. 700-704
    • Jones, G.S.1    Amirault, H.J.2    Andersen, B.R.3
  • 30
    • 0242350932 scopus 로고    scopus 로고
    • Early granuloma formation after aerosol Mycobacterium tuberculosis infection is regulated by neutrophils via CXCR3-signaling chemokines
    • Seiler P., Aichele P., Bandermann S., Hauser A.E., Lu B., Gerard N.P., et al. Early granuloma formation after aerosol Mycobacterium tuberculosis infection is regulated by neutrophils via CXCR3-signaling chemokines. Eur J Immunol 33 (2003) 2676-2686
    • (2003) Eur J Immunol , vol.33 , pp. 2676-2686
    • Seiler, P.1    Aichele, P.2    Bandermann, S.3    Hauser, A.E.4    Lu, B.5    Gerard, N.P.6
  • 31
    • 4544371275 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis triggers apoptosis in peripheral neutrophils involving toll-like receptor 2 and p38 mitogen protein kinase in tuberculosis patients
    • Aleman M., Schierloh P., de la Barrera S.S., Musella R.M., Saab M.A., Baldini M., et al. Mycobacterium tuberculosis triggers apoptosis in peripheral neutrophils involving toll-like receptor 2 and p38 mitogen protein kinase in tuberculosis patients. Infect Immun 72 (2004) 5150-5158
    • (2004) Infect Immun , vol.72 , pp. 5150-5158
    • Aleman, M.1    Schierloh, P.2    de la Barrera, S.S.3    Musella, R.M.4    Saab, M.A.5    Baldini, M.6
  • 32
    • 37749047802 scopus 로고    scopus 로고
    • Bystander macrophage apoptosis after Mycobacterium tuberculosis H37Ra infection
    • Kelly D.M., ten Bokum A.M., O'Leary S.M., O'Sullivan M.P., and Keane J. Bystander macrophage apoptosis after Mycobacterium tuberculosis H37Ra infection. Infect Immun 76 (2008) 351-360
    • (2008) Infect Immun , vol.76 , pp. 351-360
    • Kelly, D.M.1    ten Bokum, A.M.2    O'Leary, S.M.3    O'Sullivan, M.P.4    Keane, J.5
  • 33
    • 0035898449 scopus 로고    scopus 로고
    • Constitutively activated Akt-1 is vital for the survival of human monocyte-differentiated macrophages. Role of Mcl-1, independent of nuclear factor (NF)-kappaB, Bad, or caspase activation
    • Liu H., Perlman H., Pagliari L.J., and Pope R.M. Constitutively activated Akt-1 is vital for the survival of human monocyte-differentiated macrophages. Role of Mcl-1, independent of nuclear factor (NF)-kappaB, Bad, or caspase activation. J Exp Med 194 (2001) 113-126
    • (2001) J Exp Med , vol.194 , pp. 113-126
    • Liu, H.1    Perlman, H.2    Pagliari, L.J.3    Pope, R.M.4
  • 34
    • 0032189381 scopus 로고    scopus 로고
    • Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation
    • Coffer P.J., Jin J., and Woodgett J.R. Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochem J 335 Pt 1 (1998) 1-13
    • (1998) Biochem J , vol.335 , Issue.PART 1 , pp. 1-13
    • Coffer, P.J.1    Jin, J.2    Woodgett, J.R.3
  • 35
    • 0041707781 scopus 로고    scopus 로고
    • Elucidation of molecular events leading to neutrophil apoptosis following phagocytosis: cross-talk between caspase 8, reactive oxygen species, and MAPK/ERK activation
    • Zhang B., Hirahashi J., Cullere X., and Mayadas T.N. Elucidation of molecular events leading to neutrophil apoptosis following phagocytosis: cross-talk between caspase 8, reactive oxygen species, and MAPK/ERK activation. J Biol Chem 278 (2003) 28443-28454
    • (2003) J Biol Chem , vol.278 , pp. 28443-28454
    • Zhang, B.1    Hirahashi, J.2    Cullere, X.3    Mayadas, T.N.4
  • 36
    • 0032189802 scopus 로고    scopus 로고
    • Mcl-1 expression in human neutrophils: regulation by cytokines and correlation with cell survival
    • Moulding D.A., Quayle J.A., Hart C.A., and Edwards S.W. Mcl-1 expression in human neutrophils: regulation by cytokines and correlation with cell survival. Blood 92 (1998) 2495-2502
    • (1998) Blood , vol.92 , pp. 2495-2502
    • Moulding, D.A.1    Quayle, J.A.2    Hart, C.A.3    Edwards, S.W.4
  • 37
    • 33846065301 scopus 로고    scopus 로고
    • Involvement of p38 MAP kinase in not only activation of the phagocyte NADPH oxidase induced by formyl-methionyl-leucyl-phenylalanine but also determination of the extent of the activity
    • Sakamoto K., Kuribayashi F., Nakamura M., and Takeshige K. Involvement of p38 MAP kinase in not only activation of the phagocyte NADPH oxidase induced by formyl-methionyl-leucyl-phenylalanine but also determination of the extent of the activity. J Biochem 140 (2006) 739-745
    • (2006) J Biochem , vol.140 , pp. 739-745
    • Sakamoto, K.1    Kuribayashi, F.2    Nakamura, M.3    Takeshige, K.4
  • 38
    • 0029890991 scopus 로고    scopus 로고
    • Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation
    • Zu Y.L., Ai Y., Gilchrist A., Labadia M.E., Sha'afi R.I., and Huang C.K. Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation. Blood 87 (1996) 5287-5296
    • (1996) Blood , vol.87 , pp. 5287-5296
    • Zu, Y.L.1    Ai, Y.2    Gilchrist, A.3    Labadia, M.E.4    Sha'afi, R.I.5    Huang, C.K.6
  • 39
    • 0029101644 scopus 로고
    • Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death
    • Zamzami N., Marchetti P., Castedo M., Decaudin D., Macho A., Hirsch T., et al. Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death. J Exp Med 182 (1995) 367-377
    • (1995) J Exp Med , vol.182 , pp. 367-377
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Decaudin, D.4    Macho, A.5    Hirsch, T.6
  • 40
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., and Reed J.C. Mitochondrial control of cell death. Nat Med 6 (2000) 513-519
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 41
    • 0344643405 scopus 로고    scopus 로고
    • The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through Toll-like receptor-2
    • Lopez M., Sly L.M., Luu Y., Young D., Cooper H., and Reiner N.E. The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through Toll-like receptor-2. J Immunol 170 (2003) 2409-2416
    • (2003) J Immunol , vol.170 , pp. 2409-2416
    • Lopez, M.1    Sly, L.M.2    Luu, Y.3    Young, D.4    Cooper, H.5    Reiner, N.E.6
  • 42
    • 34848910546 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis infects dendritic cells with high frequency and impairs their function in vivo
    • Wolf A.J., Linas B., Trevejo-Nunez G.J., Kincaid E., Tamura T., Takatsu K., et al. Mycobacterium tuberculosis infects dendritic cells with high frequency and impairs their function in vivo. J Immunol 179 (2007) 2509-2519
    • (2007) J Immunol , vol.179 , pp. 2509-2519
    • Wolf, A.J.1    Linas, B.2    Trevejo-Nunez, G.J.3    Kincaid, E.4    Tamura, T.5    Takatsu, K.6
  • 43
    • 23944508045 scopus 로고    scopus 로고
    • Neutrophils rapidly migrate via lymphatics after Mycobacterium bovis BCG intradermal vaccination and shuttle live bacilli to the draining lymph nodes
    • Abadie V., Badell E., Douillard P., Ensergueix D., Leenen P.J., Tanguy M., et al. Neutrophils rapidly migrate via lymphatics after Mycobacterium bovis BCG intradermal vaccination and shuttle live bacilli to the draining lymph nodes. Blood 106 (2005) 1843-1850
    • (2005) Blood , vol.106 , pp. 1843-1850
    • Abadie, V.1    Badell, E.2    Douillard, P.3    Ensergueix, D.4    Leenen, P.J.5    Tanguy, M.6
  • 44
    • 58149083837 scopus 로고    scopus 로고
    • The role of the granuloma in expansion and dissemination of early tuberculous infection
    • Davis J.M., and Ramakrishnan L. The role of the granuloma in expansion and dissemination of early tuberculous infection. Cell 136 (2009) 37-49
    • (2009) Cell , vol.136 , pp. 37-49
    • Davis, J.M.1    Ramakrishnan, L.2
  • 46
    • 0017379182 scopus 로고
    • Phagocytic internalization and the requirement for membrane perturbation
    • Stendahl O., Hed J., Kihlstrom E., Magnusson K.E., and Tagesson C. Phagocytic internalization and the requirement for membrane perturbation. FEBS Lett 81 (1977) 118-120
    • (1977) FEBS Lett , vol.81 , pp. 118-120
    • Stendahl, O.1    Hed, J.2    Kihlstrom, E.3    Magnusson, K.E.4    Tagesson, C.5
  • 47
    • 0034711474 scopus 로고    scopus 로고
    • Protection against oxidant-mediated lysosomal rupture: a new anti-apoptotic activity of Bcl-2?
    • Zhao M., Eaton J.W., and Brunk U.T. Protection against oxidant-mediated lysosomal rupture: a new anti-apoptotic activity of Bcl-2?. FEBS Lett 485 (2000) 104-108
    • (2000) FEBS Lett , vol.485 , pp. 104-108
    • Zhao, M.1    Eaton, J.W.2    Brunk, U.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.