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Volumn 81, Issue 3, 2013, Pages 764-776

Mycobacterial trehalose dimycolate reprograms macrophage global gene expression and activates matrix metalloproteinases

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE 3; CORD FACTOR; CXCL1 CHEMOKINE; CXCL2 CHEMOKINE; GAMMA INTERFERON INDUCIBLE PROTEIN 10; GELATINASE B; INTERLEUKIN 1BETA; MACROPHAGE ELASTASE; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MACROPHAGE INFLAMMATORY PROTEIN 1BETA; MATRIX METALLOPROTEINASE; MONOCYTE CHEMOTACTIC PROTEIN 3; MONOCYTE CHEMOTACTIC PROTEIN 5; MYELOID DIFFERENTIATION FACTOR 88; NEUTROPHIL COLLAGENASE; TOLL LIKE RECEPTOR;

EID: 84874748904     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00906-12     Document Type: Article
Times cited : (37)

References (77)
  • 1
    • 0003514452 scopus 로고    scopus 로고
    • Global tuberculosis control. World Health Organization, Geneva, Switzerland
    • World Health Organization. 2011. Global tuberculosis control. World Health Organization, Geneva, Switzerland.
    • (2011) World Health Organization
  • 3
    • 77952409525 scopus 로고    scopus 로고
    • Epizootiologic survey of Mycobacterium bovis in wildlife and farm environments in northern Michigan
    • Witmer G, Fine AE, Gionfriddo J, Pipas M, Shively K, Piccolo K, Burke P. 2010. Epizootiologic survey of Mycobacterium bovis in wildlife and farm environments in northern Michigan. J. Wildl. Dis. 46:368-378.
    • (2010) J. Wildl. Dis. , vol.46 , pp. 368-378
    • Witmer, G.1    Fine, A.E.2    Gionfriddo, J.3    Pipas, M.4    Shively, K.5    Piccolo, K.6    Burke, P.7
  • 4
    • 0014348458 scopus 로고
    • Acute granulomatous response produced in mice by trehalose-6,6-dimycolate
    • Bekierkunst A. 1968. Acute granulomatous response produced in mice by trehalose-6,6-dimycolate. J. Bacteriol. 96:958-961.
    • (1968) J. Bacteriol. , vol.96 , pp. 958-961
    • Bekierkunst, A.1
  • 6
    • 0019777228 scopus 로고
    • The role of surface in the biological activities of trehalose 6,6=-dimycolate surface properties and development of a model system
    • Retzinger GS, Meredith SC, Takayama K, Hunter RL, Kezdy FJ. 1981. The role of surface in the biological activities of trehalose 6,6=-dimycolate. Surface properties and development of a model system. J. Biol. Chem. 256:8208-8216.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8208-8216
    • Retzinger, G.S.1    Meredith, S.C.2    Takayama, K.3    Hunter, R.L.4    Kezdy, F.J.5
  • 7
    • 17844390099 scopus 로고    scopus 로고
    • Cell wall lipids from Mycobacterium bovis BCG are inflammatory when inoculated within a gel matrix: characterization of a new model of the granulomatous response to mycobacterial components
    • Rhoades ER, Geisel RE, Butcher BA, McDonough S, Russell DG. 2005. Cell wall lipids from Mycobacterium bovis BCG are inflammatory when inoculated within a gel matrix: characterization of a new model of the granulomatous response to mycobacterial components. Tuberculosis (Edinb.) 85:159-176.
    • (2005) Tuberculosis (Edinb.) , vol.85 , pp. 159-176
    • Rhoades, E.R.1    Geisel, R.E.2    Butcher, B.A.3    McDonough, S.4    Russell, D.G.5
  • 8
    • 17044368380 scopus 로고    scopus 로고
    • In vivo activity of released cell wall lipids of Mycobacterium bovis bacillus Calmette- Guerin is due principally to trehalose mycolates
    • Geisel RE, Sakamoto K, Russell DG, Rhoades ER. 2005. In vivo activity of released cell wall lipids of Mycobacterium bovis bacillus Calmette- Guerin is due principally to trehalose mycolates. J. Immunol. 174:5007-5015.
    • (2005) J. Immunol. , vol.174 , pp. 5007-5015
    • Geisel, R.E.1    Sakamoto, K.2    Russell, D.G.3    Rhoades, E.R.4
  • 10
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL, Lopez-Boado YS. 2004. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat. Rev. 4:617-629.
    • (2004) Nat. Rev. , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 11
    • 0037942829 scopus 로고    scopus 로고
    • Differential regulation of lipopolysaccharide-induced monocyte matrix metalloproteinase (MMP)-1 and MMP-9 by p38 and extracellular signal-regulated kinase 1/2 mitogen-activated protein kinases
    • Lai WC, Zhou M, Shankavaram U, Peng G, Wahl LM. 2003. Differential regulation of lipopolysaccharide-induced monocyte matrix metalloproteinase (MMP)-1 and MMP-9 by p38 and extracellular signal-regulated kinase 1/2 mitogen-activated protein kinases. J. Immunol. 170:6244-6249.
    • (2003) J. Immunol. , vol.170 , pp. 6244-6249
    • Lai, W.C.1    Zhou, M.2    Shankavaram, U.3    Peng, G.4    Wahl, L.M.5
  • 12
    • 0025025442 scopus 로고
    • The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. 1990. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. U. S. A. 87:5578-5582.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 5578-5582
    • van Wart, H.E.1    Birkedal-Hansen, H.2
  • 13
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G. 2006. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 69:562-573.
    • (2006) Cardiovasc. Res. , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 14
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry
    • Visse R, Nagase H. 2003. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 92:827-839.
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 15
    • 0033569725 scopus 로고    scopus 로고
    • Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization
    • Barmina OY, Walling HW, Fiacco GJ, Freije JM, Lopez-Otin C, Jeffrey JJ, Partridge NC. 1999. Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization. J. Biol. Chem. 274:30087-30093.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30087-30093
    • Barmina, O.Y.1    Walling, H.W.2    Fiacco, G.J.3    Freije, J.M.4    Lopez-Otin, C.5    Jeffrey, J.J.6    Partridge, N.C.7
  • 16
    • 0042093741 scopus 로고    scopus 로고
    • Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation
    • Fu X, Kassim SY, Parks WC, Heinecke JW. 2003. Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation. J. Biol. Chem. 278:28403-28409.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28403-28409
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 17
    • 0033803609 scopus 로고    scopus 로고
    • Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis
    • Rivera-Marrero CA, Schuyler W, Roser S, Roman J. 2000. Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis. Microb. Pathog. 29: 231-244.
    • (2000) Microb. Pathog. , vol.29 , pp. 231-244
    • Rivera-Marrero, C.A.1    Schuyler, W.2    Roser, S.3    Roman, J.4
  • 18
    • 0034861026 scopus 로고    scopus 로고
    • Production of matrix metalloproteinases in response to mycobacterial infection
    • Quiding-Jarbrink M, Smith DA, Bancroft GJ. 2001. Production of matrix metalloproteinases in response to mycobacterial infection. Infect. Immun. 69:5661-5670.
    • (2001) Infect. Immun. , vol.69 , pp. 5661-5670
    • Quiding-Jarbrink, M.1    Smith, D.A.2    Bancroft, G.J.3
  • 19
    • 0029926416 scopus 로고    scopus 로고
    • Effect of Mycobacterium tuberculosis and its components on macrophages and the release of matrix metalloproteinases
    • Chang JC, Wysocki A, Tchou-Wong KM, Moskowitz N, Zhang Y, Rom WN. 1996. Effect of Mycobacterium tuberculosis and its components on macrophages and the release of matrix metalloproteinases. Thorax 51: 306-311.
    • (1996) Thorax , vol.51 , pp. 306-311
    • Chang, J.C.1    Wysocki, A.2    Tchou-Wong, K.M.3    Moskowitz, N.4    Zhang, Y.5    Rom, W.N.6
  • 21
    • 17844408723 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-9 in pleural effusions of tuberculosis and lung cancer
    • Park KJ, Hwang SC, Sheen SS, Oh YJ, Han JH, Lee KB. 2005. Expression of matrix metalloproteinase-9 in pleural effusions of tuberculosis and lung cancer. Respiration 72:166-175.
    • (2005) Respiration , vol.72 , pp. 166-175
    • Park, K.J.1    Hwang, S.C.2    Sheen, S.S.3    Oh, Y.J.4    Han, J.H.5    Lee, K.B.6
  • 24
    • 0035992397 scopus 로고    scopus 로고
    • Circulation level of matrix metalloproteinase-9 is correlated with disease severity in tuberculosis patients
    • Hrabec E, Strek M, Zieba M, Kwiatkowska S, Hrabec Z. 2002. Circulation level of matrix metalloproteinase-9 is correlated with disease severity in tuberculosis patients. Int. J. Tuberc. Lung Dis. 6:713-719.
    • (2002) Int. J. Tuberc. Lung Dis. , vol.6 , pp. 713-719
    • Hrabec, E.1    Strek, M.2    Zieba, M.3    Kwiatkowska, S.4    Hrabec, Z.5
  • 25
    • 75649141266 scopus 로고    scopus 로고
    • Tuberculous granuloma induction via interaction of a bacterial secreted protein with host epithelium
    • Volkman HE, Pozos TC, Zheng J, Davis JM, Rawls JF, Ramakrishnan L. 2010. Tuberculous granuloma induction via interaction of a bacterial secreted protein with host epithelium. Science 327:466-469.
    • (2010) Science , vol.327 , pp. 466-469
    • Volkman, H.E.1    Pozos, T.C.2    Zheng, J.3    Davis, J.M.4    Rawls, J.F.5    Ramakrishnan, L.6
  • 26
    • 0016529811 scopus 로고
    • Site of inhibitory action of isoniazid in the synthesis of mycolic acids in Mycobacterium tuberculosis
    • Takayama K, Schnoes HK, Armstrong EL, Boyle RW. 1975. Site of inhibitory action of isoniazid in the synthesis of mycolic acids in Mycobacterium tuberculosis. J. Lipid Res. 16:308-317.
    • (1975) J. Lipid Res. , vol.16 , pp. 308-317
    • Takayama, K.1    Schnoes, H.K.2    Armstrong, E.L.3    Boyle, R.W.4
  • 27
    • 0038354913 scopus 로고    scopus 로고
    • Identification and macrophage-activating activity of glycolipids released from intracellular Mycobacterium bovis BCG
    • Rhoades E, Hsu F, Torrelles JB, Turk J, Chatterjee D, Russell DG. 2003. Identification and macrophage-activating activity of glycolipids released from intracellular Mycobacterium bovis BCG. Mol. Microbiol. 48:875-888.
    • (2003) Mol. Microbiol. , vol.48 , pp. 875-888
    • Rhoades, E.1    Hsu, F.2    Torrelles, J.B.3    Turk, J.4    Chatterjee, D.5    Russell, D.G.6
  • 28
    • 0035423403 scopus 로고    scopus 로고
    • Essential role of neutrophils in the initiation and progression of a murine model of rheumatoid arthritis
    • Wipke BT, Allen PM. 2001. Essential role of neutrophils in the initiation and progression of a murine model of rheumatoid arthritis. J. Immunol. 167:1601-1608.
    • (2001) J. Immunol. , vol.167 , pp. 1601-1608
    • Wipke, B.T.1    Allen, P.M.2
  • 29
    • 81455135824 scopus 로고    scopus 로고
    • Ly6G+ neutrophils are dispensable for defense against systemic Listeria monocytogenes infection
    • Shi C, Hohl TM, Leiner I, Equinda MJ, Fan X, Pamer EG. 2011. Ly6G+ neutrophils are dispensable for defense against systemic Listeria monocytogenes infection. J. Immunol. 187:5293-5298.
    • (2011) J. Immunol. , vol.187 , pp. 5293-5298
    • Shi, C.1    Hohl, T.M.2    Leiner, I.3    Equinda, M.J.4    Fan, X.5    Pamer, E.G.6
  • 30
    • 67650904929 scopus 로고    scopus 로고
    • MARCO, TLR2, and CD14 are required for macrophage cytokine responses to mycobacterial trehalose dimycolate and Mycobacterium tuberculosis
    • doi:10.1371/journal.ppat.1000474
    • Bowdish DM, Sakamoto K, Kim MJ, Kroos M, Mukhopadhyay S, Leifer CA, Tryggvason K, Gordon S, Russell DG. 2009. MARCO, TLR2, and CD14 are required for macrophage cytokine responses to mycobacterial trehalose dimycolate and Mycobacterium tuberculosis. PLoS Pathog. 5:e1000474. doi:10.1371/journal.ppat.1000474.
    • (2009) PLoS Pathog. , vol.5
    • Bowdish, D.M.1    Sakamoto, K.2    Kim, M.J.3    Kroos, M.4    Mukhopadhyay, S.5    Leifer, C.A.6    Tryggvason, K.7    Gordon, S.8    Russell, D.G.9
  • 31
    • 14144250943 scopus 로고    scopus 로고
    • Effects of TNF-alpha and curcumin on the expression of thrombomodulin and endothelial protein C receptor in human endothelial cells
    • Nan B, Lin P, Lumsden AB, Yao Q, Chen C. 2005. Effects of TNF-alpha and curcumin on the expression of thrombomodulin and endothelial protein C receptor in human endothelial cells. Thromb. Res. 115:417-426.
    • (2005) Thromb. Res. , vol.115 , pp. 417-426
    • Nan, B.1    Lin, P.2    Lumsden, A.B.3    Yao, Q.4    Chen, C.5
  • 35
    • 0038308879 scopus 로고    scopus 로고
    • BCG promotes cord blood monocytederived dendritic cell maturation with nuclear Rel-B up-regulation and cytosolic I kappa B alpha and beta degradation
    • Liu E, Law HK, Lau YL. 2003. BCG promotes cord blood monocytederived dendritic cell maturation with nuclear Rel-B up-regulation and cytosolic I kappa B alpha and beta degradation. Pediatr. Res. 54:105-112.
    • (2003) Pediatr. Res. , vol.54 , pp. 105-112
    • Liu, E.1    Law, H.K.2    Lau, Y.L.3
  • 36
    • 70149086706 scopus 로고    scopus 로고
    • Aberrant TGF-beta signaling reduces T regulatory cells in ICAM-1-deficient mice, increasing the inflammatory response to Mycobacterium tuberculosis
    • Windish HP, Lin PL, Mattila JT, Green AM, Onuoha EO, Kane LP, Flynn JL. 2009. Aberrant TGF-beta signaling reduces T regulatory cells in ICAM-1-deficient mice, increasing the inflammatory response to Mycobacterium tuberculosis. J. Leukoc. Biol. 86:713-725.
    • (2009) J. Leukoc. Biol. , vol.86 , pp. 713-725
    • Windish, H.P.1    Lin, P.L.2    Mattila, J.T.3    Green, A.M.4    Onuoha, E.O.5    Kane, L.P.6    Flynn, J.L.7
  • 41
    • 0017237070 scopus 로고
    • Delayed hypersensitivity and granulomatous response after immunization with protein antigens associated with a mycobacterial glycolipid and oil droplets
    • Granger DL, Yamamoto KI, Ribi E. 1976. Delayed hypersensitivity and granulomatous response after immunization with protein antigens associated with a mycobacterial glycolipid and oil droplets. J. Immunol. 116: 482-488.
    • (1976) J. Immunol. , vol.116 , pp. 482-488
    • Granger, D.L.1    Yamamoto, K.I.2    Ribi, E.3
  • 42
    • 0017377972 scopus 로고
    • Adjuvanticity (immunity-inducing property) of cord factor in mice and rats
    • Saito R, Nagao S, Takamoto M, Sugiyama K, Tanaka A. 1977. Adjuvanticity (immunity-inducing property) of cord factor in mice and rats. Infect. Immun. 16:725-729.
    • (1977) Infect. Immun. , vol.16 , pp. 725-729
    • Saito, R.1    Nagao, S.2    Takamoto, M.3    Sugiyama, K.4    Tanaka, A.5
  • 44
    • 0017090165 scopus 로고
    • Nonspecific resistance against infection with Salmonella typhi and Salmonella typhimurium induced in mice by cord factor (trehalose-6,6=-dimycolate) and its analogues
    • Yarkoni E, Bekierkunst A. 1976. Nonspecific resistance against infection with Salmonella typhi and Salmonella typhimurium induced in mice by cord factor (trehalose-6,6=-dimycolate) and its analogues. Infect. Immun. 14:1125-1129.
    • (1976) Infect. Immun. , vol.14 , pp. 1125-1129
    • Yarkoni, E.1    Bekierkunst, A.2
  • 46
    • 0028880604 scopus 로고
    • Role of trehalose dimycolate-induced interferon- alpha/beta in the restriction of encephalomyocarditis virus growth in vivo and in peritoneal macrophage cultures
    • Guillemard E, Geniteau-Legendre M, Kergot R, Lemaire G, Petit JF, Labarre C, Quero AM. 1995. Role of trehalose dimycolate-induced interferon- alpha/beta in the restriction of encephalomyocarditis virus growth in vivo and in peritoneal macrophage cultures. Antiviral Res. 28: 175-189.
    • (1995) Antiviral Res. , vol.28 , pp. 175-189
    • Guillemard, E.1    Geniteau-Legendre, M.2    Kergot, R.3    Lemaire, G.4    Petit, J.F.5    Labarre, C.6    Quero, A.M.7
  • 47
    • 0021320102 scopus 로고
    • Macrophage activation by cord factor (trehalose 6,6=-dimycolate): enhanced association with and intracellular killing of Trypanosoma cruzi
    • Kierszenbaum F, Zenian A, Wirth JJ. 1984. Macrophage activation by cord factor (trehalose 6,6=-dimycolate): enhanced association with and intracellular killing of Trypanosoma cruzi. Infect. Immun. 43:531-535.
    • (1984) Infect. Immun. , vol.43 , pp. 531-535
    • Kierszenbaum, F.1    Zenian, A.2    Wirth, J.J.3
  • 48
    • 0018606677 scopus 로고
    • Protection of mice against Babesia microti with cord factor, COAM, zymosan, glucan, Salmonella and Listeria
    • Clark IA. 1979. Protection of mice against Babesia microti with cord factor, COAM, zymosan, glucan, Salmonella and Listeria. Parasite Immunol. 1:179-196.
    • (1979) Parasite Immunol. , vol.1 , pp. 179-196
    • Clark, I.A.1
  • 49
    • 0022387448 scopus 로고
    • Trehalose dimycolate from various mycobacterial species induces differing antiinfectious activities in combination with muramyl dipeptide
    • Masihi KN, Brehmer W, Lange W, Werner H, Ribi E. 1985. Trehalose dimycolate from various mycobacterial species induces differing antiinfectious activities in combination with muramyl dipeptide. Infect. Immun. 50:938-940.
    • (1985) Infect. Immun. , vol.50 , pp. 938-940
    • Masihi, K.N.1    Brehmer, W.2    Lange, W.3    Werner, H.4    Ribi, E.5
  • 54
    • 0027254436 scopus 로고
    • Induction of pulmonary granulomas, macrophage procoagulant activity, and tumor necrosis factor-alpha by trehalose glycolipids
    • Behling CA, Perez RL, Kidd MR, Staton GW, Jr, Hunter RL. 1993. Induction of pulmonary granulomas, macrophage procoagulant activity, and tumor necrosis factor-alpha by trehalose glycolipids. Ann. Clin. Lab. Sci. 23:256-266.
    • (1993) Ann. Clin. Lab. Sci. , vol.23 , pp. 256-266
    • Behling, C.A.1    Perez, R.L.2    Kidd, M.R.3    Staton Jr., G.W.4    Hunter, R.L.5
  • 55
    • 0033805739 scopus 로고    scopus 로고
    • Cytokine message and protein expression during lung granuloma formation and resolution induced by the mycobacterial cord factor trehalose-6,6=-dimycolate
    • Perez RL, Roman J, Roser S, Little C, Olsen M, Indrigo J, Hunter RL, Actor JK. 2000. Cytokine message and protein expression during lung granuloma formation and resolution induced by the mycobacterial cord factor trehalose-6,6=-dimycolate. J. Interferon Cytokine Res. 20:795-804.
    • (2000) J. Interferon Cytokine Res. , vol.20 , pp. 795-804
    • Perez, R.L.1    Roman, J.2    Roser, S.3    Little, C.4    Olsen, M.5    Indrigo, J.6    Hunter, R.L.7    Actor, J.K.8
  • 56
    • 0038355221 scopus 로고    scopus 로고
    • Mycobacterial glycolipid cord factor trehalose 6,6=- dimycolate causes a decrease in serum cortisol during the granulomatous response
    • Actor JK, Indrigo J, Beachdel CM, Olsen M, Wells A, Hunter RL, Jr, Dasgupta A. 2002. Mycobacterial glycolipid cord factor trehalose 6,6=- dimycolate causes a decrease in serum cortisol during the granulomatous response. Neuroimmunomodulation 10:270-282.
    • (2002) Neuroimmunomodulation , vol.10 , pp. 270-282
    • Actor, J.K.1    Indrigo, J.2    Beachdel, C.M.3    Olsen, M.4    Wells, A.5    Hunter Jr., R.L.6    Dasgupta, A.7
  • 57
    • 0034119172 scopus 로고    scopus 로고
    • In vivo administration of mycobacterial cord factor (trehalose 6,6=-dimycolate) can induce lung and liver granulomas and thymic atrophy in rabbits
    • Hamasaki N, Isowa K, Kamada K, Terano Y, Matsumoto T, Arakawa T, Kobayashi K, Yano I. 2000. In vivo administration of mycobacterial cord factor (trehalose 6,6=-dimycolate) can induce lung and liver granulomas and thymic atrophy in rabbits. Infect. Immun. 68:3704-3709.
    • (2000) Infect. Immun. , vol.68 , pp. 3704-3709
    • Hamasaki, N.1    Isowa, K.2    Kamada, K.3    Terano, Y.4    Matsumoto, T.5    Arakawa, T.6    Kobayashi, K.7    Yano, I.8
  • 58
    • 0023744140 scopus 로고
    • Tumor necrosis factor (cachectin) mediates induction of cachexia by cord factor from mycobacteria
    • Silva CL, Faccioli LH. 1988. Tumor necrosis factor (cachectin) mediates induction of cachexia by cord factor from mycobacteria. Infect. Immun. 56:3067-3071.
    • (1988) Infect. Immun. , vol.56 , pp. 3067-3071
    • Silva, C.L.1    Faccioli, L.H.2
  • 60
    • 3042713700 scopus 로고    scopus 로고
    • Resistance and susceptibility to tuberculosis analysed at the transcriptome level: lessons from mouse macrophages
    • Keller C, Lauber J, Blumenthal A, Buer J, Ehlers S. 2004. Resistance and susceptibility to tuberculosis analysed at the transcriptome level: lessons from mouse macrophages. Tuberculosis (Edinb.) 84:144-158.
    • (2004) Tuberculosis (Edinb.) , vol.84 , pp. 144-158
    • Keller, C.1    Lauber, J.2    Blumenthal, A.3    Buer, J.4    Ehlers, S.5
  • 63
    • 25444493823 scopus 로고    scopus 로고
    • Mycobacterial lipomannan induces matrix metalloproteinase-9 expression in human macrophagic cells through a Toll-like receptor 1 (TLR1)/TLR2- and CD14-dependent mechanism
    • Elass E, Aubry L, Masson M, Denys A, Guerardel Y, Maes E, Legrand D, Mazurier J, Kremer L. 2005. Mycobacterial lipomannan induces matrix metalloproteinase-9 expression in human macrophagic cells through a Toll-like receptor 1 (TLR1)/TLR2- and CD14-dependent mechanism. Infect. Immun. 73:7064-7068.
    • (2005) Infect. Immun. , vol.73 , pp. 7064-7068
    • Elass, E.1    Aubry, L.2    Masson, M.3    Denys, A.4    Guerardel, Y.5    Maes, E.6    Legrand, D.7    Mazurier, J.8    Kremer, L.9
  • 65
    • 0023779754 scopus 로고
    • Structure and molecular species composition of three homologous series of alpha-mycolic acids from Mycobacterium spp
    • Kaneda K, Imaizumi S, Mizuno S, Baba T, Tsukamura M, Yano I. 1988. Structure and molecular species composition of three homologous series of alpha-mycolic acids from Mycobacterium spp. J. Gen. Microbiol. 134: 2213-2229.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2213-2229
    • Kaneda, K.1    Imaizumi, S.2    Mizuno, S.3    Baba, T.4    Tsukamura, M.5    Yano, I.6
  • 66
    • 33645450141 scopus 로고    scopus 로고
    • Trehalose 6,6=- dimycolate and lipid in the pathogenesis of caseating granulomas of tuberculosis in mice
    • Hunter RL, Olsen M, Jagannath C, Actor JK. 2006. Trehalose 6,6=- dimycolate and lipid in the pathogenesis of caseating granulomas of tuberculosis in mice. Am. J. Pathol. 168:1249-1261.
    • (2006) Am. J. Pathol. , vol.168 , pp. 1249-1261
    • Hunter, R.L.1    Olsen, M.2    Jagannath, C.3    Actor, J.K.4
  • 67
    • 34249850242 scopus 로고    scopus 로고
    • Hairpin extensions enhance the efficacy of mycolyl transferase-specific antisense oligonucleotides targeting Mycobacterium tuberculosis
    • Harth G, Zamecnik PC, Tabatadze D, Pierson K, Horwitz MA. 2007. Hairpin extensions enhance the efficacy of mycolyl transferase-specific antisense oligonucleotides targeting Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 104:7199-7204.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7199-7204
    • Harth, G.1    Zamecnik, P.C.2    Tabatadze, D.3    Pierson, K.4    Horwitz, M.A.5
  • 68
    • 0034602726 scopus 로고    scopus 로고
    • Treatment of Mycobacterium tuberculosis with antisense oligonucleotides to glutamine synthetase mRNA inhibits glutamine synthetase activity, formation of the poly-L-glutamate/glutamine cell wall structure, and bacterial replication
    • Harth G, Zamecnik PC, Tang JY, Tabatadze D, Horwitz MA. 2000. Treatment of Mycobacterium tuberculosis with antisense oligonucleotides to glutamine synthetase mRNA inhibits glutamine synthetase activity, formation of the poly-L-glutamate/glutamine cell wall structure, and bacterial replication. Proc. Natl. Acad. Sci. U. S. A. 97:418-423.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 418-423
    • Harth, G.1    Zamecnik, P.C.2    Tang, J.Y.3    Tabatadze, D.4    Horwitz, M.A.5
  • 70
    • 14244260489 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis controls host innate immune activation through cyclopropane modification of a glycolipid effector molecule
    • Rao V, Fujiwara N, Porcelli SA, Glickman MS. 2005. Mycobacterium tuberculosis controls host innate immune activation through cyclopropane modification of a glycolipid effector molecule. J. Exp. Med. 201:535-543.
    • (2005) J. Exp. Med. , vol.201 , pp. 535-543
    • Rao, V.1    Fujiwara, N.2    Porcelli, S.A.3    Glickman, M.S.4
  • 71
    • 84863815961 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis lacking all mycolic acid cyclopropanation is viable but highly attenuated and hyperinflammatory in mice
    • Barkan D, Hedhli D, Yan HG, Huygen K, Glickman MS. 2012. Mycobacterium tuberculosis lacking all mycolic acid cyclopropanation is viable but highly attenuated and hyperinflammatory in mice. Infect. Immun. 80:1958-1968.
    • (2012) Infect. Immun. , vol.80 , pp. 1958-1968
    • Barkan, D.1    Hedhli, D.2    Yan, H.G.3    Huygen, K.4    Glickman, M.S.5
  • 72
    • 33745217856 scopus 로고    scopus 로고
    • Transcyclopropanation of mycolic acids on trehalose dimycolate suppresses Mycobacterium tuberculosis-induced inflammation and virulence
    • Rao V, Gao F, Chen B, Jacobs WR, Jr, Glickman MS. 2006. Transcyclopropanation of mycolic acids on trehalose dimycolate suppresses Mycobacterium tuberculosis-induced inflammation and virulence. J. Clin. Invest. 116:1660-1667.
    • (2006) J. Clin. Invest. , vol.116 , pp. 1660-1667
    • Rao, V.1    Gao, F.2    Chen, B.3    Jacobs Jr., W.R.4    Glickman, M.S.5
  • 74
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner JF, Jr. 1991. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 75
    • 0033003988 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation
    • Henriet P, Blavier L, Declerck YA. 1999. Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation. APMIS 107:111-119.
    • (1999) APMIS , vol.107 , pp. 111-119
    • Henriet, P.1    Blavier, L.2    Declerck, Y.A.3
  • 76
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. 1997. Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378:151-160.
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.