메뉴 건너뛰기




Volumn 182, Issue 9, 2009, Pages 5865-5872

Matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade

Author keywords

[No Author keywords available]

Indexed keywords

AMINOSALICYLIC ACID; CYCLOOXYGENASE 2; INTERSTITIAL COLLAGENASE; MATRILYSIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PROSTAGLANDIN E2; TISSUE INHIBITOR OF METALLOPROTEINASE 1; MMP1 PROTEIN, HUMAN; MMP7 PROTEIN, HUMAN; TUBERCULOSTATIC AGENT;

EID: 66949171433     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0801935     Document Type: Article
Times cited : (46)

References (44)
  • 1
    • 33846995990 scopus 로고    scopus 로고
    • XDR tuberculosis - Implications for Global Public Health
    • DOI 10.1056/NEJMp068273
    • Raviglione, M. C., and I. M. Smith. 2007. XDR tuberculosis: implications for global public health. N. Engl. J. Med. 356: 656-659. (Pubitemid 46257227)
    • (2007) New England Journal of Medicine , vol.356 , Issue.7 , pp. 656-659
    • Raviglione, M.C.1    Smith, I.M.2
  • 3
    • 0038557053 scopus 로고    scopus 로고
    • Phagocyte sabotage: Disruption of macrophage signalling by bacterial pathogens
    • DOI 10.1038/nrm1104
    • Rosenberger, C., and B. Finlay. 2003. Phagocyte sabotage: disruption of macrophage signalling by bacterial pathogens. Nat. Rev. Mol. Cell Biol. 4: 385-396. (Pubitemid 36565570)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.5 , pp. 385-396
    • Rosenberger, C.M.1    Finlay, B.B.2
  • 4
    • 0029926416 scopus 로고    scopus 로고
    • Effect of Mycobacterium tuberculosis and its components on macrophages and the release of matrix metalloproteinases
    • Chang, J. C., A. Wysocki, K. M. Tchou-Wong, N. Moskowitz, Y. Zhang, and W. N. Rom. 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
  • 5
    • 0242410826 scopus 로고    scopus 로고
    • Unopposed matrix metalloproteinase-9 expression in human tuberculous granuloma and the role of TNF-α-dependent monocyte networks
    • Price, N. M., R. H. Gilman, J. Uddin, S. Recavarren, and J. S. Friedland. 2003. Unopposed matrix metalloproteinase-9 expression in human tuberculous granuloma and the role of TNF-α-dependent monocyte networks. J. Immunol. 171: 5579-5586.
    • (2003) J. Immunol. , vol.171 , pp. 5579-5586
    • Price, N.M.1    Gilman, R.H.2    Uddin, J.3    Recavarren, S.4    Friedland, J.S.5
  • 6
    • 0034861026 scopus 로고    scopus 로고
    • Production of matrix metalloproteinases in response to mycobacterial infection
    • DOI 10.1128/IAI.69.9.5661-5670.2001
    • Quiding-Jarbrink, M., D. A. Smith, and G. J. Bancroft. 2001. Production of matrix metalloproteinases in response to mycobacterial infection. Infect. Immun. 69: 5661-5670. (Pubitemid 32786504)
    • (2001) Infection and Immunity , vol.69 , Issue.9 , pp. 5661-5670
    • Quiding-Jarbrink, M.1    Smith, D.A.2    Bancroft, G.J.3
  • 7
    • 0036087197 scopus 로고    scopus 로고
    • Tuberculosis induction of matrix metalloproteinase-9: The role of mannose and receptor-mediated mechanisms
    • M.
    • Rivera-Marrero, C. A., W. Schuyler, S. Roser, J. D. Ritzenthaler, S. A. Newburn, and J. Roman. M. 2002. Tuberculosis induction of matrix metalloproteinase-9: the role of mannose and receptor-mediated mechanisms. Am. J. Physiol. 282: L546-L555.
    • (2002) Am. J. Physiol. , vol.282
    • Rivera-Marrero, C.A.1    Schuyler, W.2    Roser, S.3    Ritzenthaler, J.D.4    Newburn, S.A.5    Roman, J.6
  • 9
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • DOI 10.1038/nrm2125, PII NRM2125
    • Page-McCaw, A., A. J. Ewald, and Z. Werb. 2007. Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 8: 221-233. (Pubitemid 46310551)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.3 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 10
    • 33846785537 scopus 로고    scopus 로고
    • Matrix metalloproteinases in lung: Multiple, multifarious, and multifaceted
    • DOI 10.1152/physrev.00022.2006
    • Greenlee, K. J., Z. Werb, and F. Kheradmand. 2007. Matrix metalloproteinases in lung: multiple, multifarious, and multifaceted. Physiol. Rev. 87: 69-98. (Pubitemid 46209991)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 69-98
    • Greenlee, K.J.1    Werb, Z.2    Kheradmand, F.3
  • 13
    • 0034101866 scopus 로고    scopus 로고
    • Upregulation of gelatinases a and B, collagenases 1 and 2, and increased parenchymal cell death in COPD
    • Segura-Valdez, L., A. Pardo, M. Gaxiola, B. D. Uhal, C. Becerril, and M. Selman. 2000. Upregulation of gelatinases A and B, collagenases 1 and 2, and increased parenchymal cell death in COPD. Chest 117: 684-694. (Pubitemid 30152206)
    • (2000) Chest , vol.117 , Issue.3 , pp. 684-694
    • Segura-Valdez, L.1    Pardo, A.2    Gaxiola, M.3    Uhal, B.D.4    Becerril, C.5    Selman, M.6
  • 15
    • 33645065567 scopus 로고    scopus 로고
    • Matrix metalloproteinases in destructive pulmonary pathology
    • Elkington, P. T., and J. S. Friedland. 2006. Matrix metalloproteinases in destructive pulmonary pathology. Thorax 61: 259-266.
    • (2006) Thorax , vol.61 , pp. 259-266
    • Elkington, P.T.1    Friedland, J.S.2
  • 16
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks, W. C., C. L. Wilson, and Y. S. Lopez-Boado. 2004. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat. Rev. Immunol. 4: 617-629. (Pubitemid 39025047)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.8 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 18
    • 26844441798 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis up-regulates matrix metalloproteinase-1 secretion from human airway epithelial cells via a p38 MAPK switch
    • Elkington, P. T., J. E. Emerson, L. D. Lopez-Pascua, C. M. O'Kane, D. E. Horncastle, J. J. Boyle, and J. S. Friedland. 2005. Mycobacterium tuberculosis up-regulates matrix metalloproteinase-1 secretion from human airway epithelial cells via a p38 MAPK switch. J. Immunol. 175: 5333-5340.
    • (2005) J. Immunol. , vol.175 , pp. 5333-5340
    • Elkington, P.T.1    Emerson, J.E.2    Lopez-Pascua, L.D.3    O'Kane, C.M.4    Horncastle, D.E.5    Boyle, J.J.6    Friedland, J.S.7
  • 19
    • 0344153852 scopus 로고    scopus 로고
    • Cyclooxygenase-2-derived e prostaglandins down-regulate matrix metalloproteinase-1 expression in fibroblast-like synoviocytes via inhibition of extracellular signal-regulated kinase activation
    • Pillinger, M. H., P. B. Rosenthal, S. N. Tolani, B. Apsel, V. Dinsell, J. Greenberg, E. S. Chan, P. F. Gomez, and S. B. Abramson. 2003. Cyclooxygenase-2-derived E prostaglandins down-regulate matrix metalloproteinase-1 expression in fibroblast-like synoviocytes via inhibition of extracellular signal-regulated kinase activation. J. Immunol. 171: 6080-6089.
    • (2003) J. Immunol. , vol.171 , pp. 6080-6089
    • Pillinger, M.H.1    Rosenthal, P.B.2    Tolani, S.N.3    Apsel, B.4    Dinsell, V.5    Greenberg, J.6    Chan, E.S.7    Gomez, P.F.8    Abramson, S.B.9
  • 20
    • 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, W. C., M. Zhou, U. Shankavaram, G. Peng, and L. M. Wahl. 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
  • 21
    • 0032570825 scopus 로고    scopus 로고
    • Enhancement of fibroblast collagenase (matrix metalloproteinase-1) gene expression by ceramide is mediated by extracellular signal-regulated and stress-activated protein kinase pathways
    • DOI 10.1074/jbc.273.9.5137
    • Reunanen, N., J. Westermarck, L. Hakkinen, T. H. Holmstrom, I. Elo, J. E. Eriksson, and V. M. Kahari. 1998. Enhancement of fibroblast collagenase (matrix metalloproteinase-1) gene expression by ceramide is mediated by extracellular signal-regulated and stress-activated protein kinase pathways. J. Biol. Chem. 273: 5137-5145. (Pubitemid 28108675)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.9 , pp. 5137-5145
    • Reunanen, N.1    Westermarck, J.2    Hakkinen, L.3    Holmstrom, T.H.4    Elo, I.5    Eriksson, J.E.6    Kahari, V.-M.7
  • 22
    • 2342644797 scopus 로고    scopus 로고
    • Extracellular regulated kinase/Mitogen activated protein kinase is up-regulated in pulmonary emphysema and mediates matrix metalloproteinase-1 induction by cigarette smoke
    • Mercer, B. A., N. Kolesnikova, J. Sonett, and J. D'Armiento. 2004. Extracellular regulated kinase/Mitogen activated protein kinase is up-regulated in pulmonary emphysema and mediates matrix metalloproteinase-1 induction by cigarette smoke. J. Biol. Chem. 279: 17690-17696.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17690-17696
    • Mercer, B.A.1    Kolesnikova, N.2    Sonett, J.3    D'Armiento, J.4
  • 23
    • 0025239695 scopus 로고
    • Inhibition of phospholipase activity in human monocytes by IFN-γ blocks endogenous prostaglandin E2-dependent collagenase production
    • Wahl, L. M., M. E. Corcoran, S. E. Mergenhagen, and D. S. Finbloom. 1990. Inhibition of phospholipase activity in human monocytes by IFN-γ blocks endogenous prostaglandin E2-dependent collagenase production. J. Immunol. 144: 3518-3522.
    • (1990) J. Immunol. , vol.144 , pp. 3518-3522
    • Wahl, L.M.1    Corcoran, M.E.2    Mergenhagen, S.E.3    Finbloom, D.S.4
  • 24
    • 77951755456 scopus 로고
    • The in vitro effect of para-aminosalicylic acid (PAS) in preventing acquired resistance to streptomycin by Mycobacterium tuberculosis
    • Graessle, O. E., and J. J. Pietrowski. 1949. The in vitro effect of para-aminosalicylic acid (PAS) in preventing acquired resistance to streptomycin by Mycobacterium tuberculosis. J. Bacteriol. 57: 459-464.
    • (1949) J. Bacteriol. , vol.57 , pp. 459-464
    • Graessle, O.E.1    Pietrowski, J.J.2
  • 25
    • 3142583521 scopus 로고    scopus 로고
    • The folate pathway is a target for resistance to the drug para-aminosalicylic acid (PAS) in mycobacteria
    • DOI 10.1111/j.1365-2958.2004.04120.x
    • Rengarajan, J., C. M. Sassetti, V. Naroditskaya, A. Sloutsky, B. R. Bloom, and E. J. Rubin. 2004. The folate pathway is a target for resistance to the drug para-aminosalicylic acid (PAS) in mycobacteria. Mol. Microbiol. 53: 275-282. (Pubitemid 38901397)
    • (2004) Molecular Microbiology , vol.53 , Issue.1 , pp. 275-282
    • Rengarajan, J.1    Sassetti, C.M.2    Naroditskaya, V.3    Sloutsky, A.4    Bloom, B.R.5    Rubin, E.J.6
  • 26
    • 0036064607 scopus 로고    scopus 로고
    • Tuberculosis therapy: Past, present and future
    • Iseman, M. D. 2002. Tuberculosis therapy: past, present and future. Eur. Respir. J. Suppl. 36: 87s-94s.
    • (2002) Eur. Respir. J. Suppl. , vol.36
    • Iseman, M.D.1
  • 27
    • 31944451923 scopus 로고    scopus 로고
    • Filter sterilization of highly infectious samples to prevent false negative analysis of matrix metalloproteinase activity
    • Elkington, P. T., J. A. Green, and J. S. Friedland. 2006. Filter sterilization of highly infectious samples to prevent false negative analysis of matrix metalloproteinase activity. J. Immunol. Methods 309: 115-119.
    • (2006) J. Immunol. Methods , vol.309 , pp. 115-119
    • Elkington, P.T.1    Green, J.A.2    Friedland, J.S.3
  • 28
    • 0037359601 scopus 로고    scopus 로고
    • Elevated membrane-type matrix metalloproteinases in gliomas revealed by profiling proteases and inhibitors in human cancer cells
    • Nuttall, R. K., C. J. Pennington, J. Taplin, A. Wheal, V. W. Yong, P. A. Forsyth, and D. R. Edwards. 2003. Elevated membrane-type matrix metalloproteinases in gliomas revealed by profiling proteases and inhibitors in human cancer cells. Mol. Cancer. Res. 1: 333-345.
    • (2003) Mol. Cancer. Res. , vol.1 , pp. 333-345
    • Nuttall, R.K.1    Pennington, C.J.2    Taplin, J.3    Wheal, A.4    Yong, V.W.5    Forsyth, P.A.6    Edwards, D.R.7
  • 29
    • 34047262879 scopus 로고    scopus 로고
    • Intracellular signalling cascades regulating innate immune responses to Mycobacteria: Branching out from Toll-like receptors
    • Jo, E. K., C. S. Yang, C. H. Choi, and C. V. Harding. 2007. Intracellular signalling cascades regulating innate immune responses to Mycobacteria: branching out from Toll-like receptors. Cell. Microbiol. 9: 1087-1098.
    • (2007) Cell. Microbiol. , vol.9 , pp. 1087-1098
    • Jo, E.K.1    Yang, C.S.2    Choi, C.H.3    Harding, C.V.4
  • 30
    • 34249012130 scopus 로고    scopus 로고
    • Direct extracellular interaction between the early secreted antigen ESAT-6 of Mycobacterium tuberculosis and TLR2 inhibits TLR signaling in macrophages
    • Pathak, S. K., S. Basu, K. K. Basu, A. Banerjee, S. Pathak, A. Bhattacharyya, T. Kaisho, M. Kundu, and J. Basu. 2007. Direct extracellular interaction between the early secreted antigen ESAT-6 of Mycobacterium tuberculosis and TLR2 inhibits TLR signaling in macrophages. Nat. Immunol. 8: 610-618.
    • (2007) Nat. Immunol. , vol.8 , pp. 610-618
    • Pathak, S.K.1    Basu, S.2    Basu, K.K.3    Banerjee, A.4    Pathak, S.5    Bhattacharyya, A.6    Kaisho, T.7    Kundu, M.8    Basu, J.9
  • 31
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., H. Reddy, M. Caivano, and P. Cohen. 2000. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351: 95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 32
    • 0032951716 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes
    • Dean, J. L., M. Brook, A. R. Clark, and J. Saklatvala. 1999. p38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes. J. Biol. Chem. 274: 264-269.
    • (1999) J. Biol. Chem. , vol.274 , pp. 264-269
    • Dean, J.L.1    Brook, M.2    Clark, A.R.3    Saklatvala, J.4
  • 33
    • 0037406537 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase pathways in the production of tumor necrosis factor-α, interleukin-10, and monocyte chemotactic protein-1 by Mycobacterium tuberculosis H37Rv-infected human monocytes
    • Song, C. H., J. S. Lee, S. H. Lee, K. Lim, H. J. Kim, J. K. Park, T. H. Paik, and E. K. Jo. 2003. Role of mitogen-activated protein kinase pathways in the production of tumor necrosis factor-α, interleukin-10, and monocyte chemotactic protein-1 by Mycobacterium tuberculosis H37Rv-infected human monocytes. J. Clin. Immunol. 23: 194-201.
    • (2003) J. Clin. Immunol. , vol.23 , pp. 194-201
    • Song, C.H.1    Lee, J.S.2    Lee, S.H.3    Lim, K.4    Kim, H.J.5    Park, J.K.6    Paik, T.H.7    Jo, E.K.8
  • 34
    • 24744455914 scopus 로고    scopus 로고
    • Role of the phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways in the secretion of tumor necrosis factor-α and interleukin-10 by the PPD antigen of Mycobacterium tuberculosis
    • Jung, S. B., C. H. Song, C. S. Yang, S. Y. Kim, K. S. Lee, A. R. Shin, J. S. Lee, H. S. Nam, H. J. Kim, J. K. Park, et al. 2005. Role of the phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways in the secretion of tumor necrosis factor-α and interleukin-10 by the PPD antigen of Mycobacterium tuberculosis. J. Clin. Immunol. 25: 482-490.
    • (2005) J. Clin. Immunol. , vol.25 , pp. 482-490
    • Jung, S.B.1    Song, C.H.2    Yang, C.S.3    Kim, S.Y.4    Lee, K.S.5    Shin, A.R.6    Lee, J.S.7    Nam, H.S.8    Kim, H.J.9    Park, J.K.10
  • 36
    • 34248331345 scopus 로고    scopus 로고
    • Inhibitors of stress-activated protein/mitogen-activated protein kinase pathways
    • DOI 10.1016/j.coph.2006.11.012, PII S1471489207000586, Respiratory/Musculoskeletal
    • Malemud, C. J. 2007. Inhibitors of stress-activated protein/mitogen- activated protein kinase pathways. Curr. Opin. Pharmacol. 7: 339-343. (Pubitemid 46731194)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.3 , pp. 339-343
    • Malemud, C.J.1
  • 38
    • 0027419081 scopus 로고
    • Induction of macrophage metalloproteinases by extracellular matrix: Evidence for enzyme- And substrate-specific responses involving prostaglandin-dependent mechanisms
    • Shapiro, S. D., D. K. Kobayashi, A. P. Pentland, and H. G. Welgus. 1993. Induction of macrophage metalloproteinases by extracellular matrix: evidence for enzyme- and substrate-specific responses involving prostaglandin-dependent mechanisms. J. Biol. Chem. 268: 8170-8175.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8170-8175
    • Shapiro, S.D.1    Kobayashi, D.K.2    Pentland, A.P.3    Welgus, H.G.4
  • 39
    • 35948944537 scopus 로고    scopus 로고
    • Mycobacterium avium -induced matrix metalloproteinase-9 expression occurs in a cyclooxygenase-2-dependent manner and involves phosphorylation- And acetylation-dependent chromatin modification
    • DOI 10.1111/j.1462-5822.2007.00997.x
    • Basu, S., S. Pathak, S. K. Pathak, A. Bhattacharyya, A. Banerjee, M. Kundu, and J. Basu. 2007. Mycobacterium avium-induced matrix metalloproteinase-9 expression occurs in a cyclooxygenase-2-dependent manner and involves phosphorylation- and acetylation-dependent chromatin modification. Cell. Microbiol. 9: 2804-2816. (Pubitemid 350066566)
    • (2007) Cellular Microbiology , vol.9 , Issue.12 , pp. 2804-2816
    • Basu, S.1    Pathak, S.2    Pathak, S.K.3    Bhattacharyya, A.4    Banerjee, A.5    Kundu, M.6    Basu, J.7
  • 41
    • 33947535813 scopus 로고    scopus 로고
    • Aspirin and ibuprofen enhance pyrazinamide treatment of murine tuberculosis
    • Byrne, S. T., S. M. Denkin, and Y. Zhang. 2007. Aspirin and ibuprofen enhance pyrazinamide treatment of murine tuberculosis. J. Antimicrob. Chemother. 59: 313-316.
    • (2007) J. Antimicrob. Chemother. , vol.59 , pp. 313-316
    • Byrne, S.T.1    Denkin, S.M.2    Zhang, Y.3
  • 42
    • 0002162781 scopus 로고
    • Para-Aminosalicylic acid in the treatment of tuberculosis
    • Lehman, J. 1946. para-Aminosalicylic acid in the treatment of tuberculosis. Lancet I: 15-16.
    • (1946) Lancet , vol.1 , pp. 15-16
    • Lehman, J.1
  • 43
    • 3342918498 scopus 로고    scopus 로고
    • The p38 MAP kinase pathway as a therapeutic target in inflammatory disease
    • DOI 10.1016/j.coph.2004.03.009, PII S147148920400089X
    • Saklatvala, J. 2004. The p38 MAP kinase pathway as a therapeutic target in inflammatory disease. Curr. Opin. Pharmacol. 4: 372-377. (Pubitemid 38987064)
    • (2004) Current Opinion in Pharmacology , vol.4 , Issue.4 , pp. 372-377
    • Saklatvala, J.1
  • 44
    • 21844433456 scopus 로고    scopus 로고
    • Reconsidering adjuvant immunotherapy for tuberculosis
    • Wallis, R. S. 2005. Reconsidering adjuvant immunotherapy for tuberculosis. Clin. Infect. Dis. 41: 201-208.
    • (2005) Clin. Infect. Dis. , vol.41 , pp. 201-208
    • Wallis, R.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.