메뉴 건너뛰기




Volumn 82, Issue 12, 2014, Pages 4952-4958

Recognition of Streptococcus pneumoniae and muramyl dipeptide by NOD2 results in potent induction of MMP-9, which can be controlled by lipopolysaccharide stimulation

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; GELATINASE B; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; MURAMYL DIPEPTIDE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; MMP9 PROTEIN, HUMAN; N ACETYLMURAMYLALANYL DEXTRO ISOGLUTAMINE; NOD2 PROTEIN, HUMAN;

EID: 84911367768     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.02150-14     Document Type: Article
Times cited : (13)

References (39)
  • 2
    • 33745929029 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and autoimmune diseases
    • Ram M, Sherer Y, Shoenfeld Y. 2006. Matrix metalloproteinase-9 and autoimmune diseases. J. Clin. Immunol. 26:299-307. http://dx.doi.org/10.1007/s10875-006-9022-6.
    • (2006) J. Clin. Immunol. , vol.26 , pp. 299-307
    • Ram, M.1    Sherer, Y.2    Shoenfeld, Y.3
  • 3
    • 0038278609 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and its natural inhibitor TIMP-1 expressed or secreted by peripheral blood mononuclear cells from patients with systemic lupus erythematosus
    • Matache C, Stefanescu M, Dragomir C, Tanaseanu S, Onu A, Ofiteru A, Szegli G. 2003. Matrix metalloproteinase-9 and its natural inhibitor TIMP-1 expressed or secreted by peripheral blood mononuclear cells from patients with systemic lupus erythematosus. J. Autoimmun. 20:323-331. http://dx.doi.org/10.1016/S0896-8411(03)00037-4.
    • (2003) J. Autoimmun. , vol.20 , pp. 323-331
    • Matache, C.1    Stefanescu, M.2    Dragomir, C.3    Tanaseanu, S.4    Onu, A.5    Ofiteru, A.6    Szegli, G.7
  • 5
    • 0037422243 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis
    • Böttcher T, Spreer A, Azeh I, Nau R, Gerber J. 2003. Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis. Neurosci. Lett. 338:201-204. http://dx.doi.org/10.1016/S0304-3940(02)01406-4.
    • (2003) Neurosci. Lett. , vol.338 , pp. 201-204
    • Böttcher, T.1    Spreer, A.2    Azeh, I.3    Nau, R.4    Gerber, J.5
  • 6
    • 84891429737 scopus 로고    scopus 로고
    • Lung dendritic cells facilitate extrapulmonary bacterial dissemination during pneumococcal pneumonia
    • Rosendahl A, Bergmann S, Hammerschmidt S, Goldmann O, Medina E. 2013. Lung dendritic cells facilitate extrapulmonary bacterial dissemination during pneumococcal pneumonia. Front. Cell. Infect. Microbiol. 3:21. http://dx.doi.org/10.3389/fcimb.2013.00021.
    • (2013) Front. Cell. Infect. Microbiol. , vol.3 , pp. 21
    • Rosendahl, A.1    Bergmann, S.2    Hammerschmidt, S.3    Goldmann, O.4    Medina, E.5
  • 7
    • 0043166893 scopus 로고    scopus 로고
    • Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia
    • Oggioni MR, Memmi G, Maggi T, Chiavolini D, Iannelli F, Pozzi G. 2003. Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia. Mol. Microbiol. 49:795-805. http://dx.doi.org/10.1046/j.1365-2958.2003.03596.x.
    • (2003) Mol. Microbiol. , vol.49 , pp. 795-805
    • Oggioni, M.R.1    Memmi, G.2    Maggi, T.3    Chiavolini, D.4    Iannelli, F.5    Pozzi, G.6
  • 8
    • 84902040023 scopus 로고    scopus 로고
    • An in vitro model to study immune responses of human peripheral blood mononuclear cells to human respiratory syncytial virus infection
    • Vissers M, Habets MN, Ahout IM, Jans J, de Jonge MI, Diavatopoulos DA, Ferwerda G. 2013. An in vitro model to study immune responses of human peripheral blood mononuclear cells to human respiratory syncytial virus infection. J. Vis. Exp. 2013:e50766. http://dx.doi.org/10.3791/50766.
    • (2013) J. Vis. Exp. , vol.2013
    • Vissers, M.1    Habets, M.N.2    Ahout, I.M.3    Jans, J.4    de Jonge, M.I.5    Diavatopoulos, D.A.6    Ferwerda, G.7
  • 10
    • 71049121550 scopus 로고    scopus 로고
    • Pneumolysin induces release of matrix metalloproteinase-8 and-9 from human neutrophils
    • Cockeran R, Mitchell T, Feldman C, Anderson R. 2009. Pneumolysin induces release of matrix metalloproteinase-8 and-9 from human neutrophils. Eur. Respir. J. 34:1167-1170. http://dx.doi.org/10.1183/09031936.00007109.
    • (2009) Eur. Respir. J. , vol.34 , pp. 1167-1170
    • Cockeran, R.1    Mitchell, T.2    Feldman, C.3    Anderson, R.4
  • 11
    • 50249161572 scopus 로고    scopus 로고
    • Hospital acquired pneumonia with high-risk bacteria is associated with increased pulmonary matrix metalloproteinase activity.
    • Schaaf B, Liebau C, Kurowski V, Droemann D, Dalhoff K. 2008. Hospital acquired pneumonia with high-risk bacteria is associated with increased pulmonary matrix metalloproteinase activity.BMC Pulm. Med. 8:12. http://dx.doi.org/10.1186/1471-2466-8-12.
    • (2008) BMC Pulm. Med. , vol.8 , pp. 12
    • Schaaf, B.1    Liebau, C.2    Kurowski, V.3    Droemann, D.4    Dalhoff, K.5
  • 12
    • 22144471934 scopus 로고    scopus 로고
    • Targeting neutrophil collagenase/matrix metalloproteinase-8 and gelatinase B/matrix metalloproteinase-9 with a peptidomimetic inhibitor protects against endotoxin shock
    • Hu J, Van den Steen PE, Dillen C, Opdenakker G. 2005. Targeting neutrophil collagenase/matrix metalloproteinase-8 and gelatinase B/matrix metalloproteinase-9 with a peptidomimetic inhibitor protects against endotoxin shock. Biochem. Pharmacol. 70:535-544. http://dx.doi.org/10.1016/j.bcp.2005.04.047.
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 535-544
    • Hu, J.1    Den Steen, P.E.2    Dillen, C.3    Opdenakker, G.4
  • 13
    • 38049093786 scopus 로고    scopus 로고
    • C-reactive protein induces endothelial cell apoptosis and matrix metalloproteinase-9 production in human mononuclear cells: implications for the destabilization of atherosclerotic plaque
    • Nabata A, Kuroki M, Ueba H, Hashimoto S, Umemoto T, Wada H, Yasu T, Saito M, Momomura S-I, Kawakami M. 2008. C-reactive protein induces endothelial cell apoptosis and matrix metalloproteinase-9 production in human mononuclear cells: implications for the destabilization of atherosclerotic plaque. Atherosclerosis 196:129-135. http://dx.doi.org/10.1016/j.atherosclerosis.2007.03.003.
    • (2008) Atherosclerosis , vol.196 , pp. 129-135
    • Nabata, A.1    Kuroki, M.2    Ueba, H.3    Hashimoto, S.4    Umemoto, T.5    Wada, H.6    Yasu, T.7    Saito, M.8    Momomura, S.-I.9    Kawakami, M.10
  • 14
    • 0030292766 scopus 로고    scopus 로고
    • TNF-alpha and IL-1beta selectively induce expression of 92-kDa gelatinase by human macrophages
    • Saren P, Welgus HG, Kovanen PT. 1996. TNF-alpha and IL-1beta selectively induce expression of 92-kDa gelatinase by human macrophages. J. Immunol. 157:4159-4165.
    • (1996) J. Immunol. , vol.157 , pp. 4159-4165
    • Saren, P.1    Welgus, H.G.2    Kovanen, P.T.3
  • 15
    • 84889048698 scopus 로고    scopus 로고
    • NOD1 and NOD2 regulate proinflammatory andprolabor mediators in human fetal membranes and myometrium via nuclear factor-kappa B 1
    • Lappas M. 2013. NOD1 and NOD2 regulate proinflammatory andprolabor mediators in human fetal membranes and myometrium via nuclear factor-kappa B 1. Biol. Reprod. 89:14. http://dx.doi.org/10.1095/biolreprod.113.110056.
    • (2013) Biol. Reprod. , vol.89 , pp. 14
    • Lappas, M.1
  • 16
    • 0037942829 scopus 로고    scopus 로고
    • Differential regulation of lipopolysaccharide-induced monocyte matrix metalloproteinase (MMP)-1 and MMP-9 by p38 and extracellular signalregulated kinase 1/2 mitogen-activated protein kinases
    • Lai W-C, 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 signalregulated kinase 1/2 mitogen-activated protein kinases. J. Immunol. 170: 6244-6249. http://dx.doi.org/10.4049/jimmunol.170.12.6244.
    • (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
  • 18
    • 33748846770 scopus 로고    scopus 로고
    • Live Streptococcus pneumoniae, Haemophilus influenzae, and Neisseria meningitidis activate the inflammatory response through Toll-like receptors 2, 4, and 9 in species-specific patterns
    • Mogensen TH, Paludan SR, Kilian M, Ostergaard L. 2006. Live Streptococcus pneumoniae, Haemophilus influenzae, and Neisseria meningitidis activate the inflammatory response through Toll-like receptors 2, 4, and 9 in species-specific patterns. J. Leukoc. Biol. 80:267-277. http://dx.doi.org/10.1189/jlb.1105626.
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 267-277
    • Mogensen, T.H.1    Paludan, S.R.2    Kilian, M.3    Ostergaard, L.4
  • 19
    • 0033168728 scopus 로고    scopus 로고
    • Cutting edge: recognition of Gram-positive bacterial cell wall components by the innate immune system occurs via Toll-like receptor 2
    • Yoshimura A, Lien E, Ingalls RR, Tuomanen E, Dziarski R, Golenbock D. 1999. Cutting edge: recognition of Gram-positive bacterial cell wall components by the innate immune system occurs via Toll-like receptor 2. J. Immunol. 163:1-5.
    • (1999) J. Immunol. , vol.163 , pp. 1-5
    • Yoshimura, A.1    Lien, E.2    Ingalls, R.R.3    Tuomanen, E.4    Dziarski, R.5    Golenbock, D.6
  • 20
    • 34250305202 scopus 로고    scopus 로고
    • TLR2 synergizes with both TLR4 and TLR9 for induction of the MyD88-dependent splenic cytokine and chemokine response to Streptococcus pneumoniae
    • Lee KS, Scanga CA, Bachelder EM, Chen Q, Snapper CM. 2007. TLR2 synergizes with both TLR4 and TLR9 for induction of the MyD88-dependent splenic cytokine and chemokine response to Streptococcus pneumoniae. Cell. Immunol. 245:103-110. http://dx.doi.org/10.1016/j.cellimm.2007.04.003.
    • (2007) Cell. Immunol. , vol.245 , pp. 103-110
    • Lee, K.S.1    Scanga, C.A.2    Bachelder, E.M.3    Chen, Q.4    Snapper, C.M.5
  • 21
    • 0034115114 scopus 로고    scopus 로고
    • Interplay of matrix metalloproteinases, tissue inhibitors of metalloproteinases and their regulators in cardiac matrix remodeling
    • Li YY, McTiernan CF, Feldman AM. 2000. Interplay of matrix metalloproteinases, tissue inhibitors of metalloproteinases and their regulators in cardiac matrix remodeling. Cardiovasc. Res. 46:214-224. http://dx.doi.org/10.1016/S0008-6363(00)00003-1.
    • (2000) Cardiovasc. Res. , vol.46 , pp. 214-224
    • Li, Y.Y.1    McTiernan, C.F.2    Feldman, A.M.3
  • 22
    • 0026714363 scopus 로고
    • Post-transcriptional regulation of collagenase and stromelysin gene expression by epidermal growth factor and dexamethasone in cultured human fibroblasts
    • Delany AM, Brinckerhoff CE. 1992. Post-transcriptional regulation of collagenase and stromelysin gene expression by epidermal growth factor and dexamethasone in cultured human fibroblasts. J. Cell. Biochem. 50: 400-410. http://dx.doi.org/10.1002/jcb.240500409.
    • (1992) J. Cell. Biochem. , vol.50 , pp. 400-410
    • Delany, A.M.1    Brinckerhoff, C.E.2
  • 23
    • 0025866180 scopus 로고
    • Transcriptional and posttranscriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression
    • Overall C, Wrana J, Sodek J. 1991. Transcriptional and posttranscriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression. J. Biol. Chem. 266:14064-14071.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14064-14071
    • Overall, C.1    Wrana, J.2    Sodek, J.3
  • 24
    • 0034537138 scopus 로고    scopus 로고
    • Sustained ERK phosphorylation is necessary but not sufficient for MMP-9 regulation in endothelial cells: involvement of Ras-dependent and-independent pathways
    • Genersch E, Hayess K, Neuenfeld Y, Haller H. 2000. Sustained ERK phosphorylation is necessary but not sufficient for MMP-9 regulation in endothelial cells: involvement of Ras-dependent and-independent pathways. J. Cell Sci. 113:4319-4330.
    • (2000) J. Cell Sci. , vol.113 , pp. 4319-4330
    • Genersch, E.1    Hayess, K.2    Neuenfeld, Y.3    Haller, H.4
  • 25
    • 70149120995 scopus 로고    scopus 로고
    • Cytokines and signaling pathways regulating matrix metalloproteinase-9 (MMP-9) expression in corneal epithelial cells
    • Gordon GM, Ledee DR, Feuer WJ, Fini ME. 2009. Cytokines and signaling pathways regulating matrix metalloproteinase-9 (MMP-9) expression in corneal epithelial cells. J. Cell. Physiol. 221:402-411. http://dx.doi.org/10.1002/jcp.21869.
    • (2009) J. Cell. Physiol. , vol.221 , pp. 402-411
    • Gordon, G.M.1    Ledee, D.R.2    Feuer, W.J.3    Fini, M.E.4
  • 26
    • 0036209979 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 expression in breast cancer-derived human fibroblasts is differentially regulated by stromal-epithelial interactions
    • Singer CF, Kronsteiner N, Marton E, Kubista M, Cullen KJ, Hirtenlehner K, Seifert M, Kubista E. 2002. MMP-2 and MMP-9 expression in breast cancer-derived human fibroblasts is differentially regulated by stromal-epithelial interactions. Breast Cancer Res. Treat. 72:69-77. http://dx.doi.org/10.1023/A:1014918512569.
    • (2002) Breast Cancer Res. Treat. , vol.72 , pp. 69-77
    • Singer, C.F.1    Kronsteiner, N.2    Marton, E.3    Kubista, M.4    Cullen, K.J.5    Hirtenlehner, K.6    Seifert, M.7    Kubista, E.8
  • 27
    • 0030067654 scopus 로고    scopus 로고
    • 92 kDa type IV collagenase (MMP-9) is expressed in neutrophils and macrophages but not in malignant epithelial cells in human colon cancer
    • Nielsen BS, Timshel S, Kjeldsen L, Sehested M, Pyke C, Borregaard N, Danø K. 1996. 92 kDa type IV collagenase (MMP-9) is expressed in neutrophils and macrophages but not in malignant epithelial cells in human colon cancer. Int. J. Cancer 65:57-62. http://dx.doi.org/10.1002/(SICI)10 97-0215(19960103)65:157::AID-IJC10>3.0.CO;2-F.
    • (1996) Int. J. Cancer , vol.65 , pp. 57-62
    • Nielsen, B.S.1    Timshel, S.2    Kjeldsen, L.3    Sehested, M.4    Pyke, C.5    Borregaard, N.6    Danø, K.7
  • 28
    • 38049156464 scopus 로고    scopus 로고
    • PGE2-induced metalloproteinase-9 is essential for dendritic cell migration
    • Yen J-H, Khayrullina T, Ganea D. 2008. PGE2-induced metalloproteinase-9 is essential for dendritic cell migration. Blood 111:260-270. http://dx.doi.org/10.1182/blood-2007-05-090613.
    • (2008) Blood , vol.111 , pp. 260-270
    • Yen, J.-H.1    Khayrullina, T.2    Ganea, D.3
  • 29
    • 0035813187 scopus 로고    scopus 로고
    • The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL) modulation of MMP-9 activity by NGAL
    • Yan L, Borregaard N, Kjeldsen L, Moses MA. 2001. The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL) modulation of MMP-9 activity by NGAL. J. Biol. Chem. 276: 37258-37265. http://dx.doi.org/10.1074/jbc.M106089200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37258-37265
    • Yan, L.1    Borregaard, N.2    Kjeldsen, L.3    Moses, M.A.4
  • 30
    • 0017191079 scopus 로고
    • Small molecular weight β1 serum protein which specifically inhibits human collagenases
    • Woolley DE, Roberts DR, Evanson JM. 1976. Small molecular weight β1 serum protein which specifically inhibits human collagenases. Nature 261: 325-327. http://dx.doi.org/10.1038/261325a0.
    • (1976) Nature , vol.261 , pp. 325-327
    • Woolley, D.E.1    Roberts, D.R.2    Evanson, J.M.3
  • 32
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner JF. 1991. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner, J.F.1
  • 33
    • 0027955338 scopus 로고
    • Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils
    • Kjeldsen L, Bainton DF, Sengelov H, Borregaard N. 1994. Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils. Blood 83:799-807.
    • (1994) Blood , vol.83 , pp. 799-807
    • Kjeldsen, L.1    Bainton, D.F.2    Sengelov, H.3    Borregaard, N.4
  • 34
    • 0026731852 scopus 로고
    • Distribution of the α2-macroglobulin receptor/low density lipoprotein receptor-related protein in human tissues
    • Moestrup SK, Gliemann J, Pallesen G. 1992. Distribution of the α2-macroglobulin receptor/low density lipoprotein receptor-related protein in human tissues. Cell Tissue Res. 269:375-382. http://dx.doi.org/10.1007/BF00353892.
    • (1992) Cell Tissue Res. , vol.269 , pp. 375-382
    • Moestrup, S.K.1    Gliemann, J.2    Pallesen, G.3
  • 35
    • 0032939098 scopus 로고    scopus 로고
    • Th1 (IL-2, interferongamma (IFN-)) and Th2 (IL-10, IL-4) cytokine production by peripheral blood mononuclear cells (PBMC) from patients with systemic lupus erythematosus (SLE)
    • Viallard J, Pellegrin J, Ranchin V, Schaeverbeke T, Dehais J, Longy-Boursier M, Ragnaud J, Ling B, Moreau J. 1999. Th1 (IL-2, interferongamma (IFN-)) and Th2 (IL-10, IL-4) cytokine production by peripheral blood mononuclear cells (PBMC) from patients with systemic lupus erythematosus (SLE). Clin. Exp. Immunol. 115:189-195. http://dx.doi.org/10.1046/j.1365-2249.1999.00766.x.
    • (1999) Clin. Exp. Immunol. , vol.115 , pp. 189-195
    • Viallard, J.1    Pellegrin, J.2    Ranchin, V.3    Schaeverbeke, T.4    Dehais, J.5    Longy-Boursier, M.6    Ragnaud, J.7    Ling, B.8    Moreau, J.9
  • 37
    • 0037381597 scopus 로고    scopus 로고
    • Plasma concentrations and genetic variation of matrix metalloproteinase 9 and prognosis of patients with cardiovascular disease
    • Blankenberg S, Rupprecht HJ, Poirier O, Bickel C, Smieja M, Hafner G, Meyer J, Cambien F, Tiret L. 2003. Plasma concentrations and genetic variation of matrix metalloproteinase 9 and prognosis of patients with cardiovascular disease. Circulation 107:1579-1585. http://dx.doi.org/10.1161/01.CIR.0000058700.41738.12.
    • (2003) Circulation , vol.107 , pp. 1579-1585
    • Blankenberg, S.1    Rupprecht, H.J.2    Poirier, O.3    Bickel, C.4    Smieja, M.5    Hafner, G.6    Meyer, J.7    Cambien, F.8    Tiret, L.9
  • 39
    • 84864135737 scopus 로고    scopus 로고
    • Use of MMP-8 and MMP-9 to assess disease severity in children with viral lower respiratory tract infections
    • Brand KH, Ahout IM, de Groot R, Warris A, Ferwerda G, Hermans PW. 2012. Use of MMP-8 and MMP-9 to assess disease severity in children with viral lower respiratory tract infections. J. Med. Virol. 84:1471-1480. http://dx.doi.org/10.1002/jmv.23301.
    • (2012) J. Med. Virol. , vol.84 , pp. 1471-1480
    • Brand, K.H.1    Ahout, I.M.2    de Groot, R.3    Warris, A.4    Ferwerda, G.5    Hermans, P.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.