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Volumn 213, Issue 2, 2008, Pages 109-124

Gelatinase B/MMP-9 as an inflammatory marker enzyme in mouse zymosan peritonitis: Comparison of phase-specific and cell-specific production by mast cells, macrophages and neutrophils

Author keywords

Mast cells; Matrix metalloproteinase; Monocytes macrophages; Neutrophils; Peritoneal inflammation

Indexed keywords

GELATINASE B; ZYMOSAN;

EID: 38549115153     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imbio.2007.07.005     Document Type: Article
Times cited : (45)

References (55)
  • 1
    • 0033083395 scopus 로고    scopus 로고
    • Role of resident peritoneal macrophages and mast cells in chemokine production and neutrophil migration in acute inflammation: evidence for an inhibitory loop involving endogenous IL-10
    • Ajuebor M.N., Das A.M., Virag L., Flower R.J., Szabo C., and Perretti M. Role of resident peritoneal macrophages and mast cells in chemokine production and neutrophil migration in acute inflammation: evidence for an inhibitory loop involving endogenous IL-10. J. Immunol. 162 (1999) 1685-1691
    • (1999) J. Immunol. , vol.162 , pp. 1685-1691
    • Ajuebor, M.N.1    Das, A.M.2    Virag, L.3    Flower, R.J.4    Szabo, C.5    Perretti, M.6
  • 2
    • 0035477996 scopus 로고    scopus 로고
    • Human mast cells release metalloproteinase-9 on contact with activated T cells: juxtacrine regulation by TNF-alpha
    • Baram D., Vaday G.G., Salamon P., Drucker I., Hershkoviz R., and Mekori Y.A. Human mast cells release metalloproteinase-9 on contact with activated T cells: juxtacrine regulation by TNF-alpha. J. Immunol. 167 (2001) 4008-4016
    • (2001) J. Immunol. , vol.167 , pp. 4008-4016
    • Baram, D.1    Vaday, G.G.2    Salamon, P.3    Drucker, I.4    Hershkoviz, R.5    Mekori, Y.A.6
  • 3
    • 0037422243 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis
    • Bottcher T., Spreer A., Azeh I., Nau R., and Gerber J. Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis. Neurosci. Lett. 338 (2003) 201-204
    • (2003) Neurosci. Lett. , vol.338 , pp. 201-204
    • Bottcher, T.1    Spreer, A.2    Azeh, I.3    Nau, R.4    Gerber, J.5
  • 4
    • 0035689929 scopus 로고    scopus 로고
    • Expression of proenkephalin (PENK) mRNA in inflammatory leukocytes during experimental peritonitis in Swiss mice
    • Chadzinska M., Maj M., Scislowska-Czarnecka A., Przewlocka B., and Plytycz B. Expression of proenkephalin (PENK) mRNA in inflammatory leukocytes during experimental peritonitis in Swiss mice. Pol. J. Pharmacol. 53 (2001) 715-718
    • (2001) Pol. J. Pharmacol. , vol.53 , pp. 715-718
    • Chadzinska, M.1    Maj, M.2    Scislowska-Czarnecka, A.3    Przewlocka, B.4    Plytycz, B.5
  • 5
    • 22144466166 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-9 release from IL-8-stimulated human neutrophils
    • Chakrabarti S., and Patel K.D. Regulation of matrix metalloproteinase-9 release from IL-8-stimulated human neutrophils. J. Leukoc. Biol. 78 (2005) 279-288
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 279-288
    • Chakrabarti, S.1    Patel, K.D.2
  • 6
    • 30144439195 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-9 (MMP-9) in TNF-stimulated neutrophils: novel pathways for tertiary granule release
    • Chakrabarti S., Zee J.M., and Patel K.D. Regulation of matrix metalloproteinase-9 (MMP-9) in TNF-stimulated neutrophils: novel pathways for tertiary granule release. J. Leukoc. Biol. 79 (2006) 214-222
    • (2006) J. Leukoc. Biol. , vol.79 , pp. 214-222
    • Chakrabarti, S.1    Zee, J.M.2    Patel, K.D.3
  • 7
    • 0033405818 scopus 로고    scopus 로고
    • The individual regulation of granule protein mRNA levels during neutrophil maturation explains the heterogeneity of neutrophil granules
    • Cowland J.B., and Borregaard N. The individual regulation of granule protein mRNA levels during neutrophil maturation explains the heterogeneity of neutrophil granules. J. Leukoc. Biol. 66 (1999) 989-995
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 989-995
    • Cowland, J.B.1    Borregaard, N.2
  • 8
    • 0036847897 scopus 로고    scopus 로고
    • Analysis of gelatinases in complex biological fluids and tissue extracts
    • Descamps F.J., Martens E., and Opdenakker G. Analysis of gelatinases in complex biological fluids and tissue extracts. Lab. Invest. 82 (2002) 1607-1608
    • (2002) Lab. Invest. , vol.82 , pp. 1607-1608
    • Descamps, F.J.1    Martens, E.2    Opdenakker, G.3
  • 9
    • 0022398415 scopus 로고
    • Intraperitoneal injection of zymosan in mice induces pain, inflammation and the synthesis of peptidoleukotrienes and prostaglandin E2
    • Doherty N.S., Poubelle P., Borgeat P., Beaver T.H., Westrich G.L., and Schrader N.L. Intraperitoneal injection of zymosan in mice induces pain, inflammation and the synthesis of peptidoleukotrienes and prostaglandin E2. Prostaglandins 30 (1985) 769-789
    • (1985) Prostaglandins , vol.30 , pp. 769-789
    • Doherty, N.S.1    Poubelle, P.2    Borgeat, P.3    Beaver, T.H.4    Westrich, G.L.5    Schrader, N.L.6
  • 10
    • 0028913202 scopus 로고
    • Post-capillary venules in the "milky spots" of the greater omentum are the major site of plasma protein and leukocyte extravasation in rodent models of peritonitis
    • Doherty N.S., Griffiths R.J., Hakkinen J.P., Scampoli D.N., and Milici A.J. Post-capillary venules in the "milky spots" of the greater omentum are the major site of plasma protein and leukocyte extravasation in rodent models of peritonitis. Inflamm. Res. 44 (1995) 169-177
    • (1995) Inflamm. Res. , vol.44 , pp. 169-177
    • Doherty, N.S.1    Griffiths, R.J.2    Hakkinen, J.P.3    Scampoli, D.N.4    Milici, A.J.5
  • 11
    • 0020589515 scopus 로고
    • Ultrastructural criteria for identification of mast cells and basophils in humans, guinea pigs, and mice
    • Dvorak A.M., Dvorak H.F., and Galli S.J. Ultrastructural criteria for identification of mast cells and basophils in humans, guinea pigs, and mice. Am. Rev. Respir. Dis. 128 (1983) S49-S52
    • (1983) Am. Rev. Respir. Dis. , vol.128
    • Dvorak, A.M.1    Dvorak, H.F.2    Galli, S.J.3
  • 12
    • 0029995317 scopus 로고    scopus 로고
    • Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase
    • Fang K.C., Raymond W.W., Lazarus S.C., and Caughey G.H. Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase. J. Clin. Invest. 97 (1996) 1589-1596
    • (1996) J. Clin. Invest. , vol.97 , pp. 1589-1596
    • Fang, K.C.1    Raymond, W.W.2    Lazarus, S.C.3    Caughey, G.H.4
  • 13
    • 0030845183 scopus 로고    scopus 로고
    • Dog mast cell alpha-chymase activates progelatinase B by cleaving the Phe88-Gln89 and Phe91-Glu92 bonds of the catalytic domain
    • Fang K.C., Raymond W.W., Blount J.L., and Caughey G.H. Dog mast cell alpha-chymase activates progelatinase B by cleaving the Phe88-Gln89 and Phe91-Glu92 bonds of the catalytic domain. J. Biol. Chem. 272 (1997) 25628-25635
    • (1997) J. Biol. Chem. , vol.272 , pp. 25628-25635
    • Fang, K.C.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 14
    • 0033136337 scopus 로고    scopus 로고
    • Mast cell expression of gelatinases A and B is regulated by kit ligand and TGF-beta
    • Fang K.C., Wolters P.J., Steinhoff M., Bidgol A., Blount J.L., and Caughey G.H. Mast cell expression of gelatinases A and B is regulated by kit ligand and TGF-beta. J. Immunol. 162 (1999) 5528-5535
    • (1999) J. Immunol. , vol.162 , pp. 5528-5535
    • Fang, K.C.1    Wolters, P.J.2    Steinhoff, M.3    Bidgol, A.4    Blount, J.L.5    Caughey, G.H.6
  • 15
    • 0035108793 scopus 로고    scopus 로고
    • Peritonitis increases MMP-9 activity in peritoneal effluent from CAPD patients
    • Fukudome K., Fujimoto S., Sato Y., Hisanaga S., and Eto T. Peritonitis increases MMP-9 activity in peritoneal effluent from CAPD patients. Nephron 87 (2001) 35-41
    • (2001) Nephron , vol.87 , pp. 35-41
    • Fukudome, K.1    Fujimoto, S.2    Sato, Y.3    Hisanaga, S.4    Eto, T.5
  • 16
    • 0029059037 scopus 로고
    • Regulation of mouse and human mast cell development, survival and function by stem cell factor, the ligand for the c-kit receptor
    • Galli S.J., Tsai M., Wershil B.K., Tam S.Y., and Costa J.J. Regulation of mouse and human mast cell development, survival and function by stem cell factor, the ligand for the c-kit receptor. Int. Arch. Allergy Immunol. 107 (1995) 51-53
    • (1995) Int. Arch. Allergy Immunol. , vol.107 , pp. 51-53
    • Galli, S.J.1    Tsai, M.2    Wershil, B.K.3    Tam, S.Y.4    Costa, J.J.5
  • 18
    • 0037824711 scopus 로고    scopus 로고
    • Altered function of murine mast cells in response to lipopolysaccharide and peptidoglycan
    • Ikeda T., and Funaba M. Altered function of murine mast cells in response to lipopolysaccharide and peptidoglycan. Immunol. Lett. 88 (2003) 21-26
    • (2003) Immunol. Lett. , vol.88 , pp. 21-26
    • Ikeda, T.1    Funaba, M.2
  • 20
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G., and Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256 (1975) 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 21
    • 0036867124 scopus 로고    scopus 로고
    • Shedding light on vascular permeability during peritonitis: role of mast cell histamine versus macrophage cysteinyl leukotrienes
    • Kolaczkowska E. Shedding light on vascular permeability during peritonitis: role of mast cell histamine versus macrophage cysteinyl leukotrienes. Inflamm. Res. 51 (2002) 519-521
    • (2002) Inflamm. Res. , vol.51 , pp. 519-521
    • Kolaczkowska, E.1
  • 22
    • 0034889430 scopus 로고    scopus 로고
    • Critical role of mast cells in morphine-mediated impairment of zymosan-induced peritonitis in mice
    • Kolaczkowska E., Seljelid R., and Plytycz B. Critical role of mast cells in morphine-mediated impairment of zymosan-induced peritonitis in mice. Inflamm. Res. 50 (2001) 415-421
    • (2001) Inflamm. Res. , vol.50 , pp. 415-421
    • Kolaczkowska, E.1    Seljelid, R.2    Plytycz, B.3
  • 23
    • 0035156948 scopus 로고    scopus 로고
    • Role of mast cells in zymosan-induced peritoneal inflammation in Balb/c and mast cell-deficient WBB6F1 mice
    • Kolaczkowska E., Seljelid R., and Plytycz B. Role of mast cells in zymosan-induced peritoneal inflammation in Balb/c and mast cell-deficient WBB6F1 mice. J. Leukoc. Biol. 69 (2001) 33-42
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 33-42
    • Kolaczkowska, E.1    Seljelid, R.2    Plytycz, B.3
  • 24
    • 0036217206 scopus 로고    scopus 로고
    • Early vascular permeability in murine experimental peritonitis is comediated by resident peritoneal macrophages and mast cells: crucial involvement of macrophage-derived cysteinyl-leukotrienes
    • Kolaczkowska E., Shahzidi S., Seljelid R., van Rooijen N., and Plytycz B. Early vascular permeability in murine experimental peritonitis is comediated by resident peritoneal macrophages and mast cells: crucial involvement of macrophage-derived cysteinyl-leukotrienes. Inflammation 26 (2002) 61-71
    • (2002) Inflammation , vol.26 , pp. 61-71
    • Kolaczkowska, E.1    Shahzidi, S.2    Seljelid, R.3    van Rooijen, N.4    Plytycz, B.5
  • 25
    • 33644762881 scopus 로고    scopus 로고
    • Gelatinase B/matrix metalloproteinase-9 contributes to cellular infiltration in a murine model of zymosan peritonitis
    • Kolaczkowska E., Chadzinska M., Scislowska-Czarnecka A., Plytycz B., Opdenakker G., and Arnold B. Gelatinase B/matrix metalloproteinase-9 contributes to cellular infiltration in a murine model of zymosan peritonitis. Immunobiol 211 (2006) 137-148
    • (2006) Immunobiol , vol.211 , pp. 137-148
    • Kolaczkowska, E.1    Chadzinska, M.2    Scislowska-Czarnecka, A.3    Plytycz, B.4    Opdenakker, G.5    Arnold, B.6
  • 26
    • 33747606272 scopus 로고    scopus 로고
    • Enhanced early vascular permeability in gelatinase B (MMP-9)-deficient mice: putative contribution of COX-1-derived PGE2 of macrophage origin
    • Kolaczkowska E., Scislowska-Czarnecka A., Chadzinska M., Plytycz B., van Rooijen N., Opdenakker G., and Arnold B. Enhanced early vascular permeability in gelatinase B (MMP-9)-deficient mice: putative contribution of COX-1-derived PGE2 of macrophage origin. J. Leukoc. Biol. 80 (2006) 125-132
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 125-132
    • Kolaczkowska, E.1    Scislowska-Czarnecka, A.2    Chadzinska, M.3    Plytycz, B.4    van Rooijen, N.5    Opdenakker, G.6    Arnold, B.7
  • 27
    • 0346749451 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan
    • Larsen P.H., Wells J.E., Stallcup W.B., Opdenakker G., and Yong V.W. Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan. J. Neurosci. 23 (2003) 11127-11135
    • (2003) J. Neurosci. , vol.23 , pp. 11127-11135
    • Larsen, P.H.1    Wells, J.E.2    Stallcup, W.B.3    Opdenakker, G.4    Yong, V.W.5
  • 28
    • 0034646879 scopus 로고    scopus 로고
    • Activation and inhibition of mast cells degranulation affect their morphometric parameters
    • Levi-Schaffer F., Slovik D., Armetti L., Pickholtz D., and Touitou E. Activation and inhibition of mast cells degranulation affect their morphometric parameters. Life Sci. 66 (2000) PL283-PL290
    • (2000) Life Sci. , vol.66
    • Levi-Schaffer, F.1    Slovik, D.2    Armetti, L.3    Pickholtz, D.4    Touitou, E.5
  • 29
    • 0032521238 scopus 로고    scopus 로고
    • Stromelysin-1 (MMP-3)-independent gelatinase expression and activation in mice
    • Lijnen H.R., Silence J., Van Hoef B., and Collen D. Stromelysin-1 (MMP-3)-independent gelatinase expression and activation in mice. Blood 91 (1998) 2045-2053
    • (1998) Blood , vol.91 , pp. 2045-2053
    • Lijnen, H.R.1    Silence, J.2    Van Hoef, B.3    Collen, D.4
  • 30
    • 0021732056 scopus 로고
    • Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages
    • Mainardi C.L., Hibbs M.S., Hasty K.A., and Seyer J.M. Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages. Coll. Relat. Res. 4 (1984) 479-492
    • (1984) Coll. Relat. Res. , vol.4 , pp. 479-492
    • Mainardi, C.L.1    Hibbs, M.S.2    Hasty, K.A.3    Seyer, J.M.4
  • 31
    • 0031049458 scopus 로고    scopus 로고
    • Production and characterization of recombinant active mouse gelatinase B from eukaryotic cells and in vivo effects after intravenous administration
    • Masure S., Paemen L., Van Aelst I., Fiten P., Proost P., Billiau A., Van Damme J., and Opdenakker G. Production and characterization of recombinant active mouse gelatinase B from eukaryotic cells and in vivo effects after intravenous administration. Eur. J. Biochem. 244 (1997) 21-30
    • (1997) Eur. J. Biochem. , vol.244 , pp. 21-30
    • Masure, S.1    Paemen, L.2    Van Aelst, I.3    Fiten, P.4    Proost, P.5    Billiau, A.6    Van Damme, J.7    Opdenakker, G.8
  • 32
    • 33846395782 scopus 로고    scopus 로고
    • Mast cell-expressed complement receptor, not TLR2, is the main detector of zymosan in peritonitis
    • Mullaly S.C., and Kubes P. Mast cell-expressed complement receptor, not TLR2, is the main detector of zymosan in peritonitis. Eur. J. Immunol. 37 (2007) 224-234
    • (2007) Eur. J. Immunol. , vol.37 , pp. 224-234
    • Mullaly, S.C.1    Kubes, P.2
  • 33
    • 0026903364 scopus 로고
    • The matrix metalloproteinases and their inhibitors
    • Murphy G., and Docherty A.J. The matrix metalloproteinases and their inhibitors. Am. J. Respir. Cell Mol. Biol. 7 (1992) 120-125
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.7 , pp. 120-125
    • Murphy, G.1    Docherty, A.J.2
  • 34
    • 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 B.S., Timshel S., Kjeldsen L., Sehested M., Pyke C., Borregaard N., and Dano K. 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 (1996) 57-62
    • (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    Dano, K.7
  • 35
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9
    • Ogata Y., Enghild J.J., and Nagase H. Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J. Biol. Chem. 267 (1992) 3581-3584
    • (1992) J. Biol. Chem. , vol.267 , pp. 3581-3584
    • Ogata, Y.1    Enghild, J.J.2    Nagase, H.3
  • 36
    • 0028328881 scopus 로고
    • Cytokine-regulated proteases in autoimmune diseases
    • Opdenakker G., and Van Damme J. Cytokine-regulated proteases in autoimmune diseases. Immunol. Today 15 (1994) 103-107
    • (1994) Immunol. Today , vol.15 , pp. 103-107
    • Opdenakker, G.1    Van Damme, J.2
  • 41
    • 0029584651 scopus 로고
    • Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity
    • Paemen L., Martens E., Masure S., and Opdenakker G. Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity. Eur. J. Biochem. 234 (1995) 759-765
    • (1995) Eur. J. Biochem. , vol.234 , pp. 759-765
    • Paemen, L.1    Martens, E.2    Masure, S.3    Opdenakker, G.4
  • 42
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks W.C., Wilson C.L., and Lopez-Boado Y.S. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat. Rev. Immunol. 4 (2004) 617-629
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 44
    • 0028358843 scopus 로고
    • In vivo characterization of zymosan-induced mouse peritoneal inflammation
    • Rao T.S., Currie J.L., Shaffer A.F., and Isakson P.C. In vivo characterization of zymosan-induced mouse peritoneal inflammation. J. Pharmacol. Exp. Ther. 269 (1994) 917-925
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 917-925
    • Rao, T.S.1    Currie, J.L.2    Shaffer, A.F.3    Isakson, P.C.4
  • 46
    • 3142615279 scopus 로고    scopus 로고
    • Rapid, simple, and reliable method for the diagnosis of CAPD peritonitis using the new MMP-9 test kit
    • Ro Y., Hamada C., Io H., Hayashi K., Hirahara I., and Tomino Y. Rapid, simple, and reliable method for the diagnosis of CAPD peritonitis using the new MMP-9 test kit. J. Clin. Lab. Anal. 18 (2004) 224-230
    • (2004) J. Clin. Lab. Anal. , vol.18 , pp. 224-230
    • Ro, Y.1    Hamada, C.2    Io, H.3    Hayashi, K.4    Hirahara, I.5    Tomino, Y.6
  • 47
    • 0016310888 scopus 로고
    • Presence of a gelatin-specific proteinase and its latent form in human leucocytes
    • Sopata I., and Dancewicz A.M. Presence of a gelatin-specific proteinase and its latent form in human leucocytes. Biochim. Biophys. Acta 370 (1974) 510-523
    • (1974) Biochim. Biophys. Acta , vol.370 , pp. 510-523
    • Sopata, I.1    Dancewicz, A.M.2
  • 48
    • 2942585298 scopus 로고    scopus 로고
    • IgE crosslinkage of Fcepsilon receptor I induces both production and activation of matrix metalloproteinase-9 in mast cells
    • Tanaka A., and Matsuda H. IgE crosslinkage of Fcepsilon receptor I induces both production and activation of matrix metalloproteinase-9 in mast cells. Cell Immunol. 228 (2004) 66-75
    • (2004) Cell Immunol. , vol.228 , pp. 66-75
    • Tanaka, A.1    Matsuda, H.2
  • 49
    • 0033214269 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 production, a newly identified function of mast cell progenitors, is downregulated by c-kit receptor activation
    • Tanaka A., Arai K., Kitamura Y., and Matsuda H. Matrix metalloproteinase-9 production, a newly identified function of mast cell progenitors, is downregulated by c-kit receptor activation. Blood 94 (1999) 2390-2395
    • (1999) Blood , vol.94 , pp. 2390-2395
    • Tanaka, A.1    Arai, K.2    Kitamura, Y.3    Matsuda, H.4
  • 50
    • 0035406562 scopus 로고    scopus 로고
    • Mast cell MMP-9 production enhanced by bacterial lipopolysaccharide
    • Tanaka A., Yamane Y., and Matsuda H. Mast cell MMP-9 production enhanced by bacterial lipopolysaccharide. J. Vet. Med. Sci. 63 (2001) 811-813
    • (2001) J. Vet. Med. Sci. , vol.63 , pp. 811-813
    • Tanaka, A.1    Yamane, Y.2    Matsuda, H.3
  • 51
    • 15744388309 scopus 로고    scopus 로고
    • A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2
    • Tchougounova E., Lundequist A., Fajardo I., Winberg J.O., Abrink M., and Pejler G. A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2. J. Biol. Chem. 280 (2005) 9291-9296
    • (2005) J. Biol. Chem. , vol.280 , pp. 9291-9296
    • Tchougounova, E.1    Lundequist, A.2    Fajardo, I.3    Winberg, J.O.4    Abrink, M.5    Pejler, G.6
  • 52
    • 33745267254 scopus 로고    scopus 로고
    • Cloudy peritoneal dialysate: it's not always infection
    • Teitelbaum I. Cloudy peritoneal dialysate: it's not always infection. Contrib. Nephrol. 150 (2006) 187-194
    • (2006) Contrib. Nephrol. , vol.150 , pp. 187-194
    • Teitelbaum, I.1
  • 54
    • 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 H.E., and Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87 (1990) 5578-5582
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 55
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: regulating cellular ecology
    • Werb Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91 (1997) 439-442
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.