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Volumn 65, Issue 2, 1999, Pages 137-150

The cell biology of leukocyte-mediated proteolysis

Author keywords

Inflammation; Proteinase; Proteinase inhibitor

Indexed keywords

CATHEPSIN B; CATHEPSIN D; CATHEPSIN G; CATHEPSIN H; CATHEPSIN L; CATHEPSIN S; CHYMASE; COLLAGENASE; GELATINASE; GELATINASE B; LEUKOCYTE ELASTASE; MATRILYSIN; PROTEINASE; STROMELYSIN; TRYPTASE; UROKINASE;

EID: 0033056463     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.65.2.137     Document Type: Review
Times cited : (371)

References (164)
  • 1
    • 0027968059 scopus 로고
    • Structure of the azurocidin, proteinase 3, and neutrophil elastase genes. Implications for inflammation and vasculitis
    • Jenne, D. E. (1994) Structure of the azurocidin, proteinase 3, and neutrophil elastase genes. Implications for inflammation and vasculitis. Am. J. Respir. Crit. Care Med. 150, 5147-5154.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.150 , pp. 5147-5154
    • Jenne, D.E.1
  • 4
    • 0023937510 scopus 로고
    • Structure, function, and control of neutrophil proteinases
    • Travis, J. (1988) Structure, function, and control of neutrophil proteinases, Am. J. Med. 84 (Suppl. 6A), 37-42.
    • (1988) Am. J. Med. , vol.84 , Issue.SUPPL. 6A , pp. 37-42
    • Travis, J.1
  • 5
    • 0017350112 scopus 로고
    • Proteases from purulent sputum. Purification and properties of the elastase and chymotrypsin-like enzymes
    • Twumasi, D. Y., Liener, I. E. (1977) Proteases from purulent sputum. Purification and properties of the elastase and chymotrypsin-like enzymes. J. Biol. Chem. 252, 1917-1926.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1917-1926
    • Twumasi, D.Y.1    Liener, I.E.2
  • 6
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J., Salvesen, G. S. (1983) Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52, 655-709.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 7
    • 0022348139 scopus 로고
    • Cell-mediated extracellular acidification and bone resorption: Evidence for a low pH in resorbing lacunae and localization of a 100 kD lysosomal membrane protein at the osteoclast ruffled border
    • Baron, R., Neff, L., Louvard, D., Courtoy, P. J. (1985) Cell-mediated extracellular acidification and bone resorption: Evidence for a low pH in resorbing lacunae and localization of a 100 kD lysosomal membrane protein at the osteoclast ruffled border. J. Cell Biol. 101, 2210-2222.
    • (1985) J. Cell Biol. , vol.101 , pp. 2210-2222
    • Baron, R.1    Neff, L.2    Louvard, D.3    Courtoy, P.J.4
  • 8
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar proton pump
    • Blair, H. C., Teitelbaum, S. L., Ghiselli, R., Gluck, S. (1989) Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 245, 855-857.
    • (1989) Science , vol.245 , pp. 855-857
    • Blair, H.C.1    Teitelbaum, S.L.2    Ghiselli, R.3    Gluck, S.4
  • 9
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath, H. (1981) Evolution of proteolytic enzymes, Science 224, 350-357.
    • (1981) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 10
    • 0022852281 scopus 로고
    • 1-antitrypsin: Molecular pathology, leukocytes, and tissue damage
    • 1-antitrypsin: Molecular pathology, leukocytes, and tissue damage. J. Clin. Invest. 78, 1427-1431.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1427-1431
    • Carrell, R.W.1
  • 12
    • 0027546780 scopus 로고
    • Secretion of mucus proteinase inhibitor and elafin by clara cell and type II pneumocyte cell lines
    • Sallenave, J.-M., Silva, A., Marsden, M. E., Ryle, A. P. (1993) Secretion of mucus proteinase inhibitor and elafin by Clara cell and type II pneumocyte cell lines. Am. J. Respir. Cell Mol. Biol. 8, 126-133.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 126-133
    • Sallenave, J.-M.1    Silva, A.2    Marsden, M.E.3    Ryle, A.P.4
  • 14
    • 0023214640 scopus 로고
    • Molecular cloning of human cathepsin G: Structural similarity to mast cell and cytotoxic T lymphocyte proteinases
    • Salvesen, G., Farley, D., Shuman, J., Przybyla, A., Reilly, C., Travis, J. (1987) Molecular cloning of human cathepsin G: Structural similarity to mast cell and cytotoxic T lymphocyte proteinases. Biochemistry 26, 2289-2293.
    • (1987) Biochemistry , vol.26 , pp. 2289-2293
    • Salvesen, G.1    Farley, D.2    Shuman, J.3    Przybyla, A.4    Reilly, C.5    Travis, J.6
  • 15
    • 0019800423 scopus 로고
    • Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G
    • Boudier, C., Holle, C., Bieth, J. G. (1981) Stimulation of the elastolytic activity of leukocyte elastase by leukocyte cathepsin G. J. Biol. Chem. 256, 10256-10258.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10256-10258
    • Boudier, C.1    Holle, C.2    Bieth, J.G.3
  • 16
    • 0020312338 scopus 로고
    • Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases
    • Reilly, C. F., Tewksbury, D. A., Schechter, N. M., Travis, J. (1982) Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases. J. Biol. Chem. 257, 8619-8622.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8619-8622
    • Reilly, C.F.1    Tewksbury, D.A.2    Schechter, N.M.3    Travis, J.4
  • 17
    • 0025694843 scopus 로고
    • Cloning of cDNA for proteinase 3: A serine protease, antibiotic, and autoantigen from human neutrophils
    • Campanelli, D., Melchior, M., Fu, Y., Nakata, M., Shuman, H., Nathan, C., Gabay, J. E. (1990) Cloning of cDNA for proteinase 3: A serine protease, antibiotic, and autoantigen from human neutrophils. J. Exp. Med. 172, 1709-1715.
    • (1990) J. Exp. Med. , vol.172 , pp. 1709-1715
    • Campanelli, D.1    Melchior, M.2    Fu, Y.3    Nakata, M.4    Shuman, H.5    Nathan, C.6    Gabay, J.E.7
  • 19
    • 0025353345 scopus 로고
    • Specificity of anti-neutrophil cytoplasmic autoantibodies for proteinase 3
    • Jennette, J. C., Hoidal, J. R., Falk, R. J. (1990) Specificity of anti-neutrophil cytoplasmic autoantibodies for proteinase 3. Blood 75, 2263-2265.
    • (1990) Blood , vol.75 , pp. 2263-2265
    • Jennette, J.C.1    Hoidal, J.R.2    Falk, R.J.3
  • 20
    • 0026070031 scopus 로고
    • Proteinase 3, the target antigen of anticytoplasmic antibodies circulating in Wegener's granulomatosis. Immunolocalization in normal and pathologic tissues
    • Braun, M. G., Csernok, E., Gross, W. L., Muller-Hermelink, H. K. (1991) Proteinase 3, the target antigen of anticytoplasmic antibodies circulating in Wegener's granulomatosis. Immunolocalization in normal and pathologic tissues. Am. J. Pathol. 39, 831-338.
    • (1991) Am. J. Pathol. , vol.39 , pp. 831-1338
    • Braun, M.G.1    Csernok, E.2    Gross, W.L.3    Muller-Hermelink, H.K.4
  • 21
    • 0025345612 scopus 로고
    • Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro
    • Falk, R. J., Terrell, R. S., Charles, L. A., Jennette, J. C. (1990) Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro. Proc. Natl. Acad. Sci. USA 87, 4115-4119.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4115-4119
    • Falk, R.J.1    Terrell, R.S.2    Charles, L.A.3    Jennette, J.C.4
  • 22
  • 23
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E., Seiki, M. (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61-65.
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 24
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family
    • Takino, T. H., Sato, H., Shinagawa, A., Seiki, M. (1995) Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J. Biol. Chem. 270, 23013-23020.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23013-23020
    • Takino, T.H.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 25
    • 0024009517 scopus 로고
    • Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase
    • Desrochers, P. E., Weiss, S. J. (1988) Proteolytic inactivation of alpha-1-proteinase inhibitor by a neutrophil metalloproteinase. J. Clin. Invest. 81, 1646-1650.
    • (1988) J. Clin. Invest. , vol.81 , pp. 1646-1650
    • Desrochers, P.E.1    Weiss, S.J.2
  • 26
    • 0025991867 scopus 로고
    • Interstitial collagenase (matrix metalloproteinase-1) expresses serpiriase activity
    • Desrochers, P. E., Jeffrey, J. J., Weiss, S. J. (1991) Interstitial collagenase (matrix metalloproteinase-1) expresses serpiriase activity. J. Clin. Invest. 87, 2258-2265.
    • (1991) J. Clin. Invest. , vol.87 , pp. 2258-2265
    • Desrochers, P.E.1    Jeffrey, J.J.2    Weiss, S.J.3
  • 27
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner, J. F., 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 J.F., Jr.1
  • 28
    • 0030911308 scopus 로고    scopus 로고
    • The regulation of neovascularization by matrix metalloproteinases and their inhibitors
    • Moses, M. A. (1997) The regulation of neovascularization by matrix metalloproteinases and their inhibitors. Stem Cells 15, 180-189.
    • (1997) Stem Cells , vol.15 , pp. 180-189
    • Moses, M.A.1
  • 29
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk, B., Turk, V., Turk, D. (1997) Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378, 141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 33
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin s, an elastinolytic cysteine protease
    • Shi, G. -P., Munger, J. S., Meara, J. P., Rich, D. H., Chapman, H. A. (1992) Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J. Biol. Chem. 267, 7258-7262.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7258-7262
    • Shi, G.-P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 34
    • 0026471694 scopus 로고
    • The aspartic proteases
    • Szecsi, P. B. (1992) The aspartic proteases. Scand. J. Clin. Lab. Invest. 52 (Suppl. 210), 5-22.
    • (1992) Scand. J. Clin. Lab. Invest. , vol.52 , Issue.SUPPL. 210 , pp. 5-22
    • Szecsi, P.B.1
  • 37
    • 0002016013 scopus 로고
    • Elastases: Catalytic and biological properties
    • (R. P. Mecham, ed.) Orlando. FL: Academic Press.
    • Bieth, J. G. (1986) Elastases: Catalytic and biological properties. In Biology of Extracellular Matrix: Regulation of Matrix Accumulation (R. P. Mecham, ed.) Orlando. FL: Academic Press. 217-320.
    • (1986) Biology of Extracellular Matrix: Regulation of Matrix Accumulation , pp. 217-320
    • Bieth, J.G.1
  • 38
    • 0019857661 scopus 로고
    • The collagen substrate specificity of human skin fibroblast collagenase
    • Welgus, H. G., Jeffrey, J. J., Eisen, A. Z. (1981) The collagen substrate specificity of human skin fibroblast collagenase. J. Biol. Chem. 256, 9511-9515.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9511-9515
    • Welgus, H.G.1    Jeffrey, J.J.2    Eisen, A.Z.3
  • 39
    • 0013804986 scopus 로고
    • Specific degradation of the collagen molecule by tadpole collagenolytic enzyme
    • Gross, J., Nagai, Y. (1965) Specific degradation of the collagen molecule by tadpole collagenolytic enzyme. Proc. Natl. Acad. Sci. USA 54, 1197-1204.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1197-1204
    • Gross, J.1    Nagai, Y.2
  • 40
    • 0021918104 scopus 로고
    • Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase
    • Hibbs, M. S., Hasty, K. A., Seyer, J. M., Kang, A. H., Mainardi, C. L. (1985) Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J. Biol. Chem. 260, 2493-2500.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2493-2500
    • Hibbs, M.S.1    Hasty, K.A.2    Seyer, J.M.3    Kang, A.H.4    Mainardi, C.L.5
  • 41
    • 4243351682 scopus 로고
    • Secretion of a metalloproteinase by human alveolar macrophages which degrades gelatin and native type V collagen
    • Hibbs, M. S., Hoidal, J. R., Kang, A. H. (1985) Secretion of a metalloproteinase by human alveolar macrophages which degrades gelatin and native type V collagen. J. Cell. Biol. 101, 216A.
    • (1985) J. Cell. Biol. , vol.101
    • Hibbs, M.S.1    Hoidal, J.R.2    Kang, A.H.3
  • 43
    • 0021913597 scopus 로고
    • Degradation of monomeric and fibrillar type III collagens by human skin collagenase: Kinetic constants using different animal substrates
    • Welgus, H. G., Burgesun, R. E., Wootton, J. A. M., Minor, R. R., Fliszar, C., Jeffrey, J. J. (1985) Degradation of monomeric and fibrillar type III collagens by human skin collagenase: Kinetic constants using different animal substrates. J. Biol. Chem. 260, 1052-1059.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1052-1059
    • Welgus, H.G.1    Burgesun, R.E.2    Wootton, J.A.M.3    Minor, R.R.4    Fliszar, C.5    Jeffrey, J.J.6
  • 44
    • 0024146930 scopus 로고
    • Cell-associated plasminogen activation: Regulation and physiological functions
    • Saksela, O., Rifkin, D. B. (1988) Cell-associated plasminogen activation: Regulation and physiological functions. Annu. Rev. Cell Biol. 4, 93-126.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 93-126
    • Saksela, O.1    Rifkin, D.B.2
  • 45
    • 0019962792 scopus 로고
    • Release of gelatinase from a novel secretory compartment of human neutrophils
    • Dewald, B., Bretz, U., Baggiolini, M. (1982) Release of gelatinase from a novel secretory compartment of human neutrophils. J. Clin. Invest. 70, 518-525.
    • (1982) J. Clin. Invest. , vol.70 , pp. 518-525
    • Dewald, B.1    Bretz, U.2    Baggiolini, M.3
  • 46
    • 0028031885 scopus 로고
    • The receptor for urokinase-type plasminogen activator and urokinase is translocated from two distinct intracellular compartments to the plasma membrane on stimulation of human neutrophils
    • Plesner, T., Ploug, M., Ellis, V., Ronne, E., Hoyer-Hansen, G., Wittrup, M., Pedersen, T. L., Tscherning, T., Dano, K., Hansen, N. E. (1994) The receptor for urokinase-type plasminogen activator and urokinase is translocated from two distinct intracellular compartments to the plasma membrane on stimulation of human neutrophils. Blood 83, 808-815.
    • (1994) Blood , vol.83 , pp. 808-815
    • Plesner, T.1    Ploug, M.2    Ellis, V.3    Ronne, E.4    Hoyer-Hansen, G.5    Wittrup, M.6    Pedersen, T.L.7    Tscherning, T.8    Dano, K.9    Hansen, N.E.10
  • 47
    • 0024430531 scopus 로고
    • Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity
    • Campbell, E. J., Silverman, E. K., Campbell, M. A. (1989) Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity. J. Immunol. 143, 2961-2968.
    • (1989) J. Immunol. , vol.143 , pp. 2961-2968
    • Campbell, E.J.1    Silverman, E.K.2    Campbell, M.A.3
  • 48
    • 0028802595 scopus 로고
    • Inducible binding of cathepsin g to the cell surface of neutrophils: A mechanism for mediating extracellular proteolytic activity of cathepsin G
    • Owen, C. A., Campbell, M. A., Boukedes, S. S., Campbell, E. J. (1995) Inducible binding of cathepsin G to the cell surface of neutrophils: A mechanism for mediating extracellular proteolytic activity of cathepsin G. J. Immunol. 155, 5803-5810.
    • (1995) J. Immunol. , vol.155 , pp. 5803-5810
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 49
    • 0030948848 scopus 로고    scopus 로고
    • Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity
    • Owen, C. A., Campbell, M. A., Boukedes, S. S., Campbell, E. J. (1997) Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity. Am. J. Physiol. 272. L385-L393.
    • (1997) Am. J. Physiol. , vol.272
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 50
    • 0022461972 scopus 로고
    • Human neutrophil plasminogen activator is localized in specific granules and is translocated to the cell surface by exocytosis
    • Heiple, J. M., Ossowski, L. (1986) Human neutrophil plasminogen activator is localized in specific granules and is translocated to the cell surface by exocytosis. J. Exp. Med. 164, 826-840.
    • (1986) J. Exp. Med. , vol.164 , pp. 826-840
    • Heiple, J.M.1    Ossowski, L.2
  • 51
    • 0021088716 scopus 로고
    • Neutral proteinases from human inflammatory cells: A critical review of their role in extracellular matrix degradation
    • Senior, R. M., Campbell, E. J. (1983) Neutral proteinases from human inflammatory cells: A critical review of their role in extracellular matrix degradation. Clin. Lab. Med. 3, 645-666.
    • (1983) Clin. Lab. Med. , vol.3 , pp. 645-666
    • Senior, R.M.1    Campbell, E.J.2
  • 52
    • 0025291828 scopus 로고
    • Elastase and cathepsin G of human monocytes. Heterogeneity and subcellular localization to peroxidase-positive granules
    • Kargi, H. A., Campbell, E. J., Kuhn, C., III (1990) Elastase and cathepsin G of human monocytes. Heterogeneity and subcellular localization to peroxidase-positive granules. J. Histoehem. Cytochem. 38, 1179-1186.
    • (1990) J. Histoehem. Cytochem. , vol.38 , pp. 1179-1186
    • Kargi, H.A.1    Campbell, E.J.2    Kuhn C. III3
  • 53
    • 0028607459 scopus 로고
    • A discrete subpopulation of human monocytes expresses a neutrophil-like pro-inflammatory (P) phenotype
    • Owen, C. A., Campbell, M. A., Boukedes, S. S., Stockley, R. A., Campbell, E. J. (1994) A discrete subpopulation of human monocytes expresses a neutrophil-like pro-inflammatory (P) phenotype. Am. J. Physiol. 267, L775-L785.
    • (1994) Am. J. Physiol. , vol.267
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Stockley, R.A.4    Campbell, E.J.5
  • 54
    • 0028575729 scopus 로고
    • Monocytes recruited to sites of inflammation express a distinctive pro-inflammatory (P) phenotype
    • Owen, C. A., Campbell, M. A., Boukedes, S. S., Campbell, E. J. (1994) Monocytes recruited to sites of inflammation express a distinctive pro-inflammatory (P) phenotype. Am. J. Physiol. 267, L786-L796.
    • (1994) Am. J. Physiol. , vol.267
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 55
    • 0025336879 scopus 로고
    • The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes
    • Estreicher, A., Muhlhauser, J., Carpentier, J.-L., Orci, L., Vassalli, J.-D. (1990) The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes. J. Cell Biol. 111, 783-792.
    • (1990) J. Cell Biol. , vol.111 , pp. 783-792
    • Estreicher, A.1    Muhlhauser, J.2    Carpentier, J.-L.3    Orci, L.4    Vassalli, J.-D.5
  • 56
    • 0024420806 scopus 로고
    • Endogenous receptor-bound urokinase mediates tissue invasion of human monocytes
    • Kirchheimer, J. C., Remold, H. G. (1989) Endogenous receptor-bound urokinase mediates tissue invasion of human monocytes. J. Immunol. 143, 2634-2639.
    • (1989) J. Immunol. , vol.143 , pp. 2634-2639
    • Kirchheimer, J.C.1    Remold, H.G.2
  • 57
    • 0023665299 scopus 로고
    • Monocyte procollagenase and tissue inhibitor of metalloproteinases: Identification, characterization, and regulation of secretion
    • Campbell, E. J., Cury, J. D., Lazarus, C. J., Welgus, H. G. (1987) Monocyte procollagenase and tissue inhibitor of metalloproteinases: Identification, characterization, and regulation of secretion. J. Biol. Chem. 262, 15862-15868.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15862-15868
    • Campbell, E.J.1    Cury, J.D.2    Lazarus, C.J.3    Welgus, H.G.4
  • 58
    • 0026785711 scopus 로고
    • The matrix metalloprotease matrilysin (PUMP) is expressed in developing human mononuclear phagocytes
    • Busiek, D. F., Ross, F. P., McDonnell, S., Murphy, G., Matrisian, L. M., Welgus, H. G. (1992) The matrix metalloprotease matrilysin (PUMP) is expressed in developing human mononuclear phagocytes. J. Biol. Chem. 267, 9087-9092.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9087-9092
    • Busiek, D.F.1    Ross, F.P.2    McDonnell, S.3    Murphy, G.4    Matrisian, L.M.5    Welgus, H.G.6
  • 59
    • 0026033779 scopus 로고
    • Neutral proteinases of human mononuclear phagocytes. Cellular differentiation markedly alters cell phenotype for serine proteinases, metalloproteinases, and TIMP
    • Campbell, E. J., Cury, J. D., Shapiro, S. D., Goldberg, G. I., Welgus, H. G. (1991) Neutral proteinases of human mononuclear phagocytes. Cellular differentiation markedly alters cell phenotype for serine proteinases, metalloproteinases, and TIMP. J. Immunol. 146, 1286-1293.
    • (1991) J. Immunol. , vol.146 , pp. 1286-1293
    • Campbell, E.J.1    Cury, J.D.2    Shapiro, S.D.3    Goldberg, G.I.4    Welgus, H.G.5
  • 60
    • 0018695175 scopus 로고
    • Receptor-mediated binding and internalization of leukocyte elastase by alveolar macrophages in vitro
    • Campbell, E. J., White, R. R., Senior, R. M., Rodriguez, R. J., Kuhn, C., III (1979) Receptor-mediated binding and internalization of leukocyte elastase by alveolar macrophages in vitro. J. Clin. Invest. 64, 824-833.
    • (1979) J. Clin. Invest. , vol.64 , pp. 824-833
    • Campbell, E.J.1    White, R.R.2    Senior, R.M.3    Rodriguez, R.J.4    Kuhn C. III5
  • 61
    • 0019953384 scopus 로고
    • Evidence for in vitro internalization of human leukocyte elastase by human alveolar macrophages
    • White, R. R., Janoff, A., Gordon, R., Camphell, E. J. (1982) Evidence for in vitro internalization of human leukocyte elastase by human alveolar macrophages. Am. Rev. Respir. Dis. 125, 779-781.
    • (1982) Am. Rev. Respir. Dis. , vol.125 , pp. 779-781
    • White, R.R.1    Janoff, A.2    Gordon, R.3    Camphell, E.J.4
  • 62
    • 0020375565 scopus 로고
    • Human leukocyte elastase, cathepsin g, and lactoferrin: A family of neutrophil granule glycoproteins which bind to an alveolar macrophage receptor
    • Campbell, E. J. (1982) Human leukocyte elastase, cathepsin G, and lactoferrin: A family of neutrophil granule glycoproteins which bind to an alveolar macrophage receptor. Proc. Natl. Acad. Sci. USA 79, 6941-6945.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6941-6945
    • Campbell, E.J.1
  • 63
    • 0024536234 scopus 로고
    • Macrophage phagocytosis of aging neutrophils in inflammation. Programmed cell death in the neutrophil leads to its recognition by macrophages
    • Savill, J. S., Wyllie, A. H., Henson, J. E., Walport, M. J., Henson, P. M., Haslett, C. (1989) Macrophage phagocytosis of aging neutrophils in inflammation. Programmed cell death in the neutrophil leads to its recognition by macrophages. J. Clin. Invest. 83, 865-875.
    • (1989) J. Clin. Invest. , vol.83 , pp. 865-875
    • Savill, J.S.1    Wyllie, A.H.2    Henson, J.E.3    Walport, M.J.4    Henson, P.M.5    Haslett, C.6
  • 64
    • 0020569945 scopus 로고
    • Hypoxic injury to human alveolar macrophages accelerates release of previously bound neutrophil elastase: Implications for lung connective tissue injury including pulmonary emphysema
    • Campbell, E. J., Wald, M. S. (1983) Hypoxic injury to human alveolar macrophages accelerates release of previously bound neutrophil elastase: Implications for lung connective tissue injury including pulmonary emphysema. Am. Rev. Respir. Dis. 127, 631-635.
    • (1983) Am. Rev. Respir. Dis. , vol.127 , pp. 631-635
    • Campbell, E.J.1    Wald, M.S.2
  • 65
    • 0025696753 scopus 로고
    • Alveolar macrophage urokinase receptors localize enzyme activity to the cell surface
    • Chapman, H. A., Jr., Bertozzi, P., Sailor, L. Z., Nusrat, A. R. (1990) Alveolar macrophage urokinase receptors localize enzyme activity to the cell surface. Am. J. Physiol. 259, 432-438.
    • (1990) Am. J. Physiol. , vol.259 , pp. 432-438
    • Chapman H.A., Jr.1    Bertozzi, P.2    Sailor, L.Z.3    Nusrat, A.R.4
  • 66
    • 0026641093 scopus 로고
    • Urokinase-catalyzed plasminogen activation at the monocyte/macrophage cell surface: A localized and regulated proteolytic system
    • Vassalli, J. D., Wohlwend, A., Belin, D. (1992) Urokinase-catalyzed plasminogen activation at the monocyte/macrophage cell surface: A localized and regulated proteolytic system. Curr. Top. Microbiol. Immunol. 181, 65-86.
    • (1992) Curr. Top. Microbiol. Immunol. , vol.181 , pp. 65-86
    • Vassalli, J.D.1    Wohlwend, A.2    Belin, D.3
  • 67
    • 0027174189 scopus 로고
    • Cytokines induce urokinase-dependent adhesion of human myeloid cells. A regulatory role for plasminogen activator inhibitors
    • Waltz, D. A., Sailor, L. Z., Chapman, H. A. (1993) Cytokines induce urokinase-dependent adhesion of human myeloid cells. A regulatory role for plasminogen activator inhibitors. J. Clin. Invest. 91, 1541-1552.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1541-1552
    • Waltz, D.A.1    Sailor, L.Z.2    Chapman, H.A.3
  • 68
    • 0021253844 scopus 로고
    • Eosinophil-mediated injury to lung parenchymal cells and interstitial matrix. A possible role for eosinophils in chronic inflammatory disorders of the lower respiratory tract
    • Davis, W. B., Fells, G. A., Sun, X.-H., Gadek, J. E., Venet, A., Crystal, R. G. (1984) Eosinophil-mediated injury to lung parenchymal cells and interstitial matrix. A possible role for eosinophils in chronic inflammatory disorders of the lower respiratory tract. J. Clin. Invest. 74, 269-278.
    • (1984) J. Clin. Invest. , vol.74 , pp. 269-278
    • Davis, W.B.1    Fells, G.A.2    Sun, X.-H.3    Gadek, J.E.4    Venet, A.5    Crystal, R.G.6
  • 70
    • 0019471330 scopus 로고
    • Acid hydrolases and tryptase from secretory granules of dispersed human lung mast cells
    • Schwartz, L. B., Lewis, R. A., Seldin, D., Austin, K. F. (1981) Acid hydrolases and tryptase from secretory granules of dispersed human lung mast cells. J. Immunol. 126, 1290-1296.
    • (1981) J. Immunol. , vol.126 , pp. 1290-1296
    • Schwartz, L.B.1    Lewis, R.A.2    Seldin, D.3    Austin, K.F.4
  • 71
    • 0023928915 scopus 로고
    • Activation of latent rheumatoid synovial collagenase by human mast cell tryptase
    • Graber, B. L., Schwartz, L. B., Ramamurthy, N. S., Irani, A. M., Marchese, M. J. (1988) Activation of latent rheumatoid synovial collagenase by human mast cell tryptase. J. Immunol. 140, 3936-3942.
    • (1988) J. Immunol. , vol.140 , pp. 3936-3942
    • Graber, B.L.1    Schwartz, L.B.2    Ramamurthy, N.S.3    Irani, A.M.4    Marchese, M.J.5
  • 72
    • 0024429920 scopus 로고
    • Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation
    • Gruber, B. L., Marchese, M. J., Suzuki, K., Schwartz, L. B., Okada, Y., Nagase, H., Ramamurthy, N. S. (1989) Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation. J. Clin. Invest. 84, 1657-1662.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1657-1662
    • Gruber, B.L.1    Marchese, M.J.2    Suzuki, K.3    Schwartz, L.B.4    Okada, Y.5    Nagase, H.6    Ramamurthy, N.S.7
  • 73
    • 0028113041 scopus 로고
    • Serine proteinases of mast cell and leukocyte granules. A league of their own
    • Caughey, G. H. (1994) Serine proteinases of mast cell and leukocyte granules. A league of their own. Am. J. Respir. Crit. Care Med. 150, S138-S142.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.150
    • Caughey, G.H.1
  • 74
    • 0029838802 scopus 로고    scopus 로고
    • Granzymes: A variety of serine protease specificities encoded by genetically distinct subfamilies
    • Smyth, M. J., O'Connor, M. D., Trapani, J. A. (1996) Granzymes: a variety of serine protease specificities encoded by genetically distinct subfamilies. J. Leukoc. Biol. 60, 555-562.
    • (1996) J. Leukoc. Biol. , vol.60 , pp. 555-562
    • Smyth, M.J.1    O'Connor, M.D.2    Trapani, J.A.3
  • 75
    • 0017651179 scopus 로고
    • Secretion of plasminogen activator by human polymorphonuclear leukocytes
    • Granelli-Peperno, A., Vassalli, J.-D., Reich, E. (1977) Secretion of plasminogen activator by human polymorphonuclear leukocytes. J. Exp. Med. 146, 1693-1706.
    • (1977) J. Exp. Med. , vol.146 , pp. 1693-1706
    • Granelli-Peperno, A.1    Vassalli, J.-D.2    Reich, E.3
  • 76
    • 0023856438 scopus 로고
    • Myelomonocytic cell lineage expression of the neutrophil elastase gene
    • Takahashi, H., Nukiwa, T., Basset, P., Crystal, R. G. (1988) Myelomonocytic cell lineage expression of the neutrophil elastase gene. J. Biol. Chem. 263, 2543-2547.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2543-2547
    • Takahashi, H.1    Nukiwa, T.2    Basset, P.3    Crystal, R.G.4
  • 78
    • 0021619945 scopus 로고
    • Neutrophil specific granules: A fuse that ignites the inflammatory response
    • Gallin, J. I. (1984) Neutrophil specific granules: A fuse that ignites the inflammatory response. Clin. Res. 32, 320-328.
    • (1984) Clin. Res. , vol.32 , pp. 320-328
    • Gallin, J.I.1
  • 80
    • 0028865394 scopus 로고
    • Cell-surface-bound elastase and cathepsin G on human neutrophils. A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Own, C. A., Campbell, M. A., Sannes, P. L., Boukedes, S. S., Campbell, E. J. (1995) Cell-surface-bound elastase and cathepsin G on human neutrophils. A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131, 775-789.
    • (1995) J. Cell Biol. , vol.131 , pp. 775-789
    • Own, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 81
    • 0031939933 scopus 로고    scopus 로고
    • Angiotensin II generation at the cell surface of activated neutrophils: Novel cathepsin G-mediated catalytic activity that is resistant to inhibition
    • Owen, C. A., Campbell, R. J. (1998) Angiotensin II generation at the cell surface of activated neutrophils: Novel cathepsin G-mediated catalytic activity that is resistant to inhibition. J. Imnumol. 160, 1436-1443.
    • (1998) J. Imnumol. , vol.160 , pp. 1436-1443
    • Owen, C.A.1    Campbell, R.J.2
  • 82
    • 0028307148 scopus 로고
    • Activated neutrophils express proteinase 3 on their plasma membrane in vitro and in vivo
    • Csernok, E., Ernst, M., Schmitt, W., Bainton, D. F., Gross, W. L. (1994) Activated neutrophils express proteinase 3 on their plasma membrane in vitro and in vivo. Clin. Exp. Immunol. 95, 244-250.
    • (1994) Clin. Exp. Immunol. , vol.95 , pp. 244-250
    • Csernok, E.1    Ernst, M.2    Schmitt, W.3    Bainton, D.F.4    Gross, W.L.5
  • 83
    • 0023624310 scopus 로고
    • Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells
    • Miles, L. A., Plow, E. F. (1987) Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells. Thromb. Haemost. 58, 936-942.
    • (1987) Thromb. Haemost. , vol.58 , pp. 936-942
    • Miles, L.A.1    Plow, E.F.2
  • 84
    • 0027280211 scopus 로고
    • Regulation of monocyte/macrophage metalloproteinase production by cytokines
    • Wahl, L. M., Corcoran, M. L. (1993) Regulation of monocyte/macrophage metalloproteinase production by cytokines. J. Periodontol. 64, 467-473.
    • (1993) J. Periodontol. , vol.64 , pp. 467-473
    • Wahl, L.M.1    Corcoran, M.L.2
  • 85
    • 0025134586 scopus 로고
    • Immune modulation of metalloproteinase production in human macrophages. Selective suppression of interstitial collagenase and stromelysin biosynthesis by interferon-gamma
    • Shapiro, S. D., Campbell, E. J., Kobayashi, D. K., Welgus, H. G. (1990) Immune modulation of metalloproteinase production in human macrophages. Selective suppression of interstitial collagenase and stromelysin biosynthesis by interferon-gamma. J. Clin. Invest. 86, 1204-1210.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1204-1210
    • Shapiro, S.D.1    Campbell, E.J.2    Kobayashi, D.K.3    Welgus, H.G.4
  • 86
    • 0027023849 scopus 로고
    • Ligand dependent release of activated neutrophil collagenase - A role for surface bound 1gG in the degradation of articular collagens
    • Chatham, W. W., Heck, L. W., Blackburn, W. D. (1992) Ligand dependent release of activated neutrophil collagenase - a role for surface bound 1gG in the degradation of articular collagens. Matrix (Suppl. 1), 207-208.
    • (1992) Matrix , Issue.SUPPL. 1 , pp. 207-208
    • Chatham, W.W.1    Heck, L.W.2    Blackburn, W.D.3
  • 87
    • 0027015335 scopus 로고
    • Physiological mechanisms for metalloproteinase activation
    • Murphy, G., Ward, R., Gavrilovic, J., Atkinson, S. (1992) Physiological mechanisms for metalloproteinase activation. Matrix (Suppl. 1), 224-230.
    • (1992) Matrix , Issue.SUPPL. 1 , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 88
    • 0030025404 scopus 로고    scopus 로고
    • Activation of human neutrophil procollageriase by stromelysin 2
    • Knauper, V., Murphy, G., Tschesche, H. (1996) Activation of human neutrophil procollageriase by stromelysin 2. Eur. J. Biochem. 235, 187-191.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 187-191
    • Knauper, V.1    Murphy, G.2    Tschesche, H.3
  • 90
    • 0031570730 scopus 로고    scopus 로고
    • Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: A novel mechanism for procollagenase activation involving nitric oxide
    • Okamoto, T., Akaike, T. Nagano, T., Miyajima, S., Suga, M., Ando, M., Ichimori, K., Maeda, H. (1997) Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: A novel mechanism for procollagenase activation involving nitric oxide. Arch. Biochem. Biophys. 342, 261-274.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 261-274
    • Okamoto, T.1    Akaike, T.2    Nagano, T.3    Miyajima, S.4    Suga, M.5    Ando, M.6    Ichimori, K.7    Maeda, H.8
  • 92
    • 0029910358 scopus 로고    scopus 로고
    • Membrane type matrix inetalloproteinase I activates pro-gelatinase A without furin cleavage of the N-terminal domain
    • Cao, J., Rehemtulla, A., Bahou, W., Zucker, S. (1996) Membrane type matrix inetalloproteinase I activates pro-gelatinase A without furin cleavage of the N-terminal domain. J. Biol. Chem. 271, 30174-30180.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30174-30180
    • Cao, J.1    Rehemtulla, A.2    Bahou, W.3    Zucker, S.4
  • 93
    • 0031039965 scopus 로고    scopus 로고
    • Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases
    • Butler, G. S., Will, H., Atkinson, S. J., Murphy, G. (1997) Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases. Eur. J. Biochem. 244, 653-657.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 653-657
    • Butler, G.S.1    Will, H.2    Atkinson, S.J.3    Murphy, G.4
  • 94
    • 0023840318 scopus 로고
    • Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: Effects of substrate opsonization
    • Campbell, E. J., Campbell, M. A. (1988) Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: Effects of substrate opsonization. J. Cell Biol. 106, 667-676.
    • (1988) J. Cell Biol. , vol.106 , pp. 667-676
    • Campbell, E.J.1    Campbell, M.A.2
  • 95
    • 0013622406 scopus 로고
    • Low molecular weight inhibitors of human leukocyte elastase fail to prevent pericellular proteolytic activity of neutrophils in vitro
    • Abstract
    • Morrison, H. M., Campbell, M. A., Stoekley, R. A., Campbell, E. J. (1988) Low molecular weight inhibitors of human leukocyte elastase fail to prevent pericellular proteolytic activity of neutrophils in vitro. Am. Rev. Respir. Dis. 137, 207 (Abstract).
    • (1988) Am. Rev. Respir. Dis. , vol.137 , pp. 207
    • Morrison, H.M.1    Campbell, M.A.2    Stoekley, R.A.3    Campbell, E.J.4
  • 96
    • 0025359581 scopus 로고
    • Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor
    • Rice, W. G., Weiss, S. J. (1990) Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor. Science 249, 178-181.
    • (1990) Science , vol.249 , pp. 178-181
    • Rice, W.G.1    Weiss, S.J.2
  • 97
    • 0019965228 scopus 로고
    • Proteolysis by neutrophds. Relative importance of cell-substrate contact and oxidative inactivation of proteinase inhibitors in vitro
    • Campbell, E. J., Senior, R. M., McDonald, J. A., Cox, D. L. (1982) Proteolysis by neutrophds. Relative importance of cell-substrate contact and oxidative inactivation of proteinase inhibitors in vitro. J. Clin. Invest. 70, 845-852.
    • (1982) J. Clin. Invest. , vol.70 , pp. 845-852
    • Campbell, E.J.1    Senior, R.M.2    McDonald, J.A.3    Cox, D.L.4
  • 98
    • 0019258204 scopus 로고
    • Inaetivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants
    • Carp, H., Janoff, A. (1980) Inaetivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants. Exp. Lung Res. 1, 225-237.
    • (1980) Exp. Lung Res. , vol.1 , pp. 225-237
    • Carp, H.1    Janoff, A.2
  • 99
    • 0018407613 scopus 로고
    • In vitro suppression of serum elastase-inhibitory capacity by reactive oxygen species generated by phagocytosing polymorphonuclear leukocytes
    • Carp, H., Janoff, A. (1979) In vitro suppression of serum elastase-inhibitory capacity by reactive oxygen species generated by phagocytosing polymorphonuclear leukocytes. J. Clin. Invest. 63, 793-797.
    • (1979) J. Clin. Invest. , vol.63 , pp. 793-797
    • Carp, H.1    Janoff, A.2
  • 100
  • 102
    • 0028104433 scopus 로고
    • Matrilysin is much more efficient than other metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin
    • Sires, U. I., Murphy, G., Welgus, H. G., Senior, R. M. (1994) Matrilysin is much more efficient than other metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin. Biochem. Biophys. Res. Commun. 204, 613-620.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 613-620
    • Sires, U.I.1    Murphy, G.2    Welgus, H.G.3    Senior, R.M.4
  • 103
    • 0026705310 scopus 로고
    • Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichyniotrypsin by oxidatively activated human neutrophil metalloproteinases
    • Desrochers, P. E., Mookhtiar, K., Van Wart, H. E., Hasty, K. A., Weiss, S. J. (1992) Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichyniotrypsin by oxidatively activated human neutrophil metalloproteinases. J. Biol. Chem. 267, 5005-5012.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5005-5012
    • Desrochers, P.E.1    Mookhtiar, K.2    Van Wart, H.E.3    Hasty, K.A.4    Weiss, S.J.5
  • 106
    • 0029134020 scopus 로고
    • The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: The evaluation of its physiologic relevance in fibrinolysis
    • Wu, K., Uano, T., Ihara, H., Takada, Y., Fujie, M., Shikmiori, M., Hashimoto, K., Takada, A. (1995) The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: the evaluation of its physiologic relevance in fibrinolysis. Blood 86, 1056-1061.
    • (1995) Blood , vol.86 , pp. 1056-1061
    • Wu, K.1    Uano, T.2    Ihara, H.3    Takada, Y.4    Fujie, M.5    Shikmiori, M.6    Hashimoto, K.7    Takada, A.8
  • 107
    • 0017389922 scopus 로고
    • 1 proteinase inhibitor by thiol proteinases
    • 1 proteinase inhibitor by thiol proteinases. Biochem. J. 163, 639-641.
    • (1977) Biochem. J. , vol.163 , pp. 639-641
    • Johnson, D.1    Travis, J.2
  • 108
    • 0026252652 scopus 로고
    • Different susceptibility of elastase inhibitors to inactivation by proteinases from Staphylococcus aureus and Pseudomonas aeruginosa
    • Sponer, M., Nick, H.-P., Schnebli, H.-P. (1991) Different susceptibility of elastase inhibitors to inactivation by proteinases from Staphylococcus aureus and Pseudomonas aeruginosa. Biol. Chem. Hoppe-Seyler 372, 963-970.
    • (1991) Biol. Chem. Hoppe-seyler , vol.372 , pp. 963-970
    • Sponer, M.1    Nick, H.-P.2    Schnebli, H.-P.3
  • 109
    • 0023837944 scopus 로고
    • Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases
    • Okada, Y., Watanabe, S., Nakanishi, I., Kishi, J., Hayakawa, T., Watorek, W. Travis, J., Nagase, H. (1988) Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases. FEBS Lett. 229, 157-160.
    • (1988) FEBS Lett. , vol.229 , pp. 157-160
    • Okada, Y.1    Watanabe, S.2    Nakanishi, I.3    Kishi, J.4    Hayakawa, T.5    Watorek, W.6    Travis, J.7    Nagase, H.8
  • 110
    • 0026058281 scopus 로고
    • 1-proteinase inhibitor in infected bronchial secretions from patients with cystic fibrosis
    • 1-proteinase inhibitor in infected bronchial secretions from patients with cystic fibrosis. Eur. Respir. J. 4, 40-49.
    • (1991) Eur. Respir. J. , vol.4 , pp. 40-49
    • Suter, S.1    Chevallier, I.2
  • 115
    • 0021355213 scopus 로고
    • Phagocytosing macrophages exclude proteins from zones of contact with targets
    • Wright, S. D., Silverstein, S. C. (1984) Phagocytosing macrophages exclude proteins from zones of contact with targets. Nature 309, 359-361.
    • (1984) Nature , vol.309 , pp. 359-361
    • Wright, S.D.1    Silverstein, S.C.2
  • 116
    • 0025390464 scopus 로고
    • Inhibition of human leukocyte elastase bound to elastin: Relative ineffectiveness and two mechanisms of inhibitory activity
    • Morrison, H. M., Welgus, H. G., Stockley, R. A., Burnett, D., Campbell, E. J. (1990) Inhibition of human leukocyte elastase bound to elastin: Relative ineffectiveness and two mechanisms of inhibitory activity. Am. J. Respir. Cell Mol. Biol. 2, 263-269.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.2 , pp. 263-269
    • Morrison, H.M.1    Welgus, H.G.2    Stockley, R.A.3    Burnett, D.4    Campbell, E.J.5
  • 117
    • 0022461518 scopus 로고
    • 1-proteinase inhibitor and bronchial inhibitor. Potent inhibition of elastin-bound elastase by bronchial inhibitor
    • 1-proteinase inhibitor and bronchial inhibitor. Potent inhibition of elastin-bound elastase by bronchial inhibitor. Biochem. J. 238, 269-273.
    • (1986) Biochem. J. , vol.238 , pp. 269-273
    • Bruch, M.1    Bieth, J.G.2
  • 119
    • 0023189021 scopus 로고
    • Receptor mediated binding of leukocyte elastase by chondrocytes
    • Bartholomew, J., Lowther, D. A. (1987) Receptor mediated binding of leukocyte elastase by chondrocytes. Arthritis Rheum. 30, 431-438.
    • (1987) Arthritis Rheum. , vol.30 , pp. 431-438
    • Bartholomew, J.1    Lowther, D.A.2
  • 120
    • 9244264382 scopus 로고    scopus 로고
    • Impaired activity of protease inhibitors towards neutrophil elastase bound to human articular cartilage
    • Kawabata, K., Moore, A. R., Willoughby, D. A. (1996) Impaired activity of protease inhibitors towards neutrophil elastase bound to human articular cartilage. Ann. Rheum. Dis. 55, 248-252.
    • (1996) Ann. Rheum. Dis. , vol.55 , pp. 248-252
    • Kawabata, K.1    Moore, A.R.2    Willoughby, D.A.3
  • 121
    • 0023488690 scopus 로고
    • Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cathepsin G and elastase from polymorphonuclear leukocytes
    • Velvart, M., Fehr, K. (1987) Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cathepsin G and elastase from polymorphonuclear leukocytes. Rheumatol. Int. 7, 195-202.
    • (1987) Rheumatol. Int. , vol.7 , pp. 195-202
    • Velvart, M.1    Fehr, K.2
  • 122
    • 0023231749 scopus 로고
    • 1-proteinase inhibitor: An in vitro model of enzyme inhibition in the joint space
    • 1-proteinase inhibitor: An in vitro model of enzyme inhibition in the joint space. Rheumatol. Int. 7, 133-138.
    • (1987) Rheumatol. Int. , vol.7 , pp. 133-138
    • Burkhardt, H.1    Kasten, M.2    Rauls, S.3    Rehkopf, E.4
  • 123
    • 0028360109 scopus 로고
    • Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors
    • Kolev, K., Lerant, I., Tenekejiev, K., Machovich, R. (1994) Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors. J. Biol. Chem. 269, 17030-17034.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17030-17034
    • Kolev, K.1    Lerant, I.2    Tenekejiev, K.3    Machovich, R.4
  • 127
    • 0027746203 scopus 로고
    • Animal model. Rabbit models of arthritis: Immunolocalization of matrix metalloproleinases and tissue inhibitor of metalloproteinase in synovium and cartilage
    • Hembry, R. M., Bagga, M. R., Murphy, G., Henderson, B., Reynolds, J. J. (1993) Animal model. Rabbit models of arthritis: Immunolocalization of matrix metalloproleinases and tissue inhibitor of metalloproteinase in synovium and cartilage. Am. J. Pathol. 143, 628-642.
    • (1993) Am. J. Pathol. , vol.143 , pp. 628-642
    • Hembry, R.M.1    Bagga, M.R.2    Murphy, G.3    Henderson, B.4    Reynolds, J.J.5
  • 128
    • 0025288990 scopus 로고
    • Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors
    • Ellis, V., Wun, T.-C., Behrendt, N. Bonne, E., Dano, K. (1990) Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors. J. Biol. Chem. 265, 9904-9908.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9904-9908
    • Ellis, V.1    Wun, T.-C.2    Behrendt, N.3    Bonne, E.4    Dano, K.5
  • 129
    • 0027174515 scopus 로고
    • Neutrophil mediators, Pseudomonas, and pulmonary dysfunction in cystic fibrosis
    • Meyer, K. C., Zimmerman, J. (1993) Neutrophil mediators, Pseudomonas, and pulmonary dysfunction in cystic fibrosis. J. Lab. Clin. Med 121, 654-661.
    • (1993) J. Lab. Clin. Med , vol.121 , pp. 654-661
    • Meyer, K.C.1    Zimmerman, J.2
  • 130
    • 0031449927 scopus 로고    scopus 로고
    • Potentiative effects of neutral proteinases in an inflamed lung: Relationship of neutrophil procollagenase (proMMP-8) to plasmin, calhepsin G and tryptase in bronchiectasis in vitro
    • Sepper, R., Konttinen, Y. T., Buo, L., Eklund, K. K., Lauhio, A., Sorsa, T., Tschesche, H., Aasen, A. O., Sillastu, H. (1997) Potentiative effects of neutral proteinases in an inflamed lung: relationship of neutrophil procollagenase (proMMP-8) to plasmin, calhepsin G and tryptase in bronchiectasis in vitro. Eur. Respir. J. 10, 2788-2793.
    • (1997) Eur. Respir. J. , vol.10 , pp. 2788-2793
    • Sepper, R.1    Konttinen, Y.T.2    Buo, L.3    Eklund, K.K.4    Lauhio, A.5    Sorsa, T.6    Tschesche, H.7    Aasen, A.O.8    Sillastu, H.9
  • 132
    • 0029004841 scopus 로고
    • Human neutrophil collagenase (MMP-8). Identified in bronchiectasis BAL fluid, correlates with severity of disease
    • Sepper, R., Konttinen, Y. T., Ding, Y., Takagi, M., Sorsa, T. (1995) Human neutrophil collagenase (MMP-8). identified in bronchiectasis BAL fluid, correlates with severity of disease. Chest 107, 1641-1647.
    • (1995) Chest , vol.107 , pp. 1641-1647
    • Sepper, R.1    Konttinen, Y.T.2    Ding, Y.3    Takagi, M.4    Sorsa, T.5
  • 134
    • 0028033945 scopus 로고
    • Direct degradation of articular cartilage by rheumatoid synovial fluid: Contribution of pruteolytic enzymes
    • Larbre, J. -P., Moore, A. R., Da Silva, J. A. P., Iwamura, H., Ioannou, Y., Willoughby, D. A. (1994) Direct degradation of articular cartilage by rheumatoid synovial fluid: contribution of pruteolytic enzymes. J. Rheumatol. 21, 1796-1801.
    • (1994) J. Rheumatol. , vol.21 , pp. 1796-1801
    • Larbre, J.-P.1    Moore, A.R.2    Da Silva, J.A.P.3    Iwamura, H.4    Ioannou, Y.5    Willoughby, D.A.6
  • 137
    • 0030721640 scopus 로고    scopus 로고
    • Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay
    • Beekman, B., van El, B., Drijfhout, J. W., Ronday, H. K., TeKoppele, J. M. (1997) Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay. FEBS Lett. 418, 305-309.
    • (1997) FEBS Lett. , vol.418 , pp. 305-309
    • Beekman, B.1    Van El, B.2    Drijfhout, J.W.3    Ronday, H.K.4    Tekoppele, J.M.5
  • 138
    • 0028933149 scopus 로고
    • Activated gelatinase-B (MMP-9) and urokinase-type plasminogen activator in synovial fluids of patients with arthritis. Correlation with clinical and experimental variables of inflammation
    • Koolwijk, P., Miltenburg, A. M. M., van Erck, M. G. M., Oudshoom, M., Niedbala, M. J., Breedveld, F. C., van Hinsbergh, V. W. M. (1995) Activated gelatinase-B (MMP-9) and urokinase-type plasminogen activator in synovial fluids of patients with arthritis. Correlation with clinical and experimental variables of inflammation. J. Rheumatol. 22, 385-393.
    • (1995) J. Rheumatol. , vol.22 , pp. 385-393
    • Koolwijk, P.1    Miltenburg, A.M.M.2    Van Erck, M.G.M.3    Oudshoom, M.4    Niedbala, M.J.5    Breedveld, F.C.6    Van Hinsbergh, V.W.M.7
  • 139
    • 0030805452 scopus 로고    scopus 로고
    • Plasminogen activation in synovial tissues: Differences between normal, osteoarthntis, and rheumatoid arthritis joints
    • Busso, N., Peclat. V., So, A., Sappino, A.-P. (1997) Plasminogen activation in synovial tissues: Differences between normal, osteoarthntis, and rheumatoid arthritis joints. Ann. Rheum. Dis. 56, 550-557.
    • (1997) Ann. Rheum. Dis. , vol.56 , pp. 550-557
    • Busso, N.1    Peclat, V.2    So, A.3    Sappino, A.-P.4
  • 140
    • 0022871876 scopus 로고
    • Preventive therapy of emphysema: Lessons from the elastase model
    • Campbell, E. J. (1986) Preventive therapy of emphysema: Lessons from the elastase model. Am. Rev. Respir. Dis. 134, 435-437.
    • (1986) Am. Rev. Respir. Dis. , vol.134 , pp. 435-437
    • Campbell, E.J.1
  • 141
    • 0028787054 scopus 로고
    • Non-isotropic enzyme-inhibitor interactions: A novel non-oxidative mechanism for quantum proteolysis by human neutrophils
    • Liou, T. G., Campbell, E. J. (1995) Non-isotropic enzyme-inhibitor interactions: A novel non-oxidative mechanism for quantum proteolysis by human neutrophils. Biochemistry 34, 16171-16177.
    • (1995) Biochemistry , vol.34 , pp. 16171-16177
    • Liou, T.G.1    Campbell, E.J.2
  • 142
    • 0030587118 scopus 로고    scopus 로고
    • Quantum proteolysis resulting from release of single granules by neutrophils: A novel, non-oxidative mechanism of extracellular proteolytic activity
    • Liou, T. G., Campbell, E. J. (1996) Quantum proteolysis resulting from release of single granules by neutrophils: A novel, non-oxidative mechanism of extracellular proteolytic activity. J. Imnmnol. 157, 2624-2631.
    • (1996) J. Imnmnol. , vol.157 , pp. 2624-2631
    • Liou, T.G.1    Campbell, E.J.2
  • 143
    • 0017687920 scopus 로고
    • Limited degradation of third component (C3) of human complement by human leukocyte elastase (HLE): Partial characterization of C3 fragments
    • Taylor, J. C., Crawford, I. P., Hugli, T. E. (1977) Limited degradation of third component (C3) of human complement by human leukocyte elastase (HLE): Partial characterization of C3 fragments. Biochemistry 16, 3390-3396.
    • (1977) Biochemistry , vol.16 , pp. 3390-3396
    • Taylor, J.C.1    Crawford, I.P.2    Hugli, T.E.3
  • 144
    • 0018345813 scopus 로고
    • Digestion of the fifth component of complement by leukocyte enzymes: Sequential generation of chemotactic activities for leukocytes and for tumor cells
    • Orr, F. W., Varani, J., Kreutzer, D. L., Senior, R. M., Ward, P. A. (1979) Digestion of the fifth component of complement by leukocyte enzymes: Sequential generation of chemotactic activities for leukocytes and for tumor cells. Am. J. Pathol. 94, 75-83.
    • (1979) Am. J. Pathol. , vol.94 , pp. 75-83
    • Orr, F.W.1    Varani, J.2    Kreutzer, D.L.3    Senior, R.M.4    Ward, P.A.5
  • 145
    • 0002282084 scopus 로고
    • Oxygen-independent antimicrobial systems of phagocytes
    • (J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds.) New York: Raven Press
    • Elsbach, P., Weiss, J. (1992) Oxygen-independent antimicrobial systems of phagocytes. In Inflammation. Basic Principles and Clinical Correlates (J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds.) New York: Raven Press, 603-636.
    • (1992) Inflammation. Basic Principles and Clinical Correlates , pp. 603-636
    • Elsbach, P.1    Weiss, J.2
  • 146
    • 0002032398 scopus 로고
    • Role of interleukin-1 and tumor necrosis factor in systemic responses to infection and inflammation
    • (J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds.) New York: Raven Press
    • Dinarello, C. A. (1992) Role of interleukin-1 and tumor necrosis factor in systemic responses to infection and inflammation. In Inflammation: Basic Principles and Clinical Carrelates (J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds.) New York: Raven Press, 211-232.
    • (1992) Inflammation: Basic Principles and Clinical Carrelates , pp. 211-232
    • Dinarello, C.A.1
  • 147
    • 0025732513 scopus 로고
    • Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin
    • Scuderi, P., Nez, P. A., Duerr, M. L., Wong, B. J., Valdez, C. M. (1991) Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin. Cell. Immunol. 135, 299-313.
    • (1991) Cell. Immunol. , vol.135 , pp. 299-313
    • Scuderi, P.1    Nez, P.A.2    Duerr, M.L.3    Wong, B.J.4    Valdez, C.M.5
  • 148
    • 0026056106 scopus 로고
    • Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa tumor necrosis factor (TNF) receptor
    • Porteu, F., Brockhaus, M., Wallach, D., Engelmann, H., Nathan, C. F. (1991) Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa tumor necrosis factor (TNF) receptor. J. Biol. Chem. 266. 18846-18853.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18846-18853
    • Porteu, F.1    Brockhaus, M.2    Wallach, D.3    Engelmann, H.4    Nathan, C.F.5
  • 149
    • 0029067051 scopus 로고
    • Cleavage of lymphocyte surface antigens CD2, CD4, and CD 8 by polymorphonuelear leukocyte elastase and cathepsin G in patients with cystic fibrosis
    • Doring, G., Frank, F., Boudier, C., Herbert, S., Fleischer, B., Bellon, G. (1995) Cleavage of lymphocyte surface antigens CD2, CD4, and CD 8 by polymorphonuelear leukocyte elastase and cathepsin G in patients with cystic fibrosis. J. Immunol. 154, 4842-4850.
    • (1995) J. Immunol. , vol.154 , pp. 4842-4850
    • Doring, G.1    Frank, F.2    Boudier, C.3    Herbert, S.4    Fleischer, B.5    Bellon, G.6
  • 150
    • 0027155816 scopus 로고
    • Enhancement of cathepsin g-induced platelet activation by leukocyte elastase: Consequence for the neutrophil-mediated platelet activation
    • Renesto, P., Ghignard, M. (1993) Enhancement of cathepsin G-induced platelet activation by leukocyte elastase: Consequence for the neutrophil-mediated platelet activation. Blood 82, 139-144.
    • (1993) Blood , vol.82 , pp. 139-144
    • Renesto, P.1    Ghignard, M.2
  • 152
    • 0027686133 scopus 로고
    • Release of interleukin-8, interleukin-6, and colony-stimulating factors by upper airway epithelial cells: Implications for cystic fibrosis
    • Bedard, M., McClure, C. D., Schiller, N. L., Francoeur, C., Cantin, A., Denis, M. (1993) Release of interleukin-8, interleukin-6, and colony-stimulating factors by upper airway epithelial cells: Implications for cystic fibrosis. Am. J. Respir. Cell Mol. Biol. 9, 455-462.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.9 , pp. 455-462
    • Bedard, M.1    McClure, C.D.2    Schiller, N.L.3    Francoeur, C.4    Cantin, A.5    Denis, M.6
  • 153
    • 0025773838 scopus 로고
    • Role of mast cell and neutrophil proteases in airway secretion
    • Nadel, J. A. (1991) Role of mast cell and neutrophil proteases in airway secretion. Am. Rev. Respir. Dis. 144, S48-S51.
    • (1991) Am. Rev. Respir. Dis. , vol.144
    • Nadel, J.A.1
  • 154
    • 0017064076 scopus 로고
    • Human cathepsin G. Catalytic and immunological properties
    • Starkey, P. M., Barrett, A. J. (1976) Human cathepsin G. Catalytic and immunological properties. Biochem. J. 155, 273-278.
    • (1976) Biochem. J. , vol.155 , pp. 273-278
    • Starkey, P.M.1    Barrett, A.J.2
  • 155
    • 0017089287 scopus 로고
    • Bence jones proteins and light chains of immunoglobulins. XIII. Effect of elastase-like and chymotrypsin-like neutral proteases derived from human granulocytes on bence-jones proteins
    • Solomon, A., Schmidt, W., Havemann, K. (1976) Bence Jones proteins and light chains of immunoglobulins. XIII. Effect of elastase-like and chymotrypsin-like neutral proteases derived from human granulocytes on Bence-Jones proteins. J. Immunol. 117, 1010-1014.
    • (1976) J. Immunol. , vol.117 , pp. 1010-1014
    • Solomon, A.1    Schmidt, W.2    Havemann, K.3
  • 157
    • 4243857663 scopus 로고
    • Ultrastructural localization in normal human PMN of proteinase 3, the target antigen of anti-cytoplasmic antibodies circulating in Wegener's granulomatosis
    • Abstract
    • Bainton, D. F., Csernok, E., Ludemann, J., Gross, W. L. (1990) Ultrastructural localization in normal human PMN of proteinase 3, the target antigen of anti-cytoplasmic antibodies circulating in Wegener's granulomatosis. Clin. Res. 38, 347A (Abstract).
    • (1990) Clin. Res. , vol.38
    • Bainton, D.F.1    Csernok, E.2    Ludemann, J.3    Gross, W.L.4
  • 159
    • 0030578437 scopus 로고    scopus 로고
    • Extracellular activities of human granzymes: I. Granzyme A induces IL6 and IL8 production in fibroblast and epithelial cell lines
    • Sower, L. E., Klimpel, G. R., Hanna, W., Froelich, C. J. (1996) Extracellular activities of human granzymes: I. granzyme A induces IL6 and IL8 production in fibroblast and epithelial cell lines. Cell. Immunol. 171, 159-163.
    • (1996) Cell. Immunol. , vol.171 , pp. 159-163
    • Sower, L.E.1    Klimpel, G.R.2    Hanna, W.3    Froelich, C.J.4
  • 160
    • 0029963625 scopus 로고    scopus 로고
    • Extracellular activities of human granzyme A: Monocyte activation by granzyme A versus α-thrombin
    • Sower, L. E., Froelich, C. J., Allegretto, N., Rose, P. M., Hanna, W. D., Klimpel, G. R. (1996) Extracellular activities of human granzyme A: monocyte activation by granzyme A versus α-thrombin. J. Immunol. 156, 2585-2590.
    • (1996) J. Immunol. , vol.156 , pp. 2585-2590
    • Sower, L.E.1    Froelich, C.J.2    Allegretto, N.3    Rose, P.M.4    Hanna, W.D.5    Klimpel, G.R.6
  • 161
    • 0028492075 scopus 로고
    • Degradation of kinins, angiotensins and substance P by polymorphonuelear matrix metalloproteinases MMP 8 and MMP 9
    • Diekmann, O., Tschesche, H. (1994) Degradation of kinins, angiotensins and substance P by polymorphonuelear matrix metalloproteinases MMP 8 and MMP 9. Braz. J. Med. Biol. Res. 27, 1865-1876.
    • (1994) Braz. J. Med. Biol. Res. , vol.27 , pp. 1865-1876
    • Diekmann, O.1    Tschesche, H.2
  • 162
    • 0025895193 scopus 로고
    • Matrix metalloproteinase degradation of elastin, type IV collagen, and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctated metalloproteinase (PUMP)
    • Murphy, G., Cockett, M. I., Ward, R. V., Docherty, A. J. P. (1991) Matrix
    • (1991) Biochem. J. , vol.277 , pp. 277-279
    • Murphy, G.1    Cockett, M.I.2    Ward, R.V.3    Docherty, A.J.P.4
  • 164
    • 0023237615 scopus 로고
    • Extracellular matrix injury during lung inflammation
    • Campbell, E. J., Senior, R. M., Welgus, H. G. (1987) Extracellular matrix injury during lung inflammation. Chest 92, 161-167.
    • (1987) Chest , vol.92 , pp. 161-167
    • Campbell, E.J.1    Senior, R.M.2    Welgus, H.G.3


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