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Volumn 134, Issue 4, 1999, Pages 341-351

Extracellular proteolysis: New paradigms for an old paradox

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EID: 0033215368     PISSN: 00222143     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2143(99)90148-8     Document Type: Article
Times cited : (17)

References (109)
  • 3
    • 0027930481 scopus 로고
    • Neutrophil collagenase in sputum from patients with cystic fibrosis
    • 3. Power C, O'Connor CM, Macfarlane D, et al. Neutrophil collagenase in sputum from patients with cystic fibrosis. Am J Respir Crit Care Med 1994;150:818-22.
    • (1994) Am J Respir Crit Care Med , vol.150 , pp. 818-822
    • Power, C.1    O'Connor, C.M.2    Macfarlane, D.3
  • 4
    • 0027131471 scopus 로고
    • 1-Proteinase inhibitor, elastase activity, and lung disease severity in cystic fibrosis
    • 1-proteinase inhibitor, elastase activity, and lung disease severity in cystic fibrosis. Am Rev Respir Dis 1993;148:1665-70.
    • (1993) Am Rev Respir Dis , vol.148 , pp. 1665-1670
    • O'Connor, C.M.1    Gaffney, K.2    Keane, J.3
  • 5
    • 0029383641 scopus 로고
    • The pathogenesis of emphysema: The elastase:antielastase hypothesis 30 years later
    • 5. Shapiro SD. The pathogenesis of emphysema: the elastase:antielastase hypothesis 30 years later. Proc Assoc Am Physicians 1995;107:346-52.
    • (1995) Proc Assoc Am Physicians , vol.107 , pp. 346-352
    • Shapiro, S.D.1
  • 6
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • 6. Hautamaki RD, Kobayashi DK, Senior RM, Shapiro SD. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 1997;277:2002-4.
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 7
    • 0026577352 scopus 로고
    • Proteinases in rheumatoid arthritis
    • 7. Murphy G, Hembry RM. Proteinases in rheumatoid arthritis. J Rheum 1992;32(suppl):61-4.
    • (1992) J Rheum , vol.32 , Issue.SUPPL. , pp. 61-64
    • Murphy, G.1    Hembry, R.M.2
  • 8
    • 0028033945 scopus 로고
    • Direct degradation of articular cartilage by rheumatoid synovial fluid: Contribution of proteolytic enzymes
    • 8. Larbre J-P, Moore AR, Da Silva JAP, Iwamura H, Ioannou Y, Willoughby DA. Direct degradation of articular cartilage by rheumatoid synovial fluid: contribution of proteolytic enzymes. J Rheumatol 1994;21:1796-801.
    • (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
  • 9
    • 0030911308 scopus 로고    scopus 로고
    • The regulation of neovascularization by matrix metalloproteinases and their inhibitors
    • 9. Moses MA. The regulation of neovascularization by matrix metalloproteinases and their inhibitors. Stem Cells 1997;15: 180-9.
    • (1997) Stem Cells , vol.15 , pp. 180-189
    • Moses, M.A.1
  • 10
    • 0030469517 scopus 로고    scopus 로고
    • The fibrinolytic system in neoplasia
    • 10. Bell WR. The fibrinolytic system in neoplasia. Semin Thromb Hemost 1996;22:459-78.
    • (1996) Semin Thromb Hemost , vol.22 , pp. 459-478
    • Bell, W.R.1
  • 11
    • 0032534596 scopus 로고    scopus 로고
    • Matrix metalloproteinases generate angiostatin: Effects on neovascularization
    • 11. Cornelius LA, Nehring LC, Harding E, et al. Matrix metalloproteinases generate angiostatin: effects on neovascularization. J Immunol 1998;161:6845-52.
    • (1998) J Immunol , vol.161 , pp. 6845-6852
    • Cornelius, L.A.1    Nehring, L.C.2    Harding, E.3
  • 12
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • 12. Travis J, Salvesen GS. Human plasma proteinase inhibitors. Annu Rev Biochem 1983;52:655-709.
    • (1983) Annu Rev Biochem , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 13
    • 0023840318 scopus 로고
    • Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: Effects of substrate opsonization
    • 13. Campbell EJ, Campbell MA. Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: effects of substrate opsonization. J Cell Biol 1988;106:667-76.
    • (1988) J Cell Biol , vol.106 , pp. 667-676
    • Campbell, E.J.1    Campbell, M.A.2
  • 14
    • 0019965228 scopus 로고
    • Proteolysis by neutrophils. Relative importance of cell-substrate contact and oxidative inactivation of proteinase inhibitors in vitro
    • 14. Campbell EJ, Senior RM, McDonald JA, Cox DL. Proteolysis by neutrophils. Relative importance of cell-substrate contact and oxidative inactivation of proteinase inhibitors in vitro. J Clin Invest 1982;70:845-52.
    • (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
  • 15
    • 0025359581 scopus 로고
    • Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor
    • 15. Rice WG, Weiss SJ. Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor. Science 1990;249:178-81.
    • (1990) Science , vol.249 , pp. 178-181
    • Rice, W.G.1    Weiss, S.J.2
  • 16
    • 0019321009 scopus 로고
    • Kinetics of association of serine proteinases with native and oxidised alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin
    • 16. Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidised alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem 1980; 255:3931-4.
    • (1980) J Biol Chem , vol.255 , pp. 3931-3934
    • Beatty, K.1    Bieth, J.2    Travis, J.3
  • 17
    • 0019258204 scopus 로고
    • Inactivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants
    • 17. Carp H, Janoff A. Inactivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants. Exp Lung Res 1980;1:225-37.
    • (1980) Exp Lung Res , vol.1 , pp. 225-237
    • Carp, H.1    Janoff, A.2
  • 18
    • 0018407613 scopus 로고
    • In vitro suppression of serum elastase-inhibitory capacity by reactive oxygen species generated by phagocytosing polymorphonuclear leukocytes
    • 18. Carp H, Janoff A. In vitro suppression of serum elastase-inhibitory capacity by reactive oxygen species generated by phagocytosing polymorphonuclear leukocytes. J Clin Invest 1979;63:793-7.
    • (1979) J Clin Invest , vol.63 , pp. 793-797
    • Carp, H.1    Janoff, A.2
  • 19
    • 0019185755 scopus 로고
    • 1-proteinase inhibitor in vitro
    • 1-proteinase inhibitor in vitro. J Clin Invest 1980; 66:987-95.
    • (1980) J Clin Invest , vol.66 , pp. 987-995
    • Carp, H.1    Janoff, A.2
  • 20
    • 0028060243 scopus 로고
    • Oxidative dissociation of human alpha 2-macroglobulin tetramers into dysfunctional dimers
    • 20. Reddy VY, Desrochers PE, Pizzo SV, et al. Oxidative dissociation of human alpha 2-macroglobulin tetramers into dysfunctional dimers. J Biol Chem 1994;269:4683-91.
    • (1994) J Biol Chem , vol.269 , pp. 4683-4691
    • Reddy, V.Y.1    Desrochers, P.E.2    Pizzo, S.V.3
  • 21
    • 0027174515 scopus 로고
    • Neutrophil mediators, Pseudomonas, and pulmonary dysfunction in cystic fibrosis
    • 21. Meyer KC, Zimmerman J. Neutrophil mediators, Pseudomonas, and pulmonary dysfunction in cystic fibrosis. J Lab Clin Med 1993;121:654-61.
    • (1993) J Lab Clin Med , vol.121 , pp. 654-661
    • Meyer, K.C.1    Zimmerman, J.2
  • 22
    • 0020693698 scopus 로고
    • Pathogenesis of the adult respiratory distress syndrome. Evidence of oxidant activity in bronchoalveolar lavage fluid
    • 22. Cochrane CG, Spragg R, Revak SD. Pathogenesis of the adult respiratory distress syndrome. Evidence of oxidant activity in bronchoalveolar lavage fluid. J Clin Invest 1983; 71:754-61.
    • (1983) J Clin Invest , vol.71 , pp. 754-761
    • Cochrane, C.G.1    Spragg, R.2    Revak, S.D.3
  • 23
    • 0019163627 scopus 로고
    • Isolation and properties of oxidised alpha-1-proteinase inhibitor from human rheumatoid synovial fluid
    • 23. Wong PS, Travis J. Isolation and properties of oxidised alpha-1-proteinase inhibitor from human rheumatoid synovial fluid. Biochem Biophys Res Commun 1980; 96:1449-54.
    • (1980) Biochem Biophys Res Commun , vol.96 , pp. 1449-1454
    • Wong, P.S.1    Travis, J.2
  • 24
    • 0032531422 scopus 로고    scopus 로고
    • 2-macroglobulin differentially regulates receptor binding by cytokines/growth factors: Implications for tissue injury and repair mechanisms in inflammation
    • 2-macroglobulin differentially regulates receptor binding by cytokines/growth factors: implications for tissue injury and repair mechanisms in inflammation. J Immunol 1998;161:4356-65.
    • (1998) J Immunol , vol.161 , pp. 4356-4365
    • Wu, S.M.1    Patel, D.D.2    Pizzo, S.V.3
  • 27
    • 0018611004 scopus 로고
    • Cigarette smoking induces functional antiprotease deficiency in the lower respiratory tract of humans
    • 27. Gadek JE, Fells GA, Crystal RG. Cigarette smoking induces functional antiprotease deficiency in the lower respiratory tract of humans. Science 1979;206:1315-6.
    • (1979) Science , vol.206 , pp. 1315-1316
    • Gadek, J.E.1    Fells, G.A.2    Crystal, R.G.3
  • 28
    • 0020616229 scopus 로고
    • Functional alpha-1-protease inhibitor in the lower respiratory tract of cigarette smokers is not decreased
    • 28. Stone PJ, Calore JD, McGowan SE, Bernardo J, Snider GL, Franzblau C. Functional alpha-1-protease inhibitor in the lower respiratory tract of cigarette smokers is not decreased. Science 1983;221:1187-9.
    • (1983) Science , vol.221 , pp. 1187-1189
    • Stone, P.J.1    Calore, J.D.2    McGowan, S.E.3    Bernardo, J.4    Snider, G.L.5    Franzblau, C.6
  • 29
    • 0028104433 scopus 로고
    • Matrilysin is much more efficient than other metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin
    • 29. Sires UI, Murphy G, Welgus HG, Senior RM. Matrilysin is much more efficient than other metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin. Biochem Biophys Res Commun 1994;204:613-20.
    • (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
  • 30
    • 0026705310 scopus 로고
    • Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases
    • 30. Desrochers PE, Mookhtiar K, Van Wart HE, Hasty KA, Weiss SJ. Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases. J Biol Chem 1992;267:5005-12.
    • (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
  • 31
    • 0024350420 scopus 로고
    • 1-antitrypsin in cystic fibrosis bronchopulmonary secretions
    • 1-antitrypsin in cystic fibrosis bronchopulmonary secretions. Pediatr Pulmonol 1989;7:12-7.
    • (1989) Pediatr Pulmonol , vol.7 , pp. 12-17
    • Cantin, A.1    Bilodeau, G.2    Begin, R.3
  • 32
    • 0029134020 scopus 로고
    • The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: The evaluation of its physiologic relevance in fibrinolysis
    • 32. Wu K, Urano T, Ihara H, et al. The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: the evaluation of its physiologic relevance in fibrinolysis. Blood 1995;86:1056-61.
    • (1995) Blood , vol.86 , pp. 1056-1061
    • Wu, K.1    Urano, T.2    Ihara, H.3
  • 33
    • 0017389922 scopus 로고
    • 1 proteinase inhibitor by thiol proteinases
    • 1 proteinase inhibitor by thiol proteinases. Biochem J 1977;163:639-41.
    • (1977) Biochem J , vol.163 , pp. 639-641
    • Johnson, D.1    Travis, J.2
  • 34
    • 0026252652 scopus 로고
    • Different susceptibility of elastase inhibitors to inactivation by proteinases from Staphylococcus aureus and Pseudomonas aeruginosa
    • 34. Sponer M, Nick H-P, Schnebli H-P. Different susceptibility of elastase inhibitors to inactivation by proteinases from Staphylococcus aureus and Pseudomonas aeruginosa. Biol Chem Hoppe-Seyler 1991;372:963-70.
    • (1991) Biol Chem Hoppe-Seyler , vol.372 , pp. 963-970
    • Sponer, M.1    Nick, H.-P.2    Schnebli, H.-P.3
  • 35
    • 0023837944 scopus 로고
    • Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases
    • 35. Okada Y, Watanabe S, Nakanishi I, et al. Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases. FEBS Lett 1988;229:157-60.
    • (1988) FEBS Lett , vol.229 , pp. 157-160
    • Okada, Y.1    Watanabe, S.2    Nakanishi, I.3
  • 36
    • 0025134352 scopus 로고
    • 1-proteinase inhibitor) in knee-joint synovial fluid from patients with rheumatoid arthritis
    • 1-proteinase inhibitor) in knee-joint synovial fluid from patients with rheumatoid arthritis. Biochem Soc Trans 1990;18:898-9.
    • (1990) Biochem Soc Trans , vol.18 , pp. 898-899
    • Zhang, Z.1    Winyard, P.G.2    Chidwick, K.3
  • 38
    • 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 1991;4:40-9.
    • (1991) Eur Respir J , vol.4 , pp. 40-49
    • Suter, S.1    Chevallier, I.2
  • 39
    • 0028973014 scopus 로고
    • Alpha 1-antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds. The inhibitor protects fibronectin from degradation by chronic wound fluid enzymes
    • 39. Rao CN, Ladin DA, Liu YY, Chilukuri C, Hou ZZ, Woodley DT. Alpha 1-antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds. The inhibitor protects fibronectin from degradation by chronic wound fluid enzymes. J Invest Dermatol 1995;105:572-8.
    • (1995) J Invest Dermatol , vol.105 , pp. 572-578
    • Rao, C.N.1    Ladin, D.A.2    Liu, Y.Y.3    Chilukuri, C.4    Hou, Z.Z.5    Woodley, D.T.6
  • 40
    • 0021355213 scopus 로고
    • Phagocytosing macrophages exclude proteins from zones of contact with targets
    • 40. Wright SD, Silverstein SC. Phagocytosing macrophages exclude proteins from zones of contact with targets. Nature 1984;309:359-61.
    • (1984) Nature , vol.309 , pp. 359-361
    • Wright, S.D.1    Silverstein, S.C.2
  • 41
    • 0030913467 scopus 로고    scopus 로고
    • Osteoclasts, macrophages, and the molecular mechanisms of bone resorption
    • 41. Teitelbaum SL, Tondravi MM, Ross FP. Osteoclasts, macrophages, and the molecular mechanisms of bone resorption. J Leukocyte Biol 1997;61:381-8.
    • (1997) J Leukocyte Biol , vol.61 , pp. 381-388
    • Teitelbaum, S.L.1    Tondravi, M.M.2    Ross, F.P.3
  • 42
    • 0009680995 scopus 로고
    • Proteolysis by neutrophils while in contact with substrate: Incomplete protection of substrate by proteinase inhibitors
    • Mittman C, Taylor JC, editors. New York: Academic Press
    • 42. Campbell EJ, Campbell MA. Proteolysis by neutrophils while in contact with substrate: incomplete protection of substrate by proteinase inhibitors. In: Mittman C, Taylor JC, editors. Pulmonary emphysema and proteolysis (vol II). New York: Academic Press; 1987. p. 235-44.
    • (1987) Pulmonary Emphysema and Proteolysis , vol.2 , pp. 235-244
    • Campbell, E.J.1    Campbell, M.A.2
  • 43
    • 0026144822 scopus 로고
    • Extracellular proteolysis of fibronectin by neutrophils: Characterization and the effects of recombinant cytokines
    • 43. Chamba A, Afford SC, Stockley RA, Burnett D. Extracellular proteolysis of fibronectin by neutrophils: characterization and the effects of recombinant cytokines. Am J Respir Cell Mol Biol 1990;4:330-7.
    • (1990) Am J Respir Cell Mol Biol , vol.4 , pp. 330-337
    • Chamba, A.1    Afford, S.C.2    Stockley, R.A.3    Burnett, D.4
  • 44
    • 0002835650 scopus 로고
    • Role of leukocyte-endothelial cell adhesion molecules in renal inflammation: In vitro and in vivo studies
    • 44. Briscoe DM, Cotran RS. Role of leukocyte-endothelial cell adhesion molecules in renal inflammation: in vitro and in vivo studies. Kidney Int 1993;44:S27-34.
    • (1993) Kidney Int , vol.44
    • Briscoe, D.M.1    Cotran, R.S.2
  • 45
  • 46
    • 0028034078 scopus 로고
    • Serum levels of soluble adhesion molecules intercellular adhesion molecule 1, vascular cell adhesion molecule 1, and E-selectin in patients with Wegener's granulomatosis
    • 46. Stegeman CA, Tervaert JW, Huitema MG, deJong PE, Kallenberg CG. Serum levels of soluble adhesion molecules intercellular adhesion molecule 1, vascular cell adhesion molecule 1, and E-selectin in patients with Wegener's granulomatosis. Arthritis Rheum 1994;37:1228-35.
    • (1994) Arthritis Rheum , vol.37 , pp. 1228-1235
    • Stegeman, C.A.1    Tervaert, J.W.2    Huitema, M.G.3    Dejong, P.E.4    Kallenberg, C.G.5
  • 47
    • 0028152778 scopus 로고
    • Circulating adhesion molecules ICAM-1, VCAM-1, and F-selectin in systemic vasculitis: Marked differences between Wegener's granulomatosis and systemic lupus erythematosis
    • 47. Mrowka C, Sieberth HG. Circulating adhesion molecules ICAM-1, VCAM-1, and F-selectin in systemic vasculitis: marked differences between Wegener's granulomatosis and systemic lupus erythematosis. Clin Invest 1994;72:762-8.
    • (1994) Clin Invest , vol.72 , pp. 762-768
    • Mrowka, C.1    Sieberth, H.G.2
  • 48
    • 0029939956 scopus 로고    scopus 로고
    • Glomerular vascular cell adhesion molecule-1 expression in renal vasculitis
    • 48. Pall AA, Howie AJ, Adu D, et al. Glomerular vascular cell adhesion molecule-1 expression in renal vasculitis. J Clin Pathol 1996;49:238-42.
    • (1996) J Clin Pathol , vol.49 , pp. 238-242
    • Pall, A.A.1    Howie, A.J.2    Adu, D.3
  • 49
    • 1842329163 scopus 로고    scopus 로고
    • Mechanisms of neutrophil-induced parenchymal cell injury
    • 49. Jaeschke H, Smith CW. Mechanisms of neutrophil-induced parenchymal cell injury. J Leukocyte Biol 1997;61:647-53.
    • (1997) J Leukocyte Biol , vol.61 , pp. 647-653
    • Jaeschke, H.1    Smith, C.W.2
  • 50
    • 0031843851 scopus 로고    scopus 로고
    • Neutrophildependent goblet cell degranulation: Role of membrane-bound elastase and adhesion molecules
    • 50. Takeyama K, Agusti C, Ueki I, Lausier J, Cardell LO, Nadel JA. Neutrophildependent goblet cell degranulation: role of membrane-bound elastase and adhesion molecules. Am J Physiol 1998;275:L294-302.
    • (1998) Am J Physiol , vol.275
    • Takeyama, K.1    Agusti, C.2    Ueki, I.3    Lausier, J.4    Cardell, L.O.5    Nadel, J.A.6
  • 51
    • 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
    • 51. Owen CA, Campbell MA, Sannes PL, Boukedes SS, Campbell EJ. 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 1995;131:775-89.
    • (1995) J Cell Biol , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 52
    • 0028802595 scopus 로고
    • Inducible binding of cathepsin G to the cell surface of neutrophils: A mechanism for mediating extracellular proteolytic activity of cathepsin G
    • 52. Owen CA, Campbell MA, Boukedes SS, Campbell EJ. Inducible binding of cathepsin G to the cell surface of neutrophils: a mechanism for mediating extracellular proteolytic activity of cathepsin G. J Immunol 1995;155:5803-10.
    • (1995) J Immunol , vol.155 , pp. 5803-5810
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 53
    • 0030948848 scopus 로고    scopus 로고
    • Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity
    • 53. Owen CA, Campbell MA, Boukedes SS, Campbell EJ. Cytokines regulate membrane-bound leukocyte elastase on neutrophils: a novel mechanism for effector activity. Am J Physiol 1997;272:L385-93.
    • (1997) Am J Physiol , vol.272
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 54
    • 0028307148 scopus 로고
    • Activated neutrophils express proteinase 3 on their plasma membrane in vitro and in vivo
    • 54. Csernok E, Ernst M, Schmitt W, Bainton DF, Gross WL. Activated neutrophils express proteinase 3 on their plasma membrane in vitro and in vivo. Clin Exp Immunol 1994;95: 244-50.
    • (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
  • 55
    • 0022461972 scopus 로고
    • Human neutrophil plasminogen activator is localized in specific granules and is translocated to the cell surface by exocytosis
    • 55. Heiple JM, Ossowski L. Human neutrophil plasminogen activator is localized in specific granules and is translocated to the cell surface by exocytosis. J Exp Med 1986;164:826-40.
    • (1986) J Exp Med , vol.164 , pp. 826-840
    • Heiple, J.M.1    Ossowski, L.2
  • 56
    • 0026641093 scopus 로고
    • Urokinase-catalyzed plasminogen activation at the monocyte/macrophage cell surface: A localized and regulated proteolytic system
    • 56. Vassalli JD, Wohlwend A, Belin D. Urokinase-catalyzed plasminogen activation at the monocyte/macrophage cell surface: a localized and regulated proteolytic system. Curr Top Microbiol Immunol 1992;181:65-86.
    • (1992) Curr Top Microbiol Immunol , vol.181 , pp. 65-86
    • Vassalli, J.D.1    Wohlwend, A.2    Belin, D.3
  • 57
    • 0030954151 scopus 로고    scopus 로고
    • Localization and activation of type IV collagenase/gelatinase at endothelial focal contacts
    • 57. Partridge CA, Phillips PG, Niedbala MJ, Jeffrey JJ. Localization and activation of type IV collagenase/gelatinase at endothelial focal contacts. Am J Physiol 1997;272:L813-22.
    • (1997) Am J Physiol , vol.272
    • Partridge, C.A.1    Phillips, P.G.2    Niedbala, M.J.3    Jeffrey, J.J.4
  • 59
    • 0028077527 scopus 로고
    • Cell surface-mediated activation of progelatinase A: Demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts
    • 59. Ward RV, Atkinson SJ, Reynolds JJ, Murphy G. Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts. Bioehem J 1994;304:263-9.
    • (1994) Bioehem J , vol.304 , pp. 263-269
    • Ward, R.V.1    Atkinson, S.J.2    Reynolds, J.J.3    Murphy, G.4
  • 60
    • 15844420283 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin αvβ3
    • 60. Brooks PC, Stromblad S, Sanders LC, et al. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin αvβ3. Cell 1996;85: 683-93.
    • (1996) Cell , vol.85 , pp. 683-693
    • Brooks, P.C.1    Stromblad, S.2    Sanders, L.C.3
  • 61
    • 0028890305 scopus 로고
    • Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface
    • 61. Allen DH, Tracy PB. Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface. J Biol Chem 1995;270: 1408-15.
    • (1995) J Biol Chem , vol.270 , pp. 1408-1415
    • Allen, D.H.1    Tracy, P.B.2
  • 62
    • 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
    • 62. Owen CA, Campbell EJ. Angiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition. J Immunol 1998;160:1436-43.
    • (1998) J Immunol , vol.160 , pp. 1436-1443
    • Owen, C.A.1    Campbell, E.J.2
  • 63
    • 0025288990 scopus 로고
    • Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors
    • 63. Ellis V, Wun T-C, Behrendt N, Ronne E, Dano K. Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors. J Biol Chem 1990;265:9904-8.
    • (1990) J Biol Chem , vol.265 , pp. 9904-9908
    • Ellis, V.1    Wun, T.-C.2    Behrendt, N.3    Ronne, E.4    Dano, K.5
  • 64
    • 0027302286 scopus 로고
    • 'Classic' anti-neutrophil cytoplasmic autoantibodies (cANCA), 'Wegener's autoantigen' and their immunopathogenic role in Wegener's granulomatosis
    • 64. Gross WL, Csernok E, Flesch BK. 'Classic' anti-neutrophil cytoplasmic autoantibodies (cANCA), 'Wegener's autoantigen' and their immunopathogenic role in Wegener's granulomatosis. J Autoimmun 1993;6:171-84.
    • (1993) J Autoimmun , vol.6 , pp. 171-184
    • Gross, W.L.1    Csernok, E.2    Flesch, B.K.3
  • 66
    • 0025345612 scopus 로고
    • Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro
    • 66. Falk RJ, Terrell RS, Charles LA, Jennette JC. Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro. Proc Natl Acad Sci USA 1990;87:4115-9.
    • (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
  • 68
    • 0026467070 scopus 로고
    • Membrane proteases: Roles in tissue remodeling and tumour invasion
    • 24947
    • 68. Chen W-T. Membrane proteases: roles in tissue remodeling and tumour invasion. Curr Opin Cell Biol 1992;24947: 802-9.
    • (1992) Curr Opin Cell Biol , pp. 802-809
    • Chen, W.-T.1
  • 70
    • 0031955355 scopus 로고    scopus 로고
    • Metalloproteases and urokinase in angiogenesis and tumor progression
    • 70. Rabbani SA. Metalloproteases and urokinase in angiogenesis and tumor progression. In Vivo 1998;12:135-42.
    • (1998) In Vivo , vol.12 , pp. 135-142
    • Rabbani, S.A.1
  • 73
    • 0027746203 scopus 로고
    • Animal model. Rabbit models of arthritis: Immunolocalization of matrix metalloproteinases and tissue inhibitor of metalloproteinase in synovium and cartilage
    • 73. Hembry RM, Bagga MR, Murphy G, Henderson B, Reynolds JJ. Animal model. Rabbit models of arthritis: immunolocalization of matrix metalloproteinases and tissue inhibitor of metalloproteinase in synovium and cartilage. Am J Pathol 1993;143:628-42.
    • (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
  • 74
    • 0022500794 scopus 로고
    • Immunolocalization of elastase in human emphysematous lungs
    • 74. Damiano VV, Tsang A, Kucich U, et al. Immunolocalization of elastase in human emphysematous lungs. J Clin Invest 1986;78:482-93.
    • (1986) J Clin Invest , vol.78 , pp. 482-493
    • Damiano, V.V.1    Tsang, A.2    Kucich, U.3
  • 75
    • 0025390464 scopus 로고
    • Inhibition of human leukocyte elastase bound to elastin: Relative ineffectiveness and two mechanisms of inhibitory activity
    • 75. Morrison HM, Welgus HG, Stockley RA, Burnett D, Campbell EJ. Inhibition of human leukocyte elastase bound to elastin: relative ineffectiveness and two mechanisms of inhibitory activity. Am J Respir Cell Mol Biol 1990;2: 263-9.
    • (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
  • 76
    • 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 1986;238:269-73.
    • (1986) Biochem J , vol.238 , pp. 269-273
    • Bruch, M.1    Bieth, J.G.2
  • 77
    • 0023189021 scopus 로고
    • Receptor mediated binding of leukocyte elastase by chondrocytes
    • 77. Bartholomew J, Lowther DA. Receptor mediated binding of leukocyte elastase by chondrocytes. Arthritis Rheum 1987; 30:431-8.
    • (1987) Arthritis Rheum , vol.30 , pp. 431-438
    • Bartholomew, J.1    Lowther, D.A.2
  • 78
    • 9244264382 scopus 로고    scopus 로고
    • Impaired activity of protease inhibitors towards neutrophil elastase bound to human articular cartilage
    • 78. Kawabata K, Moore AR, Willoughby DA. Impaired activity of protease inhibitors towards neutrophil elastase bound to human articular cartilage. Ann Rheum Dis 1996;55:248-52.
    • (1996) Ann Rheum Dis , vol.55 , pp. 248-252
    • Kawabata, K.1    Moore, A.R.2    Willoughby, D.A.3
  • 79
    • 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 1987;7:133-8.
    • (1987) Rheumatol Int , vol.7 , pp. 133-138
    • Burkhardt, H.1    Kasten, M.2    Rauls, S.3    Rehkopf, E.4
  • 80
    • 0023488690 scopus 로고
    • Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cathepsin G and elastase from polymorphonuclear leukocytes
    • 80. Velvart M, Fehr K. Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cathepsin G and elastase from polymorphonuclear leukocytes. Rheumatol Int 1987;7:195-202.
    • (1987) Rheumatol Int , vol.7 , pp. 195-202
    • Velvart, M.1    Fehr, K.2
  • 81
    • 0032408076 scopus 로고    scopus 로고
    • Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms
    • 81. Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW. Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms. J Clin Invest 1998;102:1900-10.
    • (1998) J Clin Invest , vol.102 , pp. 1900-1910
    • Curci, J.A.1    Liao, S.2    Huffman, M.D.3    Shapiro, S.D.4    Thompson, R.W.5
  • 82
    • 0032496145 scopus 로고    scopus 로고
    • Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids
    • 82. Kainulainen V, Wang H, Schick C, Bernfield M. Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids. J Biol Chem 1998;273:11563-9.
    • (1998) J Biol Chem , vol.273 , pp. 11563-11569
    • Kainulainen, V.1    Wang, H.2    Schick, C.3    Bernfield, M.4
  • 83
    • 0031004487 scopus 로고    scopus 로고
    • Apoptosis in resolution of inflammation
    • 83. Savill J. Apoptosis in resolution of inflammation. J Leukocyte Biol 1997;61:375-80.
    • (1997) J Leukocyte Biol , vol.61 , pp. 375-380
    • Savill, J.1
  • 84
    • 0031449927 scopus 로고    scopus 로고
    • Potentiative effects of neutral proteinases in an inflamed lung: Relationship of neutrophil procollagenase (proMMP-8) to plasmin, cathepsin G and tryptase in bronchiectasis in vivo
    • 84. Sepper R, Konttinen YT, Buo L, et al. Potentiative effects of neutral proteinases in an inflamed lung: relationship of neutrophil procollagenase (proMMP-8) to plasmin, cathepsin G and tryptase in bronchiectasis in vivo. Eur Respir J 1997;10:2788-93.
    • (1997) Eur Respir J , vol.10 , pp. 2788-2793
    • Sepper, R.1    Konttinen, Y.T.2    Buo, L.3
  • 85
    • 0029004841 scopus 로고
    • Human neutrophil collagenase (MMP-8), identified in bronchiectasis BAL fluid, correlates with severity of disease
    • 85. Sepper R, Konttinen YT, Ding Y, Takagi M, Sorsa T. Human neutrophil collagenase (MMP-8), identified in bronchiectasis BAL fluid, correlates with severity of disease. Chest 1995;107:1641-7.
    • (1995) Chest , vol.107 , pp. 1641-1647
    • Sepper, R.1    Konttinen, Y.T.2    Ding, Y.3    Takagi, M.4    Sorsa, T.5
  • 86
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocyte-mediated proteolysis
    • 86. Owen CA, Campbell EJ. The cell biology of leukocyte-mediated proteolysis. J Leukocyte Biol 1999;65:137-50.
    • (1999) J Leukocyte Biol , vol.65 , pp. 137-150
    • Owen, C.A.1    Campbell, E.J.2
  • 87
    • 0019462327 scopus 로고
    • Elastolytic activity in pulmonary lavage fluid from patients with adult respiratory-distress syndrome
    • 87. Lee CT, Fein AM, Lippmann M, Holtzman M, Kimbel P, Weinbaum G. Elastolytic activity in pulmonary lavage fluid from patients with adult respiratory-distress syndrome. N Engl J Med 1981;304:192-6.
    • (1981) N Engl J Med , vol.304 , pp. 192-196
    • Lee, C.T.1    Fein, A.M.2    Lippmann, M.3    Holtzman, M.4    Kimbel, P.5    Weinbaum, G.6
  • 88
    • 0020691819 scopus 로고
    • The presence of neutrophil elastase and evidence of oxidation activity in bronchoalveolar lavage fluid of patients with adult respiratory distress syndrome
    • 88. Cochrane CG, Spragg RG, Revak SD, Cohen AB, McGuire WW. The presence of neutrophil elastase and evidence of oxidation activity in bronchoalveolar lavage fluid of patients with adult respiratory distress syndrome. Am Rev Respir Dis 1983;127:S25-7.
    • (1983) Am Rev Respir Dis , vol.127
    • Cochrane, C.G.1    Spragg, R.G.2    Revak, S.D.3    Cohen, A.B.4    McGuire, W.W.5
  • 89
    • 0021836998 scopus 로고
    • Collagenase in the lower respiratory-tract of patients with adult respiratory-distress syndrome
    • 89. Christner P, Fein A, Goldberg S, Lippmann M, Abrams W, Weinbaum G. Collagenase in the lower respiratory-tract of patients with adult respiratory-distress syndrome. Am Rev Respir Dis 1985;131:690-5.
    • (1985) Am Rev Respir Dis , vol.131 , pp. 690-695
    • Christner, P.1    Fein, A.2    Goldberg, S.3    Lippmann, M.4    Abrams, W.5    Weinbaum, G.6
  • 91
    • 0030910511 scopus 로고    scopus 로고
    • Gelatinases in epithelial lining fluid of patients with adult respiratory distress syndrome
    • 91. Delclaux C, D'Ortho M-P, Delacourt C, et al. Gelatinases in epithelial lining fluid of patients with adult respiratory distress syndrome. Am J Physiol 1997;272:L442-51.
    • (1997) Am J Physiol , vol.272
    • Delclaux, C.1    D'Ortho, M.-P.2    Delacourt, C.3
  • 92
    • 0030025905 scopus 로고    scopus 로고
    • Cathepsin G and elastase in synovial fluid and peripheral blood in reactive and rheumatoid arthritis
    • 92. Nordstrom D, Lindy O, Konttinen YT, et al. Cathepsin G and elastase in synovial fluid and peripheral blood in reactive and rheumatoid arthritis. Clin Rheumatol 1996;15:35-41.
    • (1996) Clin Rheumatol , vol.15 , pp. 35-41
    • Nordstrom, D.1    Lindy, O.2    Konttinen, Y.T.3
  • 93
    • 0026744846 scopus 로고
    • Collagenase in synovitis of rheumatoid arthritis
    • 93. Sorsa T, Konttinen YT, Lindy O, et al. Collagenase in synovitis of rheumatoid arthritis. Semin Arthritis Rheum 1992;22:44-53.
    • (1992) Semin Arthritis Rheum , vol.22 , pp. 44-53
    • Sorsa, T.1    Konttinen, Y.T.2    Lindy, O.3
  • 94
    • 0030721640 scopus 로고    scopus 로고
    • Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay
    • 94. Beekman B, van El B, Drijfhout JW, Ronday HK, TeKoppele JM. Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay. FEBS Lett 1997;418:305-9.
    • (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
  • 95
    • 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
    • 95. Koolwijk P, Miltenburg AMM, van Erck MGM, et al. 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 1995;22:385-93.
    • (1995) J Rheumatol , vol.22 , pp. 385-393
    • Koolwijk, P.1    Miltenburg, A.M.M.2    Van Erck, M.G.M.3
  • 96
    • 0022871876 scopus 로고
    • Preventive therapy of emphysema: Lessons from the elastase model
    • 96. Campbell EJ. Preventive therapy of emphysema: lessons from the elastase model. Am Rev Respir Dis 1986;134:435-7.
    • (1986) Am Rev Respir Dis , vol.134 , pp. 435-437
    • Campbell, E.J.1
  • 97
    • 0028787054 scopus 로고
    • Non-isotropic enzyme-inhibitor interactions: A novel non-oxidative mechanism for quantum proteolysis by human neutrophils
    • 97. Liou TG, Campbell EJ. Non-isotropic enzyme-inhibitor interactions: a novel non-oxidative mechanism for quantum proteolysis by human neutrophils. Biochemistry 1995;34: 16171-7.
    • (1995) Biochemistry , vol.34 , pp. 16171-16177
    • Liou, T.G.1    Campbell, E.J.2
  • 98
    • 0030587118 scopus 로고    scopus 로고
    • Quantum proteolysis resulting from release of single granules by neutrophils: A novel, non-oxidative mechanism of extracellular proteolytic activity
    • 98. Liou TG, Campbell EJ. Quantum proteolysis resulting from release of single granules by neutrophils: a novel, non-oxidative mechanism of extracellular proteolytic activity. J Immunol 1996;157:2624-31.
    • (1996) J Immunol , vol.157 , pp. 2624-2631
    • Liou, T.G.1    Campbell, E.J.2
  • 99
    • 0020663341 scopus 로고
    • 1-antitrypsin deficiency: Clinical and physiological features in heterozygotes of type Pi SZ. A survey by the British Thoracic Association
    • 1-antitrypsin deficiency: clinical and physiological features in heterozygotes of type Pi SZ. A survey by the British Thoracic Association. Br J Dis Chest 1983;77:28-34.
    • (1983) Br J Dis Chest , vol.77 , pp. 28-34
    • Hutchison, D.C.S.1    Tobin, M.J.2    Cook, P.J.L.3
  • 100
    • 0023898072 scopus 로고
    • Natural history of alpha-1-protease inhibitor deficiency
    • 100. Hutchison DCS. Natural history of alpha-1-protease inhibitor deficiency. Am J Med 1988;84(suppl 6A):3-12.
    • (1988) Am J Med , vol.84 , Issue.SUPPL. 6A , pp. 3-12
    • Hutchison, D.C.S.1
  • 101
    • 0030446288 scopus 로고    scopus 로고
    • Clinical features of individuals with Pi *SZ phenotype of alpha 1-antitrypsin deficiency. Alpha 1-antitrypsin deficiency registry study group
    • 101. Turino GM, Barker AF, Brantly ML, et al. Clinical features of individuals with Pi *SZ phenotype of alpha 1-antitrypsin deficiency. Alpha 1-antitrypsin deficiency registry study group. Am J Respir Crit Care Med 1996;154:1718-25.
    • (1996) Am J Respir Crit Care Med , vol.154 , pp. 1718-1725
    • Turino, G.M.1    Barker, A.F.2    Brantly, M.L.3
  • 104
    • 0026041548 scopus 로고
    • Oxidation-resistant variants of recombinant antileucoprotease are better inhibitors of human-neutrophil-elastase-induced emphysema in hamsters than natural recombinant antileucoprotease
    • 104. Rudolphus A, Heinzel-Wieland R, Vincent VA, et al. Oxidation-resistant variants of recombinant antileucoprotease are better inhibitors of human-neutrophil-elastase-induced emphysema in hamsters than natural recombinant antileucoprotease. Clin Sci 1991;81:777-84.
    • (1991) Clin Sci , vol.81 , pp. 777-784
    • Rudolphus, A.1    Heinzel-Wieland, R.2    Vincent, V.A.3
  • 105
    • 0027195975 scopus 로고
    • Neutrophil elastase inhibitors, SC-37698 and SC-39026, reduce endotoxin-induced lung dysfunction in awake sheep
    • 105. Gossage JR, Kuratomi Y, Davidson JM, Lefferts PL, Snapper JR. Neutrophil elastase inhibitors, SC-37698 and SC-39026, reduce endotoxin-induced lung dysfunction in awake sheep. Am Rev Respir Dis 1993;147:1371-9.
    • (1993) Am Rev Respir Dis , vol.147 , pp. 1371-1379
    • Gossage, J.R.1    Kuratomi, Y.2    Davidson, J.M.3    Lefferts, P.L.4    Snapper, J.R.5
  • 106
    • 0027511577 scopus 로고
    • Effect of a synthetic leukocyte elastase inhibitor on thrombin-induced pulmonary edema in the rat
    • 106. Ahn CM, Sandler H, Glass M, Saldeen T. Effect of a synthetic leukocyte elastase inhibitor on thrombin-induced pulmonary edema in the rat. Exp Lung Res 1993; 19:125-35.
    • (1993) Exp Lung Res , vol.19 , pp. 125-135
    • Ahn, C.M.1    Sandler, H.2    Glass, M.3    Saldeen, T.4
  • 107
    • 0032110436 scopus 로고    scopus 로고
    • 1-antitrypsin
    • 1-antitrypsin. Am J Respir Crit Care Med 1998;158:49-59.
    • (1998) Am J Respir Crit Care Med , vol.158 , pp. 49-59
  • 109
    • 0030345018 scopus 로고    scopus 로고
    • Therapeutic potential of neutrophil-elastase inhibition in pulmonary disease
    • 109. Vender RL. Therapeutic potential of neutrophil-elastase inhibition in pulmonary disease. J Invest Med 1997;44: 531-9.
    • (1997) J Invest Med , vol.44 , pp. 531-539
    • Vender, R.L.1


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