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Volumn 4, Issue , 2010, Pages 20-31

Antiproteases as therapeutics to target inflammation in cystic fibrosis

Author keywords

Bacteria; Macrophage; Neutrophil; Protease inhibitors; Proteases

Indexed keywords

ADAM PROTEIN; ALPHA 1 ANTITRYPSIN; BACTERIAL ENZYME; CATHEPSIN B; CATHEPSIN G; CYSTATIN; DX 890; ELAFIN; LEUKOCYTE ELASTASE; MATRIX METALLOPROTEINASE; MYELOBLASTIN; ONO 6818; PLACEBO; PROTEASOME; PROTEINASE INHIBITOR; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 77953398632     PISSN: None     EISSN: 18743064     Source Type: Journal    
DOI: 10.2174/1874306401004020020     Document Type: Article
Times cited : (29)

References (156)
  • 3
    • 0036783680 scopus 로고    scopus 로고
    • Interleukin-8: A very important chemokine of the human airway epithelium
    • Strieter RM. Interleukin-8: a very important chemokine of the human airway epithelium. Am J Physiol 2002; 283: L688-L9.
    • (2002) Am J Physiol , vol.283
    • Strieter, R.M.1
  • 4
    • 0027401795 scopus 로고
    • Consequences of unbalanced protease in the lung: Protease involvement in destruction and local defence mechanisms of the lung
    • Birrer P. Consequences of unbalanced protease in the lung: protease involvement in destruction and local defence mechanisms of the lung. Agents Actions Suppl 1993; 40: 3-12.
    • (1993) Agents Actions Suppl , vol.40 , pp. 3-12
    • Birrer, P.1
  • 5
    • 0025228983 scopus 로고
    • Neutrophil elastase and cathepsin G stimulate secretion from bovine airway gland serous cells
    • Sommerhoff CP, Nadel JA, Basbaum CB, Caughey GH. Neutrophil elastase and cathepsin G stimulate secretion from bovine airway gland serous cells. J Clin Invest 1990; 85: 682-89.
    • (1990) J Clin Invest , vol.85 , pp. 682-689
    • Sommerhoff, C.P.1    Nadel, J.A.2    Basbaum, C.B.3    Caughey, G.H.4
  • 6
    • 0027531015 scopus 로고
    • Elastase causes secretory discharge in bronchi of hamsters with elastase-induced secretory cell metaplasia
    • Breuer R, Christensen TG, Lucey EC, Bolbochan G, Stone PJ, Snider GL. Elastase causes secretory discharge in bronchi of hamsters with elastase-induced secretory cell metaplasia. Exp Lung Res 1993; 19: 273-82.
    • (1993) Exp Lung Res , vol.19 , pp. 273-282
    • Breuer, R.1    Christensen, T.G.2    Lucey, E.C.3    Bolbochan, G.4    Stone, P.J.5    Snider, G.L.6
  • 7
    • 0027131471 scopus 로고
    • 1-Proteinase inhibitor, elastase activity, and lung disease severity in cystic fibrosis
    • O'Connor CM, Gaffney K, Keane J, et al. 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
  • 10
    • 0036838657 scopus 로고    scopus 로고
    • Cytosolic pH and the inflammatory microenvironment modulate cell death in human neutrophils after phagocytosis
    • Coakley RJ, Taggart C, McElvaney NG, O'Neill SJ. Cytosolic pH and the inflammatory microenvironment modulate cell death in human neutrophils after phagocytosis. Blood 2002; 100: 3383-91.
    • (2002) Blood , vol.100 , pp. 3383-3391
    • Coakley, R.J.1    Taggart, C.2    McElvaney, N.G.3    O'Neill, S.J.4
  • 11
    • 0025908061 scopus 로고
    • Alginate synthesis by Pseudomonas aeruginosa: A key pathogenic factor in chronic pulmonary infections of cystic fibrosis patients
    • May TB, Shinabarger D, Maharaj R, et al. Alginate synthesis by Pseudomonas aeruginosa: a key pathogenic factor in chronic pulmonary infections of cystic fibrosis patients. Clin Microbiol Rev 1991; 4: 191-206.
    • (1991) Clin Microbiol Rev , vol.4 , pp. 191-206
    • May, T.B.1    Shinabarger, D.2    Maharaj, R.3
  • 12
    • 0034641962 scopus 로고    scopus 로고
    • Quorum sensing signals indicate that cystic fibrosis lungs are infected with bacterial biofilms
    • Singh PK, Schaefer AL, Paresk MR, Moninger TO, Welsh MJ, Greenberg EP. Quorum sensing signals indicate that cystic fibrosis lungs are infected with bacterial biofilms. Nature 2000; 407: 762-4.
    • (2000) Nature , vol.407 , pp. 762-764
    • Singh, P.K.1    Schaefer, A.L.2    Paresk, M.R.3    Moninger, T.O.4    Welsh, M.J.5    Greenberg, E.P.6
  • 13
    • 0017724327 scopus 로고
    • Polymorphonuclear leukocyte bactericidal activity and oxidative metabolism during glutathione peroxidase deficiency
    • Bass DA, DeChatlet LR, Burk RF, Shirley P, Szedja P. Polymorphonuclear leukocyte bactericidal activity and oxidative metabolism during glutathione peroxidase deficiency. Infect Immun 1977; 18: 78-84.
    • (1977) Infect Immun , vol.18 , pp. 78-84
    • Bass, D.A.1    Dechatlet, L.R.2    Burk, R.F.3    Shirley, P.4    Szedja, P.5
  • 14
    • 0027998135 scopus 로고
    • The role of neutrophil elastase in chronic inflammation
    • Doring G. The role of neutrophil elastase in chronic inflammation. Am J Respir Crit Care Med 1994; 150: S114-117.
    • (1994) Am J Respir Crit Care Med , vol.150
    • Doring, G.1
  • 15
    • 0022979529 scopus 로고
    • Complement activation in cystic fibrosis respiratory fluids: In vivo and in vitro generation of C5a and chemotatic activity
    • Fick PA, Robins RA, Squier SU, Schoderbek WE, Russ WD. Complement activation in cystic fibrosis respiratory fluids: in vivo and in vitro generation of C5a and chemotatic activity. Pediatr Res 1986; 20: 1258-68.
    • (1986) Pediatr Res , vol.20 , pp. 1258-1268
    • Fick, P.A.1    Robins, R.A.2    Squier, S.U.3    Schoderbek, W.E.4    Russ, W.D.5
  • 16
    • 0024459145 scopus 로고
    • Complement receptor expression on neutrophils at an inflammatory site, the Pseudomonas infected lung in cystic fibrosis
    • Berger M, Soerensen RJ, Tosi MF, Dearborn DG, Doring G. Complement receptor expression on neutrophils at an inflammatory site, the Pseudomonas infected lung in cystic fibrosis. J Clin Invest 1989; 84: 1302-13.
    • (1989) J Clin Invest , vol.84 , pp. 1302-1313
    • Berger, M.1    Soerensen, R.J.2    Tosi, M.F.3    Dearborn, D.G.4    Doring, G.5
  • 18
    • 0036195343 scopus 로고    scopus 로고
    • Elastase-mediated phosphatidylserine receptor cleavage impairs apopotic cell clearance in cystic fibrosis and bronchiectasis
    • Vandivier RW, Fadok VA, Hoffmann PR, et al. Elastase-mediated phosphatidylserine receptor cleavage impairs apopotic cell clearance in cystic fibrosis and bronchiectasis. J Clin Invest 2002; 109: 661-70.
    • (2002) J Clin Invest , vol.109 , pp. 661-670
    • Vandivier, R.W.1    Fadok, V.A.2    Hoffmann, P.R.3
  • 19
    • 0035929634 scopus 로고    scopus 로고
    • Interleukin-8 up-regulation by neutrophil elastase is mediated by MyD88/IRAK/TRAF-6 in human bronchial epithelium
    • Walsh DE, Greene CM, Carroll TP, et al. Interleukin-8 up-regulation by neutrophil elastase is mediated by MyD88/IRAK/TRAF-6 in human bronchial epithelium. J Biol Chem 2001; 276: 35494-9.
    • (2001) J Biol Chem , vol.276 , pp. 35494-35499
    • Walsh, D.E.1    Greene, C.M.2    Carroll, T.P.3
  • 20
  • 21
    • 0031041367 scopus 로고    scopus 로고
    • Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury
    • Ferry G, Longchampt M, Pennel L, de Nanteuil G, Canet E, Tucker GC. Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury. FEBS Lett 1997; 402: 111-15.
    • (1997) FEBS Lett , vol.402 , pp. 111-115
    • Ferry, G.1    Longchampt, M.2    Pennel, L.3    de Nanteuil, G.4    Canet, E.5    Tucker, G.C.6
  • 22
    • 0029019838 scopus 로고
    • Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase
    • Itoh Y, Nagase H. Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase. J Biol Chem 1995; 270: 16518-21.
    • (1995) J Biol Chem , vol.270 , pp. 16518-16521
    • Itoh, Y.1    Nagase, H.2
  • 23
    • 0034783941 scopus 로고    scopus 로고
    • Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: A role for inflammatory cells in tumor invasion and angiogenesis
    • Shamamian P, Schwartz JD, Pocock BJ, et al. Activation of progelatinase A (MMP-2) by neutrophil elastase, cathepsin G, and proteinase-3: a role for inflammatory cells in tumor invasion and angiogenesis. J Cell Physiol 2001; 189: 197-206.
    • (2001) J Cell Physiol , vol.189 , pp. 197-206
    • Shamamian, P.1    Schwartz, J.D.2    Pocock, B.J.3
  • 24
    • 39449133330 scopus 로고    scopus 로고
    • Airway inflammation in cystic fibrosis
    • Elizur A, Cannon CL, Ferkol TW. Airway inflammation in cystic fibrosis. Chest 2008; 133: 489-95.
    • (2008) Chest , vol.133 , pp. 489-495
    • Elizur, A.1    Cannon, C.L.2    Ferkol, T.W.3
  • 25
  • 26
    • 1942437649 scopus 로고    scopus 로고
    • Linkage of neutrophil serine proteases and decreased surfactant protein-A (SP-A) levels in inflammatory lung disease
    • Rubio F, Cooley J, Accurso FJ, Remold-O'Donnell E. Linkage of neutrophil serine proteases and decreased surfactant protein-A (SP-A) levels in inflammatory lung disease. Thorax 2004; 59: 318-23.
    • (2004) Thorax , vol.59 , pp. 318-323
    • Rubio, F.1    Cooley, J.2    Accurso, F.J.3    Remold-O'Donnell, E.4
  • 27
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines M, Wolf M, Walz A, Baggiolini M. Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett 1994; 352: 231-5.
    • (1994) FEBS Lett , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 28
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact
    • Van den Steen PE, Proost P, Wuyts A, Van Damme J, Opdenakker G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood 2000; 96: 2673-81.
    • (2000) Blood , vol.96 , pp. 2673-2681
    • van den Steen, P.E.1    Proost, P.2    Wuyts, A.3    van Damme, J.4    Opdenakker, G.5
  • 29
    • 0033113290 scopus 로고    scopus 로고
    • Proteinase 3, a potent secretagogue in airways, is present in cystic fibrosis sputum
    • Witko-Sarsat V, Halbwachs-Mecarelli L, Schuster A, et al. Proteinase 3, a potent secretagogue in airways, is present in cystic fibrosis sputum. Am J Respir Cell Mol Biol 1999; 20: 729-36.
    • (1999) Am J Respir Cell Mol Biol , vol.20 , pp. 729-736
    • Witko-Sarsat, V.1    Halbwachs-Mecarelli, L.2    Schuster, A.3
  • 30
    • 0037789214 scopus 로고    scopus 로고
    • Inhibition of proteinase 3 by [alpha] 1-antitrypsin in vitro predicts very fast inhibition in vivo
    • Duranton J, Bieth JG. Inhibition of proteinase 3 by [alpha] 1-antitrypsin in vitro predicts very fast inhibition in vivo. Am J Respir Cell Mol Biol 2003 1: 57-61.
    • (2003) Am J Respir Cell Mol Biol , vol.1 , pp. 57-61
    • Duranton, J.1    Bieth, J.G.2
  • 31
    • 0032930510 scopus 로고    scopus 로고
    • The protease-antiprotease battle in the cystic fibrosis lung
    • Balfour-Lynn IM. The protease-antiprotease battle in the cystic fibrosis lung. J R Soc Med 1999; 92(Suppl 37): 23-30.
    • (1999) J R Soc Med , vol.92 , Issue.SUPPL. 37 , pp. 23-30
    • Balfour-Lynn, I.M.1
  • 32
    • 0028240276 scopus 로고
    • Protease-antiprotease imbalance in the lungs of children with cystic fibrosis
    • Birrer P, McElvaney N, Rüderberg A, et al. Protease-antiprotease imbalance in the lungs of children with cystic fibrosis. Am J Respir Crit Care Med 1994; 150: 207-213.
    • (1994) Am J Respir Crit Care Med , vol.150 , pp. 207-213
    • Birrer, P.1    McElvaney, N.2    Rüderberg, A.3
  • 33
    • 0022642346 scopus 로고
    • Levels of free granulocyte elastase in bronchial secretions from patients with cystic fibrosis: Effect of antimicrobial treatment against Pseudomonas aeruginosa
    • Suter S, Schaad UB, Tegner H, Ohlsson K, Desgrandchamps D, Waldvogel FA. Levels of free granulocyte elastase in bronchial secretions from patients with cystic fibrosis: effect of antimicrobial treatment against Pseudomonas aeruginosa. J Infect Dis 1986; 153: 902-9.
    • (1986) J Infect Dis , vol.153 , pp. 902-909
    • Suter, S.1    Schaad, U.B.2    Tegner, H.3    Ohlsson, K.4    Desgrandchamps, D.5    Waldvogel, F.A.6
  • 34
    • 0022496447 scopus 로고
    • Imbalance between polymorphonuclear leukocyte proteases and antiproteases in chronic pyogenic infections and its relation to the proteolysis of complement component C3
    • Suter S. Imbalance between polymorphonuclear leukocyte proteases and antiproteases in chronic pyogenic infections and its relation to the proteolysis of complement component C3. Complement 1986; 3: 1-24.
    • (1986) Complement , vol.3 , pp. 1-24
    • Suter, S.1
  • 35
    • 0027406841 scopus 로고
    • Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin
    • Ying QL, Simon SR. Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry 1993; 32: 1866-74.
    • (1993) Biochemistry , vol.32 , pp. 1866-1874
    • Ying, Q.L.1    Simon, S.R.2
  • 36
    • 0027581925 scopus 로고
    • Characterization and gene sequence of the precursor of elafin, an elastase-specific inhibitor in bronchial secretions
    • Sallenave JM, Silva A. Characterization and gene sequence of the precursor of elafin, an elastase-specific inhibitor in bronchial secretions. Am J Respir Cell Mol Biol 1993; 8: 439-45.
    • (1993) Am J Respir Cell Mol Biol , vol.8 , pp. 439-445
    • Sallenave, J.M.1    Silva, A.2
  • 37
    • 77953403242 scopus 로고    scopus 로고
    • Cysteine cathepsins in pulmonary diseases
    • In: Taggart CC, Greene CM, Eds., India: Research Signpost
    • Burden RE, Scott CJ. Cysteine cathepsins in pulmonary diseases. In: Taggart CC, Greene CM, Eds. Mechanisms of pulmonary innate immunity. India: Research Signpost 2008; pp. 135-56.
    • (2008) Mechanisms of Pulmonary Innate Immunity , pp. 135-156
    • Burden, R.E.1    Scott, C.J.2
  • 38
    • 33644752722 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in the respiratory tract: Potential implications in asthma and other lung diseases
    • Gueders MM, Foidart JM, Noel A, Cataldo DD. Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in the respiratory tract: potential implications in asthma and other lung diseases. Eur J Pharmacol 2006; 533: 133-44.
    • (2006) Eur J Pharmacol , vol.533 , pp. 133-144
    • Gueders, M.M.1    Foidart, J.M.2    Noel, A.3    Cataldo, D.D.4
  • 39
    • 0021752456 scopus 로고
    • Complete sequence of the cDNA for human alpha 1-antitrypsin and the gene for the S variant
    • Long GL, Chandra T, Woo SL, Davie EW, Kurachi K. Complete sequence of the cDNA for human alpha 1-antitrypsin and the gene for the S variant. Biochemistry 1984; 23: 4828-37.
    • (1984) Biochemistry , vol.23 , pp. 4828-4837
    • Long, G.L.1    Chandra, T.2    Woo, S.L.3    Davie, E.W.4    Kurachi, K.5
  • 40
    • 0023898432 scopus 로고
    • Molecular basis of alpha-1-antitrypsin deficiency
    • Brantly M, Nukiwa T, Crystal RG. Molecular basis of alpha-1-antitrypsin deficiency. Am J Med 1988; 84: 13-31.
    • (1988) Am J Med , vol.84 , pp. 13-31
    • Brantly, M.1    Nukiwa, T.2    Crystal, R.G.3
  • 41
    • 0024529042 scopus 로고
    • The alpha 1-antitrypsin gene and its mutations. Clinical consequences and strategies for therapy
    • Crystal RG, Brantly ML, Hubbard RC, Curiel DT, States DJ, Holmes MD. The alpha 1-antitrypsin gene and its mutations. Clinical consequences and strategies for therapy. Chest 1989; 95: 196-208.
    • (1989) Chest , vol.95 , pp. 196-208
    • Crystal, R.G.1    Brantly, M.L.2    Hubbard, R.C.3    Curiel, D.T.4    States, D.J.5    Holmes, M.D.6
  • 42
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • 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
  • 43
    • 0022472015 scopus 로고
    • Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals
    • Mornex JF, Chytil-Weir A, Martinet Y, Courtney M, LeCocq JP, Crystal RG. Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals. J Clin Invest 1986; 77: 1952-61.
    • (1986) J Clin Invest , vol.77 , pp. 1952-1961
    • Mornex, J.F.1    Chytil-Weir, A.2    Martinet, Y.3    Courtney, M.4    Lecocq, J.P.5    Crystal, R.G.6
  • 44
    • 0025833475 scopus 로고
    • Human neutrophils express the alpha 1-antitrypsin gene and produce alpha 1-antitrypsin
    • du Bois RM, Bernaudin JF, Paakko P, et al. Human neutrophils express the alpha 1-antitrypsin gene and produce alpha 1-antitrypsin. Blood 1991; 77: 2724-30.
    • (1991) Blood , vol.77 , pp. 2724-2730
    • du Bois, R.M.1    Bernaudin, J.F.2    Paakko, P.3
  • 45
    • 34247884585 scopus 로고    scopus 로고
    • Alpha1-antitrypsin, old dog, new tricks. Alpha1-antitrypsin exerts in vitro anti-inflammatory activity in human monocytes by elevating cAMP
    • Janciauskiene SM, Stevens T. Alpha1-antitrypsin, old dog, new tricks. Alpha1-antitrypsin exerts in vitro anti-inflammatory activity in human monocytes by elevating cAMP. J Biol Chem 2007; 282: 8573-82.
    • (2007) J Biol Chem , vol.282 , pp. 8573-8582
    • Janciauskiene, S.M.1    Stevens, T.2
  • 46
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas DA, Carrell RW. Serpinopathies and the conformational dementias. Nat Rev Genet 2002; 3: 759-68.
    • (2002) Nat Rev Genet , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 48
    • 0023894870 scopus 로고
    • The inhibitory complex of human alpha 1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant
    • Banda MJ, Rice AG, Griffin GL, Senior RM. The inhibitory complex of human alpha 1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant. J Exp Med 1988; 167: 1608-15.
    • (1988) J Exp Med , vol.167 , pp. 1608-1615
    • Banda, M.J.1    Rice, A.G.2    Griffin, G.L.3    Senior, R.M.4
  • 49
    • 0019321009 scopus 로고
    • Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin
    • Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidized 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
  • 50
    • 0018800894 scopus 로고
    • The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center
    • Johnson D, Travis J. The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center. J Biol Chem 1979; 254: 4022-6.
    • (1979) J Biol Chem , vol.254 , pp. 4022-4026
    • Johnson, D.1    Travis, J.2
  • 51
    • 0034282683 scopus 로고    scopus 로고
    • Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity
    • Taggart C, Cervantes-Laurean D, Kim G, et al. Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity. J Biol Chem 2000; 275: 27258-65.
    • (2000) J Biol Chem , vol.275 , pp. 27258-27265
    • Taggart, C.1    Cervantes-Laurean, D.2    Kim, G.3
  • 52
    • 0037150069 scopus 로고    scopus 로고
    • Relationship between protein structure and methionine oxidation in recombinant human alpha 1-antitrypsin
    • Griffiths SW, Cooney CL. Relationship between protein structure and methionine oxidation in recombinant human alpha 1-antitrypsin. Biochemistry 2002; 41: 6245-52.
    • (2002) Biochemistry , vol.41 , pp. 6245-6252
    • Griffiths, S.W.1    Cooney, C.L.2
  • 53
    • 0024501812 scopus 로고
    • Inhibition of neutrophil elastase by alpha-1-proteinase inhibitor oxidized by activated neutrophils
    • Padrines M, Schneider-Pozzer M, Bieth JG. Inhibition of neutrophil elastase by alpha-1-proteinase inhibitor oxidized by activated neutrophils. Am Rev Respir Dis 1989; 139: 783-90.
    • (1989) Am Rev Respir Dis , vol.139 , pp. 783-790
    • Padrines, M.1    Schneider-Pozzer, M.2    Bieth, J.G.3
  • 55
    • 0024498944 scopus 로고
    • Tissue distribution of antileukoprotease and lysozyme in humans
    • Franken C, Meijer CJ, Dijkman JH. Tissue distribution of antileukoprotease and lysozyme in humans. J Histochem Cytochem 1989; 37: 493-8.
    • (1989) J Histochem Cytochem , vol.37 , pp. 493-498
    • Franken, C.1    Meijer, C.J.2    Dijkman, J.H.3
  • 56
    • 0022978893 scopus 로고
    • Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus
    • Heinzel R, Appelhans H, Gassen G, et al. Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus. Eur J Biochem 1986; 160: 61-7.
    • (1986) Eur J Biochem , vol.160 , pp. 61-67
    • Heinzel, R.1    Appelhans, H.2    Gassen, G.3
  • 58
    • 0023056196 scopus 로고
    • Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases
    • Stetler G, Brewer MT, Thompson RC. Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases. Nucleic Acids Res 1986; 14: 7883-96.
    • (1986) Nucleic Acids Res , vol.14 , pp. 7883-7896
    • Stetler, G.1    Brewer, M.T.2    Thompson, R.C.3
  • 59
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase
    • Thompson RC, Ohlsson K. Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc Natl Acad Sci USA 1986; 83: 6692-6.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6692-6696
    • Thompson, R.C.1    Ohlsson, K.2
  • 60
    • 0037113123 scopus 로고    scopus 로고
    • A locus on human chromosome 20 contains several genes expressing protease inhibitor domains with homology to whey acidic protein
    • Clauss A, Lilja H, Lundwall A. A locus on human chromosome 20 contains several genes expressing protease inhibitor domains with homology to whey acidic protein. Biochem J 2002; 368: 233-42.
    • (2002) Biochem J , vol.368 , pp. 233-242
    • Clauss, A.1    Lilja, H.2    Lundwall, A.3
  • 61
    • 77953402693 scopus 로고    scopus 로고
    • SLPI and elafin: Multifunctional components of the respiratory tract
    • In: Taggart CC & Greene CM, Eds., India: Research Signpost
    • Weldon S, McGarry N, Taggart CC. SLPI and elafin: multifunctional components of the respiratory tract. In: Taggart CC & Greene CM, Eds. Mechanisms of pulmonary innate immunity. India: Research Signpost 2008; p. 201.
    • (2008) Mechanisms of Pulmonary Innate Immunity , pp. 201
    • Weldon, S.1    McGarry, N.2    Taggart, C.C.3
  • 62
    • 49849089121 scopus 로고    scopus 로고
    • Novel innate immune functions of the whey acidic protein family
    • Bingle CD, Vyakarnam A. Novel innate immune functions of the whey acidic protein family. Trends Immunol 2008; 29: 444-53.
    • (2008) Trends Immunol , vol.29 , pp. 444-453
    • Bingle, C.D.1    Vyakarnam, A.2
  • 63
    • 38649083162 scopus 로고    scopus 로고
    • Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family
    • Moreau T, Baranger K, Dadé S, Dallet-Choisy S, Guyot N, Zani ML. Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family. Biochimie 2008; 90: 284-95.
    • (2008) Biochimie , vol.90 , pp. 284-295
    • Moreau, T.1    Baranger, K.2    Dadé, S.3    Dallet-Choisy, S.4    Guyot, N.5    Zani, M.L.6
  • 64
  • 66
    • 0030941175 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor: A macrophage product induced by and antagonistic to bacterial lipopolysaccharide
    • Jin FY, Nathan C, Radzioch D, Ding A. Secretory leukocyte protease inhibitor: a macrophage product induced by and antagonistic to bacterial lipopolysaccharide. Cell 1997; 88: 417-26.
    • (1997) Cell , vol.88 , pp. 417-426
    • Jin, F.Y.1    Nathan, C.2    Radzioch, D.3    Ding, A.4
  • 67
    • 0030977618 scopus 로고    scopus 로고
    • Secretory leukocyte proteinase inhibitor is a major leukocyte elastase inhibitor in human neutrophils
    • Sallenave JM, Si-Ta Har M, Cox G, Chignard M, Gauldie J. Secretory leukocyte proteinase inhibitor is a major leukocyte elastase inhibitor in human neutrophils. J Leukoc Biol 1997; 61: 695-702.
    • (1997) J Leukoc Biol , vol.61 , pp. 695-702
    • Sallenave, J.M.1    Si-Ta Har, M.2    Cox, G.3    Chignard, M.4    Gauldie, J.5
  • 70
    • 0037416147 scopus 로고    scopus 로고
    • Increased susceptibility to LPS-induced endotoxin shock in secretory leukoprotease inhibitor (SLPI)-deficient mice
    • Nakamura A, Mori Y, Hagiwara K, et al. Increased susceptibility to LPS-induced endotoxin shock in secretory leukoprotease inhibitor (SLPI)-deficient mice. J Exp Med 2003; 197: 669-74.
    • (2003) J Exp Med , vol.197 , pp. 669-674
    • Nakamura, A.1    Mori, Y.2    Hagiwara, K.3
  • 71
    • 0032590012 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB activation and augmentation of IkappaBbeta by secretory leukocyte protease inhibitor during lung inflammation
    • Lentsch AB, Jordan JA, Czermak BJ, et al. Inhibition of NF-kappaB activation and augmentation of IkappaBbeta by secretory leukocyte protease inhibitor during lung inflammation. Am J Pathol 1999; 154: 239-47.
    • (1999) Am J Pathol , vol.154 , pp. 239-247
    • Lentsch, A.B.1    Jordan, J.A.2    Czermak, B.J.3
  • 72
    • 0033871521 scopus 로고    scopus 로고
    • Anti-inflammatory effects of mutant forms of secretory leukocyte protease inhibitor
    • Mulligan MS, Lentsch AB, Huber-Lang M, et al. Anti-inflammatory effects of mutant forms of secretory leukocyte protease inhibitor. Am J Pathol 2000; 156: 1033-9.
    • (2000) Am J Pathol , vol.156 , pp. 1033-1039
    • Mulligan, M.S.1    Lentsch, A.B.2    Huber-Lang, M.3
  • 73
    • 29144439305 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor binds to NF-{kappa}B binding sites in monocytes and inhibits p65 binding
    • Taggart CC, Cryan SA, Weldon S, et al. Secretory leukocyte protease inhibitor binds to NF-{kappa}B binding sites in monocytes and inhibits p65 binding. J Exp Med 2005; 202: 1659-68.
    • (2005) J Exp Med , vol.202 , pp. 1659-1668
    • Taggart, C.C.1    Cryan, S.A.2    Weldon, S.3
  • 74
    • 0141501110 scopus 로고    scopus 로고
    • Local impairment of anti-neutrophil elastase capacity in community acquired pneumonia
    • Greene C, Taggart C, Lowe G, Gallagher P, McElvaney N, O'Neill S. Local impairment of anti-neutrophil elastase capacity in community acquired pneumonia. J Infect Dis 2003; 188: 769-76.
    • (2003) J Infect Dis , vol.188 , pp. 769-776
    • Greene, C.1    Taggart, C.2    Lowe, G.3    Gallagher, P.4    McElvaney, N.5    O'Neill, S.6
  • 75
    • 0037072766 scopus 로고    scopus 로고
    • Secretory leucoprotease inhibitor prevents lipopolysaccharide-induced IkappaBalpha degradation without affecting phosphorylation or ubiquitination
    • Taggart CC, Greene CM, McElvaney NG, O'Neill S. Secretory leucoprotease inhibitor prevents lipopolysaccharide-induced IkappaBalpha degradation without affecting phosphorylation or ubiquitination. J Biol Chem 2002; 277: 33648-53.
    • (2002) J Biol Chem , vol.277 , pp. 33648-33653
    • Taggart, C.C.1    Greene, C.M.2    McElvaney, N.G.3    O'Neill, S.4
  • 76
    • 0040469390 scopus 로고
    • The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucus secretions analysed in its complex with bovine alpha-chymotrypsin
    • Grutter MG, Fendrich G, Huber R, Bode W. The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucus secretions analysed in its complex with bovine alpha-chymotrypsin. EMBO J 1988; 7: 345-51.
    • (1988) EMBO J , vol.7 , pp. 345-351
    • Grutter, M.G.1    Fendrich, G.2    Huber, R.3    Bode, W.4
  • 77
    • 0025943193 scopus 로고
    • Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP)
    • Heinzel-Wieland R, Steffens GJ, Flohe L. Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP). Biomed Biochim Acta 1991; 50: 677-81.
    • (1991) Biomed Biochim Acta , vol.50 , pp. 677-681
    • Heinzel-Wieland, R.1    Steffens, G.J.2    Flohe, L.3
  • 78
    • 0035823570 scopus 로고    scopus 로고
    • Cathepsin B, L, and S cleave and inactivate secretory leucoprotease inhibitor
    • Taggart CC, Lowe GJ, Greene CM, et al. Cathepsin B, L, and S cleave and inactivate secretory leucoprotease inhibitor. J Biol Chem 2001; 276: 33345-52.
    • (2001) J Biol Chem , vol.276 , pp. 33345-33352
    • Taggart, C.C.1    Lowe, G.J.2    Greene, C.M.3
  • 79
    • 0025970641 scopus 로고
    • Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor
    • Sallenave JM, Ryle AP. Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor. Biol Chem Hoppe Seyler 1991; 372: 13-21.
    • (1991) Biol Chem Hoppe Seyler , vol.372 , pp. 13-21
    • Sallenave, J.M.1    Ryle, A.P.2
  • 80
    • 0027173236 scopus 로고
    • SKALP/elafin: An elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking
    • Molhuizen HO, Alkemade HA, Zeeuwen PL, de Jongh GJ, Wieringa B, Schalkwijk J. SKALP/elafin: an elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking. J Biol Chem 1993; 268: 12028-32.
    • (1993) J Biol Chem , vol.268 , pp. 12028-12032
    • Molhuizen, H.O.1    Alkemade, H.A.2    Zeeuwen, P.L.3    de Jongh, G.J.4    Wieringa, B.5    Schalkwijk, J.6
  • 81
    • 0036145207 scopus 로고    scopus 로고
    • Expression of tissue transglutaminase and elafin in human coronary artery: Implication for plaque instability
    • Sumi Y, Inoue N, Azumi H, et al. Expression of tissue transglutaminase and elafin in human coronary artery: implication for plaque instability. Atherosclerosis 2002; 160: 31-9.
    • (2002) Atherosclerosis , vol.160 , pp. 31-39
    • Sumi, Y.1    Inoue, N.2    Azumi, H.3
  • 82
    • 0035024013 scopus 로고    scopus 로고
    • Human alveolar macrophages express elafin and secretory leukocyte protease inhibitor
    • Mihaila A, Tremblay GM. Human alveolar macrophages express elafin and secretory leukocyte protease inhibitor. Z Naturforsch [C] 2001; 56: 291-7.
    • (2001) Z Naturforsch [C] , vol.56 , pp. 291-297
    • Mihaila, A.1    Tremblay, G.M.2
  • 83
    • 0030882327 scopus 로고    scopus 로고
    • Re-expression of elafin in 21MT2 breast carcinomas by phorbol 12-myristate 13-acetate is mediated by the Ap1 site in the elafin promoter
    • Zhang M, Magit D, Pardee AB, Sager R. Re-expression of elafin in 21MT2 breast carcinomas by phorbol 12-myristate 13-acetate is mediated by the Ap1 site in the elafin promoter. Cancer Res 1997; 57: 4631-6.
    • (1997) Cancer Res , vol.57 , pp. 4631-4636
    • Zhang, M.1    Magit, D.2    Pardee, A.B.3    Sager, R.4
  • 84
    • 0034926680 scopus 로고    scopus 로고
    • Cytokine-mediated induction of the human elafin gene in pulmonary epithelial cells is regulated by nuclear factor-kappaB
    • Bingle L, Tetley TD, Bingle CD. Cytokine-mediated induction of the human elafin gene in pulmonary epithelial cells is regulated by nuclear factor-kappaB. Am J Respir Cell Mol Biol 2001; 25: 84-91.
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 84-91
    • Bingle, L.1    Tetley, T.D.2    Bingle, C.D.3
  • 85
    • 0035141593 scopus 로고    scopus 로고
    • Kinetics of the inhibition of proteinase 3 by elafin
    • Ying QL, Simon SR. Kinetics of the inhibition of proteinase 3 by elafin. Am J Respir Cell Mol Biol 2001; 24: 83-9.
    • (2001) Am J Respir Cell Mol Biol , vol.24 , pp. 83-89
    • Ying, Q.L.1    Simon, S.R.2
  • 86
    • 0035424123 scopus 로고    scopus 로고
    • Adenoviral augmentation of elafin protects the lung against acute injury mediated by activated neutrophils and bacterial infection
    • Simpson AJ, Wallace WA, Marsden ME, et al. Adenoviral augmentation of elafin protects the lung against acute injury mediated by activated neutrophils and bacterial infection. J Immunol 2001; 167: 1778-86.
    • (2001) J Immunol , vol.167 , pp. 1778-1786
    • Simpson, A.J.1    Wallace, W.A.2    Marsden, M.E.3
  • 87
    • 0036661152 scopus 로고    scopus 로고
    • Anti-inflammatory effect of pre-elafin in lipopolysaccharide-induced acute lung inflammation
    • Vachon E, Bourbonnais Y, Bingle CD, Rowe SJ, Janelle MF, Tremblay GM. Anti-inflammatory effect of pre-elafin in lipopolysaccharide-induced acute lung inflammation. Biol Chem 2002; 383: 1249-56.
    • (2002) Biol Chem , vol.383 , pp. 1249-1256
    • Vachon, E.1    Bourbonnais, Y.2    Bingle, C.D.3    Rowe, S.J.4    Janelle, M.F.5    Tremblay, G.M.6
  • 88
    • 57749104104 scopus 로고    scopus 로고
    • Elafin, an elastase-specific inhibitor, is cleaved by its cognate enzyme neutrophil elastase in sputum from individuals with cystic fibrosis
    • Guyot N, Butler MW, McNally P, et al. Elafin, an elastase-specific inhibitor, is cleaved by its cognate enzyme neutrophil elastase in sputum from individuals with cystic fibrosis. J Biol Chem 2008; 283: 32377-85.
    • (2008) J Biol Chem , vol.283 , pp. 32377-32385
    • Guyot, N.1    Butler, M.W.2    McNally, P.3
  • 89
    • 0036800045 scopus 로고    scopus 로고
    • Synthetic serine elastase inhibitor reduces cigarette smoke-induced emphysema in guinea pigs
    • Wright JL, Farmer SG, Churg A. Synthetic serine elastase inhibitor reduces cigarette smoke-induced emphysema in guinea pigs. Am J Respir Crit Care Med 2002; 166: 954-60.
    • (2002) Am J Respir Crit Care Med , vol.166 , pp. 954-960
    • Wright, J.L.1    Farmer, S.G.2    Churg, A.3
  • 90
    • 0032568249 scopus 로고    scopus 로고
    • Biochemical and pharmacological characterization of FR134043, a novel elastase inhibitor
    • Shinguh Y, Yamazaki A, Inamura N, et al. Biochemical and pharmacological characterization of FR134043, a novel elastase inhibitor. Eur J Pharmacol 1998; 345: 299-308.
    • (1998) Eur J Pharmacol , vol.345 , pp. 299-308
    • Shinguh, Y.1    Yamazaki, A.2    Inamura, N.3
  • 91
    • 0026404402 scopus 로고
    • Biochemistry and pharmacology of ICI 200, 880, a synthetic peptide inhibitor of human neutrophil elastase
    • Williams JC, Stein RL, Giles RE, Krell RD. Biochemistry and pharmacology of ICI 200, 880, a synthetic peptide inhibitor of human neutrophil elastase. Ann N Y Acad Sci 1991; 624: 230-43.
    • (1991) Ann N Y Acad Sci , vol.624 , pp. 230-243
    • Williams, J.C.1    Stein, R.L.2    Giles, R.E.3    Krell, R.D.4
  • 92
    • 0021240432 scopus 로고
    • Protective effect of specific elastase inhibitor in experimental pulmonary emphysema
    • Tarjan E, Peto L, Appel J, Tolnay P. Protective effect of specific elastase inhibitor in experimental pulmonary emphysema. Schweiz Med Wochenschr 1984; 114: 918-20.
    • (1984) Schweiz Med Wochenschr , vol.114 , pp. 918-920
    • Tarjan, E.1    Peto, L.2    Appel, J.3    Tolnay, P.4
  • 93
    • 0023107891 scopus 로고
    • Comparison of alpha-1-antitrypsin levels and antineutrophil elastase capacity of blood and lung in a patient with the alpha-1-antitrypsin phenotype null-null before and during alpha-1-antitrypsin augmentation therapy
    • Wewers MD, Casolaro MA, Crystal RG. Comparison of alpha-1-antitrypsin levels and antineutrophil elastase capacity of blood and lung in a patient with the alpha-1-antitrypsin phenotype null-null before and during alpha-1-antitrypsin augmentation therapy. Am Rev Respir Dis 1987; 135: 539-43.
    • (1987) Am Rev Respir Dis , vol.135 , pp. 539-543
    • Wewers, M.D.1    Casolaro, M.A.2    Crystal, R.G.3
  • 94
    • 0023784904 scopus 로고
    • Biochemical efficacy and safety of monthly augmentation therapy for alpha 1-antitrypsin deficiency
    • Hubbard RC, Sellers S, Czerski D, Stephens L, Crystal RG. Biochemical efficacy and safety of monthly augmentation therapy for alpha 1-antitrypsin deficiency. JAMA 1988; 260: 1259-64.
    • (1988) JAMA , vol.260 , pp. 1259-1264
    • Hubbard, R.C.1    Sellers, S.2    Czerski, D.3    Stephens, L.4    Crystal, R.G.5
  • 95
    • 4644279975 scopus 로고    scopus 로고
    • Reduction in neutrophil elastase concentration by recombinant alphal-antitrypsin (recAAT) does not alter bacterial loading in the sputum of cystic fibrosis patients
    • Moore JE, Shaw A, Millar BC, et al. Reduction in neutrophil elastase concentration by recombinant alphal-antitrypsin (recAAT) does not alter bacterial loading in the sputum of cystic fibrosis patients. Br J Biomed Sci 2004; 61(3): 146-7.
    • (2004) Br J Biomed Sci , vol.61 , Issue.3 , pp. 146-147
    • Moore, J.E.1    Shaw, A.2    Millar, B.C.3
  • 97
  • 98
    • 33846907545 scopus 로고    scopus 로고
    • alpha1-Antitrypsin inhalation reduces airway inflammation in cystic fibrosis patients
    • Griese M, Latzin P, Kappler M, et al. alpha1-Antitrypsin inhalation reduces airway inflammation in cystic fibrosis patients. Eur Respir J 2007; 2: 240-50.
    • (2007) Eur Respir J , vol.2 , pp. 240-250
    • Griese, M.1    Latzin, P.2    Kappler, M.3
  • 99
    • 69249120315 scopus 로고    scopus 로고
    • Lung deposition of inhaled alpha1-proteinase inhibitor in cystic fibrosis and alpha1-antitrypsin deficiency
    • Brand P, Schulte M, Wencker M, et al. Lung deposition of inhaled alpha1-proteinase inhibitor in cystic fibrosis and alpha1-antitrypsin deficiency. Eur Respir J 2009; 34(2): 354-60.
    • (2009) Eur Respir J , vol.34 , Issue.2 , pp. 354-360
    • Brand, P.1    Schulte, M.2    Wencker, M.3
  • 100
    • 0037952712 scopus 로고    scopus 로고
    • Targeted delivery of antiprotease to the epithelial surface of human tracheal xenografts
    • Ferkol T, Cohn LA, Phillips TE, Smith A, Davis PB. Targeted delivery of antiprotease to the epithelial surface of human tracheal xenografts. Am J Respir Crit Care Med 2003; 167: 1374-9.
    • (2003) Am J Respir Crit Care Med , vol.167 , pp. 1374-1379
    • Ferkol, T.1    Cohn, L.A.2    Phillips, T.E.3    Smith, A.4    Davis, P.B.5
  • 102
    • 0026474443 scopus 로고
    • Modulation of airway inflammation in cystic fibrosis. In vivo suppression of interleukin-8 levels on the respiratory epithelial surface by aerosolization of recombinant secretory leukoprotease inhibitor
    • McElvaney NG, Nakamura H, Birrer P, et al. Modulation of airway inflammation in cystic fibrosis. In vivo suppression of interleukin-8 levels on the respiratory epithelial surface by aerosolization of recombinant secretory leukoprotease inhibitor. J Clin Invest 1992; 90: 1296-301.
    • (1992) J Clin Invest , vol.90 , pp. 1296-1301
    • McElvaney, N.G.1    Nakamura, H.2    Birrer, P.3
  • 103
    • 0027495712 scopus 로고
    • Pharmacokinetics of recombinant secretory leukoprotease inhibitor aerosolized to normals and individuals with cystic fibrosis
    • McElvaney NG, Doujaiji B, Moan MJ, Burnham MR, Wu MC, Crystal RG. Pharmacokinetics of recombinant secretory leukoprotease inhibitor aerosolized to normals and individuals with cystic fibrosis. Am Rev Respir Dis 1993; 148: 1056-60.
    • (1993) Am Rev Respir Dis , vol.148 , pp. 1056-1060
    • McElvaney, N.G.1    Doujaiji, B.2    Moan, M.J.3    Burnham, M.R.4    Wu, M.C.5    Crystal, R.G.6
  • 104
    • 0027184036 scopus 로고
    • Recombinant secretory leukoprotease inhibitor augments glutathione levels in lung epithelial lining fluid
    • Gillissen A, Birrer P, McElvaney NG, et al. Recombinant secretory leukoprotease inhibitor augments glutathione levels in lung epithelial lining fluid. J Appl Physiol 1993; 75: 825-32.
    • (1993) J Appl Physiol , vol.75 , pp. 825-832
    • Gillissen, A.1    Birrer, P.2    McElvaney, N.G.3
  • 105
    • 77953458035 scopus 로고    scopus 로고
    • Available from, [Accessed: October 26
    • Proteo Biotech AG. Available from: www.proteo.de/framesets/r-and-d.php?lang=en [Accessed: October 26, 2009].
    • (2009) Proteo Biotech AG
  • 106
    • 0037794398 scopus 로고    scopus 로고
    • Characteristics of EPI-hNE4 aerosol: A new elastase inhibitor for treatment of cystic fibrosis
    • Grimbert D, Vecellio L, Delépine P, et al. Characteristics of EPI-hNE4 aerosol: a new elastase inhibitor for treatment of cystic fibrosis. J Aerosol Med 2003; 16(2): 121-9.
    • (2003) J Aerosol Med , vol.16 , Issue.2 , pp. 121-129
    • Grimbert, D.1    Vecellio, L.2    Delépine, P.3
  • 107
    • 33745941917 scopus 로고    scopus 로고
    • EPI-hNE4, a proteolysis-resistant inhibitor of human neutrophil elastase and potential anti-inflammatory drug for treating cystic fibrosis
    • Attucci S, Gauthier A, Korkmaz B, et al. EPI-hNE4, a proteolysis-resistant inhibitor of human neutrophil elastase and potential anti-inflammatory drug for treating cystic fibrosis. J Pharmacol Exp Ther 2006; 318(2): 803-9.
    • (2006) J Pharmacol Exp Ther , vol.318 , Issue.2 , pp. 803-809
    • Attucci, S.1    Gauthier, A.2    Korkmaz, B.3
  • 108
    • 77953364776 scopus 로고    scopus 로고
    • Ono Pharmaceutical Co., Ltd. Available from, Accessed: October 26
    • Ono Pharmaceutical Co., Ltd. Available from: http://www.ono.co.jp/eng/default.htm [Accessed: October 26, 2009].
    • (2009)
  • 109
    • 0012330613 scopus 로고    scopus 로고
    • Importance of lysosomal cysteine proteases in lung disease
    • Wolters PJ, Chapman HA. Importance of lysosomal cysteine proteases in lung disease. Respir Res 2001; 1: 170-7.
    • (2001) Respir Res , vol.1 , pp. 170-177
    • Wolters, P.J.1    Chapman, H.A.2
  • 110
    • 1842428713 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases in the lung: Role in protein processing and immunoregulation
    • Bühling F, Waldburg N, Reisenauer A, Heimburg A, Golpon H, Welte T. Lysosomal cysteine proteases in the lung: role in protein processing and immunoregulation. Eur Respir J 2004; 23: 620-8.
    • (2004) Eur Respir J , vol.23 , pp. 620-628
    • Bühling, F.1    Waldburg, N.2    Reisenauer, A.3    Heimburg, A.4    Golpon, H.5    Welte, T.6
  • 111
    • 0343091361 scopus 로고    scopus 로고
    • Protease injury in the development of COPD: Thomas A. Neff Lecture
    • Chapman HA Jr, Shi GP. Protease injury in the development of COPD: Thomas A. Neff Lecture. Chest 2000; 117: 295S-99S.
    • (2000) Chest , vol.117
    • Chapman, H.A.1    Shi, G.P.2
  • 113
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • Shi GP, Munger JS, Meara JP, Rich DH, Chapman HA. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J Biol Chem 1992; 267: 7258-62.
    • (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
  • 114
    • 0036014822 scopus 로고    scopus 로고
    • Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes
    • Brasch F, Ten Brinke A, Johnen G, et al. Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am J Respir Cell Mol Biol 2002; 26: 659-70.
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 659-670
    • Brasch, F.1    Ten Brinke, A.2    Johnen, G.3
  • 115
    • 0028673153 scopus 로고
    • Cathepsin S and related lysosomal endopeptidases
    • Kirschke H, Wiederanders B. Cathepsin S and related lysosomal endopeptidases. Methods Enzymol 1994; 244: 500-11.
    • (1994) Methods Enzymol , vol.244 , pp. 500-511
    • Kirschke, H.1    Wiederanders, B.2
  • 116
    • 0032546934 scopus 로고    scopus 로고
    • Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I
    • Wolters PJ, Raymond WW, Blount JL, Caughey GH. Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I. J Biol Chem 1998; 273: 15514-20.
    • (1998) J Biol Chem , vol.273 , pp. 15514-15520
    • Wolters, P.J.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 117
    • 0036847496 scopus 로고    scopus 로고
    • Airways in cystic fibrosis are acidified: Detection by exhaled breath condensate
    • Tate S, MacGregor G, Davis M, Innes JA, Greening AP. Airways in cystic fibrosis are acidified: detection by exhaled breath condensate. Thorax 2002; 57: 926-9.
    • (2002) Thorax , vol.57 , pp. 926-929
    • Tate, S.1    MacGregor, G.2    Davis, M.3    Innes, J.A.4    Greening, A.P.5
  • 118
    • 34247588138 scopus 로고    scopus 로고
    • Neutrophil elastase up-regulates cathepsin B and matrix metalloprotease-2 expression
    • Geraghty P, Rogan MP, Greene CM, et al. Neutrophil elastase up-regulates cathepsin B and matrix metalloprotease-2 expression. J Immunol 2007; 178: 5871-8.
    • (2007) J Immunol , vol.178 , pp. 5871-5878
    • Geraghty, P.1    Rogan, M.P.2    Greene, C.M.3
  • 119
    • 0028939165 scopus 로고
    • Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: Modulation of cathepsin B activity by neutrophil elastase
    • Burnett D, Abrahamson M, Devalia JL, Sapsford RJ, Davies RJ, Buttle DJ. Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by neutrophil elastase. Arch Biochem. Biophys 1995; 317: 305-10.
    • (1995) Arch Biochem. Biophys , vol.317 , pp. 305-310
    • Burnett, D.1    Abrahamson, M.2    Devalia, J.L.3    Sapsford, R.J.4    Davies, R.J.5    Buttle, D.J.6
  • 120
    • 0037768888 scopus 로고    scopus 로고
    • Inactivation of human -defensins 2 and 3 by elastolytic cathepsins
    • Taggart CC, Greene CM, Smith SG, et al. Inactivation of human -defensins 2 and 3 by elastolytic cathepsins. J Immunol 2003; 171: 931-7.
    • (2003) J Immunol , vol.171 , pp. 931-937
    • Taggart, C.C.1    Greene, C.M.2    Smith, S.G.3
  • 121
    • 4644263748 scopus 로고    scopus 로고
    • Loss of microbicidal activity and increased formation of biofilm due to decreased lactoferrin activity in patients with cystic fibrosis
    • Rogan MP, Taggart CC, Greene CM, Murphy PG, O'Neill SJ, McElvaney NG. Loss of microbicidal activity and increased formation of biofilm due to decreased lactoferrin activity in patients with cystic fibrosis. J Infect Dis 2004; 190: 1245-53.
    • (2004) J Infect Dis , vol.190 , pp. 1245-1253
    • Rogan, M.P.1    Taggart, C.C.2    Greene, C.M.3    Murphy, P.G.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 122
    • 0023614980 scopus 로고
    • Activity of the lysosomal cysteine proteinases (cathepsin B,H,L) and a metalloproteinase (MMP-7-ase) in the serum of cystic fibrosis homozygous children
    • László A, Sohár I, Gyurkovits K. Activity of the lysosomal cysteine proteinases (cathepsin B,H,L) and a metalloproteinase (MMP-7-ase) in the serum of cystic fibrosis homozygous children. Acta Paediatr Hung 1987; 28: 175-8.
    • (1987) Acta Paediatr Hung , vol.28 , pp. 175-178
    • László, A.1    Sohár, I.2    Gyurkovits, K.3
  • 123
    • 0027518670 scopus 로고
    • Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I
    • McGuire MJ, Lipsky PE, Thiele DL. Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I. J Biol Chem 1993; 268: 2458-67.
    • (1993) J Biol Chem , vol.268 , pp. 2458-2467
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 124
    • 0028945071 scopus 로고
    • Human prochymase activation. A novel role for heparin in zymogen processing
    • Murakami M, Karnik SS, Husain A. Human prochymase activation. A novel role for heparin in zymogen processing. J Biol Chem 1995; 270: 2218-23.
    • (1995) J Biol Chem , vol.270 , pp. 2218-2223
    • Murakami, M.1    Karnik, S.S.2    Husain, A.3
  • 125
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham CT, Ley TJ. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc Natl Acad Sci USA 1999; 96: 8627-32.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 126
    • 0022843745 scopus 로고
    • Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region
    • Johnson DA, Barrett AJ, Mason RW. Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region. J Biol Chem 1986; 261: 14748-51.
    • (1986) J Biol Chem , vol.261 , pp. 14748-14751
    • Johnson, D.A.1    Barrett, A.J.2    Mason, R.W.3
  • 127
    • 0026040859 scopus 로고
    • Regulation of cystatin C activity by serine proteinases
    • Abrahamson M, Buttle DJ, Mason RW, et al. Regulation of cystatin C activity by serine proteinases. Biomed Biochim Acta 1991; 50: 587-93.
    • (1991) Biomed Biochim Acta , vol.50 , pp. 587-593
    • Abrahamson, M.1    Buttle, D.J.2    Mason, R.W.3
  • 128
    • 33947604810 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva O, Reinheckel T, Peters C, Turk D, Turk V, Turk B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr Pharm Des 2007; 13: 387-40.
    • (2007) Curr Pharm Des , vol.13 , pp. 387-340
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 129
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17: 463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 130
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloprotein-ases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL, Lopez-Boado YS. Matrix metalloprotein-ases as modulators of inflammation and innate immunity. Nat Rev Immunol 2004; 4: 617-29.
    • (2004) Nat Rev Immunol , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 131
    • 66749185766 scopus 로고    scopus 로고
    • Association of lower airway inflammation with physiologic findings in young children with cystic fibrosis
    • Peterson-Carmichael SL, Harris WT, Goel R, et al. Association of lower airway inflammation with physiologic findings in young children with cystic fibrosis. Pediatr Pulmonol 2009; 44: 503-11.
    • (2009) Pediatr Pulmonol , vol.44 , pp. 503-511
    • Peterson-Carmichael, S.L.1    Harris, W.T.2    Goel, R.3
  • 132
    • 0036845446 scopus 로고    scopus 로고
    • Matrix metalloproteases in BAL fluid of patients with cystic fibrosis and their modulation by treatment with dornase alpha
    • Ratjen F, Hartog CM, Paul K, Wermelt J, Braun J. Matrix metalloproteases in BAL fluid of patients with cystic fibrosis and their modulation by treatment with dornase alpha. Thorax 2002; 57: 930-4.
    • (2002) Thorax , vol.57 , pp. 930-934
    • Ratjen, F.1    Hartog, C.M.2    Paul, K.3    Wermelt, J.4    Braun, J.5
  • 133
    • 36048972322 scopus 로고    scopus 로고
    • Airway remodelling in children with cystic fibrosis
    • Hilliard TN, Regamey N, Shute JK, et al. Airway remodelling in children with cystic fibrosis. Thorax 2007; 62: 1074-80.
    • (2007) Thorax , vol.62 , pp. 1074-1080
    • Hilliard, T.N.1    Regamey, N.2    Shute, J.K.3
  • 134
    • 34447522038 scopus 로고    scopus 로고
    • Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients
    • Gaggar A, Li Y, Weathington N, et al. Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients. Am J Physiol Lung Cell Mol Physiol 2007; 293: L96-L104.
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.293
    • Gaggar, A.1    Li, Y.2    Weathington, N.3
  • 135
    • 16244368754 scopus 로고    scopus 로고
    • Induced sputum matrix metalloproteinase-9 correlates with lung function and airway inflammation in children with cystic fibrosis
    • Sagel SD, Kapsner RK, Osberg I. Induced sputum matrix metalloproteinase-9 correlates with lung function and airway inflammation in children with cystic fibrosis. Pediatr Pulmonol 2005; 39: 224-32.
    • (2005) Pediatr Pulmonol , vol.39 , pp. 224-232
    • Sagel, S.D.1    Kapsner, R.K.2    Osberg, I.3
  • 136
    • 0031041367 scopus 로고    scopus 로고
    • Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury
    • Ferry G, Lonchampt M, Pennel L, de Nanteuil G, Canet E, Tucker GC. Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury. FEBS Lett 1997; 402: 111-15.
    • (1997) FEBS Lett , vol.402 , pp. 111-115
    • Ferry, G.1    Lonchampt, M.2    Pennel, L.3    de Nanteuil, G.4    Canet, E.5    Tucker, G.C.6
  • 137
    • 36849094431 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation
    • Manicone AM, McGuire JK. Matrix metalloproteinases as modulators of inflammation. Semin Cell Dev Biol 2008; 19: 34-41.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 34-41
    • Manicone, A.M.1    McGuire, J.K.2
  • 138
    • 0025991867 scopus 로고
    • Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity
    • Desrochers PE, Jeffrey JJ, Weiss SJ. Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity. J Clin Invest 1991; 87: 2258-65.
    • (1991) J Clin Invest , vol.87 , pp. 2258-2265
    • Desrochers, P.E.1    Jeffrey, J.J.2    Weiss, S.J.3
  • 139
    • 0028201849 scopus 로고
    • Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin
    • Zhang Z, Winyard PG, Chidwick K, et al. Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin. Biochim Biophys Acta 1994; 1199: 224-8.
    • (1994) Biochim Biophys Acta , vol.1199 , pp. 224-228
    • Zhang, Z.1    Winyard, P.G.2    Chidwick, K.3
  • 140
    • 0027033055 scopus 로고
    • Cleavage of alpha 1-antitrypsin by human neutrophil collagenase
    • Michaelis J, Vissers MC, Winterbourn CC. Cleavage of alpha 1-antitrypsin by human neutrophil collagenase. Matrix Suppl 1992; 1: 80-1.
    • (1992) Matrix Suppl , vol.1 , pp. 80-81
    • Michaelis, J.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 141
    • 0034257889 scopus 로고    scopus 로고
    • The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 S
    • Liu Z, Zhou X, Shapiro SD, et al. The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 S. Cell 2000; 102: 647-55.
    • (2000) Cell , vol.102 , pp. 647-655
    • Liu, Z.1    Zhou, X.2    Shapiro, S.D.3
  • 143
    • 63149116632 scopus 로고    scopus 로고
    • Surfactant protein A enhances production of secretory leukoprotease inhibitor and protects it from cleavage by matrix metalloproteinases
    • Ramadas RA, Wu L, LeVine AM. Surfactant protein A enhances production of secretory leukoprotease inhibitor and protects it from cleavage by matrix metalloproteinases. J Immunol 2009; 182: 1560-7.
    • (2009) J Immunol , vol.182 , pp. 1560-1567
    • Ramadas, R.A.1    Wu, L.2    Levine, A.M.3
  • 144
    • 0036172155 scopus 로고    scopus 로고
    • Secretory leukocyte proteinase inhibitor and elafin are resistant to degradation by MMP-8
    • Henry MT, McMahon K, Costello C, Fitzgerald MX, O'Connor CM. Secretory leukocyte proteinase inhibitor and elafin are resistant to degradation by MMP-8. Exp Lung Res 2002; 28: 85-97.
    • (2002) Exp Lung Res , vol.28 , pp. 85-97
    • Henry, M.T.1    McMahon, K.2    Costello, C.3    Fitzgerald, M.X.4    O'Connor, C.M.5
  • 145
    • 63949084246 scopus 로고    scopus 로고
    • Expression of ADAMs (a disintegrin and metalloprotease) in the human lung
    • Dijkstra A, Postma DS, Noordhoek JA, et al. Expression of ADAMs (a disintegrin and metalloprotease) in the human lung. Virchows Arch 2009; 454: 441-9.
    • (2009) Virchows Arch , vol.454 , pp. 441-449
    • Dijkstra, A.1    Postma, D.S.2    Noordhoek, J.A.3
  • 146
    • 24744464353 scopus 로고    scopus 로고
    • Neutrophil elastase induces MUC5AC mucin production in human airway epithelial cells via a cascade involving protein kinase C, reactive oxygen species, and TNF-alpha-converting enzyme
    • Shao MX, Nadel JA. Neutrophil elastase induces MUC5AC mucin production in human airway epithelial cells via a cascade involving protein kinase C, reactive oxygen species, and TNF-alpha-converting enzyme. J Immunol 2005; 175: 4009-16.
    • (2005) J Immunol , vol.175 , pp. 4009-4016
    • Shao, M.X.1    Nadel, J.A.2
  • 147
    • 0037474312 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding
    • Thathiah A, Blobel CP, Carson DD. Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding. J Biol Chem 2003; 278: 3386-94.
    • (2003) J Biol Chem , vol.278 , pp. 3386-3394
    • Thathiah, A.1    Blobel, C.P.2    Carson, D.D.3
  • 148
    • 4344714770 scopus 로고    scopus 로고
    • MT1-MMP mediates MUC1 shedding independently of TACE/ADAM17
    • Thathiah A, Carson DD. MT1-MMP mediates MUC1 shedding independently of TACE/ADAM17. Biochem J 2004; 362: 363-73.
    • (2004) Biochem J , vol.362 , pp. 363-373
    • Thathiah, A.1    Carson, D.D.2
  • 149
    • 0035021424 scopus 로고    scopus 로고
    • Muc1 mucins on the cell surface are adhesion sites for Pseudomonas aeruginosa
    • Lillehoj EP, Hyun SW, Kim BT, et al. Muc1 mucins on the cell surface are adhesion sites for Pseudomonas aeruginosa. Am J Physiol Lung Cell Mol Physiol 2001; 280: L181-L187.
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.280
    • Lillehoj, E.P.1    Hyun, S.W.2    Kim, B.T.3
  • 150
    • 33745190973 scopus 로고    scopus 로고
    • Selective inhibition of endoplasmic reticulum-associated degradation rescues F508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels
    • Vij N, Fang S, Zeitlin PL. Selective inhibition of endoplasmic reticulum-associated degradation rescues F508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels. J Biol Chem 2006; 281: 17369-78.
    • (2006) J Biol Chem , vol.281 , pp. 17369-17378
    • Vij, N.1    Fang, S.2    Zeitlin, P.L.3
  • 151
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995; 83: 121-7.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 152
    • 0038649638 scopus 로고    scopus 로고
    • A phase 2 study of bortezomib in relapsed refractory myeloma
    • Mitchell BS. A phase 2 study of bortezomib in relapsed refractory myeloma. N Eng J Med 2003; 348: 2597-8.
    • (2003) N Eng J Med , vol.348 , pp. 2597-2598
    • Mitchell, B.S.1
  • 153
    • 0034615573 scopus 로고    scopus 로고
    • Bacterial proteinases as targets for the development of second-generation antibiotics
    • Travis J, Potempa J. Bacterial proteinases as targets for the development of second-generation antibiotics. Biochimica Biophysica Acta 2000; 1477: 35-50.
    • (2000) Biochimica Biophysica Acta , vol.1477 , pp. 35-50
    • Travis, J.1    Potempa, J.2
  • 154
    • 0031769858 scopus 로고    scopus 로고
    • Cellular function of elastase in Pseudomonas aeruginosa: Role in the cleavage of nucleoside disphosphate kinase and in alginate synthesis
    • Kamath S, Kapatral V, Chakrabarty AM. Cellular function of elastase in Pseudomonas aeruginosa: role in the cleavage of nucleoside disphosphate kinase and in alginate synthesis. Mol Microbiol 1998; 30: 933-41.
    • (1998) Mol Microbiol , vol.30 , pp. 933-941
    • Kamath, S.1    Kapatral, V.2    Chakrabarty, A.M.3
  • 155
    • 34547622484 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain-specific endoproteolysis
    • Leduc D, Beaufort N, de Bentzmann S, et al. The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain-specific endoproteolysis. Infect Immun 2007; 75(8): 3848-58.
    • (2007) Infect Immun , vol.75 , Issue.8 , pp. 3848-3858
    • Leduc, D.1    Beaufort, N.2    de Bentzmann, S.3
  • 156
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan JRW, Deretic V. Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol Rev 1996; 660: 539-74.
    • (1996) Microbiol Rev , vol.660 , pp. 539-574
    • Govan, J.R.W.1    Deretic, V.2


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