메뉴 건너뛰기




Volumn 405, Issue 3, 2007, Pages 455-463

Characterization of human pre-elafin mutants: Full antipeptidase activity is essential to preserve lung tissue integrity in experimental emphysema

Author keywords

Antipeptidase function; Experimental emphysema; Human pre elafin; Inhibitory loop mutant; Myeloblastin; Neutrophil elastase

Indexed keywords

ANTIPEPTIDASE FUNCTION; EXPERIMENTAL EMPHYSEMA; HUMAN PRE-ELAFIN; INHIBITORY LOOP MUTANT; MYELOBLASTIN; NEUTROPHIL ELASTASE;

EID: 34547490798     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070020     Document Type: Article
Times cited : (17)

References (41)
  • 2
    • 0012350913 scopus 로고
    • Pathology of chronic airflow obstruction
    • Cherniack, N. S, ed, pp, W.B. Saunders Co, Philadelphia
    • Thurlbeck, W. M. (1991) Pathology of chronic airflow obstruction. In Chronic Obstructive Pulmonary Disease (Cherniack, N. S., ed.), pp. 3-20, W.B. Saunders Co., Philadelphia
    • (1991) Chronic Obstructive Pulmonary Disease , pp. 3-20
    • Thurlbeck, W.M.1
  • 3
    • 0035157158 scopus 로고    scopus 로고
    • Neutrophil-derived elastases and their inhibitors: Potential role in the pathogenesis of lung disease
    • Reid, P. T. and Sallenave, J. M. (2001) Neutrophil-derived elastases and their inhibitors: potential role in the pathogenesis of lung disease. Curr. Opin. Investig. Drugs 2, 59-67
    • (2001) Curr. Opin. Investig. Drugs , vol.2 , pp. 59-67
    • Reid, P.T.1    Sallenave, J.M.2
  • 4
    • 0037361991 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): A therapeutic role for inhibitors of MMPs?
    • Belvisi, M. G. and Bottomley, K. M. (2003) The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): a therapeutic role for inhibitors of MMPs? Inflamm. Res. 52, 95-100
    • (2003) Inflamm. Res , vol.52 , pp. 95-100
    • Belvisi, M.G.1    Bottomley, K.M.2
  • 5
    • 0035722954 scopus 로고    scopus 로고
    • Matrix metalloproteinases in lung biology
    • Parks, W. C. and Shapiro, S. D. (2001) Matrix metalloproteinases in lung biology. Respir. Res. 2, 10-19
    • (2001) Respir. Res , vol.2 , pp. 10-19
    • Parks, W.C.1    Shapiro, S.D.2
  • 7
    • 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. and Tucker, G. C. (1997) Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury. FEBS Lett. 402, 111-115
    • (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
  • 9
    • 0029168711 scopus 로고
    • Structural, biochemical, and cell biological aspects of the serine proteinase inhibitor SKALP/elafin/ESI
    • Molhuizen, H. O. and Schalkwijk, J. (1995) Structural, biochemical, and cell biological aspects of the serine proteinase inhibitor SKALP/elafin/ESI. Biol. Chem. 376, 1-7
    • (1995) Biol. Chem , vol.376 , pp. 1-7
    • Molhuizen, H.O.1    Schalkwijk, J.2
  • 10
    • 0033662863 scopus 로고    scopus 로고
    • Production of full-length human pre-elafin, an elastase specific inhibitor, from yeast requires the absence of a functional yapsin 1 (Yps1p) endoprotease
    • Bourbonnais, Y., Larouche, C. and Tremblay, G. M. (2000) Production of full-length human pre-elafin, an elastase specific inhibitor, from yeast requires the absence of a functional yapsin 1 (Yps1p) endoprotease. Protein Expr. Purif. 20, 485-491
    • (2000) Protein Expr. Purif , vol.20 , pp. 485-491
    • Bourbonnais, Y.1    Larouche, C.2    Tremblay, G.M.3
  • 11
    • 0036170699 scopus 로고    scopus 로고
    • Inhibition of human neutrophil elastase-induced acute lung injury in hamsters by recombinant human pre-elafin (trappin-2)
    • Tremblay, G. M., Vachon, E., Larouche, C. and Bourbonnais, Y. (2002) Inhibition of human neutrophil elastase-induced acute lung injury in hamsters by recombinant human pre-elafin (trappin-2). Chest 121, 582-588
    • (2002) Chest , vol.121 , pp. 582-588
    • Tremblay, G.M.1    Vachon, E.2    Larouche, C.3    Bourbonnais, Y.4
  • 12
    • 3042565155 scopus 로고    scopus 로고
    • Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris
    • Zani, M. L., Nobar, S. M., Lacour, S. A., Lemoine, S., Boudier, C., Bieth, J. G. and Moreau, T. (2004) Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris. Eur. J. Biochem. 271, 2370-2378
    • (2004) Eur. J. Biochem , vol.271 , pp. 2370-2378
    • Zani, M.L.1    Nobar, S.M.2    Lacour, S.A.3    Lemoine, S.4    Boudier, C.5    Bieth, J.G.6    Moreau, T.7
  • 13
    • 0027406841 scopus 로고
    • Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kDa elastase-specific inhibitor from human skin
    • Ying, Q. L. and Simon, S. R. (1993) Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kDa elastase-specific inhibitor from human skin. Biochemistry 32, 1866-1874
    • (1993) Biochemistry , vol.32 , pp. 1866-1874
    • Ying, Q.L.1    Simon, S.R.2
  • 14
    • 0035141593 scopus 로고    scopus 로고
    • Kinetics of the inhibition of proteinase 3 by elafin
    • Ying, Q. L. and Simon, S. R. (2001) Kinetics of the inhibition of proteinase 3 by elafin. Am. J. Respir. Cell Mol. Biol. 24, 83-69
    • (2001) Am. J. Respir. Cell Mol. Biol , vol.24 , pp. 83-69
    • Ying, Q.L.1    Simon, S.R.2
  • 15
    • 0036661152 scopus 로고    scopus 로고
    • Anti-inflammatory effect of pre-elafin in lipopolysaccharide-induced acute lung inflammation
    • Vachon, E., Bourbonnais, Y., Bingle, C. D., Rowe, S. J., Janelle, M. F. and Tremblay, G. M. (2002) Anti-inflammatory effect of pre-elafin in lipopolysaccharide-induced acute lung inflammation. Biol. Chem. 383, 1249-1256
    • (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
  • 16
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. U.S.A. 82, 488-492
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 17
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D. and Zakour, R. A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 18
    • 28044448502 scopus 로고    scopus 로고
    • Oxidized elafin and trappin poorly inhibit the elastolytic activity of neutrophil elastase and proteinase 3
    • Nobar, S. M., Zani, M. L., Boudier, C., Moreau, T. and Bieth, J. G. (2005) Oxidized elafin and trappin poorly inhibit the elastolytic activity of neutrophil elastase and proteinase 3. FEBS J. 272, 5883-5893
    • (2005) FEBS J , vol.272 , pp. 5883-5893
    • Nobar, S.M.1    Zani, M.L.2    Boudier, C.3    Moreau, T.4    Bieth, J.G.5
  • 20
    • 0029003409 scopus 로고
    • Theoretical and practical aspects of proteinase inhibition kinetics
    • Bieth, J. G. (1995) Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol. 248, 59-84
    • (1995) Methods Enzymol , vol.248 , pp. 59-84
    • Bieth, J.G.1
  • 21
    • 0037348961 scopus 로고    scopus 로고
    • The pathobiological mechanisms of emphysema models: What do they have in common?
    • Tuder, R. M., McGrath, S. and Neptune, E. (2003) The pathobiological mechanisms of emphysema models: what do they have in common? Pulm. Pharmacol. Ther. 16, 67-78
    • (2003) Pulm. Pharmacol. Ther , vol.16 , pp. 67-78
    • Tuder, R.M.1    McGrath, S.2    Neptune, E.3
  • 22
    • 0023806790 scopus 로고
    • Defenses of the hamster lung against human neutrophil and porcine pancreatic elastase
    • Stone, P. J., Lucey, E. C., Calore, J. D., McMahon, M. P., Snider, G. L. and Franzblau, C. (1988) Defenses of the hamster lung against human neutrophil and porcine pancreatic elastase. Respiration 54, 1-15
    • (1988) Respiration , vol.54 , pp. 1-15
    • Stone, P.J.1    Lucey, E.C.2    Calore, J.D.3    McMahon, M.P.4    Snider, G.L.5    Franzblau, C.6
  • 23
    • 0036141863 scopus 로고    scopus 로고
    • Severity of elastase-induced emphysema is decreased in tumor necrosis factor-α and interleukin-1β receptor-deficient mice
    • Lucey, E. C., Keane, J., Kuang, P. P., Snider, G. L. and Goldstein, R. H. (2002) Severity of elastase-induced emphysema is decreased in tumor necrosis factor-α and interleukin-1β receptor-deficient mice. Lab. Invest. 82, 79-85
    • (2002) Lab. Invest , vol.82 , pp. 79-85
    • Lucey, E.C.1    Keane, J.2    Kuang, P.P.3    Snider, G.L.4    Goldstein, R.H.5
  • 24
    • 0014155288 scopus 로고
    • Internal surface area and other measurements in emphysema
    • Thurlbeck, W. M. (1967) Internal surface area and other measurements in emphysema. Thorax 22, 483-196
    • (1967) Thorax , vol.22 , pp. 483-196
    • Thurlbeck, W.M.1
  • 25
    • 0029811088 scopus 로고    scopus 로고
    • Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 Å resolution
    • Tsunemi, M., Matsuura, Y., Sakakibara, S. and Katsube, Y. (1996) Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 Å resolution. Biochemistry 35, 11570-11576
    • (1996) Biochemistry , vol.35 , pp. 11570-11576
    • Tsunemi, M.1    Matsuura, Y.2    Sakakibara, S.3    Katsube, Y.4
  • 27
    • 33746216559 scopus 로고    scopus 로고
    • Increased local levels of granulocyte colony-stimulating factor are associated with the beneficial effect of pre-elafin (SKALP/trappin-2WAP3) in experimental emphysema
    • Janelle, M. F., Doucet, A., Bouchard, D., Bourbonnais, Y. and Tremblay, G. M. (2006) Increased local levels of granulocyte colony-stimulating factor are associated with the beneficial effect of pre-elafin (SKALP/trappin-2WAP3) in experimental emphysema. Biol. Chem. 387, 903-909
    • (2006) Biol. Chem , vol.387 , pp. 903-909
    • Janelle, M.F.1    Doucet, A.2    Bouchard, D.3    Bourbonnais, Y.4    Tremblay, G.M.5
  • 29
    • 0026773337 scopus 로고
    • Demonstration of skin-derived antileukoproteinase (SKALP) in urine of psoriatic patients
    • Alkemade, H., van de Kerkhof, P. and Schalkwijk, J. (1992) Demonstration of skin-derived antileukoproteinase (SKALP) in urine of psoriatic patients. J. Invest. Dermatol. 99, 3-7
    • (1992) J. Invest. Dermatol , vol.99 , pp. 3-7
    • Alkemade, H.1    van de Kerkhof, P.2    Schalkwijk, J.3
  • 30
    • 0025274374 scopus 로고
    • Location of the protease-inhibitory region of secretory leukocyte protease inhibitor
    • Eisenberg, S. P., Hale, K. K., Heimdal, P. and Thompson, R. C. (1990) Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. J. Biol. Chem. 265, 7976-7981
    • (1990) J. Biol. Chem , vol.265 , pp. 7976-7981
    • Eisenberg, S.P.1    Hale, K.K.2    Heimdal, P.3    Thompson, R.C.4
  • 31
    • 0001918129 scopus 로고
    • Ligand binding: Proteinase-protein inhibitor interactions
    • Bode, W. and Huber, R. (1991) Ligand binding: proteinase-protein inhibitor interactions. Curr. Opin. Struct. Biol. 1, 45-52
    • (1991) Curr. Opin. Struct. Biol , vol.1 , pp. 45-52
    • Bode, W.1    Huber, R.2
  • 32
    • 0025168332 scopus 로고
    • Elafin: An elastase-specific inhibitor of human skin: purification, characterization, and complete amino acid sequence
    • Wiedow, O., Schroder, J. M., Gregory, H., Young, J. A. and Christophers, E. (1990) Elafin: an elastase-specific inhibitor of human skin: purification, characterization, and complete amino acid sequence. J. Biol. Chem. 265, 14791-14795
    • (1990) J. Biol. Chem , vol.265 , pp. 14791-14795
    • Wiedow, O.1    Schroder, J.M.2    Gregory, H.3    Young, J.A.4    Christophers, E.5
  • 33
    • 0031008576 scopus 로고    scopus 로고
    • Hydrophobicity regained
    • Karplus, P. A. (1997) Hydrophobicity regained. Protein Sci 6, 1302-1307
    • (1997) Protein Sci , vol.6 , pp. 1302-1307
    • Karplus, P.A.1
  • 34
    • 0029833222 scopus 로고    scopus 로고
    • The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies
    • Fujinaga, M., Chernaia, M. M., Halenbeck, R., Koths, K. and James, M. N. (1996) The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies. J. Mol. Biol. 261, 267-278
    • (1996) J. Mol. Biol , vol.261 , pp. 267-278
    • Fujinaga, M.1    Chernaia, M.M.2    Halenbeck, R.3    Koths, K.4    James, M.N.5
  • 35
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F. and Walsh, C. T. (1988) The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 37
    • 25844445300 scopus 로고    scopus 로고
    • Differences between human proteinase 3 and neutrophil elastase and their murine homologues are relevant for murine model experiments
    • Wiesner, O., Litwiller, R. D., Hummel, A. M., Viss, M. A., McDonald, C. J., Jenne, D. E., Fass, D. N. and Specks, U. (2005) Differences between human proteinase 3 and neutrophil elastase and their murine homologues are relevant for murine model experiments. FEBS Lett. 579, 5305-5312
    • (2005) FEBS Lett , vol.579 , pp. 5305-5312
    • Wiesner, O.1    Litwiller, R.D.2    Hummel, A.M.3    Viss, M.A.4    McDonald, C.J.5    Jenne, D.E.6    Fass, D.N.7    Specks, U.8
  • 39
    • 0035424123 scopus 로고    scopus 로고
    • Adenoviral augmentation of elafin protects the lung against acute injury mediated by activated neutrophils and bacterial infection
    • Simpson, A. J., Wallace, W. A., Marsden, M. E., Govan, J. R., Porteous, D. J., Haslett, C. and Sallenave, J. M. (2001) Adenoviral augmentation of elafin protects the lung against acute injury mediated by activated neutrophils and bacterial infection. J. Immunol. 167, 1778-1786
    • (2001) J. Immunol , vol.167 , pp. 1778-1786
    • Simpson, A.J.1    Wallace, W.A.2    Marsden, M.E.3    Govan, J.R.4    Porteous, D.J.5    Haslett, C.6    Sallenave, J.M.7
  • 40
    • 0043065436 scopus 로고    scopus 로고
    • Supernatants of Pseudomonas aeruginosa induce the Pseudomonas-specific antibiotic elafin in human keratinocytes
    • Meyer-Hoffert, U., Wichmann, N., Schwichtenberg, L., White, P. C. and Wiedow, O. (2003) Supernatants of Pseudomonas aeruginosa induce the Pseudomonas-specific antibiotic elafin in human keratinocytes. Exp. Dermatol. 12, 418-425
    • (2003) Exp. Dermatol , vol.12 , pp. 418-425
    • Meyer-Hoffert, U.1    Wichmann, N.2    Schwichtenberg, L.3    White, P.C.4    Wiedow, O.5
  • 41
    • 18244405296 scopus 로고    scopus 로고
    • The antimicrobial antiproteinase elafin binds to lipopolysaccharide and modulates macrophage responses
    • McMichael, J. W., Roghanian, A., Jiang, L., Ramage, R. and Sallenave, J. M. (2005) The antimicrobial antiproteinase elafin binds to lipopolysaccharide and modulates macrophage responses. Am. J. Respir. Cell Mol. Biol. 32, 443-452
    • (2005) Am. J. Respir. Cell Mol. Biol , vol.32 , pp. 443-452
    • McMichael, J.W.1    Roghanian, A.2    Jiang, L.3    Ramage, R.4    Sallenave, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.