Design and use of highly specific substrates of neutrophil elastase and proteinase 3

American Journal of Respiratory Cell and Molecular Biology

Volumn 30, Issue 6, 2004, Pages 801-807

  Korkmaz, Brice ^b   Attucci, Sylvie ^b   Moreau, Thierry ^b   Godat, Emmanuel ^b   Juliano, Luiz ^b   Gauthier, Francis ^a  

^a UNIVERSITÉ DE TOURS   (France)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; ARGININE; LEUKOCYTE ELASTASE; MYELOBLASTIN; PROLINE DERIVATIVE; SERINE PROTEINASE INHIBITOR;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; IN VIVO STUDY; NEUTROPHIL;

ANIMALS; BINDING SITES; ENZYME INHIBITORS; HUMANS; LEUKOCYTE ELASTASE; MODELS, MOLECULAR; MYELOBLASTIN; NEUTROPHILS; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; SURFACE PROPERTIES;

FELIS CATUS;

EID: 2942582571     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/rcmb.2003-0139OC     Document Type: Article

References (40)

1. Birrer, P. 1993. Consequences of unbalanced protease in the lung: protease involvement in destruction and local defense mechanisms of the lung. Agents Actions Suppl. 40:3-12.
2. Doring, G. 1994. The role of neutrophil elastase in chronic inflammation. Am. J. Respir. Crit. Care Med. 150:S114-S117.
3. Rao, N. V., N. G. Wehner, B. C. Marshall, W. R. Gray, B. H. Gray, and J. R. Hoidal. 1991. Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase: structural and functional properties. J. Biol. Chem. 266:9540-9548.
4. Bonnefoy, A., and C. Legrand. 2000. Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase. Thromb. Res. 98:323-332.
5. Nakamura, H., K. Yoshimura, N. G. McElvaney, and R. G. Crystal. 1992. Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line. J. Clin. Invest. 89:1478-1484.
6. Ruef, C., D. M. Jefferson, S. E. Schlegel-Haueter, and S. Suter. 1993. Regulation of cytokine secretion by cystic fibrosis airway epithelial cells. Eur. Respir. J. 6:1429-1436.
7. Bank, U., and S. Ansorge. 2001. More than destructive: neutrophil-derived serine proteases in cytokine bioactivity control. J. Leukoc. Biol. 69:197-206.
8. Owen, C. A., and E. J. Campbell. 1999. The cell biology of leukocyte-mediated proteolysis. J. Leukoc. Biol. 65:137-150.
9. Attucci, S., B. Korkmaz, L. Juliano, E. Hazouard, C. Girardin, M. Brillard-Bourdet, S. Rehault, P. Anthonioz, and F. Gauthier. 2002. Measurement of free and membrane-bound cathepsin G in human neutrophils using new sensitive fluorogenic substrates. Biochem. J. 366:965-970.
10. Korkmaz, B., S. Attucci, E. Hazouard, M. Ferrandiere, M. L. Jourdan, M. Brillard-Bourdet, L. Juliano, and F. Gauthier. 2002. Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates. J. Biol. Chem. 277:39074-39081.
11. Campbell, E. J., M. A. Campbell, and C. A. Owen. 2000. Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J. Immunol. 165:3366-3374.
12. Owen, C. A., M. A. Campbell, P. L. Sannes, S. S. Boukedes, and E. J. Campbell. 1995. Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131:775-789.
13. Ying, Q. L., and S. R. Simon. 2002. Elastolysis by proteinase 3 and its inhibition by α(1)-proteinase inhibitor; a mechanism for the incomplete inhibition of ongoing elastolysis. Am. J. Respir. Cell Mol. Biol. 26:356-361.
14. Duranton, J., D. Belorgey, J. Carrere, L. Donato, T. Moritz, and J. G. Bieth. 2000. Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA. FEBS Lett. 473:154-156.
15. Dolman, K. M., B. A. van de Wiel, C. M. Kam, J. E. Kerrigan, C. E. Hack, A. E. von dem Borne, J. C. Powers, and R. Goldschmeding. 1993. Proteinase 3: Substrate specificity and possible pathogenetic effect of Wegener's granulomatosis autoantibodies (c-ANCA) by dysregulation of the enzyme. Adv. Exp. Med. Biol. 336:55-60.
16. Ermolieff, J., J. Duranton, M. Petitou, and J. G. Bieth. 1998. Heparin accelerates the inhibition of cathepsin G by mucus proteinase inhibitor: potent effect of O-butyrylated heparin. Biochem. J. 330:1369-1374.
17. Faller, B., Y. Mely, D. Gerard, and J. G. Bieth. 1992. Heparin-induced conformational change and activation of mucus proteinase inhibitor. Biochemistry 31:8285-8290.
18. Boudier, C., M. Cadene, and J. G. Bieth. 1999. Inhibition of neutrophil cathepsin G by oxidized mucus proteinase inhibitor. Effect of heparin. Biochemistry 38:8451-8457.
19. Sponer, M., H. P. Nick, and H. P. Schnebli. 1991. Different susceptibility of elastase inhibitors to inactivation by proteinases from Staphylococcus aureus and Pseudomonas aeruginosa. Biol. Chem. Hoppe Seyler 372:963-970.
20. Witko-Sarsat, V., E. M. Cramer, C. Hieblot, J. Guichard, P. Nusbaum, S. Lopez, P. Lesavre, and L. Halbwachs-Mecarelli. 1999. Presence of proteinase 3 in secretory vesicles: evidence of a novel, highly mobilizable intracellular pool distinct from azurophil granules. Blood 94:2487-2496.
21. Halbwachs-Mecarelli, L., G. Bessou, P. Lesavre, S. Lopez, and V. Witko-Sarsat. 1995. Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool. FEBS Lett. 374:29-33.
22. Fujinaga, M., M. M. Chernaia, R. Halenbeck, K. Koths, and M. N. James. 1996. The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies. J. Mol. Biol. 261:267-278.
23. Hirata, I. Y., M. H. S. Cezari, C. R. Nakaie, P. Boschcov, A. S. Ito, and M. A. Juliano. 1994. Internally quenched fluorogenic protease substrates: solid phase synthesis and fluorescence spectroscopy of peptides containing orthoaminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett. Pept. Sci. 1:299-308.
24. Serveau, C., T. Moreau, G. X. Zhou, A. ElMoujahed, J. Chao, and F. Gauthier. 1992. Inhibition of rat tissue kallikrein gene family members by rat kallikrein-binding protein and alpha 1-proteinase inhibitor. FEBS Lett. 309: 405-408.
25. Silverman, G. A., P. I. Bird, R. W. Carrell, F. C. Church, P. B. Coughlin, P. G. Gettins, J. A. Irving, D. A. Lomas, C. J. Luke, R. W. Moyer, P. A. Pemberton, E. Remold-O'Donnell, G. S. Salvesen, J. Travis, and J. C. Whisstock. 2001. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins: evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276:33293-33296.
26. Stein, R. L., and A. M. Strimpler. 1987. Catalysis by human leukocyte elastase: aminolysis of acyl-enzymes by amino acid amides and peptides. Biochemistry 26:2238-2242.
27. Owen, C. A., M. A. Campbell, S. S. Boukedes, and E. J. Campbell. 1997. Cytokines regulate membrane-bound leukocyte elastase on neutrophils: a novel mechanism for effector activity. Am. J. Physiol. 272:L385-L393.
28. Hermant, B., S. Bibert, E. Concord, B. Dublet, M. Weidenhaupt, T. Vernet, and D. Gulino-Debrac. 2003. Identification of proteases involved in the proteolysis of vascular endothelium cadherin during neutrophil transmigration. J. Biol. Chem. 278:14002-14012.
29. Witko-Sarsat, V., L. Halbwachs-Mecarelli, A. Schuster, P. Nusbaum, I. Ueki, S. Canteloup, G. Lenoir, B. Descamps-Latscha, and J. A. Nadel. 1999. Proteinase 3, a potent secretagogue in airways, is present in cystic fibrosis sputum. Am. J. Respir. Cell Mol. Biol. 20:729-736.
30. Capodici, C., and R. A. Berg. 1991. Neutrophil collagenase activation: the role of oxidants and cathepsin G. Agents Actions 34:8-10.
31. Ferry, G., M. Lonchampt, L. Pennel, G. de Nanteuil, E. Canet, and G. C. Tucker. 1997. Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury. FEBS Lett. 402:111-115.
32. Niles, J. L., R. T. McCluskey, M. F. Ahmad, and M. A. Arnaout. 1989. Wegener's granulomatosis autoantigen is a novel neutrophil serine proteinase. Blood 74:1888-1893.
33. Dengler, R., U. Munstermann, S. al-Batran, I. Hausner, S. Faderl, C. Nerl, and B. Emmerich. 1995. Immunocytochemical and flow cytometric detection of proteinase 3 (myeloblastin) in normal and leukaemic myeloid cells. Br. J. Haematol. 89:250-257.
34. Witko-Sarsat, V., S. Canteloup, S. Durant, C. Desdouets, R. Chabernaud, P. Lemarchand, and B. Descamps-Latscha. 2002. Cleavage of p21waf1 by proteinase-3, a myeloid-specific serine protease, potentiates cell proliferation. J. Biol. Chem. 277:47338-47347.
35. Yang, J. J., G. A. Preston, W. F. Pendergraft, M. Segelmark, P. Heeringa, S. L. Hogan, J. C. Jennette, and R. J. Falk. 2001. Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants. Am. J. Pathol. 158: 581-592.
36. Koehl, C., C. G. Knight, and J. G. Bieth. 2003. Compared action of neutrophil proteinase 3 and elastase on model substrates: favorable effect of S′-P′ interactions on proteinase 3 catalysis. J. Biol. Chem. 278:12609-12612.
37. Rapala-Kozik, M., J. Potempa, D. Nelson, A. Kozik, and J. Travis. 1999. Comparative cleavage sites within the reactive-site loop of native and oxidized alpha1-proteinase inhibitor by selected bacterial proteinases. Biol. Chem. 380:1211-1216.
38. Bangalore, N., and J. Travis. 1994. Comparison of properties of membrane bound versus soluble forms of human leukocytic elastase and cathepsin G. Biol. Chem. Hoppe Seyler 375:659-666.
39. Goldmann, W. H., J. L. Niles, and M. A. Arnaout. 1999. Interaction of purified human proteinase 3 (PR3) with reconstituted lipid bilayers. Eur. J. Biochem. 261:155-162.
40. Schechter, I., and A. Berger. 1967. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-162.