C. T. Pham, Neutrophil serine proteases: specific regulators of inflammation, Nature Reviews Immunology, vol.69, issue.7, pp.541-550, 2006.
DOI : 10.1038/nri1841

C. C. Taggart, C. M. Greene, T. P. Carroll, S. J. O-'neill, and N. G. Mcelvaney, Elastolytic Proteases, American Journal of Respiratory and Critical Care Medicine, vol.171, issue.10, pp.1070-1076, 2005.
DOI : 10.1164/rccm.200407-881PP

B. Korkmaz, T. Moreau, and F. Gauthier, Neutrophil elastase, proteinase 3 and cathepsin G: Physicochemical properties, activity and physiopathological functions, Biochimie, vol.90, issue.2, pp.227-242, 2008.
DOI : 10.1016/j.biochi.2007.10.009

L. Halbwachs-mecarelli, G. Bessou, P. Lesavre, S. Lopez, and V. Witko-sarsat, Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool, FEBS Letters, vol.24, issue.1, pp.29-33, 1995.
DOI : 10.1016/0014-5793(95)01073-N

A. Schreiber, A. Busjahn, F. C. Luft, and R. Kettritz, Membrane Expression of Proteinase 3 Is Genetically Determined, Journal of the American Society of Nephrology, vol.14, issue.1, pp.68-75, 2003.
DOI : 10.1097/01.ASN.0000040751.83734.D1

S. Bauer, M. Abdgawad, L. Gunnarsson, M. Segelmark, H. Tapper et al., Proteinase 3 and CD177 are expressed on the plasma membrane of the same subset of neutrophils, Journal of Leukocyte Biology, vol.81, issue.2, pp.458-464, 2007.
DOI : 10.1189/jlb.0806514

S. Von-vietinghoff, C. Eulenberg, M. Wellner, F. C. Luft, and R. Kettritz, Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing, Clinical & Experimental Immunology, vol.44, issue.3, pp.508-516, 2004.
DOI : 10.1111/j.1365-2249.2008.03663.x

A. Schreiber, F. C. Luft, and R. Kettritz, Membrane proteinase 3 expression and ANCA-induced neutrophil activation, Kidney International, vol.65, issue.6, pp.2172-2183, 2004.
DOI : 10.1111/j.1523-1755.2004.00640.x

C. P. Rooney, C. Taggart, R. Coakley, N. G. Mcelvaney, O. Neill et al., Anti???Proteinase 3 Antibody Activation of Neutrophils Can Be Inhibited by ?? 1-Antitrypsin, American Journal of Respiratory Cell and Molecular Biology, vol.24, issue.6, pp.747-754, 2001.
DOI : 10.1165/ajrcmb.24.6.4147

B. Korkmaz, S. Attucci, E. Hazouard, M. Ferrandiere, M. L. Jourdan et al., Discriminating between the Activities of Human Neutrophil Elastase and Proteinase 3 Using Serpin-derived Fluorogenic Substrates, Journal of Biological Chemistry, vol.277, issue.42, pp.39074-39081, 2002.
DOI : 10.1074/jbc.M202918200

B. Korkmaz, S. Attucci, M. L. Jourdan, L. Juliano, and F. Gauthier, Inhibition of Neutrophil Elastase by ??1-Protease Inhibitor at the Surface of Human Polymorphonuclear Neutrophils, The Journal of Immunology, vol.175, issue.5, pp.3329-3338, 2005.
DOI : 10.4049/jimmunol.175.5.3329

S. Attucci, A. Gauthier, B. Korkmaz, P. Delepine, M. F. Martino et al., EPI-hNE4, a Proteolysis-Resistant Inhibitor of Human Neutrophil Elastase and Potential Anti-Inflammatory Drug for Treating Cystic Fibrosis, Journal of Pharmacology and Experimental Therapeutics, vol.318, issue.2, pp.803-809, 2006.
DOI : 10.1124/jpet.106.103440

B. Korkmaz, P. Poutrain, E. Hazouard, M. De-monte, S. Attucci et al., Competition between Elastase and Related Proteases from Human Neutrophil for Binding to ??1-Protease Inhibitor, American Journal of Respiratory Cell and Molecular Biology, vol.32, issue.6, pp.553-559, 2005.
DOI : 10.1165/rcmb.2004-0374OC

B. Korkmaz, S. Attucci, M. A. Juliano, T. Kalupov, M. L. Jourdan et al., Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates, Nature Protocols, vol.29, issue.6, pp.991-1000, 2008.
DOI : 10.1038/nprot.2008.63

E. J. Campbell, M. A. Campbell, and C. A. Owen, Bioactive Proteinase 3 on the Cell Surface of Human Neutrophils: Quantification, Catalytic Activity, and Susceptibility to Inhibition, The Journal of Immunology, vol.165, issue.6, pp.3366-3374, 2000.
DOI : 10.4049/jimmunol.165.6.3366

V. Brinkmann, U. Reichard, C. Goosmann, B. Fauler, Y. Uhlemann et al., Neutrophil Extracellular Traps Kill Bacteria, Science, vol.303, issue.5663, pp.1532-1535, 2004.
DOI : 10.1126/science.1092385

C. Serveau, T. Moreau, G. X. Zhou, A. Elmoujahed, J. Chao et al., Inhibition of rat tissue kallikrein gene family members by rat kallikrein-binding protein and ??1-proteinase inhibitor, FEBS Letters, vol.6, issue.3, pp.405-408, 1992.
DOI : 10.1016/0014-5793(92)80817-Z

B. Korkmaz, S. Attucci, T. Moreau, E. Godat, L. Juliano et al., Design and Use of Highly Specific Substrates of Neutrophil Elastase and Proteinase 3, American Journal of Respiratory Cell and Molecular Biology, vol.30, issue.6, pp.801-807, 2004.
DOI : 10.1165/rcmb.2003-0139OC

T. A. Fuchs, U. Abed, C. Goosmann, R. Hurwitz, I. Schulze et al., Novel cell death program leads to neutrophil extracellular traps, The Journal of Cell Biology, vol.74, issue.2, pp.231-241, 2007.
DOI : 10.1073/pnas.85.22.8531
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063942

C. A. Owen, Leukocyte cell surface proteinases: Regulation of expression, functions, and mechanisms of surface localization, The International Journal of Biochemistry & Cell Biology, vol.40, issue.6-7, pp.1246-1272, 2008.
DOI : 10.1016/j.biocel.2008.01.020

W. H. Goldmann, J. L. Niles, and M. A. Arnaout, Interaction of purified human proteinase 3 (PR3) with reconstituted lipid bilayers, European Journal of Biochemistry, vol.9, issue.1, pp.155-162, 1999.
DOI : 10.1016/0014-5793(94)00404-8

E. Hajjar, M. Mihajlovic, V. Witko-sarsat, T. Lazaridis, and N. Reuter, Computational prediction of the binding site of proteinase 3 to the plasma membrane, Proteins: Structure, Function, and Bioinformatics, vol.75, issue.4, pp.1655-1669, 2008.
DOI : 10.1002/prot.21853

A. David, R. Fridlich, I. Aviram, R. Fridlich, A. David et al., Exp Cell Res 30, J Cell Biochem, vol.99, pp.117-125, 2005.

A. David, Y. Kacher, U. Specks, and I. Aviram, Interaction of proteinase 3 with CD11b/CD18 (??2integrin) on the cell membrane of human neutrophils, Journal of Leukocyte Biology, vol.74, issue.4, pp.551-557, 2003.
DOI : 10.1189/jlb.1202624

S. Von-vietinghoff, G. Tunnemann, C. Eulenberg, M. Wellner, C. Cardoso et al., NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils, Blood, vol.109, issue.10, pp.4487-4493, 2007.
DOI : 10.1182/blood-2006-10-055327

B. Korkmaz, A. Kuhl, B. Bayat, S. Santoso, J. et al., A Hydrophobic Patch on Proteinase 3, the Target of Autoantibodies in Wegener Granulomatosis, Mediates Membrane Binding via NB1 Receptors, Journal of Biological Chemistry, vol.283, issue.51, pp.35976-35982, 2008.
DOI : 10.1074/jbc.M806754200

A. P. Van-rossum, Y. M. Van-der-geld, P. C. Limburg, and C. G. Kallenberg, Human anti-neutrophil cytoplasm autoantibodies to proteinase 3 (PR3-ANCA) bind to neutrophils, Kidney International, vol.68, issue.2, pp.537-541, 2005.
DOI : 10.1111/j.1523-1755.2005.00431.x

B. Abdel-salam, C. Iking-konert, M. Schneider, K. Andrassy, and G. M. Hansch, Autoantibodies to neutrophil cytoplasmic antigens (ANCA) do not bind to polymorphonuclear neutrophils in blood, Kidney International, vol.66, issue.3, pp.1009-1017, 2004.
DOI : 10.1111/j.1523-1755.2004.00849.x

T. Matsumoto, T. Kaneko, M. Seto, H. Wada, T. Kobayashi et al., The Membrane Proteinase 3 Expression on Neutrophils Was Downregulated After Treatment With Infliximab in Patients With Rheumatoid Arthritis, Clinical and Applied Thrombosis/Hemostasis, vol.116, issue.6, pp.186-192, 2002.
DOI : 10.1177/1076029607303961

A. A. Rarok, C. A. Stegeman, P. C. Limburg, and C. G. Kallenberg, Neutrophil Membrane Expression of Proteinase 3 (PR3) Is Related to Relapse in PR3-ANCA-Associated Vasculitis, Journal of the American Society of Nephrology, vol.13, issue.9, pp.2232-2238, 2002.
DOI : 10.1097/01.ASN.0000028642.26222.00

. Fig, Distribution and activity of membrane-bound proteinase 3 at the surface of quiescent and activated blood neutrophils. (Top) Box plot (n=12) of Pr3 activity measured by incubating 300,000 cells/150 µL with the FRET substrate Abz-VADnorVADRQ-EDDnp. The lowest concentration of Pr3 activity that can be quantified is 0.1 nM. The width of the boxes reflects the percentage of mPr3 high cells in each sample of quiescent and activated neutrophils