M. J. Banda, E. J. Clark, S. Sinha, T. , and J. , Interaction of mouse macrophage elastase with native and oxidized human ?1-proteinase inhibitor, J. Clin. Invest, vol.79, pp.1314-1317, 1987.

M. J. Banda, E. J. Clark, and Z. Werb, Limited proteolysis by macrophage elastase inactivates human ?1-proteinase inhibitor, J. Exp. Med, vol.152, pp.1563-1570, 1980.

I. Bertini, V. Calderone, M. Fragai, R. Jaiswal, C. Luchinat et al., Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12, J. Am. Chem. Soc, vol.130, pp.7011-7021, 2008.

I. Bertini, V. Calderone, M. Fragai, C. Luchinat, M. Maletta et al., Snapshots of the reaction mechanism of matrix metalloproteinases, Angew Chem. Int. Ed, vol.45, pp.7952-7955, 2006.

R. Bhaskaran, M. O. Palmier, J. L. Lauer-fields, G. B. Fields, and S. R. Van-doren, MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity, J. Biol. Chem, vol.283, pp.21779-21788, 2008.

M. Cadene and B. T. Chait, A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins, Anal. Chem, vol.72, pp.5655-5658, 2000.
URL : https://hal.archives-ouvertes.fr/hal-02150358

J. R. Chagas, L. Juliano, and E. S. Prado, Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins, Anal. Biochem, vol.192, pp.419-425, 1991.

E. I. Chen, S. J. Kridel, E. W. Howard, W. Li, A. Godzik et al., A unique substrate recognition profile for matrix metalloproteinase-2, J. Biol. Chem, vol.277, pp.4485-4491, 2002.

E. I. Chen, W. Li, A. Godzik, E. W. Howard, and J. W. Smith, A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9, J. Biol. Chem, vol.278, pp.17158-17163, 2003.

A. Cobos-correa, J. B. Trojanek, S. Diemer, M. A. Mall, and C. Schultz, Membrane-bound FRET probe visualizes MMP12 activity in pulmonary inflammation, Nat. Chem. Biol, vol.5, pp.628-630, 2009.

J. A. Curci, S. Liao, M. D. Huffman, S. D. Shapiro, and R. W. Thompson, Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms, J. Clin. Invest, vol.102, pp.1900-1910, 1998.

R. A. Dean, J. H. Cox, C. L. Bellac, A. Doucet, A. E. Starr et al., , 2008.

M. Metalloelastase, MMP-12) truncates and inactivates ELR + CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx, vol.112, pp.3455-3464

I. K. Demedts, A. Morel-montero, S. Lebecque, Y. Pacheco, D. Cataldo et al., Elevated MMP-12 protein levels in induced sputum from patients with COPD, Thorax, vol.61, pp.196-201, 2006.

S. J. Deng, D. M. Bickett, J. L. Mitchell, M. H. Lambert, R. K. Blackburn et al., Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library, J. Biol. Chem, vol.275, pp.31422-31427, 2000.

A. Lamort, R. Gravier, A. Laffitte, L. Juliano, M. Zani et al., New insights into the substrate specificity of macrophage elastase MMP-12, Biological Chemistry, vol.397, issue.5, pp.469-484, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01398704

, Substrate specificity of MMP-12

L. Devel, V. Rogakos, A. David, A. Makaritis, F. Beau et al., Development of selective inhibitors and substrate of matrix metalloproteinase-12, J. Biol. Chem, vol.281, pp.11152-11160, 2006.

G. A. Finlay, L. R. O'driscoll, K. J. Russell, E. M. D'arcy, J. B. Masterson et al., Matrix metalloproteinase expression and production by alveolar macrophages in emphysema, Am. J. Respir. Crit. Care Med, vol.156, pp.240-247, 1997.

J. Y. Fu, A. Lyga, H. Shi, M. L. Blue, B. Dixon et al., Cloning, expression, purification, and characterization of rat MMP-12, Protein Expr. Purif, vol.21, pp.268-274, 2001.

G. Gabant, C. , and M. , Mass spectrometry of full-length integral membrane proteins to define functionally relevant structural features, Methods, vol.46, pp.54-61, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00512469

T. J. Gronski, . Jr, R. L. Martin, D. K. Kobayashi, B. C. Walsh et al., Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase, J. Biol. Chem, vol.272, pp.12189-12194, 1997.

I. Haq, G. E. Lowrey, N. Kalsheker, J. , and S. R. , Matrix metalloproteinase-12 (MMP-12) SNP affects MMP activity, lung macrophage infiltration and protects against emphysema in COPD, Thorax, vol.66, pp.970-976, 2011.

R. D. Hautamaki, D. K. Kobayashi, R. M. Senior, and S. D. Shapiro, Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice, Science, vol.277, pp.2002-2004, 1997.

A. Heinz, M. C. Jung, L. Duca, W. Sippl, S. Taddese et al., Degradation of tropoelastin by matrix metalloproteinases -cleavage site specificities and release of matrikines, FEBS J, vol.277, pp.1939-1956, 2010.
URL : https://hal.archives-ouvertes.fr/hal-00497122

I. Y. Hirata, M. H. Cezari, C. R. Nakaie, P. Boschcov, A. S. Ito et al., Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescent spectroscopy of peptides containing ortho-aminobenzoyldinitrophenyl groups as donor-acceptor pairs, Lett. Pept. Sci, vol.1, pp.299-308, 1994.

A. M. Houghton, P. A. Quintero, D. L. Perkins, D. K. Kobayashi, D. G. Kelley et al., Elastin fragments drive disease progression in a murine model of emphysema, J. Clin. Invest, vol.116, pp.753-759, 2006.

G. M. Hunninghake, M. H. Cho, Y. Tesfaigzi, M. E. Soto-quiros, L. Avila et al., MMP12, lung function, and COPD in high-risk populations, N. Engl. J. Med, vol.361, pp.2599-2608, 2009.

T. Kalupov, M. Brillard-bourdet, S. Dade, H. Serrano, J. Wartelle et al., Structural characterization of mouse neutrophil serine proteases and identification of their substrate specificities: relevance to mouse models of human inflammatory diseases, J. Biol. Chem, vol.284, pp.34084-34091, 2009.

M. Kaynar, S. D. Shapiro, A. Lamort, R. Gravier, A. Laffitte et al., New insights into the substrate specificity of macrophage elastase MMP-12, Handbook of Proteolytic Enzymes, vol.397, pp.469-484, 2012.

, Substrate specificity of MMP-12

K. Kis-toth, I. Bacskai, P. Gogolak, A. Mazlo, I. Szatmari et al., , 2013.

, Monocyte-derived dendritic cell subpopulations use different types of matrix metalloproteinases inhibited by GM6001, Immunobiology, vol.218, pp.1361-1369

C. G. Knight, F. Willenbrock, M. , and G. , A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases, FEBS Lett, vol.296, pp.263-266, 1992.

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, Nat. Protoc, vol.3, pp.991-1000, 2008.

S. J. Kridel, E. Chen, L. P. Kotra, E. W. Howard, S. Mobashery et al., , 2001.

, Substrate hydrolysis by matrix metalloproteinase-9, J. Biol. Chem, vol.276, pp.20572-20578

S. J. Kridel, H. Sawai, B. I. Ratnikov, E. I. Chen, W. Li et al., A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases, J. Biol. Chem, vol.277, pp.23788-23793, 2002.

M. C. Lavigne, P. Thakker, J. Gunn, A. Wong, J. S. Miyashiro et al., Human bronchial epithelial cells express and secrete MMP-12, Biochem. Biophys. Res. Commun, vol.324, pp.534-546, 2004.

M. Liu, H. Sun, X. Wang, T. Koike, H. Mishima et al., Association of increased expression of macrophage elastase (matrix metalloproteinase 12) with rheumatoid arthritis, Arthritis Rheum, vol.50, pp.3112-3117, 2004.

N. London, B. Raveh, E. Cohen, G. Fathi, and O. Schueler-furman, Rosetta FlexPepDock web server--high resolution modeling of peptide-protein interactions, Nucleic Acids Res, vol.39, pp.249-253, 2011.

D. J. Marchant, C. L. Bellac, T. J. Moraes, S. J. Wadsworth, A. Dufour et al., A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity, Nat. Med, vol.20, pp.493-502, 2014.

S. Matsumoto, T. Kobayashi, M. Katoh, S. Saito, Y. Ikeda et al., Expression and localization of matrix metalloproteinase-12 in the aorta of cholesterol-fed rabbits: relationship to lesion development, Am. J. Pathol, vol.153, pp.109-119, 1998.

S. Molet, C. Belleguic, H. Lena, N. Germain, C. P. Bertrand et al., Increase in macrophage elastase (MMP-12) in lungs from patients with chronic obstructive pulmonary disease, Inflamm Res, vol.54, pp.31-36, 2005.

U. Neumann, H. Kubota, K. Frei, V. Ganu, D. Leppert et al., Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme, Biological Chemistry, vol.328, issue.5, pp.469-484, 2004.

, Substrate specificity of MMP-12

M. O. Palmier and S. R. Van-doren, Rapid determination of enzyme kinetics from fluorescence: overcoming the inner filter effect, Anal. Biochem, vol.371, pp.43-51, 2007.

B. I. Ratnikov, P. Cieplak, K. Gramatikoff, J. Pierce, A. Eroshkin et al., Basis for substrate recognition and distinction by matrix metalloproteinases, Proc. Natl. Acad. Sci. USA, vol.111, pp.4148-4155, 2014.

N. D. Rawlings, M. Waller, A. J. Barrett, and A. Bateman, MEROPS: the database of proteolytic enzymes, their substrates and inhibitors, Nucleic Acids Res, vol.42, pp.503-509, 2014.

I. Schechter and A. Berger, On the size of the active site in proteases, I. Papain. Biochem. Biophys. Res. Commun, vol.27, pp.157-162, 1967.

H. Schirmer, L. Basso-da-silva, P. J. Teixeira, J. S. Moreira, A. L. Moreira et al., Matrix metalloproteinase gene polymorphisms: lack of association with chronic obstructive pulmonary disease in a Brazilian population, Genet. Mol. Res, vol.8, pp.1028-1034, 2009.

S. D. Shapiro, Animal models for chronic obstructive pulmonary disease: age of klotho and marlboro mice, Am. J. Respir. Cell. Mol. Biol, vol.22, pp.4-7, 2000.

S. D. Shapiro, Proteolysis in the lung, Eur. Respir. J, vol.44, pp.30-32, 2003.

S. D. Shapiro, D. K. Kobayashi, and T. J. Ley, Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages, J. Biol. Chem, vol.268, pp.23824-23829, 1993.

J. M. Shipley, R. L. Wesselschmidt, D. K. Kobayashi, T. J. Ley, and S. D. Shapiro, Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice, Proc. Natl. Acad. Sci. USA, vol.93, pp.3942-3946, 1996.

S. Taddese, M. C. Jung, C. Ihling, A. Heinz, R. H. Neubert et al., , 2009.

, MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III, Biochim. Biophys. Acta, vol.1804, pp.731-739

S. Taddese, M. C. Jung, C. Ihling, A. Heinz, R. H. Neubert et al., , 2010.

, MMP-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type I and type III, Biochim. Biophys. Acta, vol.1804, pp.731-739

S. Taddese, A. S. Weiss, G. Jahreis, R. H. Neubert, and C. E. Schmelzer, In vitro degradation of human tropoelastin by MMP-12 and the generation of matrikines from domain 24, Matrix Biol, vol.28, pp.84-91, 2009.

A. M. Wallace and A. J. Sandford, Genetic polymorphisms of matrix metalloproteinases: functional importance in the development of chronic obstructive pulmonary disease?, Am. J. Pharmacogenomics, vol.2, pp.167-175, 2002.

X. Wang, J. Liang, T. Koike, H. Sun, T. Ichikawa et al., Overexpression of human matrix metalloproteinase-12 enhances the development of inflammatory arthritis in transgenic rabbits, Am. J. Pathol, vol.165, pp.1375-1383, 2004.

H. Zhou, Y. Wu, Y. Jin, J. Zhou, C. Zhang et al., Genetic polymorphism of matrix metalloproteinase family and chronic obstructive pulmonary disease susceptibility: a meta-analysis. Sci. Rep. 3, 2818. Brought to you by | University of California Authenticated Download Date | 1/25/16 2:18 AM Comment citer ce document : Lamort, A, Biological Chemistry, vol.397, issue.5, pp.469-484, 2013.

, Substrate specificity of MMP-12

, murine full-length MMP-12 (m-FL-MMP12). ? and ? indicate major and secondary minor cleavage sites by human MMP-12 respectively

A. Lamort, R. Gravier, A. Laffitte, L. Juliano, M. Zani et al., Kinetic data (K m, k cat and k cat /K m ) for the hydrolysis of selected Abz-peptidyl-Comment citer ce document, Biological Chemistry, vol.397, issue.5, pp.469-484, 2016.

A. Lamort, R. Gravier, A. Laffitte, L. Juliano, M. Zani et al., New insights into the substrate specificity of macrophage elastase MMP-12, Biological Chemistry, vol.397, issue.5, pp.469-484, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01398704

, Substrate specificity of MMP-12

, Figure S1 SDS-PAGE analysis of the various forms of human and mouse MMP-12

, The proform of MMP-12 (PRO-MMP-12) was converted to the full length form

, Tris-HCl buffer, pH 7.5, 10 mM CaCl 2 , 150 mM NaCl

, 05% (w/v) Brij 35. For mouse MMP-12, 5 µM ZnCl 2 was added in the activation buffer