F. Adam, T. J. Verbeuren, J. Fauchère, M. Guillin, and M. Jandrot-perrus, Thrombininduced platelet PAR4 activation: role of glycoprotein Ib and ADP, J Thromb Haemost, vol.1, pp.798-804, 2003.

R. A. Al-horani and U. R. Desai, Factor XIa inhibitors: A review of the patent literature, Expert Opin Ther Pat, vol.26, pp.323-368, 2016.

A. Al-shanqeeti, A. Van-hylckama-vlieg, E. Berntorp, F. R. Rosendaal, and G. J. Broze, , 2005.

, Protein Z and protein Z-dependent protease inhibitor. Determinants of levels and risk of venous thrombosis, Thromb Haemost, vol.93, pp.411-414

A. L. Amati, A. Zakrzewicz, R. Siebers, S. Wilker, S. Heldmann et al., Chemokines (CCL3, CCL4, and CCL5) Inhibit, 2017.

, ATP-Induced Release of IL-1? by Monocytic Cells, Mediators Inflamm, vol.2017, p.1434872

A. Butschkau, P. Nagel, E. Grambow, D. Zechner, G. J. Broze et al., Contribution of protein Z and protein Z-dependent protease inhibitor in generalized Shwartzman reaction, 2013.

, Crit Care Med, vol.41, pp.447-56

K. Conlon, A. Lloyd, U. Chattopadhyay, N. Lukacs, S. Kunkel et al., CD8+ and CD45RA+ human peripheral blood lymphocytes are potent sources of macrophage inflammatory protein 1 alpha, interleukin-8 and RANTES, Eur J Immunol, vol.25, pp.751-757, 1995.

J. Corral, R. González-conejero, D. Hernández-espinosa, and V. V. , Protein Z/Zdependent protease inhibitor (PZ/ZPI) anticoagulant system and thrombosis, Br J Haematol, vol.137, pp.99-108, 2007.
DOI : 10.1111/j.1365-2141.2007.06548.x

URL : https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-2141.2007.06548.x

T. J. Girard, N. M. Lasky, E. A. Tuley, and G. J. Broze, Protein Z, protein Z-dependent protease inhibitor (serpinA10), and the acute-phase response, J Thromb Haemost, vol.11, pp.375-383, 2013.

X. Han, Z. F. Huang, R. Fiehler, and G. J. Broze, The protein Z-dependent protease inhibitor is a serpin, Biochemistry, vol.38, pp.11073-11081, 1999.

X. Han, R. Fiehler, and G. J. Broze, Characterization of the protein Z-dependent protease inhibitor, Blood, vol.96, pp.3049-55, 2000.

M. Hayakawa, D. Kudo, S. Saito, S. Uchino, K. Yamakawa et al., Antithrombin Supplementation and Mortality in Sepsis-Induced Disseminated Intravascular Coagulation: A Multicenter Retrospective Observational Study. Shock, vol.46, pp.623-631, 2016.

T. Iba, A. Kidokoro, M. Fukunaga, K. Nagakari, M. Suda et al., , 2005.

, Antithrombin ameliorates endotoxin-induced organ dysfunction more efficiently when combined with danaparoid sodium than with unfractionated heparin, Intensive Care Med, vol.31, pp.1101-1109

S. Janciauskiene, S. Larsson, P. Larsson, R. Virtala, L. Jansson et al., Inhibition of lipopolysaccharide-mediated human monocyte activation, in vitro, p.1, 2004.

, Biochem Biophys Res Commun, vol.321, pp.592-600

N. Kalsheker, S. Morley, and K. Morgan, Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin, Biochem Soc Trans, vol.30, pp.93-101, 2002.

A. J. Martí-carvajal, I. Solà, C. Gluud, D. Lathyris, and A. F. Cardona, Human recombinant protein C for severe sepsis and septic shock in adult and paediatric patients, Cochrane Database Syst Rev, vol.12, p.4388, 2012.

C. Oelschläger, J. Römisch, A. Staubitz, H. Stauss, B. Leithäuser et al., Antithrombin III inhibits nuclear factor kappaB activation in human monocytes and vascular endothelial cells, Blood, vol.99, pp.4015-4035, 2002.

R. J. Richmond and K. M. Zellner, Alpha1-antitrypsin deficiency: incidence and implications, 2005.

, Dimens Crit Care Nurs, vol.24, pp.255-60

D. Subramaniyam, C. Steele, T. Köhnlein, T. Welte, O. Grip et al., Effects of alpha 1-antitrypsin on endotoxin-induced lung inflammation in vivo, Inflamm Res, vol.59, pp.571-579, 2010.

A. Tabatabai, R. Fiehler, and G. J. Broze, Protein Z circulates in plasma in a complex with protein Z-dependent protease inhibitor, Thromb Haemost, vol.85, pp.655-60, 2001.

T. Yoshida, M. Souri, T. Osaki, S. Saito, J. Meijers et al., The plasma levels of protein Zdependent protease inhibitor increase after gynecological surgery independently of estrogen, Thromb Res, vol.136, issue.5, pp.980-986, 2015.

S. Doat, D. Borgel, J. François, E. Bianchini, J. Botton et al., Unbalance between plasma levels of Protein Z and protein Z-dependent inhibitor in patients with colorectal and pancreatic cancer: A pilot study, Thromb Res. févr, vol.133, issue.2, pp.299-300, 2014.

C. Gabay and I. Kushner, Acute-phase proteins and other systemic responses to inflammation, N Engl J Med. 11 févr, vol.340, issue.6, pp.448-54, 1999.

B. Engelmann and S. Massberg, Thrombosis as an intravascular effector of innate immunity, Nat Rev Immunol. janv, vol.13, issue.1, pp.34-45, 2013.

K. J. Clemetson, Platelets and primary haemostasis, Thromb Res. mars, vol.129, issue.3, pp.220-224, 2012.

S. A. Smith, R. J. Travers, and J. H. Morrissey, How it all starts: Initiation of the clotting cascade, Crit Rev Biochem Mol Biol, vol.50, issue.4, pp.326-362, 2015.

E. Stavrou and A. H. Schmaier, Factor XII: what does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis, Thromb Res. mars, vol.125, issue.3, pp.210-215, 2010.

J. Björkqvist, K. F. Nickel, E. Stavrou, and T. Renné, In vivo activation and functions of the protease factor XII, Thromb Haemost, vol.112, issue.5, pp.868-75, 2014.

H. Weidmann, L. Heikaus, A. T. Long, C. Naudin, H. Schlüter et al., The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity, Biochim Biophys Acta, vol.1864, issue.11, pp.2118-2145, 2017.

B. M. Mohammed, A. Matafonov, I. Ivanov, M. Sun, Q. Cheng et al., An update on factor XI structure and function, Thromb Res, vol.161, pp.94-105, 2018.

C. E. Bane, I. Ivanov, A. Matafonov, K. L. Boyd, Q. Cheng et al., Factor XI Deficiency Alters the Cytokine Response and Activation of Contact Proteases during Polymicrobial Sepsis in Mice, PloS One, vol.11, issue.4, p.152968, 2016.

M. Pathak, B. G. Kaira, A. Slater, and J. Emsley, Cell Receptor and Cofactor Interactions of the Contact Activation System and Factor XI, Front Med, vol.5, p.66, 2018.

R. E. Thompson, R. Mandle, and A. P. Kaplan, Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain, Proc Natl Acad Sci, vol.76, issue.10, pp.4862-4868, 1979.

C. Naudin, E. Burillo, S. Blankenberg, L. Butler, and T. Renné, Factor XII Contact Activation, Semin Thromb Hemost, vol.43, issue.8, pp.814-840, 2017.

K. Joseph, Y. Shibayama, B. Ghebrehiwet, and A. P. Kaplan, Factor XII-dependent contact activation on endothelial cells and binding proteins gC1qR and cytokeratin 1, Thromb Haemost. janv, vol.85, issue.1, pp.119-143, 2001.

R. A. Pixley, R. G. Espinola, B. Ghebrehiwet, K. Joseph, A. Kao et al., Interaction of highmolecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore), Thromb Haemost. juin, vol.105, issue.6, pp.1053-1062, 2011.

R. Couture, N. Blaes, and J. Girolami, Kinin receptors in vascular biology and pathology, Curr Vasc Pharmacol. mars, vol.12, issue.2, pp.223-271, 2014.

C. Maas and T. Renné, Coagulation factor XII in thrombosis and inflammation, Blood. 26 févr, 2018.

T. C. White-adams, M. A. Berny, E. I. Tucker, J. M. Gertz, D. Gailani et al., Identification of coagulation factor XI as a ligand for platelet apolipoprotein E receptor 2 (ApoER2), Arterioscler Thromb Vasc Biol, vol.29, issue.10, pp.1602-1609, 2009.

T. F. Ottaiano, S. S. Andrade, C. De-oliveira, M. Silva, M. V. Buri et al., Plasma kallikrein enhances platelet aggregation response by subthreshold doses of ADP, Biochimie. avr, vol.135, pp.72-81, 2017.

J. H. Morrissey and S. A. Smith, Polyphosphate as modulator of hemostasis, thrombosis, and inflammation, J Thromb Haemost JTH. juin, vol.13, issue.1, pp.92-97, 2015.

L. M. Henderson, C. D. Figueroa, W. Müller-esterl, and K. D. Bhoola, Assembly of contact-phase factors on the surface of the human neutrophil membrane, Blood. 15 juill, vol.84, issue.2, pp.474-82, 1994.

T. Renné, A. H. Schmaier, K. F. Nickel, M. Blombäck, and C. Maas, vivo roles of factor XII. Blood, vol.120, pp.4296-303, 2012.

D. M. Monroe and N. S. Key, The tissue factor-factor VIIa complex: procoagulant activity, regulation, and multitasking, J Thromb Haemost. 1 juin, vol.5, issue.6, pp.1097-105, 2007.

S. A. Maroney, P. E. Ellery, and A. E. Mast, Alternatively spliced isoforms of tissue factor pathway inhibitor, Thromb Res. avr, vol.125, issue.1, pp.52-56, 2010.

A. E. Mast, Tissue Factor Pathway Inhibitor: Multiple Anticoagulant Activities for a Single Protein, Arterioscler Thromb Vasc Biol. janv, vol.36, issue.1, pp.9-14, 2016.

G. J. Broze and T. J. Girard, Tissue factor pathway inhibitor: structure-function, Front Biosci Landmark Ed. 1 janv, vol.17, pp.262-80, 2012.

J. H. Griffin, B. V. Zlokovic, and L. O. Mosnier, Protein C anticoagulant and cytoprotective pathways, Int J Hematol. avr, vol.95, issue.4, pp.333-378, 2012.

P. Fuentes-prior, Y. Iwanaga, R. Huber, R. Pagila, G. Rumennik et al., Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex, Nature. 30 mars, vol.404, issue.6777, pp.518-543, 2000.

D. J. Stearns-kurosawa, S. Kurosawa, J. S. Mollica, G. L. Ferrell, and C. T. Esmon, The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex, Proc Natl Acad Sci, vol.93, pp.10212-10218, 1996.

B. Dahlbäck and B. O. Villoutreix, Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition, Arterioscler Thromb Vasc Biol. juill, vol.25, issue.7, pp.1311-1331, 2005.

J. Conard, F. Brosstad, L. Larsen, M. Samama, M. Abildgaard et al., Molar antithrombin concentration in normal human plasma, Haemostasis, vol.13, issue.6, pp.363-371, 1983.

J. C. Rau, L. M. Beaulieu, J. A. Huntington, and F. C. Church, Serpins in thrombosis, hemostasis and fibrinolysis, J Thromb Haemost JTH. juill, vol.5, issue.1, pp.102-117, 2007.

E. F. Mammen, Antithrombin: its physiological importance and role in DIC, Semin Thromb Hemost, vol.24, issue.1, pp.19-25, 1998.

J. Dedio, W. Jahnen-dechent, M. Bachmann, and W. Müller-esterl, The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein, J Immunol Baltim Md 1950. 1 avr, vol.160, issue.7, pp.3534-3576, 1998.

H. C. Van-leeuwen, O. Hare, and P. , Retargeting of the mitochondrial protein p32/gC1Qr to a cytoplasmic compartment and the cell surface, J Cell Sci. juin, vol.114, pp.2115-2138, 2001.

B. Ghebrehiwet, C. Cebadamora, L. Tantral, J. Jesty, and E. Peerschke, gC1qR/p33 serves as a molecular bridge between the complement and contact activation systems and is an important catalyst in inflammation, Adv Exp Med Biol, vol.586, pp.95-105, 2006.

W. X. Guo, B. Ghebrehiwet, B. Weksler, K. Schweitzer, and E. I. Peerschke, Up-regulation of endothelial cell binding proteins/receptors for complement component C1q by inflammatory cytokines, J Lab Clin Med. juin, vol.133, issue.6, pp.541-50, 1999.

S. R. Reddigari, Y. Shibayama, T. Brunnée, and A. P. Kaplan, Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells, J Biol Chem. 5 juin, vol.268, issue.16, pp.11982-11989, 1993.

F. Mahdi, Z. S. Madar, C. D. Figueroa, and A. H. Schmaier, Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes, Blood. 15 mai, vol.99, issue.10, pp.3585-96, 2002.

S. Zeerleder, C1-inhibitor: more than a serine protease inhibitor, Semin Thromb Hemost. juin, vol.37, issue.4, pp.362-74, 2011.

G. J. Broze and J. P. Miletich, Human Protein Z. J Clin Invest. avr, vol.73, issue.4, pp.933-941, 1984.

K. Fujimaki, T. Yamazaki, M. Taniwaki, and A. Ichinose, The gene for human protein Z is localized to chromosome 13 at band q34 and is coded by eight regular exons and one alternative exon, Biochemistry. 12 mai, vol.37, pp.6838-6884, 1998.

G. I. Rice, T. S. Futers, and P. J. Grant, Identification of novel polymorphisms within the protein Z gene, haplotype distribution and linkage analysis, Thromb Haemost. juin, vol.85, issue.6, pp.1123-1127, 2001.

A. Ichinose, H. Takeya, E. Espling, S. Iwanaga, W. Kisiel et al., Amino acid sequence of human protein Z, a vitamin K-dependent plasma glycoprotein, Biochem Biophys Res Commun, vol.172, issue.3, pp.1139-1183, 1990.

P. J. Hogg and J. Stenflo, Interaction of human protein Z with thrombin: evaluation of the species difference in the interaction between bovine and human protein Z and thrombin, Biochem Biophys Res Commun. 15 août, vol.178, issue.3, pp.801-808, 1991.

J. P. Miletich and G. J. Broze, Human plasma protein Z antigen: range in normal subjects and effect of warfarin therapy, Blood. juin, vol.69, issue.6, pp.1580-1586, 1987.

H. Sejima, T. Hayashi, Y. Deyashiki, J. Nishioka, and K. Suzuki, Primary structure of vitamin K-dependent human protein Z, Biochem Biophys Res Commun. 14 sept, vol.171, issue.2, pp.661-669, 1990.

W. Y. Almawi, F. S. Al-shaikh, O. K. Melemedjian, and A. W. Almawi, Protein Z, an anticoagulant protein with expanding role in reproductive biology, Reproduction. 8 janv, vol.146, issue.2, pp.73-80, 2013.

M. Souri, S. Koseki-kuno, H. Iwata, B. Kemkes-matthes, and A. Ichinose, A naturally occurring E30Q mutation in the Gla domain of protein Z causes its impaired secretion and subsequent deficiency, Blood. 15 avr, vol.105, issue.8, pp.3149-54, 2005.

H. Iwata, M. Souri, B. Kemkes-matthes, and A. Ichinose, An additional Glu30Lys substitution in the Gla domain of the protein Z gene is not a common polymorphism but a rare mutation, which would cause its deficiency, J Thromb Haemost JTH, vol.3, issue.10, pp.2360-2361, 2005.

M. Souri, H. Iwata, W. G. Zhang, and A. Ichinose, Unique secretion mode of human protein Z: its Gla domain is responsible for inefficient, vitamin K-dependent and warfarin-sensitive secretion, Blood. 16 avr, vol.113, issue.16, pp.3857-64, 2009.

B. Kemkes-matthes and K. J. Matthes, Protein Z, a new haemostatic factor, in liver diseases, Haemostasis. déc, vol.25, issue.6, pp.312-318, 1995.

J. Greten, I. Kreis, B. Liliensiek, J. Allenberg, J. Amiral et al., Localisation of protein Z in vascular lesions of patients with atherosclerosis, VASA Z Gefasskrankheiten. août, vol.27, issue.3, pp.144-152, 1998.

M. Vasse, C. Denoyelle, C. Corbière, P. Litzler, E. Legrand et al., Human endothelial cells synthesize protein Z, but not the protein Z dependent inhibitor, Thromb Haemost. mars, vol.95, issue.3, pp.519-542, 2006.

X. Han, R. Fiehler, and G. J. Broze, Isolation of a protein Z-dependent plasma protease inhibitor, Proc Natl Acad Sci, vol.95, issue.16, pp.9250-9255, 1998.

X. Han, Z. Huang, R. Fiehler, and G. J. Broze, The Protein Z-Dependent Protease Inhibitor Is a Serpin, Biochemistry. 1 août, vol.38, issue.34, pp.11073-11081, 1999.

N. Van-de-water, T. Tan, F. Ashton, O. Grady, A. Day et al., Mutations within the protein Z-dependent protease inhibitor gene are associated with venous thromboembolic disease: a new form of thrombophilia, Br J Haematol, vol.127, issue.2, pp.190-194, 2004.

J. Corral, R. González-conejero, J. M. Soria, J. R. González-porras, E. Pérez-ceballos et al., A nonsense polymorphism in the protein Z-dependent protease inhibitor increases the risk for venous thrombosis, Blood. 1 juill, vol.108, issue.1, pp.177-83, 2006.

F. Dentali, M. Gianni, F. Lussana, A. Squizzato, M. Cattaneo et al., Polymorphisms of the Z protein protease inhibitor and risk of venous thromboembolism: a meta-analysis, Br J Haematol, vol.143, issue.2, pp.284-291, 2008.

Z. Wei, Y. Yan, R. W. Carrell, and A. Zhou, Crystal structure of protein Z-dependent inhibitor complex shows how protein Z functions as a cofactor in the membrane inhibition of factor X, Blood, vol.114, issue.17, pp.3662-3669, 2009.

X. Han, R. Fiehler, and G. J. Broze, Characterization of the protein Z-dependent protease inhibitor, Blood, vol.96, issue.9, pp.3049-55, 2000.

L. New, K. Liu, V. Kamali, G. Plowman, B. A. Naughton et al., cDNA cloning of rasp-1, a novel gene encoding a plasma protein associated with liver regeneration, Biochem Biophys Res Commun. 14 juin, vol.223, issue.2, pp.404-416, 1996.

T. Sengupta and N. Manoj, Phosphatidylserine and Phosphatidylethanolamine Bind to Protein Z Cooperatively and with Equal Affinity, PloS One, vol.11, issue.9, p.161896, 2016.

P. Gettins, Serpin structure, mechanism, and function, Chem Rev. déc, vol.102, issue.12, pp.4751-804, 2002.
DOI : 10.1021/cr010170+

X. Huang, R. Swanson, G. J. Broze, and S. T. Olson, Kinetic characterization of the protein Z-dependent protease inhibitor reaction with blood coagulation factor Xa, J Biol Chem, vol.283, issue.44, pp.29770-83, 2008.

X. Huang, A. Dementiev, S. T. Olson, and P. Gettins, Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa, J Biol Chem. 25 juin, vol.285, issue.26, pp.20399-409, 2010.

S. T. Olson, R. Swanson, E. Raub-segall, T. Bedsted, M. Sadri et al., Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin, Thromb Haemost, vol.92, issue.5, pp.929-968, 2004.

J. A. Huntington, Natural inhibitors of thrombin, Thromb Haemost. 1 avr, vol.111, issue.4, pp.583-592, 2014.

X. Huang, A. R. Rezaie, G. J. Broze, and S. T. Olson, Heparin is a major activator of the anticoagulant serpin, protein Z-dependent protease inhibitor, J Biol Chem. 18 mars, vol.286, issue.11, pp.8740-51, 2011.

L. Yang, Q. Ding, X. Huang, S. T. Olson, and A. R. Rezaie, Characterization of the heparin-binding site of the protein z-dependent protease inhibitor, Biochemistry. 15 mai, vol.51, pp.4078-85, 2012.

M. Vasse, The protein Z/protein Z-dependent protease inhibitor complex, Hamostaseologie. août, vol.31, issue.3, pp.160-164, 2011.

X. Huang, B. Liu, Y. Wei, R. Beyea, H. Yan et al., Lipid oxidation inactivates the anticoagulant function of protein Z-dependent protease inhibitor (ZPI), J Biol Chem, vol.01, issue.35, pp.14625-14660, 2017.

A. R. Rezaie, M. Sun, and D. Gailani, Contributions of basic amino acids in the autolysis loop of factor XIa to serpin specificity, Biochemistry. 8 août, vol.45, issue.31, pp.9427-9460, 2006.

M. J. Heeb, K. M. Cabral, and L. Ruan, Down-regulation of factor IXa in the factor Xase complex by protein Z-dependent protease inhibitor, J Biol Chem, vol.280, issue.40, pp.33819-33844, 2005.

L. Yang and A. R. Rezaie, Residues of the 39-loop restrict the plasma inhibitor specificity of factor IXa, J Biol Chem. 3 mai, vol.288, issue.18, pp.12692-12700, 2013.

L. Yang and A. R. Rezaie, Characterization of Protein Z-Dependent Protease Inhibitor/Antithrombin Chimeras Provides Insight into the Serpin Specificity of Coagulation Proteases, ACS Omega. 31 juill, vol.2, issue.7, pp.3276-83, 2017.

A. Tabatabai, R. Fiehler, and G. J. Broze, Protein Z circulates in plasma in a complex with protein Zdependent protease inhibitor, Thromb Haemost. avr, vol.85, issue.4, pp.655-60, 2001.

T. J. Girard, N. M. Lasky, E. A. Tuley, and G. J. Broze, Protein Z, Protein Z-Dependent Protease Inhibitor (SerpinA10) and the Acute Phase Response, J Thromb Haemost JTH. févr, vol.11, issue.2, pp.375-383, 2013.

X. Huang, Y. Yan, Y. Tu, J. Gatti, G. J. Broze et al., Structural basis for catalytic activation of protein Z-dependent protease inhibitor (ZPI) by protein Z, Blood. 23 août, vol.120, issue.8, pp.1726-1759, 2012.

J. Zhang, Y. Tu, L. Lu, N. Lasky, and G. J. Broze, Protein Z-dependent protease inhibitor deficiency produces a more severe murine phenotype than protein Z deficiency, Blood. 15 mai, vol.111, issue.10, pp.4973-4981, 2008.

Z. F. Yin, Z. F. Huang, J. Cui, R. Fiehler, N. Lasky et al., Prothrombotic phenotype of protein Z deficiency, Proc Natl Acad Sci, vol.97, issue.12, pp.6734-6742, 2000.

M. A. Refaai, C. Ahn, L. Lu, K. Wu, and G. J. Broze, Protein Z and ZPI levels and cardiovascular events, J Thromb Haemost JTH. juill, vol.4, issue.7, pp.1628-1637, 2006.

M. J. Heeb, M. Fisher, and A. Paganini-hill, Association of low protein Z levels with ischemic stroke in young women, Thromb Haemost. mars, vol.97, issue.3, pp.495-501, 2007.

A. M. Mcquillan, J. W. Eikelboom, G. J. Hankey, R. Baker, J. Thom et al., Protein Z in ischemic stroke and its etiologic subtypes. Stroke, vol.34, pp.2415-2424, 2003.

B. Steffano, R. Forastiero, M. Martinuzzo, and L. Kordich, Low plasma protein Z levels in patients with antiphospholipid antibodies, Blood Coagul Fibrinolysis Int J Haemost Thromb. juill, vol.12, issue.5, pp.411-413, 2001.

M. Vasse, E. Guegan-massardier, J. Y. Borg, F. Woimant, and C. Soria, Frequency of protein Z deficiency in patients with ischaemic stroke, Lancet Lond Engl. 24 mars, vol.357, issue.9260, pp.933-937, 2001.

K. Kobelt, F. D. Biasiutti, H. P. Mattle, B. Lämmle, and W. A. Wuillemin, Protein Z in ischaemic stroke, Br J Haematol. juill, vol.114, issue.1, pp.169-73, 2001.

F. Cesari, C. Fatini, E. Sticchi, S. Fedi, R. Abbate et al., Protein Z gene polymorphisms (intron F 79 G>A; -13 A>G) are not associated with acute coronary syndromes, Thromb Haemost. juill, vol.96, issue.1, pp.98-107, 2006.

S. Lopaciuk, K. Bykowska, H. Kwiecinski, A. Czlonkowska, and A. Kuczynska-zardzewialy, Protein Z in young survivors of ischemic stroke, Thromb Haemost. sept, vol.88, issue.3, p.536, 2002.

J. Pardos-gea, J. Ordi-ros, S. Serrano, E. Balada, I. Nicolau et al., Protein Z levels and antiprotein Z antibodies in patients with arterial and venous thrombosis, Thromb Res, vol.121, issue.6, pp.727-761, 2008.

M. A. Oztürk, Z. Ozbalkan, A. M. Onat, I. Ertenli, S. Kiraz et al., Decreased protein Z concentrations complicating the hypercoagulable state of Behçet's disease, Clin Appl Thromb Off J Int Acad Clin Appl Thromb. juill, vol.9, issue.3, pp.259-63, 2003.

C. Hinterleitner, K. Kreisselmeier, A. Pecher, P. Mauz, L. Kanz et al., Low plasma protein Z levels are associated with an increased risk for perioperative bleedings, Eur J Haematol. mai, vol.100, issue.5, pp.403-414, 2018.

R. Santacroce, F. Cappucci, D. Perna, P. Sessa, F. Margaglione et al., Protein Z gene polymorphisms are associated with protein Z plasma levels, J Thromb Haemost JTH. juill, vol.2, issue.7, pp.1197-1206, 2004.

S. Ravi, T. Mauron, B. Lämmle, and W. A. Wuillemin, Protein Z in healthy human individuals and in patients with a bleeding tendency, Br J Haematol. sept, vol.102, issue.5, pp.1219-1242, 1998.

S. Fedi, F. Sofi, D. Brogi, I. Tellini, F. Cesari et al., Low protein Z plasma levels are independently associated with acute coronary syndromes, Thromb Haemost. déc, vol.90, issue.6, pp.1173-1181, 2003.

M. Yurdakök, B. Gürakan, E. Ozba?, S. Vi?it, S. Dündar et al., Plasma protein Z levels in healthy newborn infants, Am J Hematol. mars, vol.48, issue.3, pp.206-213, 1995.

F. Schettini, N. Laforgia, M. Altomare, A. Mautone, D. Vecchio et al., Plasma protein Z levels in healthy and high-risk newborn infants, Acta Paediatr Oslo Nor, vol.93, issue.5, pp.654-661, 1992.

S. Fedi, F. Sofi, D. Brogi, I. Tellini, F. Cesari et al., Low protein Z plasma levels are independently associated with acute coronary syndromes, Thromb Haemost. déc, vol.90, issue.6, pp.1173-1181, 2003.

A. Al-shanqeeti, A. Van-hylckama-vlieg, E. Berntorp, F. R. Rosendaal, and G. J. Broze, Protein Z and protein Z-dependent protease inhibitor. Determinants of levels and risk of venous thrombosis, Thromb Haemost. mars, vol.93, issue.3, pp.411-414, 2005.

G. Gamba, G. Bertolino, N. Montani, P. Spedini, and C. L. Balduini, Bleeding tendency of unknown origin and protein Z levels, Thromb Res. 15 juin, vol.90, issue.6, pp.291-296, 1998.

D. Thommen, I. Sulzer, E. Buhrfeind, R. Naef, M. Furlan et al., Measurement of bleeding time and study of thrombocyte aggregation. Standardization of methods, normal values and results in patients with

, Schweiz Med Wochenschr, vol.118, issue.43, pp.1559-67, 1988.

F. Sofi, F. Cesari, R. Abbate, G. F. Gensini, G. Broze et al., A meta-analysis of potential risks of low levels of protein Z for diseases related to vascular thrombosis, Thromb Haemost. avr, vol.103, issue.4, pp.749-56, 2010.

L. Zhang, A. Z. Segal, D. Leifer, R. L. Silverstein, L. M. Gerber et al., Circulating protein Z concentration, PROZ variants, and unexplained cerebral infarction in young and middle-aged adults, Thromb Haemost. 05, vol.117, issue.1, pp.149-57, 2017.

S. B. Jensen, K. Hindberg, T. Solomon, E. N. Smith, J. D. Lapek et al., Discovery of novel plasma biomarkers for future incident venous thromboembolism by untargeted synchronous precursor selection mass spectrometry proteomics, J Thromb Haemost JTH. sept, vol.16, issue.9, pp.1763-74, 2018.

F. Sofi, F. Cesari, Y. Tu, G. Pratesi, R. Pulli et al., Protein Z-dependent protease inhibitor and protein Z in peripheral arterial disease patients, J Thromb Haemost JTH. mai, vol.7, issue.5, pp.731-736, 2009.

M. Souri, M. Sugiura-ogasawara, S. Saito, B. Kemkes-matthes, J. Meijers et al., Increase in the plasma levels of protein Z-dependent protease inhibitor in normal pregnancies but not in non-pregnant patients with unexplained recurrent miscarriage, Thromb Haemost. mars, vol.107, issue.3, pp.507-519, 2012.

O. Erez, D. Hoppensteadt, R. Romero, J. Espinoza, L. Goncalves et al., Preeclampsia is associated with low concentrations of protein Z, J Matern-Fetal Neonatal Med Off J Eur Assoc Perinat Med Fed Asia Ocean Perinat Soc Int Soc Perinat Obstet. sept, vol.20, issue.9, pp.661-668, 2007.

V. Gowri, M. Mathew, D. Gravell, K. Alfalahi, I. Zakwani et al., Protein Z levels in pregnant Omani women: correlation with pregnancy outcome, J Thromb Thrombolysis, vol.32, issue.4, pp.453-461, 2011.

J. Gris, I. Quéré, H. Dechaud, E. Mercier, C. Pinçon et al., High frequency of protein Z deficiency in patients with unexplained early fetal loss, Blood. 1 avr, vol.99, issue.7, pp.2606-2614, 2002.

J. K. Nien, R. Romero, D. Hoppensteadt, O. Erez, J. Espinoza et al., Pyelonephritis during pregnancy: a cause for an acquired deficiency of protein Z, J Matern-Fetal Neonatal Med Off J Eur Assoc Perinat Med Fed Asia Ocean Perinat Soc Int Soc Perinat Obstet. sept, vol.21, issue.9, pp.629-666, 2008.

E. Grandone, D. Colaizzo, F. Cappucci, N. Cocomazzi, and M. Margaglione, Protein Z levels and unexplained fetal losses. Fertil Steril, vol.82, pp.982-985, 2004.

F. Bretelle, D. Arnoux, R. Shojai, D. 'ercole, C. Sampol et al., Protein Z in patients with pregnancy complications, Am J Obstet Gynecol, vol.193, issue.5, pp.1698-702, 2005.

M. J. Paidas, D. Ku, M. Lee, M. S. Thurston, A. Lockwood et al., Protein Z, protein S levels are lower in patients with thrombophilia and subsequent pregnancy complications, J Thromb Haemost JTH. mars, vol.3, issue.3, pp.497-501, 2005.

J. P. Kusanovic, J. Espinoza, R. Romero, D. Hoppensteadt, J. K. Nien et al., Plasma protein Z concentrations in pregnant women with idiopathic intrauterine bleeding and in women with spontaneous preterm labor, J Matern-Fetal Neonatal Med Off J Eur Assoc Perinat Med Fed Asia Ocean Perinat Soc Int Soc Perinat Obstet. juin, vol.20, issue.6, pp.453-63, 2007.

M. Topalidou, S. Effraimidou, D. Farmakiotis, E. Papadakis, G. Papaioannou et al., Low protein Z levels, but not the intron F G79A polymorphism, are associated with unexplained pregnancy loss, Thromb Res. mai, vol.124, issue.1, pp.24-31, 2009.

I. Kaygusuz, T. Firatli-tuglular, T. Toptas, V. Ugurel, and M. Demir, Low levels of protein Z are associated with HELLP syndrome and its severity, Clin Appl Thromb Off J Int Acad Clin Appl Thromb. avr, vol.17, issue.2, pp.214-223, 2011.

F. S. Al-shaikh, M. S. Sater, R. R. Finan, E. Racoubian, T. M. Abu-hijleh et al., Protein Z variants associated with protein Z plasma levels and with risk of idiopathic recurrent miscarriage, Reprod Sci Thousand Oaks Calif. sept, vol.20, issue.9, pp.1062-1070, 2013.

J. Gris, C. Amadio, E. Mercier, G. Lavigne-lissalde, H. Déchaud et al., Anti-protein Z antibodies in women with pathologic pregnancies, Blood. 15 juin, vol.101, issue.12, pp.4850-4852, 2003.

J. Gris, E. Mercier, I. Quéré, G. Lavigne-lissalde, E. Cochery-nouvellon et al., Lowmolecular-weight heparin versus low-dose aspirin in women with one fetal loss and a constitutional thrombophilic disorder, Blood. 15 mai, vol.103, issue.10, pp.3695-3704, 2004.

O. Erez, R. Romero, E. Vaisbuch, S. Mazaki-tovi, J. P. Kusanovic et al., Maternal anti-protein Z antibodies in pregnancies complicated by pre-eclampsia, SGA and fetal death, J Matern-Fetal Neonatal Med Off J Eur Assoc Perinat Med Fed Asia Ocean Perinat Soc Int Soc Perinat Obstet. août, vol.22, issue.8, pp.662-71, 2009.

M. S. Sater, R. R. Finan, A. Sa, F. A. Mohammed, A. A. Issa et al., High Frequency of anti-protein Z IgM and IgG autoantibodies in women with idiopathic recurrent spontaneous miscarriage, Am J Reprod Immunol N Y N, vol.65, issue.5, pp.526-557, 1989.

J. Amiral, M. Peyrafitte, C. Dunois, A. M. Vissac, and J. Seghatchian, Anti-phospholipid syndrome: Current opinion on mechanisms involved, laboratory characterization and diagnostic aspects, Transfus Apher Sci Off J World Apher Assoc Off J Eur Soc Haemapheresis. août, vol.56, issue.4, pp.612-637, 2017.

M. D. Mccoll, A. Deans, P. Maclean, R. C. Tait, I. A. Greer et al., Plasma protein Z deficiency is common in women with antiphospholipid antibodies, Br J Haematol. mars, vol.120, issue.5, pp.913-917, 2003.

R. R. Forastiero, M. E. Martinuzzo, L. Lu, and G. J. Broze, Autoimmune antiphospholipid antibodies impair the inhibition of activated factor X by protein Z/protein Z-dependent protease inhibitor, J Thromb Haemost JTH. août, vol.1, issue.8, pp.1764-70, 2003.

T. Sailer, R. Vormittag, S. Koder, P. Quehenberger, A. Kaider et al., Clinical significance of anti-protein Z antibodies in patients with lupus anticoagulant, Thromb Res, vol.122, issue.2, pp.153-60, 2008.

T. Andriamandimbisoa, J. Kahn, F. Bourdain, D. François, and M. Vasse, High frequency of antiprotein Z antibodies in patients with anticardiolipin antibodies, Immunobiology. 6 août, 2018.

S. M. Yousry, R. Shahin, E. Refai, and R. M. , Contribution of protein Z gene single-nucleotide polymorphism to systemic lupus erythematosus in Egyptian patients, Blood Coagul Fibrinolysis Int J Haemost Thromb. sept, vol.27, issue.6, pp.691-696, 2016.

M. Vasse, C. Denoyelle, E. Legrand, J. Vannier, and C. Soria, Weak Regulation of Protein Z Biosynthesis by Inflammatory Cytokines, Thromb Haemost, vol.87, issue.2, pp.350-351, 2002.

L. Undar, I. Karado?an, and F. Oztürk, Plasma protein Z levels inversely correlate with plasma interleukin-6 levels in patients with acute leukemia and non-Hodgkin's lymphoma, Thromb Res. 15 avr, vol.94, issue.2, pp.131-135, 1999.

O. Gutwein, N. Rahimi-levene, K. Herzog-tzarfati, O. Garach-jehoshua, A. Nagler et al., Low Protein Z levels in patients with plasma cell neoplasms are inversely correlated with IL-6 levels, Leuk Res, vol.62, pp.104-111, 2017.

F. Cesari, A. M. Gori, S. Fedi, R. Abbate, G. F. Gensini et al., Modifications of protein Z and interleukin-6 during the acute phase of coronary artery disease, Blood Coagul Fibrinolysis Int J Haemost Thromb, issue.1, pp.85-91, 2007.

G. Freue, M. Sasaki, A. Meredith, O. P. Günther, A. Bergman et al., Proteomic signatures in plasma during early acute renal allograft rejection, Mol Cell Proteomics MCP. sept, vol.9, issue.9, pp.1954-67, 2010.

S. Y. Kim, J. Kim, Y. J. Kim, K. Han, and H. K. Kim, Prominent protein Z-induced thrombin inhibition in cirrhosis: a new functional assay for hypercoagulability assessment, J Gastroenterol Hepatol. avr, vol.30, issue.4, pp.784-93, 2015.

Y. Shang, X. Pan, C. Ding, Y. Cai, X. Ding et al.,

, Ai Zheng Aizheng Chin J Cancer. sept, vol.24, issue.9, pp.1144-1151, 2005.

G. Capurso, S. Lattimore, T. Crnogorac-jurcevic, F. Panzuto, M. Milione et al., Gene expression profiles of progressive pancreatic endocrine tumours and their liver metastases reveal potential novel markers and therapeutic targets, Endocr Relat Cancer. juin, vol.13, issue.2, pp.541-58, 2006.

J. Leja, A. Essaghir, M. Essand, K. Wester, K. Oberg et al., Novel markers for enterochromaffin cells and gastrointestinal neuroendocrine carcinomas, Mod Pathol Off J U S Can Acad Pathol Inc. févr, vol.22, issue.2, pp.261-72, 2009.

E. Sierko, M. Z. Wojtukiewicz, K. Ostrowska-cichocka, and L. Zimnoch, Protein Z-dependent protease inhibitor (ZPI) is present in loco in human breast cancer tissue, Thromb Haemost. juill, vol.104, issue.1, pp.183-188, 2010.

E. Sierko, M. Z. Wojtukiewicz, L. Zimnoch, P. Tokajuk, and W. Kisiel, Protein Z is present in human breast cancer tissue, Int J Hematol. mai, vol.93, issue.5, pp.681-684, 2011.

E. Sierko, M. Z. Wojtukiewicz, L. Zimnoch, K. Ostrowska-cichocka, P. Tokajuk et al., Protein Z/protein Z-dependent protease inhibitor system in human non-small-cell lung cancer tissue, Thromb Res. avr, vol.129, issue.4, pp.92-96, 2012.

E. Sierko, M. Z. Wojtukiewicz, L. Zimnoch, P. Tokajuk, K. Ostrowska-cichocka et al., Colocalization of Protein Z, Protein Z-Dependent protease inhibitor and coagulation factor X in human colon cancer tissue: implications for coagulation regulation on tumor cells, Thromb Res. avr, vol.129, issue.4, pp.112-118, 2012.

E. Sierko, M. Z. Wojtukiewicz, L. Zimnoch, P. Tokajuk, K. Ostrowska-cichocka et al., Protein Z/protein Z-dependent protease inhibitor system in loco in human gastric cancer, Ann Hematol. mai, vol.93, issue.5, pp.779-84, 2014.
DOI : 10.1007/s00277-013-1941-8

URL : https://link.springer.com/content/pdf/10.1007%2Fs00277-013-1941-8.pdf

S. A. El-hamid and W. El-khayat, Relationship of the protein Z intron F G79A and IL6 C634G gene polymorphisms with the risk of recurrent pregnancy loss in Egyptian women, J Investig Med Off Publ Am Fed Clin Res. avr, vol.59, issue.4, pp.655-60, 2011.

E. Grandone, D. Colaizzo, F. Cappucci, D. 'ambrosio, R. L. Vecchione et al., An unreported mutation within protein Z gene is associated with very low protein levels in women with fetal loss, Fertil Steril. sept, vol.90, issue.3, pp.864-869, 2008.

C. Vl, C. Soria, C. B. Dit-sollier, J. Borg, M. Coudert et al., Rare genotypes of protein Z gene are a risk factor for premature myocardial infarction but not protein Z plasma level, Thromb Haemost, vol.12, 2009.

D. Sur,

D. Fabbro, G. Barillari, and G. Damante, Mutations R67X and W303X of the protein Z-dependent protease inhibitor gene and venous thromboembolic disease: a case-control study in Italian subjects, J Thromb Thrombolysis. févr, vol.23, issue.1, pp.77-85, 2007.

F. S. Alshaikh, R. R. Finan, A. W. Almawi, F. E. Mustafa, and W. Y. Almawi, Association of the R67X and W303X non-sense polymorphisms in the protein Z-dependent protease inhibitor gene with idiopathic recurrent miscarriage, Mol Hum Reprod. mars, vol.18, issue.3, pp.156-60, 2012.

S. Karakoyun, M. O. Gürsoy, M. Kalç?k, M. Yesin, S. Gündüz et al., The role of protein Z and protein Z-dependent protease inhibitor polymorphisms in the development of prosthetic heart valve thrombosis, Anatol J Cardiol. mai, vol.16, issue.5, pp.361-364, 2016.

M. M. Gorski, L. A. Lotta, E. Pappalardo, H. G. De-haan, S. M. Passamonti et al., Single Nucleotide Variant rs2232710 in the Protein Z-Dependent Protease Inhibitor (ZPI, SERPINA10) Gene Is Not Associated with Deep Vein Thrombosis, PloS One, vol.11, issue.3, p.151347, 2016.

S. Akira, S. Uematsu, and O. Takeuchi, Pathogen recognition and innate immunity, Cell. 24 févr, vol.124, issue.4, pp.783-801, 2006.

N. Feldman, A. Rotter-maskowitz, and E. Okun, DAMPs as mediators of sterile inflammation in aging-related pathologies, Ageing Res Rev. nov, vol.24, pp.29-39, 2015.

M. O'brien, The reciprocal relationship between inflammation and coagulation, Top Companion Anim Med. mai, vol.27, issue.2, pp.46-52, 2012.

P. L. Giesen, U. Rauch, B. Bohrmann, D. Kling, M. Roqué et al., Blood-borne tissue factor: another view of thrombosis, Proc Natl Acad Sci, vol.96, issue.5, pp.2311-2316, 1999.

I. Müller, A. Klocke, A. M. Kotzsch, M. Luther, T. Morgenstern et al., Intravascular tissue factor initiates coagulation via circulating microvesicles and platelets, FASEB J Off Publ Fed Am Soc Exp Biol. mars, vol.17, issue.3, pp.476-484, 2003.

R. Darbousset, G. M. Thomas, S. Mezouar, C. Frère, R. Bonier et al., Tissue factorpositive neutrophils bind to injured endothelial wall and initiate thrombus formation, Blood. 6 sept, vol.120, issue.10, pp.2133-2176, 2012.

C. Moosbauer, E. Morgenstern, S. L. Cuvelier, D. Manukyan, K. Bidzhekov et al., Eosinophils are a major intravascular location for tissue factor storage and exposure, Blood. 1 févr, vol.109, issue.3, pp.995-1002, 2007.

A. Zillmann, T. Luther, I. Müller, M. Kotzsch, M. Spannagl et al., Platelet-associated tissue factor contributes to the collagen-triggered activation of blood coagulation, Biochem Biophys Res Commun. 23 févr, vol.281, issue.2, pp.603-612, 2001.

S. Massberg, L. Grahl, V. Bruehl, M. Manukyan, D. Pfeiler et al., Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases, Nat Med. août, vol.16, issue.8, pp.887-96, 2010.

S. Hippenstiel and N. Suttorp, Interaction of pathogens with the endothelium, Thromb Haemost. janv, vol.89, issue.1, pp.18-24, 2003.

M. L. Kahn, M. Nakanishi-matsui, M. J. Shapiro, H. Ishihara, and S. R. Coughlin, Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin, J Clin Invest. mars, vol.103, issue.6, pp.879-87, 1999.

N. V. Bogatcheva, J. Garcia, and A. D. Verin, Molecular mechanisms of thrombin-induced endothelial cell permeability, Biochem Biokhimiia. janv, vol.67, issue.1, pp.75-84, 2002.

R. Pawlinski and N. Mackman, Tissue factor, coagulation proteases, and protease-activated receptors in endotoxemia and sepsis, Crit Care Med. mai, vol.32, issue.5, pp.293-297, 2004.

V. Brinkmann, U. Reichard, C. Goosmann, B. Fauler, Y. Uhlemann et al., Neutrophil extracellular traps kill bacteria, Science. 5 mars, vol.303, issue.5663, pp.1532-1537, 2004.

V. Brinkmann, Neutrophil Extracellular Traps in the Second Decade, J Innate Immun. 15 juin, pp.1-8, 2018.

S. L. Wong and D. D. Wagner, Peptidylarginine deiminase 4: a nuclear button triggering neutrophil extracellular traps in inflammatory diseases and aging, FASEB J Off Publ Fed Am Soc Exp Biol. 20 juin, 2018.

M. Von-brühl, K. Stark, A. Steinhart, S. Chandraratne, K. I. Lorenz et al., Monocytes, neutrophils, and platelets cooperate to initiate and propagate venous thrombosis in mice in vivo, J Exp Med. 9 avr, vol.209, issue.4, pp.819-854, 2012.

T. A. Fuchs, A. Brill, D. Duerschmied, D. Schatzberg, M. Monestier et al., Extracellular DNA traps promote thrombosis, Proc Natl Acad Sci, vol.107, issue.36, pp.15880-15885, 2010.

S. R. Clark, A. C. Ma, S. A. Tavener, B. Mcdonald, Z. Goodarzi et al., Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood, Nat Med. avr, vol.13, issue.4, pp.463-472, 2007.

B. F. Kraemer, R. A. Campbell, H. Schwertz, M. J. Cody, Z. Franks et al., Novel antibacterial activities of ?-defensin 1 in human platelets: suppression of pathogen growth and signaling of neutrophil extracellular trap formation, PLoS Pathog, vol.7, issue.11, p.1002355, 2011.

J. W. Semple, J. E. Italiano, and J. Freedman, Platelets and the immune continuum, Nat Rev Immunol. avr, vol.11, issue.4, pp.264-74, 2011.

P. Haselmayer, L. Grosse-hovest, V. Landenberg, P. Schild, H. Radsak et al., TREM-1 ligand expression on platelets enhances neutrophil activation, Blood. 1 août, vol.110, issue.3, pp.1029-1064, 2007.

C. Reinhardt, V. Brühl, M. Manukyan, D. Grahl, L. Lorenz et al., Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation, J Clin Invest. mars, vol.118, issue.3, pp.1110-1132, 2008.

M. Brown and A. Kornberg, Inorganic polyphosphate in the origin and survival of species, Proc Natl Acad Sci, vol.101, issue.46, pp.16085-16092, 2004.

E. S. Gershom, M. R. Sutherland, P. Lollar, and E. Pryzdial, Involvement of the contact phase and intrinsic pathway in herpes simplex virus-initiated plasma coagulation, J Thromb Haemost JTH. mai, vol.8, issue.5, pp.1037-1080, 2010.

I. Frick, L. Björck, and H. Herwald, The dual role of the contact system in bacterial infectious disease, Thromb Haemost. sept, vol.98, issue.3, pp.497-502, 2007.

J. Scharfstein, D. Andrade, E. Svensjö, A. C. Oliveira, and C. R. Nascimento, The kallikrein-kinin system in experimental Chagas disease: a paradigm to investigate the impact of inflammatory edema on GPCR-mediated pathways of host cell invasion by Trypanosoma cruzi, Front Immunol, vol.3, p.396, 2012.

K. F. Nickel and T. Renné, Crosstalk of the plasma contact system with bacteria, Thromb Res, vol.130, issue.1, pp.78-83, 2012.

A. Ben-nasr, H. Herwald, U. Sjöbring, T. Renné, W. Müller-esterl et al., Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin, Biochem J. 15 sept, vol.326, pp.657-60, 1997.

W. Waldetoft, K. Svensson, L. Mörgelin, M. Olin, A. I. Nitsche-schmitz et al., Streptococcal surface proteins activate the contact system and control its antibacterial activity, J Biol Chem. 20 juill, vol.287, issue.30, pp.25010-25018, 2012.

N. N. Rao, M. R. Gómez-garcía, and A. Kornberg, Inorganic polyphosphate: essential for growth and survival, Annu Rev Biochem, vol.78, pp.605-652, 2009.

T. Imamura, J. Potempa, R. N. Pike, and J. Travis, Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis, Infect Immun. mai, vol.63, issue.5, pp.1999-2003, 1995.

O. Roeise, B. N. Bouma, J. O. Stadaas, and A. O. Aasen, Dose dependence of endotoxin-induced activation of the plasma contact system: an in vitro study, Circ Shock. déc, vol.26, issue.4, pp.419-449, 1988.

E. S. Kalter, W. C. Van-dijk, A. Timmerman, J. Verhoef, and B. N. Bouma, Activation of purified human plasma prekallikrein triggered by cell wall fractions of Escherichia coli and Staphylococcus aureus, J Infect Dis, vol.148, issue.4, pp.682-91, 1983.

D. Cadena, R. A. Suffredini, A. F. Page, J. D. Pixley, R. A. Kaufman et al., Activation of the kallikrein-kinin system after endotoxin administration to normal human volunteers, Blood. 15 juin, vol.81, issue.12, pp.3313-3320, 1993.

M. C. Minnema, D. Pajkrt, W. A. Wuillemin, D. Roem, W. K. Bleeker et al., Activation of clotting factor XI without detectable contact activation in experimental human endotoxemia, Blood, vol.92, issue.9, pp.3294-301, 1998.

B. Ghebrehiwet, A. P. Kaplan, K. Joseph, and E. Peerschke, The complement and contact activation systems: partnership in pathogenesis beyond angioedema, Immunol Rev, vol.274, issue.1, pp.281-290, 2016.

P. Madeddu, C. Emanueli, L. Gaspa, B. Salis, A. F. Milia et al., Role of the bradykinin B2 receptor in the maturation of blood pressure phenotype: lesson from transgenic and knockout mice, Immunopharmacology, vol.44, issue.1-2, pp.9-13, 1999.

A. H. Schmaier, The elusive physiologic role of Factor XII, J Clin Invest. sept, vol.118, issue.9, pp.3006-3015, 2008.

R. G. Discipio, The activation of the alternative pathway C3 convertase by human plasma kallikrein, Immunology. mars, vol.45, issue.3, pp.587-95, 1982.

Z. Toossi, J. R. Sedor, M. A. Mettler, B. Everson, T. Young et al., Induction of expression of monocyte interleukin 1 by Hageman factor (factor XII), Proc Natl Acad Sci U S A. 15 déc, vol.89, issue.24, pp.11969-72, 1992.

M. M. Khan, H. N. Bradford, I. Isordia-salas, Y. Liu, Y. Wu et al., High-molecular-weight kininogen fragments stimulate the secretion of cytokines and chemokines through uPAR, Mac-1, and gC1qR in monocytes, Arterioscler Thromb Vasc Biol, vol.26, issue.10, pp.2260-2266, 2006.

E. Sato, S. Koyama, H. Nomura, K. Kubo, and M. Sekiguchi, Bradykinin stimulates alveolar macrophages to release neutrophil, monocyte, and eosinophil chemotactic activity, J Immunol Baltim Md, vol.157, issue.7, pp.3122-3131, 1950.

I. Paegelow, S. Trzeczak, S. Böckmann, and G. Vietinghoff, Migratory responses of polymorphonuclear leukocytes to kinin peptides, Pharmacology, vol.66, issue.3, pp.153-61, 2002.

I. Frick, P. Akesson, H. Herwald, M. Mörgelin, M. Malmsten et al., The contact system--a novel branch of innate immunity generating antibacterial peptides, EMBO J, vol.29, issue.23, pp.5569-78, 2006.

E. A. Nordahl, V. Rydengård, M. Mörgelin, and A. Schmidtchen, Domain 5 of high molecular weight kininogen is antibacterial, J Biol Chem, vol.280, issue.41, pp.34832-34841, 2005.

D. C. Morrison and C. G. Cochrane, Direct evidence for Hageman factor (factor XII) activation by bacterial lipopolysaccharides (endotoxins), J Exp Med. 1 sept, vol.140, issue.3, pp.797-811, 1974.

F. Müller, N. J. Mutch, W. A. Schenk, S. A. Smith, L. Esterl et al., Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo, Cell. 11 déc, vol.139, issue.6, pp.1143-56, 2009.

S. Bergmann and S. Hammerschmidt, Fibrinolysis and host response in bacterial infections, Thromb Haemost. sept, vol.98, issue.3, pp.512-532, 2007.

H. Sun, U. Ringdahl, J. W. Homeister, W. P. Fay, N. C. Engleberg et al., Plasminogen is a critical host pathogenicity factor for group A streptococcal infection, Science. 27 août, vol.305, issue.5688, pp.1283-1289, 2004.

J. T. Buchanan, A. J. Simpson, R. K. Aziz, G. Y. Liu, S. A. Kristian et al., DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps, Curr Biol CB. 21 févr, vol.16, issue.4, pp.396-400, 2006.

K. Beiter, F. Wartha, B. Albiger, S. Normark, A. Zychlinsky et al., An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps, Curr Biol CB. 21 févr, vol.16, issue.4, pp.401-408, 2006.

A. G. Cheng, M. Mcadow, H. K. Kim, T. Bae, D. M. Missiakas et al., Contribution of coagulases towards Staphylococcus aureus disease and protective immunity, PLoS Pathog. 5 août, vol.6, issue.8, p.1001036, 2010.

C. Guggenberger, C. Wolz, J. A. Morrissey, and J. Heesemann, Two distinct coagulase-dependent barriers protect Staphylococcus aureus from neutrophils in a three dimensional in vitro infection model, PLoS Pathog. janv, vol.8, issue.1, p.1002434, 2012.

M. Lipinska-gediga, Coagulopathy in sepsis -a new look at an old problem, Anaesthesiol Intensive Ther, vol.48, issue.5, pp.352-361, 2016.

T. Tsukamoto, R. S. Chanthaphavong, and H. Pape, Current theories on the pathophysiology of multiple organ failure after trauma, Injury. janv, vol.41, issue.1, pp.21-27, 2010.

X. Delabranche, J. Helms, and F. Meziani, Immunohaemostasis: a new view on haemostasis during sepsis. Ann Intensive Care, vol.2

M. Singer, C. S. Deutschman, C. W. Seymour, M. Shankar-hari, D. Annane et al., The Third International Consensus Definitions for Sepsis and Septic Shock (Sepsis-3), JAMA. 23 févr, vol.315, issue.8, pp.801-811, 2016.

J. Vincent, D. Backer, and D. , Circulatory shock, N Engl J Med, vol.369, issue.18, pp.1726-1760, 2013.

R. C. Bone, R. A. Balk, F. B. Cerra, R. P. Dellinger, A. M. Fein et al., Definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis, The ACCP/SCCM Consensus Conference Committee, vol.101, pp.1644-55, 1992.

J. M. Dulhunty, J. Lipman, and S. Finfer, Sepsis Study Investigators for the ANZICS Clinical Trials Group. Does severe non-infectious SIRS differ from severe sepsis? Results from a multi-centre Australian and New Zealand intensive care unit study, Intensive Care Med. sept, vol.34, issue.9, pp.1654-61, 2008.

S. Gando, T. Iba, Y. Eguchi, Y. Ohtomo, K. Okamoto et al., A multicenter, prospective validation of disseminated intravascular coagulation diagnostic criteria for critically ill patients: comparing current criteria, Crit Care Med. mars, vol.34, issue.3, pp.625-656, 2006.

M. Hayakawa, S. Gando, and H. Hoshino, A prospective comparative study of three sets of criteria for disseminated intravascular coagulation: ISTH criteria vs Japanese criteria, Clin Appl Thromb Off J Int Acad Clin Appl Thromb. janv, vol.13, issue.1, pp.65-72, 2007.

F. B. Taylor, C. H. Toh, W. K. Hoots, H. Wada, and M. Levi, Towards definition, clinical and laboratory criteria, and a scoring system for disseminated intravascular coagulation, Scientific Subcommittee on Disseminated Intravascular Coagulation (DIC) of the International Society on Thrombosis and Haemostasis (ISTH), vol.86, pp.1327-1357, 2001.

W. Schulte, J. Bernhagen, and R. Bucala, Cytokines in sepsis: potent immunoregulators and potential therapeutic targets--an updated view, Mediators Inflamm, p.165974, 2013.

E. Kumolosasi, E. Salim, I. Jantan, and W. Ahmad, Kinetics of Intracellular, Extracellular and Production of Pro-Inflammatory Cytokines in Lipopolysaccharide-Stimulated Human Peripheral Blood Mononuclear Cells, Trop J Pharm Res. 1 janv, vol.13, issue.4, pp.536-543, 2014.

M. Bhatia and S. Moochhala, Role of inflammatory mediators in the pathophysiology of acute respiratory distress syndrome, J Pathol. févr, vol.202, issue.2, pp.145-56, 2004.

N. Parameswaran and S. Patial, Tumor necrosis factor-? signaling in macrophages, Crit Rev Eukaryot Gene Expr, vol.20, issue.2, pp.87-103, 2010.

P. Damas, D. Ledoux, M. Nys, Y. Vrindts, D. Groote et al., Cytokine serum level during severe sepsis in human IL-6 as a marker of severity, Ann Surg. avr, vol.215, issue.4, pp.356-62, 1992.

J. C. Preiser, D. Schmartz, P. Van-der-linden, J. Content, V. Bussche et al., Interleukin-6 administration has no acute hemodynamic or hematologic effect in the dog, Cytokine. janv, vol.3, issue.1, pp.1-4, 1991.

R. E. Marques, R. Guabiraba, R. C. Russo, and M. M. Teixeira, Targeting CCL5 in inflammation, Expert Opin Ther Targets. déc, vol.17, issue.12, pp.1439-60, 2013.

S. Shahrara, A. Proudfoot, J. M. Woods, J. H. Ruth, M. A. Amin et al., Amelioration of rat adjuvant-induced arthritis by Met-RANTES, Arthritis Rheum. juin, vol.52, issue.6, pp.1907-1926, 2005.

J. Cavaillon, M. Adib-conquy, C. Fitting, C. Adrie, and D. Payen, Cytokine cascade in sepsis, Scand J Infect Dis, vol.35, issue.9, pp.535-579, 2003.

J. R. Delanghe and M. M. Speeckaert, Translational research and biomarkers in neonatal sepsis, Clin Chim Acta Int J Clin Chem. 7 déc, vol.451, pp.46-64, 2015.

K. J. Tracey, Y. Fong, D. G. Hesse, K. R. Manogue, A. T. Lee et al., Anti-cachectin/TNF monoclonal antibodies prevent septic shock during lethal bacteraemia, Nature. 17 déc, vol.330, issue.6149, pp.662-666, 1987.
DOI : 10.1038/330662a0

Y. Fong, K. J. Tracey, L. L. Moldawer, D. G. Hesse, K. B. Manogue et al., Antibodies to cachectin/tumor necrosis factor reduce interleukin 1 beta and interleukin 6 appearance during lethal bacteremia, J Exp Med, vol.170, issue.5, pp.1627-1660, 1989.

S. M. Opal, A. S. Cross, N. M. Kelly, J. C. Sadoff, M. W. Bodmer et al., Efficacy of a monoclonal antibody directed against tumor necrosis factor in protecting neutropenic rats from lethal infection with Pseudomonas aeruginosa, J Infect Dis. juin, vol.161, issue.6, pp.1148-52, 1990.

L. B. Hinshaw, P. Tekamp-olson, A. C. Chang, P. A. Lee, F. B. Taylor et al., Survival of primates in LD100 septic shock following therapy with antibody to tumor necrosis factor (TNF alpha), Circ Shock. mars, vol.30, issue.3, pp.279-92, 1990.

L. B. Hinshaw, T. E. Emerson, F. B. Taylor, A. C. Chang, M. Duerr et al., Lethal Staphylococcus aureus-induced shock in primates: prevention of death with anti-TNF antibody, J Trauma. oct, vol.33, issue.4, pp.568-73, 1992.

J. Cohen and J. Carlet, INTERSEPT: an international, multicenter, placebo-controlled trial of monoclonal antibody to human tumor necrosis factor-alpha in patients with sepsis. International Sepsis Trial Study Group, Crit Care Med. sept, vol.24, issue.9, pp.1431-1471, 1996.

E. Abraham, A. Anzueto, G. Gutierrez, S. Tessler, S. Pedro et al., Double-blind randomised controlled trial of monoclonal antibody to human tumour necrosis factor in treatment of septic shock. NORASEPT II Study Group, Lancet Lond Engl. 28 mars, vol.351, issue.9107, pp.929-962, 1998.

D. G. Remick, Cytokine therapeutics for the treatment of sepsis: why has nothing worked?, Curr Pharm Des, vol.9, issue.1, pp.75-82, 2003.

F. Fourrier, M. Jourdain, A. Tournois, C. Caron, J. Goudemand et al., Coagulation inhibitor substitution during sepsis, Intensive Care Med. nov, vol.21, issue.2, pp.264-268, 1995.

Y. Sakr, K. Reinhart, S. Hagel, M. Kientopf, and F. Brunkhorst, Antithrombin levels, morbidity, and mortality in a surgical intensive care unit, Anesth Analg. sept, vol.105, issue.3, pp.715-738, 2007.

C. J. Wiedermann and J. Römisch, The anti-inflammatory actions of antithrombin--a review, Acta Med Austriaca, vol.29, issue.3, pp.89-92, 2002.

C. J. Wiedermann, J. N. Hoffmann, M. Juers, H. Ostermann, J. Kienast et al., High-dose antithrombin III in the treatment of severe sepsis in patients with a high risk of death: efficacy and safety, Crit Care Med. févr, vol.34, issue.2, pp.285-92, 2006.

J. Kienast, M. Juers, C. J. Wiedermann, J. N. Hoffmann, H. Ostermann et al., Treatment effects of high-dose antithrombin without concomitant heparin in patients with severe sepsis with or without disseminated intravascular coagulation, J Thromb Haemost JTH. janv, vol.4, issue.1, pp.90-97, 2006.

M. Allingstrup, J. Wetterslev, F. B. Ravn, A. M. Møller, and A. Afshari, Antithrombin III for critically ill patients, Cochrane Database Syst Rev. 8 févr, vol.2, p.5370, 2016.

C. J. Wiedermann, Antithrombin concentrate use in disseminated intravascular coagulation of sepsis: meta-analyses revisited, J Thromb Haemost JTH. mars, vol.16, issue.3, pp.455-462, 2018.

. Bouwens-e-a.-m, F. Stavenuiter, and L. O. Mosnier, Mechanisms of anticoagulant and cytoprotective actions of the protein C pathway, J Thromb Haemost JTH. juin, vol.11, issue.1, pp.242-53, 2013.

F. B. Taylor, A. Chang, C. T. Esmon, D. Angelo, A. Vigano et al., Protein C prevents the coagulopathic and lethal effects of Escherichia coli infusion in the baboon, J Clin Invest. mars, vol.79, issue.3, pp.918-943, 1987.

G. R. Bernard, J. L. Vincent, P. F. Laterre, S. P. Larosa, J. F. Dhainaut et al., Efficacy and safety of recombinant human activated protein C for severe sepsis, N Engl J Med. 8 mars, vol.344, issue.10, pp.699-709, 2001.

V. M. Ranieri, B. T. Thompson, P. S. Barie, J. Dhainaut, I. S. Douglas et al., Drotrecogin Alfa (Activated) in Adults with Septic Shock, N Engl J Med. 31 mai, vol.366, issue.22, pp.2055-64, 2012.
URL : https://hal.archives-ouvertes.fr/inserm-00865183

A. C. Kalil and S. P. Larosa, Effectiveness and safety of drotrecogin alfa (activated) for severe sepsis: a meta-analysis and metaregression, Lancet Infect Dis. sept, vol.12, issue.9, pp.678-86, 2012.

F. Pappalardo, M. Crivellari, D. Prima, A. L. Agracheva, N. Celinska-spodar et al., Protein C zymogen in severe sepsis: a double-blinded, placebo-controlled, randomized study, Intensive Care Med. nov, vol.42, issue.11, pp.1706-1720, 2016.

T. Ito, K. Kawahara, K. Okamoto, S. Yamada, M. Yasuda et al., Proteolytic cleavage of high mobility group box 1 protein by thrombin-thrombomodulin complexes, Arterioscler Thromb Vasc Biol, vol.28, issue.10, pp.1825-1855, 2008.

T. Ito and I. Maruyama, Thrombomodulin: protectorate God of the vasculature in thrombosis and inflammation, J Thromb Haemost JTH. juill, vol.9, issue.1, pp.168-73, 2011.

J. Vincent, M. K. Ramesh, D. Ernest, S. P. Larosa, J. Pachl et al., A randomized, doubleblind, placebo-controlled, Phase 2b study to evaluate the safety and efficacy of recombinant human soluble thrombomodulin, ART-123, in patients with sepsis and suspected disseminated intravascular coagulation, Crit Care Med. sept, vol.41, issue.9, pp.2069-79, 2013.

K. S. Allen, E. Sawheny, and G. T. Kinasewitz, Anticoagulant modulation of inflammation in severe sepsis, World J Crit Care Med. 4 mai, vol.4, issue.2, pp.105-120, 2015.

H. Saito, I. Maruyama, S. Shimazaki, Y. Yamamoto, N. Aikawa et al., Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: results of a phase III, randomized, double-blind clinical trial, J Thromb Haemost JTH. janv, vol.5, issue.1, pp.31-41, 2007.

M. Hayakawa, K. Yamakawa, S. Saito, S. Uchino, D. Kudo et al., Recombinant human soluble thrombomodulin and mortality in sepsis-induced disseminated intravascular coagulation. A multicentre retrospective study, Thromb Haemost, vol.02, issue.6, pp.1157-66, 2016.

A. A. Creasey and K. Reinhart, Tissue factor pathway inhibitor activity in severe sepsis, Crit Care Med. juill, vol.29, issue.7, pp.126-129, 2001.

F. E. Van-den-boogaard, J. J. Hofstra, C. Van-'t-veer, M. M. Levi, J. Roelofs et al., Feasibility and Safety of Local Treatment with Recombinant Human Tissue Factor Pathway Inhibitor in a Rat Model of Streptococcus pneumoniae Pneumonia, PloS One, vol.10, issue.5, p.127261, 2015.

A. A. Creasey, A. C. Chang, L. Feigen, T. C. Wün, F. B. Taylor et al., Tissue factor pathway inhibitor reduces mortality from Escherichia coli septic shock, J Clin Invest. juin, vol.91, issue.6, pp.2850-60, 1993.

B. Koudsi, D. M. Chatman, B. A. Ballinger, E. W. Ferguson, B. A. Kraemer et al., Tissue factor pathway inhibitor protects the ischemic spinal cord, J Surg Res. juin, vol.63, issue.1, pp.174-182, 1996.

E. Abraham, K. Reinhart, P. Svoboda, A. Seibert, D. Olthoff et al., Assessment of the safety of recombinant tissue factor pathway inhibitor in patients with severe sepsis: a multicenter, randomized, placebo-controlled, single-blind, dose escalation study, Crit Care Med. nov, vol.29, issue.11, pp.2081-2090, 2001.

E. Abraham, K. Reinhart, S. Opal, I. Demeyer, C. Doig et al., Efficacy and safety of tifacogin (recombinant tissue factor pathway inhibitor) in severe sepsis: a randomized controlled trial, JAMA. 9 juill, vol.290, issue.2, pp.238-285, 2003.

E. Kenne and T. Renné, Factor XII: a drug target for safe interference with thrombosis and inflammation, Drug Discov Today. sept, vol.19, issue.9, pp.1459-64, 2014.

Z. Chen, D. Seiffert, and B. Hawes, Inhibition of Factor XI activity as a promising antithrombotic strategy, Drug Discov Today. sept, vol.19, issue.9, pp.1435-1444, 2014.

R. W. Leid, B. E. Ballieux, I. Van-der-heijden, C. Kleyburg-van-der-keur, E. C. Hagen et al., Cleavage and inactivation of human C1 inhibitor by the human leukocyte proteinase, proteinase 3, Eur J Immunol. nov, vol.23, issue.11, pp.2939-2983, 1993.

J. H. Nuijens, A. J. Eerenberg-belmer, C. C. Huijbregts, W. O. Schreuder, R. J. Felt-bersma et al., Proteolytic inactivation of plasma C1-inhibitor in sepsis, J Clin Invest. août, vol.84, issue.2, pp.443-50, 1989.

A. A. Igonin, D. N. Protsenko, G. M. Galstyan, A. V. Vlasenko, N. N. Khachatryan et al., C1-esterase inhibitor infusion increases survival rates for patients with sepsis*, Crit Care Med. mars, vol.40, issue.3, pp.770-777, 2012.

R. A. Pixley, R. De-la-cadena, J. D. Page, N. Kaufman, E. G. Wyshock et al., The contact system contributes to hypotension but not disseminated intravascular coagulation in lethal bacteremia. In vivo use of a monoclonal anti-factor XII antibody to block contact activation in baboons, J Clin Invest. janv, vol.91, issue.1, pp.61-69, 1993.

M. Larsson, V. Rayzman, M. W. Nolte, K. F. Nickel, J. Björkqvist et al., A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk, Sci Transl Med. 5 févr, vol.6, issue.222, pp.222-239, 2014.

E. I. Tucker, N. G. Verbout, P. Y. Leung, S. Hurst, O. Mccarty et al., Inhibition of factor XI activation attenuates inflammation and coagulopathy while improving the survival of mouse polymicrobial sepsis, Blood. 17 mai, vol.119, issue.20, pp.4762-4770, 2012.

C. E. Bane, I. Ivanov, A. Matafonov, K. L. Boyd, Q. Cheng et al., Factor XI Deficiency Alters the Cytokine Response and Activation of Contact Proteases during Polymicrobial Sepsis in Mice, PLoS ONE, vol.11, issue.4

M. Nakamura, T. Takeuchi, T. Kawahara, J. Hirose, K. Nakayama et al., Simultaneous targeting of CD14 and factor XIa by a fusion protein consisting of an anti-CD14 antibody and the modified second domain of bikunin improves survival in rabbit sepsis models, Eur J Pharmacol. 5 mai, vol.802, pp.60-68, 2017.

I. Stroo, S. Zeerleder, C. Ding, B. M. Luken, J. Roelofs et al., Coagulation factor XI improves host defence during murine pneumonia-derived sepsis independent of factor XII activation, Thromb Haemost, vol.26, issue.8, pp.1601-1615, 2017.

A. Butschkau, P. Nagel, E. Grambow, D. Zechner, G. J. Broze et al., Contribution of protein Z and protein Z-dependent protease inhibitor in generalized Shwartzman reaction, Crit Care Med. déc, vol.41, issue.12, pp.447-456, 2013.

Q. Choi, K. H. Hong, J. Kim, and H. K. Kim, Changes in plasma levels of natural anticoagulants in disseminated intravascular coagulation: high prognostic value of antithrombin and protein C in patients with underlying sepsis or severe infection, Ann Lab Med. mars, vol.34, issue.2, pp.85-91, 2014.

N. Lee, J. Kim, J. Gu, H. J. Yoo, I. Kim et al., Protein Z efficiently depletes thrombin generation in disseminated intravascular coagulation with poor prognosis, Blood Coagul Fibrinolysis Int J Haemost Thromb. janv, vol.27, issue.1, pp.84-93, 2016.

T. Sipahi, A. Kuybulu, A. Ozturk, and N. Akar, Protein Z G79A polymorphism in patients with severe sepsis, Clin Appl Thromb Off J Int Acad Clin Appl Thromb. juin, vol.16, issue.3, pp.334-340, 2010.

L. Dejager, I. Pinheiro, E. Dejonckheere, and C. Libert, Cecal ligation and puncture: the gold standard model for polymicrobial sepsis?, Trends Microbiol. avr, vol.19, issue.4, pp.198-208, 2011.

J. Zhang, G. J. Broze, and J. , Mouse Protein Z-Dependent Protease Inhibitor cDNA, Thromb Haemost, vol.85, issue.5, pp.861-866, 2001.

D. Rittirsch, M. S. Huber-lang, M. A. Flierl, and P. A. Ward, Immunodesign of experimental sepsis by cecal ligation and puncture, Nat Protoc, vol.4, issue.1, pp.31-37, 2009.

F. Liu, Y. Song, and D. Liu, Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA, Gene Ther. juill, vol.6, issue.7, pp.1258-66, 1999.

I. Marx, P. J. Lenting, T. Adler, R. Pendu, O. D. Christophe et al., Correction of bleeding symptoms in von Willebrand factor-deficient mice by liver-expressed von Willebrand factor mutants, Arterioscler Thromb Vasc Biol. mars, vol.28, issue.3, pp.419-443, 2008.

R. E. Jordan, J. Kilpatrick, and R. M. Nelson, Heparin promotes the inactivation of antithrombin by neutrophil elastase, Science. 14 août, vol.237, issue.4816, pp.777-786, 1987.

D. A. Higuchi, T. C. Wun, K. M. Likert, and G. J. Broze, The effect of leukocyte elastase on tissue factor pathway inhibitor, Blood. 1 avr, vol.79, issue.7, pp.1712-1721, 1992.

A. M. Oates and H. H. Salem, The binding and regulation of protein S by neutrophils, Blood Coagul Fibrinolysis Int J Haemost Thromb, vol.2, issue.5, pp.601-608, 1991.

I. Eckle, R. Seitz, R. Egbring, G. Kolb, and K. Havemann, Protein S degradation in vitro by neutrophil elastase, Scand J Clin Lab Invest. mai, vol.53, issue.3, pp.281-289, 1993.

M. Levi, T. Cate, and H. , Disseminated intravascular coagulation, N Engl J Med. 19 août, vol.341, issue.8, pp.586-92, 1999.

W. A. Wuillemin, M. Minnema, J. C. Meijers, D. Roem, A. J. Eerenberg et al., Inactivation of factor XIa in human plasma assessed by measuring factor XIa-protease inhibitor complexes: major role for C1-inhibitor, Blood. 15 mars, vol.85, issue.6, pp.1517-1543, 1995.

D. J. Knauer, D. Majumdar, P. C. Fong, and M. F. Knauer, SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor, J Biol Chem. 1 déc, vol.275, issue.48, pp.37340-37346, 2000.

F. R. Rosendaal, C. J. Doggen, A. Zivelin, V. R. Arruda, M. Aiach et al., Geographic distribution of the 20210 G to A prothrombin variant, Thromb Haemost. avr, vol.79, issue.4, pp.706-714, 1998.

P. G. Lindqvist and B. Dahlbäck, Carriership of Factor V Leiden and evolutionary selection advantage, Curr Med Chem, vol.15, issue.15, pp.1541-1545, 2008.

I. Elisia, H. B. Pae, V. Lam, R. Cederberg, E. Hofs et al., Comparison of RAW264.7, human whole blood and PBMC assays to screen for immunomodulators, J Immunol Methods, vol.452, pp.26-31, 2018.

F. H. Van-dooren, N. W. Duijvis, and A. A. Te-velde, Analysis of cytokines and chemokines produced by whole blood, peripheral mononuclear and polymorphonuclear cells, J Immunol Methods, vol.396, issue.1-2, pp.128-161, 2013.

T. Krakauer, Stimulant-dependent modulation of cytokines and chemokines by airway epithelial cells: cross talk between pulmonary epithelial and peripheral blood mononuclear cells, Clin Diagn Lab Immunol. janv, vol.9, issue.1, pp.126-157, 2002.

S. J. Allen, S. E. Crown, and T. M. Handel, Chemokine: receptor structure, interactions, and antagonism, Annu Rev Immunol, vol.25, pp.787-820, 2007.

M. Thelen and J. V. Stein, How chemokines invite leukocytes to dance, Nat Immunol. sept, vol.9, issue.9, pp.953-962, 2008.

J. Yoon, H. Kim, Y. Lee, and J. Lee, Cytokine induction by respiratory syncytial virus and adenovirus in bronchial epithelial cells, Pediatr Pulmonol. mars, vol.42, issue.3, pp.277-82, 2007.

F. J. Culley, A. Pennycook, J. S. Tregoning, J. S. Dodd, G. Walzl et al., Role of CCL5 (RANTES) in viral lung disease, J Virol. août, vol.80, issue.16, pp.8151-8158, 2006.

S. Shahrara, C. C. Park, V. Temkin, J. W. Jarvis, M. V. Volin et al., RANTES modulates TLR4-induced cytokine secretion in human peripheral blood monocytes, J Immunol Baltim Md, vol.177, issue.8, pp.5077-87, 1950.

A. Amati, A. Zakrzewicz, R. Siebers, S. Wilker, S. Heldmann et al., Chemokines (CCL3, CCL4, and CCL5) Inhibit ATP-Induced Release of IL-1? by Monocytic Cells, Mediators Inflamm, p.1434872, 2017.

A. Møller, A. Bjerre, B. Brusletto, G. B. Joø, P. Brandtzaeg et al., Chemokine patterns in meningococcal disease, J Infect Dis. 1 mars, vol.191, issue.5, pp.768-75, 2005.

E. Cavusoglu, C. Eng, V. Chopra, L. T. Clark, D. J. Pinsky et al., Low plasma RANTES levels are an independent predictor of cardiac mortality in patients referred for coronary angiography, Arterioscler Thromb Vasc Biol. avr, vol.27, issue.4, pp.929-964, 2007.

K. Conlon, A. Lloyd, U. Chattopadhyay, N. Lukacs, S. Kunkel et al., CD8+ and CD45RA+ human peripheral blood lymphocytes are potent sources of macrophage inflammatory protein 1 alpha, interleukin-8 and RANTES, Eur J Immunol. mars, vol.25, issue.3, pp.751-757, 1995.

P. Conti, R. C. Barbacane, C. Feliciani, and M. Reale, Expression and secretion of RANTES by human peripheral blood CD4+ cells are dependent on the presence of monocytes, Ann Clin Lab Sci. janv, vol.31, issue.1, pp.75-84, 2001.

J. M. Dayer, How T-lymphocytes are activated and become activators by cell-cell interaction, Eur Respir J Suppl. sept, vol.44, pp.10-15, 2003.

P. Isler, E. Vey, J. H. Zhang, and J. M. Dayer, Cell surface glycoproteins expressed on activated human T cells induce production of interleukin-1 beta by monocytic cells: a possible role of CD69, Eur Cytokine Netw. févr, vol.4, issue.1, pp.15-23, 1993.

S. Manié, J. Kubar, M. Limouse, B. Ferrua, M. Ticchioni et al., CD3-stimulated Jurkat T cells mediate IL-1 beta production in monocytic THP-1 cells. Role of LFA-1 molecule and participation of CD69 T cell antigen, Eur Cytokine Netw. févr, vol.4, issue.1, pp.7-13, 1993.

I. B. Mcinnes, B. P. Leung, R. D. Sturrock, M. Field, and F. Y. Liew, Interleukin-15 mediates T celldependent regulation of tumor necrosis factor-alpha production in rheumatoid arthritis, Nat Med. févr, vol.3, issue.2, pp.189-95, 1997.

C. Ribbens, J. M. Dayer, and C. Chizzolini, CD40-CD40 ligand (CD154) engagement is required but may not be sufficient for human T helper 1 cell induction of interleukin-2-or interleukin-15-driven, contact-dependent, interleukin-1beta production by monocytes, Immunology. févr, vol.99, issue.2, pp.279-86, 2000.

O. Guttman, B. M. Baranovski, R. Schuster, Z. Kaner, G. S. Freixo-lima et al., Acute-phase protein ?1-anti-trypsin: diverting injurious innate and adaptive immune responses from nonauthentic threats, Clin Exp Immunol. févr, vol.179, issue.2, pp.161-72, 2015.

M. R. Ehlers, Immune-modulating effects of alpha-1 antitrypsin, Biol Chem. oct, vol.395, issue.10, pp.1187-93, 2014.

S. Janciauskiene, S. Larsson, P. Larsson, R. Virtala, L. Jansson et al., Inhibition of lipopolysaccharide-mediated human monocyte activation, in vitro, by alpha1-antitrypsin, Biochem Biophys Res Commun. 27 août, vol.321, issue.3, pp.592-600, 2004.

R. Ross, Atherosclerosis--an inflammatory disease, N Engl J Med. 14 janv, vol.340, issue.2, pp.115-141, 1999.

A. Butschkau, N. Wagner, L. Bierhansl, B. Genz, and B. Vollmar, Protein Z-deficiency is associated with enhanced neointima formation and inflammatory response after vascular injury in mice, Int J Clin Exp Pathol, vol.7, issue.9, pp.6064-71, 2014.

C. F. Vogelmeier, G. J. Criner, F. J. Martinez, A. Anzueto, P. J. Barnes et al., Global Strategy for the Diagnosis, Management, and Prevention of Chronic Obstructive Lung Disease, Report. GOLD Executive Summary. Am J Respir Crit Care Med, vol.01, issue.5, pp.557-82, 2017.

B. R. Celli, W. Macnee, and A. Force, Standards for the diagnosis and treatment of patients with COPD: a summary of the ATS/ERS position paper, Eur Respir J. juin, vol.23, issue.6, pp.932-978, 2004.

L. Zuo, B. K. Pannell, T. Zhou, and C. Chuang, Historical role of alpha-1-antitrypsin deficiency in respiratory and hepatic complications, Gene. 10 sept, vol.589, issue.2, pp.118-140, 2016.

E. D. Janus, N. T. Phillips, and R. W. Carrell, Smoking, lung function, and alpha 1-antitrypsin deficiency, Lancet Lond Engl. 19 janv, vol.1, issue.8421, pp.152-156, 1985.

S. M. Janciauskiene, R. Bals, R. Koczulla, C. Vogelmeier, T. Köhnlein et al., The discovery of ?1-antitrypsin and its role in health and disease, Respir Med. août, vol.105, issue.8, pp.1129-1168, 2011.

T. Dziedzic, Systemic inflammation as a therapeutic target in acute ischemic stroke, Expert Rev Neurother. mai, vol.15, issue.5, pp.523-554, 2015.

M. Berger, M. Liu, M. E. Uknis, and M. Koulmanda, Alpha-1-antitrypsin in cell and organ transplantation, Am J Transplant Off J Am Soc Transplant Am Soc Transpl Surg. juill, vol.18, issue.7, pp.1589-95, 2018.

W. Gao, J. Zhao, H. Kim, S. Xu, M. Chen et al., ?1-Antitrypsin inhibits ischemia reperfusioninduced lung injury by reducing inflammatory response and cell death, J Heart Lung Transplant Off Publ Int Soc Heart Transplant. mars, vol.33, issue.3, pp.309-324, 2014.

M. Koulmanda, M. Bhasin, Z. Fan, D. Hanidziar, N. Goel et al., Alpha 1-antitrypsin reduces inflammation and enhances mouse pancreatic islet transplant survival, Proc Natl Acad Sci, vol.109, issue.38, pp.15443-15451, 2012.

C. Deboudt, J. Branchereau, F. Luyckx, J. Rigaud, P. Glemain et al.,

, Progres En Urol J Assoc Francaise Urol Soc Francaise Urol. juin, vol.22, issue.7, pp.402-409, 2012.

E. Terpos, M. Politou, N. Viniou, and A. Rahemtulla, Significance of macrophage inflammatory protein-1 alpha (MIP-1alpha) in multiple myeloma, Leuk Lymphoma. déc, vol.46, issue.12, pp.1699-707, 2005.

K. Osman, R. Comenzo, and S. V. Rajkumar, Deep venous thrombosis and thalidomide therapy for multiple myeloma, N Engl J Med. 21 juin, vol.344, issue.25, pp.1951-1953, 2001.