Complement and coagulation: strangers or partners in crime?

Trends in Immunology

Volumn 28, Issue 4, 2007, Pages 184-192

  Markiewski, Maciej M ^a   Nilsson, Bo ^b   Nilsson Ekdahl, Kristina ^b,c   Mollnes, Tom Eirik ^d,e   Lambris, John D ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UPPSALA UNIVERSITY   (Sweden)

^c LINNAEUS UNIVERSITY   (Sweden)

^d OSLO UNIVERSITY HOSPITAL   (Norway)

^e Nordlandssykehuse   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

ALTERNATIVE COMPLEMENT PATHWAY C3 C5 CONVERTASE; AUTOANTIBODY; BLOOD CLOTTING FACTOR 10; COAGULASE; COMPLEMENT; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C5; COMPLEMENT MEMBRANE ATTACK COMPLEX; KALLIKREIN; KININ; LECTIN; PLASMIN; PLASMINOGEN; THROMBIN;

ANGIONEUROTIC EDEMA; ANTICOAGULATION; ANTIPHOSPHOLIPID SYNDROME; BIOCOMPATIBILITY; BLOOD CLOTTING; CELL SURFACE; COMPLEMENT ACTIVATION; COMPLEMENT SYSTEM; FIBRINOLYSIS; HEMOLYTIC UREMIC SYNDROME; HEMOSTASIS; HUMAN; IMMUNITY; INFLAMMATION; INHIBITION KINETICS; MAST CELL; MOLECULAR INTERACTION; PAROXYSMAL NOCTURNAL HEMOGLOBINURIA; PATHOGENESIS; PHENOTYPE; PHOSPHOLIPID MEMBRANE; PLEIOTROPY; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; REVIEW; SYSTEMIC INFLAMMATORY RESPONSE SYNDROME; SYSTEMIC LUPUS ERYTHEMATOSUS; THROMBOCYTE ACTIVATION;

ANIMALS; BLOOD COAGULATION; COMPLEMENT ACTIVATION; COMPLEMENT SYSTEM PROTEINS; HUMANS; SIGNAL TRANSDUCTION;

EID: 33947602404     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2007.02.006     Document Type: Review

References (85)

1. Nathan C. Points of control in inflammation. Nature 420 (2002) 846-852
2. Esmon C.T. The impact of the inflammatory response on coagulation. Thromb. Res. 114 (2004) 321-327
3. Keel M., and Trentz O. Pathophysiology of polytrauma. Injury 36 (2005) 691-709
4. Sun H. The interaction between pathogens and the host coagulation system. Physiology (Bethesda) 21 (2006) 281-288
5. Schroeder B., et al. Species specificity of plasminogen activation and acquisition of surface-associated proteolytic activity by group C streptococci grown in plasma. Infect. Immun. 67 (1999) 6487-6495
6. Ruiz-Irastorza G., et al. Systemic lupus erythematosus. Lancet 357 (2001) 1027-1032
7. Guo R.F., and Ward P.A. Role of C5a in inflammatory responses. Annu. Rev. Immunol. 23 (2005) 821-852
8. Walport M.J. Complement. First of two parts. New Engl. J. Med. 344 (2001) 1058-1066
9. Bhole D., and Stahl G.L. Molecular basis for complement component 6 (C6) deficiency in rats and mice. Immunobiology 209 (2004) 559-568
10. Krem M.M., and Di Cera E. Evolution of enzyme cascades from embryonic development to blood coagulation. Trends Biochem. Sci. 27 (2002) 67-74
11. Dissing M., et al. Autoproteolysis and feedback in a protease cascade directing Drosophila dorsal-ventral cell fate. EMBO J. 20 (2001) 2387-2393
12. LeMosy E.K., et al. Activation of a protease cascade involved in patterning the Drosophila embryo. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 5055-5060
13. Nangaku M., and Couser W.G. Mechanisms of immune-deposit formation and the mediation of immune renal injury. Clin. Exp. Nephrol. 9 (2005) 183-191
14. Wojta J., et al. New aspects in thrombotic research: complement induced switch in mast cells from a profibrinolytic to a prothrombotic phenotype. Pathophysiol. Haemost. Thromb. 33 (2003) 438-441
15. Wojta J., et al. C5a stimulates production of plasminogen activator inhibitor-1 in human mast cells and basophils. Blood 100 (2002) 517-523
16. Zwaal R.F., et al. Loss of membrane phospholipid asymmetry during activation of blood platelets and sickled red cells; mechanisms and physiological significance. Mol. Cell. Biochem. 91 (1989) 23-31
17. Sims P.J., and Wiedmer T. The response of human platelets to activated components of the complement system. Immunol. Today 12 (1991) 338-342
18. Sims P.J., et al. Complement proteins C5b-9 cause release of membrane vesicles from the platelet surface that are enriched in the membrane receptor for coagulation factor Va and express prothrombinase activity. J. Biol. Chem. 263 (1988) 18205-18212
19. Ando B., et al. Complement proteins C5b-9 initiate secretion of platelet storage granules without increased binding of fibrinogen or von Willebrand factor to newly expressed cell surface GPIIb-IIIa. J. Biol. Chem. 263 (1988) 11907-11914
20. Peerschke E.I.B., et al. Platelet activation by C1q results in the induction of alpha IIb/beta 3 integrins (GPIIb-IIIa) and the expression of P-selectin and procoagulant activity. J. Exp. Med. 178 (1993) 579-587
21. Polley M.J., and Nachman R.L. Human platelet activation by C3a and C3a des-arg. J. Exp. Med. 158 (1983) 603-615
22. Drake T.A., et al. Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. Am. J. Pathol. 134 (1989) 1087-1097
23. Drake T.A., et al. Functional tissue factor is entirely cell surface expressed on lipopolysaccharide-stimulated human blood monocytes and a constitutively tissue factor-producing neoplastic cell line. J. Cell Biol. 109 (1989) 389-395
24. Muhlfelder T.W., et al. C5 chemotactic fragment induces leukocyte production of tissue factor activity: a link between complement and coagulation. J. Clin. Invest. 63 (1979) 147-150
25. Ikeda K., et al. C5a induces tissue factor activity on endothelial cells. Thromb. Haemost. 77 (1997) 394-398
26. Tedesco F., et al. The cytolytically inactive terminal complement complex activates endothelial cells to express adhesion molecules and tissue factor procoagulant activity. J. Exp. Med. 185 (1997) 1619-1627
27. Ritis K., et al. A novel C5a receptor-tissue factor cross-talk in neutrophils links innate immunity to coagulation pathways. J. Immunol. 177 (2006) 4794-4802
28. Platt J.L., et al. The role of C5a and antibody in the release of heparan sulfate from endothelial cells. Eur. J. Immunol. 21 (1991) 2887-2890
29. Marcum J.A., et al. Cloned bovine aortic endothelial cells synthesize anticoagulantly active heparan sulfate proteoglycan. J. Biol. Chem. 261 (1986) 7507-7517
30. Lozada C., et al. Identification of C1q as the heat-labile serum cofactor required for immune complexes to stimulate endothelial expression of the adhesion molecules E-selectin and intercellular and vascular cell adhesion molecules 1. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 8378-8382
31. Hamilton K.K., et al. Complement proteins C5b-9 induce vesiculation of the endothelial plasma membrane and expose catalytic surface for assembly of the prothrombinase enzyme complex. J. Biol. Chem. 265 (1990) 3809-3814
32. Bossi F., et al. Platelet-activating factor and kinin-dependent vascular leakage as a novel functional activity of the soluble terminal complement complex. J. Immunol. 173 (2004) 6921-6927
33. Rezende S.M., et al. Coagulation, inflammation, and apoptosis: different roles for protein S and the protein S-C4b binding protein complex. Blood 103 (2004) 1192-1201
34. Garcia de Frutos P., et al. Differential regulation of α and β chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S. Blood 84 (1994) 815-822
35. Trouw L.A., et al. C4b-binding protein binds to necrotic cells and DNA, limiting DNA release and inhibiting complement activation. J. Exp. Med. 201 (2005) 1937-1948
36. Mastellos D., et al. Novel biological networks modulated by complement. Clin. Immunol. 115 (2005) 225-235
37. Markiewski M.M., et al. Liver inflammation and regeneration: Two distinct biological phenomena or parallel pathophysiologic processes?. Mol. Immunol. 43 (2006) 45-56
38. Shebuski R.J., and Kilgore K.S. Role of inflammatory mediators in thrombogenesis. J. Pharmacol. Exp. Ther. 300 (2002) 729-735
39. Spath P., and Gabl F. Critical role of the conversion of the third complement component C3 (β1C/β1A) for its immunochemical quantitation. Clin. Chim. Acta 73 (1976) 171-175
40. 2-terminal structure and cleavage of guinea pig pro-C3 the precursor of the third complement component. J. Biol. Chem. 256 (1981) 12617-12619
41. Lachmann P.J., et al. Breakdown of C3 after complement activation. Identification of a new fragment, C3g, using monoclonal antibodies. J. Exp. Med. 156 (1982) 205-216
42. Thoman M.L., et al. C3d-K, a kallikrein cleavage fragment of iC3b is a potent inhibitor of cellular proliferation. J. Immunol. 133 (1984) 2629-2633
43. Ghebrehiwet B., et al. Mechanisms of activation of the classical pathway of complement by Hageman factor fragment. J. Clin. Invest. 71 (1983) 1450-1456
44. Huber-Lang M., et al. Generation of C5a in the absence of C3: a new complement activation pathway. Nat. Med. 12 (2006) 682-687
45. Mollnes T.E., et al. Effect of time, temperature and anticoagulants on in vitro complement activation: consequences for collection and preservation of samples to be examined for complement activation. Clin. Exp. Immunol. 73 (1988) 484-488
46. Kalowski S., et al. Effects of intravascular clotting on the activation of the complement system: The role of the platelet. Am. J. Pathol. 78 (1975) 525-536
47. Del Conde I., et al. Platelet activation leads to activation and propagation of the complement system. J. Exp. Med. 201 (2005) 871-879
48. Peerschke E.I., et al. Blood platelets activate the classical pathway of human complement. J. Thromb. Haemost. 4 (2006) 2035-2042
49. Ekdahl K.N., and Nilsson B. Phosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase. Inhibition of factor I-mediated cleavage of C3b. J. Immunol. 154 (1995) 6502-6510
50. Ekdahl K.N., et al. Increased phosphate content in complement component C3, fibrinogen, vitronectin, and other plasma proteins in systemic lupus erythematosus: covariation with platelet activation and possible association with thrombosis. Arthritis Rheum. 40 (1997) 2178-2186
51. Ekdahl K.N., and Nilsson B. Alterations in C3 activation and binding caused by phosphorylation by a casein kinase released from activated human platelets. J. Immunol. 162 (1999) 7426-7433
52. No authors listed (1992) American College of Chest Physicians/Society of Critical Care Medicine Consensus Conference: definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis. Crit. Care Med. 20, 864-874
53. Laudes I.J., et al. Anti-c5a ameliorates coagulation/fibrinolytic protein changes in a rat model of sepsis. Am. J. Pathol. 160 (2002) 1867-1875
54. Pierangeli S.S., et al. Complement activation: a novel pathogenic mechanism in the antiphospholipid syndrome. Ann. N. Y. Acad. Sci. 1051 (2005) 413-420
55. Holers V.M., et al. Complement C3 activation is required for antiphospholipid antibody-induced fetal loss. J. Exp. Med. 195 (2002) 211-220
56. Inanc M., et al. Anti-β2-glycoprotein I, anti-prothrombin and anticardiolipin antibodies in a longitudinal study of patients with systemic lupus erythematosus and the antiphospholipid syndrome. Br. J. Rheumatol. 37 (1998) 1089-1094
57. Nojima J., et al. Platelet activation induced by combined effects of anticardiolipin and lupus anticoagulant IgG antibodies in patients with systemic lupus erythematosus - possible association with thrombotic and thrombocytopenic complications. Thromb. Haemost. 81 (1999) 436-441
58. Warwicker P., et al. Genetic studies into inherited and sporadic hemolytic uremic syndrome. Kidney Int. 53 (1998) 836-844
59. Rougier N., et al. Human complement factor H deficiency associated with hemolytic uremic syndrome. J. Am. Soc. Nephrol. 9 (1998) 2318-2326
60. Dragon-Durey M.A., et al. Anti-factor H autoantibodies associated with atypical hemolytic uremic syndrome. J. Am. Soc. Nephrol. 16 (2005) 555-563
61. Manuelian T., et al. Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome. J. Clin. Invest. 111 (2003) 1181-1190
62. Caprioli J., et al. Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical presentation, response to treatment, and outcome. Blood 108 (2006) 1267-1279
63. Goicoechea de Jorge E., et al. Gain-of-function mutations in complement factor B are associated with atypical hemolytic uremic syndrome. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 240-245
64. Takeda J., et al. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell 73 (1993) 703-711
65. Liebman H.A., and Feinstein D.I. Thrombosis in patients with paroxysmal noctural hemoglobinuria is associated with markedly elevated plasma levels of leukocyte-derived tissue factor. Thromb. Res. 111 (2003) 235-238
66. Hillmen P., et al. The complement inhibitor eculizumab in paroxysmal nocturnal hemoglobinuria. New Engl. J. Med. 355 (2006) 1233-1243
67. Davis III A.E. The pathophysiology of hereditary angioedema. Clin. Immunol. 114 (2005) 3-9
68. Cichon S., et al. Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am. J. Hum. Genet. 79 (2006) 1098-1104
69. Gorbet M.B., and Sefton M.V. Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes. Biomaterials 25 (2004) 5681-5703
70. Mollnes T.E., et al. Essential role of the C5a receptor in E. coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation. Blood 100 (2002) 1869-1877
71. Moberg L., et al. Production of tissue factor by pancreatic islet cells as a trigger of detrimental thrombotic reactions in clinical islet transplantation. Lancet 360 (2002) 2039-2045
72. Ozmen L., et al. Inhibition of thrombin abrogates the instant blood-mediated inflammatory reaction triggered by isolated human islets: possible application of the thrombin inhibitor melagatran in clinical islet transplantation. Diabetes 51 (2002) 1779-1784
73. Walport M.J. Complement. Second of two parts. New Engl. J. Med. 344 (2001) 1140-1144
74. McVey J.H. Tissue factor pathway. Best Pract. Res. Clin. Haematol. 12 (1999) 361-372
75. Stassen J.M., et al. The hemostatic system. Curr. Med. Chem. 11 (2004) 2245-2260
76. Dihanich M., et al. Prothrombin mRNA is expressed by cells of the nervous system. Neuron 6 (1991) 575-581
77. Ishihara H., et al. Protease-activated receptor 3 is a second thrombin receptor in humans. Nature 386 (1997) 502-506
78. Donovan F.M., et al. Thrombin induces apoptosis in cultured neurons and astrocytes via a pathway requiring tyrosine kinase and RhoA activities. J. Neurosci. 17 (1997) 5316-5326
79. Donovan F.M., and Cunningham D.D. Signaling pathways involved in thrombin-induced cell protection. J. Biol. Chem. 273 (1998) 12746-12752
80. Chinni C., et al. Thrombin, a survival factor for cultured myoblasts. J. Biol. Chem. 274 (1999) 9169-9174
81. Bizios R., et al. Thrombin-induced chemotaxis and aggregation of neutrophils. J. Cell. Physiol. 128 (1986) 485-490
82. Bar-Shavit R., et al. Monocyte chemotaxis: stimulation by specific exosite region in thrombin. Science 220 (1983) 728-731
83. Sarker K.P., et al. Inhibition of thrombin-induced neuronal cell death by recombinant thrombomodulin and E5510, a synthetic thrombin receptor signaling inhibitor. Thromb. Haemost. 82 (1999) 1071-1077
84. Henrikson K.P., et al. Role of thrombin receptor in breast cancer invasiveness. Br. J. Cancer 79 (1999) 401-406
85. Kaiser B., et al. A synthetic inhibitor of factor Xa, DX-9065a, reduces proliferation of vascular smooth muscle cells in vivo in rats. Thromb. Res. 98 (2000) 175-185