Abstract
Coagulation is a constant attendant of inflammation and is fundamental to confine infection and/or the inflammatory response to a limited area. Coagulation is tightly controlled by various factors, such as tissue factor (TF), finally activating thrombin, which cleaves fibrinogen to initiate fibrin clot formation. Systemic inflammatory response syndrome (SIRS) and sepsis remain a major health concern on intensive care units (ICUs) in the western world often ending in multiple organ dysfunction and death. The pathogenesis of both systemic disorders are attributed to an uncontrolled inflammatory response and dysregulated coagulation, the latter often causing disseminated intravascular coagulation (DIC), microvascular failure and multiple organ dysfunction [1, 2]. Fibrin(ogen) degradation products, D-dimers, Bβ15-42 and soluble fibrin are increased in septic patients with organ dysfunction [3, 4], but the contribution of these fragments to the pathogenesis of sepsis remains unclear.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Taylor FB Jr, Toh CH, Hoots WK, Wada H, Levi M (2001) Towards definition, clinical and laboratory criteria, and a scoring system for disseminated intravascular coagulation. Thromb Haemost 86: 1327–1330
Levi M, Ten Cate H (1999) Disseminated intravascular coagulation. N Engl J Med 341: 586–592
Iba T, Kidokoro A, Fukunaga M, et al (2005) Association between the severity of sepsis and the changes in hemostatic molecular markers and vascular endothelial damage markers. Shock 23: 25–29
Fareed J, Hoppensteadt DA, Leya F, et al (1998) Useful laboratory tests for studying throm-bogenesis in acute cardiac syndromes. Clin Chem 44: 1845–1853
Levi M, van der Poll T, Buller HR (2004) Bidirectional relation between inflammation and coagulation. Circulation 109: 2698–2704
Medcalf RL (2007) Fibrinolysis, inflammation, and regulation of the plasminogen activating system. J Thromb Haemost 5 Suppl 1: 132–142
Knoebl P (2010) Blood coagulation disorders in septic patients. Wien Med Wochenschr 160: 129–138
Levi M (2010) The coagulant response in sepsis and inflammation. Hamostaseologie 30: 10–12, 14–16
Mosesson MW (2005) Fibrinogen and fibrin structure and functions. J Thromb Haemost 3: 1894–1904
Lord ST (2007) Fibrinogen and fibrin: scaffold proteins in hemostasis. Curr Opin Hematol 14: 236–241
Smith EB, Keen GA, Grant A, Stirk C (1990) Fate of fibrinogen in human arterial intima. Arteriosclerosis 10: 263–275
Walker JB, Nesheim ME (1999) The molecular weights, mass distribution, chain composition, and structure of soluble fibrin degradation products released from a fibrin clot per-fused with plasmin. J Biol Chem 274: 5201–5212
Hynes RO (1992) Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11–25
Altieri DC (1999) Regulation of leukocyte-endothelium interaction by fibrinogen. Thromb Haemost 82: 781–786
Ugarova TP, Yakubenko VP (2001) Recognition of fibrinogen by leukocyte integrins. Ann N Y Acad Sci 936: 368–385
Flick MJ, Du X, Degen JL (2004) Fibrin(ogen)-alpha M beta 2 interactions regulate leukocyte function and innate immunity in vivo. Exp Biol Med (Maywood) 229: 1105–1110
Languino LR, Plescia J, Duperray A, et al (1993) Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway. Cell 73: 1423–1434
Harley SL, Sturge J, Powell JT (2000) Regulation by fibrinogen and its products of intercellular adhesion molecule-1 expression in human saphenous vein endothelial cells. Arterioscler Thromb Vasc Biol 20: 652–658
Lishko VK, Burke T, Ugarova T (2007) Antiadhesive effect of fibrinogen: a safeguard for thrombus stability. Blood 109: 1541–1549
Lishko VK, Yermolenko IS, Ugarova TP (2010) Plasminogen on the surfaces of fibrin clots prevents adhesion of leukocytes and platelets. J Thromb Haemost 8: 799–807
Qi J, Goralnick S, Kreutzer DL (1997) Fibrin regulation of interleukin-8 gene expression in human vascular endothelial cells. Blood 90: 3595–3602
Smiley ST, King JA, Hancock WW (2001) Fibrinogen stimulates macrophage chemokine secretion through toll-like receptor 4. J Immunol 167: 2887–2894
Szaba FM, Smiley ST (2002) Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood 99: 1053–1059
Cunningham MA, Rondeau E, Chen X, et al (2000) Protease-activated receptor 1 mediates thrombin-dependent, cell-mediated renal inflammation in crescentic glomerulonephritis. J Exp Med 191: 455–462
Senior RM, Skogen WF, Griffin GL, Wilner GD (1986) Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B. J Clin Invest 77: 1014–1019
Persson K, Russell W, Morgelin M, Herwald H (2003) The conversion of fibrinogen to fibrin at the surface of curliated Escherichia coli bacteria leads to the generation of proinflammatory fibrinopeptides. J Biol Chem 278: 31884–31890
Hamaguchi M, Morishita Y, Takahashi I, et al (1991) FDP D-dimer induces the secretion of interleukin-1, urokinase-type plasminogen activator, and plasminogen activator inhibitor-2 in a human promonocytic leukemia cell line. Blood 77: 94–100
Robson SC, Shephard EG, Kirsch RE (1994) Fibrin degradation product D-dimer induces the synthesis and release of biologically active IL-1 beta, IL-6 and plasminogen activator inhibitors from monocytes in vitro. Br J Haematol 86: 322–326
Lee ME, Rhee KJ, Nham SU (1999) Fragment E derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages. Mol Cells 9: 7–13
Lee ME, Kweon SM, Ha KS, Nham SU (2001) Fibrin stimulates microfilament reorganization and IL-1beta production in human monocytic THP-1 cells. Mol Cells 11: 13–20
Olexa SA, Budzynski AZ, Doolittle RF, Cottrell BA, Greene TC (1981) Structure of fragment E species from human cross-linked fibrin. Biochemistry 20: 6139–6145
Vali Z, Scheraga HA (1988) Localization of the binding site on fibrin for the secondary binding site of thrombin. Biochemistry 27: 1956–1963
Bach TL, Barsigian C, Yaen CH, Martinez J (1998) Endothelial cell VE-cadherin functions as a receptor for the beta15-42 sequence of fibrin. J Biol Chem 273: 30719–30728
Petzelbauer P, Zacharowski PA, Miyazaki Y, et al (2005) The fibrin-derived peptide Bbeta15-42 protects the myocardium against ischemia-reperfusion injury. Nat Med 11: 298–304
Atar D, Petzelbauer P, Schwitter J, et al (2009) Effect of intravenous FX06 as an adjunct to primary percutaneous coronary intervention for acute ST-segment elevation myocardial infarction results of the F.I.R.E. (Efficacy of FX06 in the Prevention of Myocardial Reperfusion Injury) trial. J Am Coll Cardiol 53: 720–729
Roesner JP, Petzelbauer P, Koch A, et al (2009) Bbeta15-42 (FX06) reduces pulmonary, myocardial, liver, and small intestine damage in a pig model of hemorrhagic shock and reperfusion. Crit Care Med 37: 598–605
Groger M, Pasteiner W, Ignatyev G, et al (2009) Peptide Bbeta(15–42) preserves endothelial barrier function in shock. PLoS One 4: e5391
Wiedemann D, Schneeberger S, Friedl P, et al (2010) The fibrin-derived peptide Bbeta(15–42) significantly attenuates ischemia-reperfusion injury in a cardiac transplant model. Transplantation 89: 824–829
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Springer Science+Business Media LLC
About this chapter
Cite this chapter
Jennewein, C., Tran, N., Zacharowski, K. (2011). The Inflammatory Potential of Fibrin(ogen) and its Degradation Products. In: Vincent, JL. (eds) Annual Update in Intensive Care and Emergency Medicine 2011. Annual Update in Intensive Care and Emergency Medicine 2011, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18081-1_6
Download citation
DOI: https://doi.org/10.1007/978-3-642-18081-1_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-18080-4
Online ISBN: 978-3-642-18081-1
eBook Packages: MedicineMedicine (R0)