Mathematical modeling of blood coagulation cascade: Kinetics of intrinsic and extrinsic pathways in normal and deficient conditions

Blood Coagulation and Fibrinolysis

Volumn 18, Issue 7, 2007, Pages 637-646

  Zhu, Donghui ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

Blood coagulation; Contact activation; Thrombin; Thrombosis; Tissue factor

Indexed keywords

BLOOD CLOTTING FACTOR; PROTEIN; THROMBIN;

ARTICLE; BLOOD CLOTTING; BLOOD CLOTTING DISORDER; BLOOD CLOTTING PARAMETERS; BLOOD CLOTTING TIME; KINETICS; MATHEMATICAL MODEL; PREDICTION; PRIORITY JOURNAL; SENSITIVITY ANALYSIS; SIGNAL TRANSDUCTION;

ALGORITHMS; ANIMALS; ANTICOAGULANTS; BLOOD COAGULATION; BLOOD COAGULATION FACTORS; BLOOD COAGULATION TESTS; COAGULANTS; COAGULATION PROTEIN DISORDERS; COMPUTER SIMULATION; HUMANS; KINETICS; MODELS, CARDIOVASCULAR; NUMERICAL ANALYSIS, COMPUTER-ASSISTED; THROMBIN;

EID: 34748820001     PISSN: 09575235     EISSN: None     Source Type: Journal    
DOI: 10.1097/MBC.0b013e3282a167bb     Document Type: Article

References (56)

1. Davie EW, Fujikawa K, Kisiel W. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991; 30:10363-10370.
2. Schenone M, Furie BC, Furie B. The blood coagulation cascade. Curr Opin Hematol 2004; 11:272-277.
3. Mann KG. Biochemistry and physiology of blood coagulation. Thromb Haemost 1999; 82:165-174.
4. Ataullakhanov FI, Panteleev MA. Mathematical modeling and computer simulation in blood coagulation. Pathophysiol Haemost Thromb 2005; 34:60-70.
5. Jones KC, Mann KG. A model for the tissue factor pathway to thrombin. II. A mathematical simulation. J Biol Chem 1994; 269:23367-23373.
6. Khanin MA, Rakov DV, Kogan AE. Mathematical model for the blood coagulation prothrombin time test. Thromb Res 1998; 89:227-232.
7. Kogan AE, Kardakov DV, Khanin MA. Analysis of the activated partial thromboplastin time test using mathematical modeling. Thromb Res 2001; 101:299-310.
8. Pohl B, Beringer C, Bomhard M, Keller F. The quick machine - a mathematical model for the extrinsic activation of coagulation. Haemostasis 1994; 24:325-337.
9. Zarnitsina VI, Pokhilko AV, Ataullakhanov FI. A mathematical model for the spatio-temporal dynamics of intrinsic pathway of blood coagulation. I. The model description. Thromb Res 1996; 84:225-236.
10. Obraztsov IF, Kardakov DV, Kogan AE, Khanin MA. A mathematical model of the background state of the blood coagulation system. Dokl Biochem Biophys 2001; 376:10-12.
11. Warn-Cramer BJ, Bajaj SP. Intrinsic versus extrinsic coagulation. Kinetic considerations. Biochem J 1986; 239:757-762.
12. Zarnitsina VI, Pokhilko AV, Ataullakhanov FI. A mathematical model for the spatio-temporal dynamics of intrinsic pathway of blood coagulation. II. Results. Thromb Res 1996; 84:333-344.
13. Tapper H, Herwald H. Modulation of hemostatic mechanisms in bacterial infectious diseases. Blood 2000; 96:2329-2337.
14. Brummel KE, Butenas S, Mann KG. An integrated study of fibrinogen during blood coagulation. J Biol Chem 1999; 274:22862-22870.
15. Greenberg CS, Miraglia CC, Rickles FR, Shuman MA. Cleavage of blood coagulation factor XIII and fibrinogen by thrombin during in vitro clotting. J Clin Invest 1985; 75:1463-1470.
16. Ellis V, Scully MF, Kakkar VV. Inhibition of prothrombinase complex by plasma proteinase inhibitors. Biochemistry 1984; 23:5882-5887.
17. Hultin MB. Role of human factor VIII in factor X activation. J Clin Invest 1982; 69:950-958.
18. Krishnaswamy S, Church WR, Nesheim ME, Mann KG. Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism. J Biol Chem 1987; 262:3291-3299.
19. Rawala-Sheikh R, Ahmad SS, Ashby B, Walsh PN. Kinetics of coagulation factor X activation by platelet-bound factor IXa. Biochemistry 1990; 29:2606-2611.
20. Tracy PB, Eide LL, Mann KG. Human prothrombinase complex assembly and function on isolated peripheral blood cell populations. J Biol Chem 1985; 260:2119-2124.
21. Horsti J, Uppa H, Vilpo JA. Poor agreement among prothrombin time international normalized ratio methods: comparison of seven commercial reagents. Clin Chem 2005; 51:553-560.
22. Naito K, Fujikawa K. Activation of human blood coagulation factor XI independent of factor XII. Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces. J Biol Chem 1991; 266:7353-7358.
23. Camerer E, Kolsto AB, Prydz H. Cell biology of tissue factor, the principal initiator of blood coagulation. Thromb Res 1996; 81:1-41.
24. Colman RW, Schmaier AH. Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 1997; 90:3819-3843.
25. Saito H, Poon MC, Vicic W, Goldsmith GH Jr, Menitove JE. Human plasma prekallikrein (Fletcher factor) clotting activity and antigen in health and disease. J Lab Clin Med 1978; 92:84-95.
26. Wuillemin WA, Furlan M, Lammle B. A quantitative dot immunobinding assay for coagulation factor XII in plasma. J Immunol Methods 1990; 130:133-140.
27. Pritchard D, Creighton R, Craig D, Shanahan R, Creagmile S. An automated assay for the determination of activated factor XII [abstract]. Thromb Haemost 1999; Suppl:571.
28. Bouma BN, Griffin JH. Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII. J Biol Chem 1977; 252:6432-6437.
29. Epstein DJ, Bergum PW, Bajaj SP, Rapaport SI. Radioimmunoassays for protein C and factor X. Plasma antigen levels in abnormal hemostatic states. Am J Clin Pathol 1984; 82:573-581.
30. Suomela H. Human coagulation factor IX. Isolation and characterization. Eur J Biochem 1976; 71:145-154.
31. Tracy PB, Eide LL, Bowie EJ, Mann KG. Radioimmunoassay of factor V in human plasma and platelets. Blood 1982; 60:59-63.
32. Krishnan G. Radioimmunoassay for human prothrombin. Clin Chem 1983; 29:842-844.
33. Ratnoff OD, Menzie C. A new method for the determination of fibrinogen in small samples of plasma. J Lab Clin Med 1951; 37:316-320.
34. Harpel P. Blood proteolytic enzyme inhibitors: their role in modulating blood coagulation and fibrinolytic enzyme pathways. Philadelphia, PA: Lippincott; 1987.
35. Collen D, Schetz J, de Cock F, Holmer E, Verstraete M. Metabolism of antithrombin III (heparin cofactor) in man: effects of venous thrombosis and of heparin administration. Eur J Clin Invest 1977; 7:27-35.
36. Kruithof EK, Gudinchet A, Bachmann F. Plasminogen activator inhibitor 1 and plasminogen activator inhibitor 2 in various disease states. Thromb Haemost 1988; 59:7-12.
37. Novotny WF, Girard TJ, Miletich JP, Broze GJ Jr. Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma. J Biol Chem 1989; 264:18832-18837.
38. Aso Y, Fujiwara Y, Tayama K, Takebayashi K, Inukai T, Takemura Y. Relationship between soluble thrombomodulin in plasma and coagulation or fibrinolysis in type 2 diabetes. Clin Chim Acta 2000; 301:135-145.
39. Vaziri ND, Alikhani S, Patel B, Nguyen Q, Barton CH, Gonzales EV. Increased levels of protein C activity, protein C concentration, total and free protein S in nephrotic syndrome. Nephron 1988; 49:20-23.
40. Tankersley DL, Finlayson JS. Kinetics of activation and autoactivation of human factor XII. Biochemistry 1984; 23:273-279.
41. Gailani D, Broze GJ Jr. Factor XI activation in a revised model of blood coagulation. Science 1991; 253:909-912.
42. Rosing J, Tans G, Govers-Riemslag JW, Zwaal RF, Hemker HC. The role of phospholipids and factor Va in the prothrombinase complex. J Biol Chem 1980; 255:274-283.
43. Monkovic DD, Tracy PB. Activation of human factor V by factor Xa and thrombin. Biochemistry 1990; 29:1118-1128.
44. Hill-Eubanks DC, Lollar P. von Willebrand factor is a cofactor for thrombin-catalyzed cleavage of the factor VIII light chain. J Biol Chem 1990; 265:17854-17858.
45. Higgins DL, Lewis SD, Shafer JA. Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin. J Biol Chem 1983; 258:9276-9282.
46. Matsushita T, Kojima T, Emi N, Takahashi I, Saito H. Impaired human tissue factor-mediated activity in blood clotting factor VIINagoya (Arg304 → Trp). Evidence that a region in the catalytic domain of factor VII is important for the association with tissue factor. J Biol Chem 1994; 269:7355-7363.
47. Yang L, Manithody C, Rezaie AR. Activation of protein C by the thrombin-thrombomodulin complex: cooperative roles of Arg-35 of thrombin and Arg-67 of protein C. Proc Natl Acad Sci U S A 2006; 103:879-884.
48. Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem 1980; 255:3931-3934.
49. Jesty J, Wun TC, Lorenz A. Kinetics of the inhibition of factor Xa and the tissue factor-factor VIIa complex by the tissue factor pathway inhibitor in the presence and absence of heparin. Biochemistry 1994; 33:12686-12694.
50. Jordan RE, Oosta GM, Gardner WT, Rosenberg RD. The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin. J Biol Chem 1980; 255:10081-10090.
51. Berrettini M, Schleef RR, Espana F, Loskutoff DJ, Griffin JH. Interaction of type 1 plasminogen activator inhibitor with the enzymes of the contact activation system. J Biol Chem 1989; 264:11738-11743.
52. Pixley RA, Schapira M, Colman RW. The regulation of human factor XIIa by plasma proteinase inhibitors. J Biol Chem 1985; 260:1723-1729.
53. de Agostini A, Lijnen HR, Pixley RA, Colman RW, Schapira M. Inactivation of factor XII active fragment in normal plasma. Predominant role of C-1-inhibitor. J Clin Invest 1984; 73:1542-1549.
54. Olson ST, Sheffer R, Francis AM. High molecular weight kininogen potentiates the heparin-accelerated inhibition of plasma kallikrein by antithrombin: role for antithrombin in the regulation of kallikrein. Biochemistry 1993; 32:12136-12147.
55. Lawson JH, Butenas S, Ribarik N, Mann KG. Complex-dependent inhibition of factor VIIa by antithrombin III and heparin. J Biol Chem 1993; 268:767-770.
56. Baerga-Ortiz A, Rezaie AR, Komives EA. Electrostatic dependence of the thrombin-thrombomodulin interaction. J Mol Biol 2000; 296:651-658.