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New biological concepts on coagulation inhibitors

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References

  1. Jackson CM, Nemerson Y (1980) Blood coagulation. Ann Rev Biochem 49:765–811

    Google Scholar 

  2. Mann KG, Nesheim ME, Church WR, Haley P, Krishanaswamy S (1990) Surface-dependent reactions of the vitamin k-dependent enzyme complexes. Blood 76:1–16

    Google Scholar 

  3. Broze GJ Jr (1992) The role of tissue factor pathway inhibitor in a revised coagulation cascade. Semin Hematol 29:159–169

    Google Scholar 

  4. Lämmle B, Griffin JH (1985) Formation of the fibrin clot: the balance of procoagulant and inhibitory factors. Clin Hematol 14:281–342

    Google Scholar 

  5. Rosenberg RD, Rosenberg JS (1984) Natural anticoagulant mechanisms. J Clin Invest 74:1–12

    Google Scholar 

  6. Esmon CT (1987) The regulation of natural anticoagulant pathways. Science 235:1348–1352

    Google Scholar 

  7. Thaler E, Lechner K (1981) Antithroombin III deficiency and thromboembolism. Clin Haematol 10:369–390

    Google Scholar 

  8. Bovill EG, Bauer KA, Dickerman JD, Callas P, West B (1989) The clinical spectrum of heterozygous protein C deficiency in a large New England kindred. Blood 73:712–717

    Google Scholar 

  9. Engesser L, Broekmans AW, Briët E, Brommer EJP, Bertina RM (1987) Hereditary protein S deficiency: clinical manifestations. Ann Intern Med 106:677–682

    Google Scholar 

  10. Rapaport SI (1991) The extrinsic pathway inhibitor: a regulator of tissue factor-dependent blood coagulation. Thromb Haemost 66:6–15

    Google Scholar 

  11. Bertina RM, van der Linden IK, Engesser L, Muller HP, Brommer EJP (1987) Hereditary heparin cofactor II deficiency and the risk of development of thrombosis. Thromb Haemost 57:196–200

    Google Scholar 

  12. Huber R, Carrell RW (1989) Implications of the three dimensional structure of α1-antitrypsin for structure and function of serpins. Biochemistry 28:8951–8966

    Google Scholar 

  13. Lane DA, Olds RR, Thein SL (1992) Antithrombin and its deficiency states. Blood Coagul Fibrinolysis 3:315–341

    Google Scholar 

  14. Carrell RW, Christey PB, Boswell DR (1987) Serpins: antithrombin and other inhibitors of coagulation and fibrinolysis. Evidence from amino acid sequence. In: Verstraete M, Vermylen J, Lijnen HR, Arnout J (eds) Thrombosis and haemostasis. International Society on Thrombosis and Haemostasis and Leuven University Press, Leuven, pp 1–15

    Google Scholar 

  15. Carrell RW, Evans DL, Stein PE (1991) Mobile reactive centre of serpins and the control of thrombosis. Nature 353:576–578

    Google Scholar 

  16. Carrell RW (1992) Antithrombin and heparin. Br J Haematol 82:189–190 (Abstr.State of the art Symposia)

    Google Scholar 

  17. Olson ST, Shore JD (1982) Demonstration of a two-step reaction mechanism for inhibition of α-thrombin by antithrombin III and identification of the step affected by heparin. J Biol Chem 257:14891–14895

    Google Scholar 

  18. Zuazu-Jausoro I, Borrell M, Urrutia T, Oliver A, Monserrat I, Mateo J, Ribera L, Fontcuberta J (1990) Detection de complejos trombina-antitrombina-III en estados de hipercoagulabilidad. Sangre 35:375–380

    Google Scholar 

  19. Choay J, Petitou M, Lormeau JC, Sinay P, Casu BJ, Gatti G (1983) Structure-activity relationship in heparin: a synthetic pentasacharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity. Biochem Biophys Res Commun 116:492–499

    Google Scholar 

  20. Clouse LH, Comp PC (1986) The regulation of hemostasis: the protein C system. N Engl J Med 314:1298–1304

    Google Scholar 

  21. Stenflo J (1988) The biochemistry of protein C. In: Bertina RM (ed) Protein C and related proteins. Churchill Livingstone, Edinburgh London Melbourne New York, pp 21–54

    Google Scholar 

  22. Esmon CT (1989) The roles of protein C and thrombomodulin in the regulation of blood coagulation. J Biol Chem 264:4743–4746

    Google Scholar 

  23. Bajzár L, Fredenburgh JC, Nesheim M (1990) The activated protein C-mediated enhancement of tissue type plasminogen activatorinduced fibrinolysis in a cell-free system. J Biol Chem, 265: 16948–16954

    Google Scholar 

  24. Esmon NL, Owen WG, Esmon CT (1982) Isolation of a membranebound cofactor for thrombin-catalyzed activation of protein C. J Biol Chem, 257:859–864

    Google Scholar 

  25. Dittman WA, Majerus PW (1990) Structure and function of thrombomodulin: a natural anticoagulant. Blood 75:329–336

    Google Scholar 

  26. Dahlbäck B (1991) Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system. Thromb Haemost 66:49–61

    Google Scholar 

  27. Walker FJ (1988) Interactions of protein S with membranes. Sem Thromb Hemost 14:216–221

    Google Scholar 

  28. Harris KW, Esmon CT (1985) Protein S is required for bovine platelets to support activated protein C binding and activity. J Biol Chem. 260:2007–2010

    Google Scholar 

  29. Stern DM, Nawroth PP, Harris K, Esmon CT (1986) Cultured bovine aortic endothelial cells promote activated protein C-protein S-mediated inactivation of factor Va. J Biol Chem, 261:713–718

    Google Scholar 

  30. Solymoss S, Tucker MM, Tracy PB (1988) Kinetics of inactivation of membrane-bound factor Va by activated protein C. J Biol Chem 263:14884–14890

    Google Scholar 

  31. Gershagen S, Ferlund P, Lundvall A (1987) A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S. FEBS Lett 220:129–135

    Google Scholar 

  32. Bertina RM, van Wijngaarden A, Reinalda-Poot J, Poort SR, Bom VJJ (1985) Determination of plasma protein S. The protein cofactor of activated protein C. Thromb Haemost 53:268–272

    Google Scholar 

  33. Dahlbäck B (1986) Inhibition of protein Ca cofactor function of human and bovine protein S by C4b-binding protein. Biol Chem 261:12022–12027

    Google Scholar 

  34. Griffin JH, Gruber A, Fernández JA (1992) Reevaluation of total, free and bound protein S and C4b-binding protein levels in plasma anticoagulated with citrate or hirudin. Blood 79:3203–3211

    Google Scholar 

  35. Schwalbe R, Dahlbäck B, Hillarp A, Nelsestuen G (1990) Assembly of protein S and C4b-binding protein on membranes. J Biol Chem 265:16074–16081

    Google Scholar 

  36. Suzuki K, Deyashiki Y, Nishioka J, Toma K (1989) Protein C inhibitor: structure and function. Thromb Haemost 61:337–342

    Google Scholar 

  37. Heeb MJ, Griffin JH (1988) Physiologic inhibition of human activated protein C by alpha 1-antitrypsin. J Biol Chem 263:11613–11616

    Google Scholar 

  38. España F, Vicente V, Tabernero D, Scharrer I, Griffin JH (1990) Determination of plasma protein C inhibitor and of two activated protein C-inhibitor complexes in normals and in patients with intravascular coagulation and thrombotic disease. Thromb Res 59:593–608

    Google Scholar 

  39. España F, Gilabert J, Vicente V, Estellés A, Vázquez L, Hendl S, Aznar J (1992) Activated protein C: α1-antitrypsin (APC: α1AT) complex as a marker for in vitro diagnosis of prethrombotics states. Thromb Res 66:499–508

    Google Scholar 

  40. Esmon CT, Taylor FB Jr, Snow TR (1991) Inflammation and coagulation: linked processes potentialy regulated through a common pathway mediated by protein C. Thromb Haemost 66:160–165

    Google Scholar 

  41. Conway EM, Rosenberg RD (1988) Tumor necrosis factor supresses transcription of the thrombomodulin gene in endothelial cells. Mol Cell Biol 8:5588–5592

    Google Scholar 

  42. Moore K, Esmon CT, Esmon NL (1989) Tumor necrosis factor leads to the internalization and degradation of thrombomodulin from the surface of bovine aortic endothelial cells in culture. Blood 73:159–165

    Google Scholar 

  43. Oates AM, Salem HH (1991) The binding and regulation of protein S by neutrophils. Blood Coagul Fibrinolysis, 2:601–607

    Google Scholar 

  44. Taylor FB, Chang A, Esmon CT, D'Angelo A, Vigano-D'Angelo S, Blick KE (1987) Protein C prevents the coagulopathic and lethal effects ofEscherichia coli infusion in the baboon. J Clin Invest 79:918–925

    Google Scholar 

  45. Taylor F, Chang A, Ferrell G, Mather T, Catlett R, Blick K, Esmon CT (1991) C4b-binding protein exacerbates the host response toEscherichia coli. Blood 78:357–363

    Google Scholar 

  46. Rao LVM, Rapaport SI (1987) Studies of a mechanism inhibiting the initiation of the extrinsics pathway of coagulation. Blood 69:645–651

    Google Scholar 

  47. Broze GJ Jr, Warren LA, Novotny WF, Higuchi DA, Girard TJ, Miletich JP (1988) The lipoprotein associated coagulation inhibitor that inhibits factor VIIa-tissue factor complex also inhibits Xa: insight into its possible mechanism of action. Blood 71:335–343

    Google Scholar 

  48. Novotny WF, Girard TJ, Miletich JP, Broze GJ Jr (1988) Platelets secrete a coagulation inhibitor functionally and antigenically similar to the lipoprotein-associated coagulation inhibitor. Blood 72:2020–2025

    Google Scholar 

  49. Bajaj MS, Kuppuswamy MN, Saito H, Spitzer SG, Bajaj SP (1990) Cultured normal human hepatocytes do not synthesize lipoproteinassociated coagulation inhibitor. Evidence that endothelium is the principal site of its synthesis. Proc Natl Acad Sci USA 87:8869–8873

    Google Scholar 

  50. Sandset PM, Abildgaard U, Larsen ML (1988) Heparin induces release of extrinsic coagulation pathway inhibitor. Thromb Res50:803–813

    Google Scholar 

  51. Novotny WF, Girard TJ, Miletich JP, Broze GJ Jr (1989) Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma. J Biol Chem 264:18832–18837

    Google Scholar 

  52. Wun TC, Kretzmer KK, Girard TJ, Miletich JP, Broze GJ Jr (1988) Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains. J Biol Chem 263:6001–6004

    Google Scholar 

  53. Girard TJ, Warren LA, Novotny WF, Likert KM, Brown SG, Miletich JP, Broze GJ Jr (1989) Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature 338:518–520

    Google Scholar 

  54. Sandset PM, Warn-Cramer BJ, Rao LVM, Maki SL, Rapaport SI (1991) Depletion of extrinsic pathway inhibitor (EPI) sensitizes rabbits to disseminated intravascular coagulation induced with tissue factor: evidence supporting a physiologic role for EPI, as a natural anticoagulant. Proc Natl Acad Sci USA 88:708–712

    Google Scholar 

  55. Sandset PM, Warn-Cramer BJ, Maki SL, Rapaport SI (1991) Immunodepletion of extrinsic pathway inhibitor (EPI) sensitizes rabbits to endotoxin-induced intravascular coagulation and the generalized shwartzman reaction. Thromb Haemost 65:862 (Abstr 591)

    Google Scholar 

  56. Bock SC, Harris JF, Balazs I, Trent JM (1985) Assignment of the human antithrombin III structural gene to chromosome 1 q23–25. Cytogenet Cell Genet 39:67–69

    Google Scholar 

  57. Tollefsen DM, Majerus DW, Blank MK (1982) Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma. J Biol Chem 257:2162–2169

    Google Scholar 

  58. Blinder MA, Marasa JC, Reynolds CH, Deaven LL, Tollefse DM (1988) Heparin cofactor II: cDNA sequence, chromosome location, restriction fragment length polymorphism, and expression inEscherichia coli. Biochemistry 27:752–759

    Google Scholar 

  59. Kato A, Miura O, Sumi Y, Aoki N (1988) Assignment of the human protein C gene (PROC) to chromosome region 2q 14–q21 by in situ hibridization. Cytogenet Cell Genet 47:46–47

    Google Scholar 

  60. Watkins PC, Eddy R, Fukushima Y, Byers MG, Cohen EH, Dackowski WR, Wydro RM, Shows TB (1988) The gene for protein S maps near the centromere of human chromosome 3. Blood 71:238–241

    Google Scholar 

  61. Wen D, Dittman WA, Ye RD, Deaven LL, Majerus PW, Sadler JE (1987) Human thrombomodulin Complete cDNA sequence and chromosome localization of the gene. Biochemistry 26:4350–4357

    Google Scholar 

  62. McAlpine PJ, Stranc LC, Boucheix C, Shows TB (1990) The 1990 catalog of mapped genes and report of the nomenclature committee. Human gene mapping 10.5: update to the tenth International workshop on human gene mapping. Cytogenet Cell Genet 55:5–76

    Google Scholar 

  63. Carrell RW, Jeppsson JO, Laurell CB, Brennan SO, Owen MC, Vaughan L, Boswell DR (1982) Structure and variation of human α1-antitrypsin. Nature 298:329–334

    Google Scholar 

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Sala, N., Fontcuberta, J. & Rutllant, M.L. New biological concepts on coagulation inhibitors. Intensive Care Med 19 (Suppl 1), S3–S7 (1993). https://doi.org/10.1007/BF01738943

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