Fibrinspezifische thrombolytische Substanzen

  • D. Collen
Conference paper

Zusammenfassung

Das fibrinolytische System, welches schematisch in Abb. 3.1 dargestellt ist, enthält ein Proenzym, das Plasminogen, welches von verschiedenen Plasminogenaktivatoren in das aktive Enzym Plasmin umgewandelt werden kann. Eine Hemmung des fibrinolytischen Systems kann auf der Stufe der Plasminogenaktivatoren oder des Plasmins erfolgen. Definition und Nomenklatur der Komponenten des fibrinolytischen Systems sind aus Tabelle 3.1 ersichtlich.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literatur

  1. 1.
    Sottrup-Jensen L, Petersen TE, Magnusson S (1978) Atlas of protein sequence and structure. In: Dayhoff MO (ed), vol 5, suppl 3. National Biochemical Research Foundation, Washington D.C., p 91Google Scholar
  2. 2.
    Rabiner SF, Goldfine JD, Hart A, Summaria L, Robbins KC (1969) Radioimmunoassay of human plasminogen and plasmin. J Lab Clin Med 74:265–274PubMedGoogle Scholar
  3. 3.
    Friberger P, Knos M (1979) Plasminogen determination in human plasma. In: Scully MF, Kakkar W (eds) Chromogenic peptide substrates, Churchill Livingstone, Edinburgh, pp 128–140Google Scholar
  4. 4.
    Deutsch DG, Mertz ET (1970) Plasminogen: purification from human plasma by affinity chromatography. Science 170:1095–1096PubMedCrossRefGoogle Scholar
  5. 5.
    Robbins KC, Summaria L, Hsieh B, Shah RJ (1967) The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin. J Biol Chem 242:2333–2342PubMedGoogle Scholar
  6. 6.
    Groskopf WR, Summaria L, Robbins KC (1969) Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue. J Biol Chem 244:3590–3597PubMedGoogle Scholar
  7. 7.
    Wiman B, Wallen P (1973) Activation of human plasminogen by an insoluble derivative of urokinase. Structural changes of plasminogen in the course of activation to plasmin and demonstration of a possible intermediate compound. Eur J Biochem 36:25–31PubMedCrossRefGoogle Scholar
  8. 8.
    Holvoet P, Lijnen HR, Collen D (1985) A monoclonal antibody specific for lys-plasminogen. Application of the study of the activation pathways of plasminogen in vivo. J Biol Chem 260:12106–12111PubMedGoogle Scholar
  9. 9.
    Wohl RC, Sinio L, Summaria L, Robbins KC (1983) Comparative activation kinetics of mammalian plasminogen. Biochim Biophys Acta 745:20–31PubMedCrossRefGoogle Scholar
  10. 10.
    Christensen U, Müllertz S (1977) Kinetic studies on the urokinase catalyzed conversion of NH2-terminal lysine plasminogen to plasmin. Biochim Biophys Acta 480:275–281PubMedGoogle Scholar
  11. 11.
    Hoylaerts M, Rijken DC, Lijnen HR, Collen D (1982) Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 257:2912–2919PubMedGoogle Scholar
  12. 12.
    Ranby M (1982) Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim Biophys Acta 704:461–469PubMedCrossRefGoogle Scholar
  13. 13.
    Zamarron C, Lijnen HR, Collen D (1984) Kinetics of the activation of plasminogen by natural and recombinant tissue-type plasminogen activator. J Biol Chem 259:2080–2083PubMedGoogle Scholar
  14. 14.
    Nieuwenhuizen W, Voskuilen M, Vermond A, Hoegee B, Traas DW, Verheijen JH (1984) Kinetics of plasminogen activation by t-PA; the role of fibrinogen fragments. Haemostasis 14:71Google Scholar
  15. 15.
    Suenson E, Lützen O, Thorsen S (1984) Initial plasmin-degradation of fibrin as the basis of a positive feedback mechanism in fibrinolysis. Eur J Biochem 140:513–522PubMedCrossRefGoogle Scholar
  16. 16.
    Ranby M, Bergsdorf N, Norrman B, Suenson E, Wallen P (1983) Tissue plasminogen activator kinetics. In: Davidson JF, Bachman F, Bouvier CA, Kruithof EKO (eds) Progress in fibrinolysis vol 6, Churchill Livingstone, Edinburgh, pp 182–184Google Scholar
  17. 17.
    Rijken DC, Hoylaerts M, Collen D (1982) Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator. J Biol Chem 257:2920–2925PubMedGoogle Scholar
  18. 18.
    Gurewich V, Pannell R, Louie S, Kelley P, Suddith RL, Greenlee R (1984) Effective and fibrin-speciflc clot lysis by a zymogen precursor form of urokinase (pro-UK). A study in vitro and in two animal species. J Clin Invest 73:1731–1739PubMedCrossRefGoogle Scholar
  19. 19.
    Lijnen HR, Zamarron C, Blaber M, Winkler ME, Collen D (1986) Activation of plasminogen by pro-urokinase. I. Mechanism. J Biol Chem 261:1253–1258Google Scholar
  20. 20.
    Collen D, Zamarron C, Lijnen HR, Hoylaerts M (1986) Activation of plasminogen by prourokinase. II. Kinetics. J Biol Chem 261:1259–1266Google Scholar
  21. 21.
    Alkjaersig N (1964) The purification and properties of human plasminogen. Biochem J 93:171–182PubMedGoogle Scholar
  22. 22.
    Hoylaerts M, Lijnen HR, Collen D (1981) Studies on the mechanism of the antifibrinolytic action of tranexamic acid. Biochim Biophys Acta 673:75–85PubMedGoogle Scholar
  23. 23.
    Rickli EE, Otavsky WI (1975) A new method of isolation and some properties of heavy chain of human plasmin. Eur J Biochem 9:441–447CrossRefGoogle Scholar
  24. 24.
    Wiman B, Lijnen HR, Collen D (1979) On the specific interaction between the lysine-binding sites in plasmin and complementary sites in a2-antiplasmin and in fibrinogen. Biochim Biophys Acta 579:142–159PubMedGoogle Scholar
  25. 25.
    Thorsen S (1975) Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-amino-carboxylic acids. Biochim Biophys Acta 393:55–65PubMedGoogle Scholar
  26. 26.
    Rakoczi I, Wiman B, Collen D (1978) On the biological significance of the specific interaction between fibrin, plasminogen and antiplasmin. Biochim Biophys Acta 540:295–300PubMedGoogle Scholar
  27. 27.
    Wiman B, Collen D (1978) Molecular mechanism of physiological fibrinolysis. Nature (Lond) 272:549–550CrossRefGoogle Scholar
  28. 28.
    Ratnoff OD (1977) The surface-mediated initiation of blood coagulation and related phenomena. In: Ogston D, Bennett B (eds) Haemostasis: Biochemistry, physiology and pathology. Wiley, London, pp 25–55Google Scholar
  29. 29.
    White WF, Barlow GH, Mozen MM (1966) The isolation and characterization of plasminogen activators (urokinase) from human urine. Biochemistry 5:2160–2169PubMedCrossRefGoogle Scholar
  30. 30.
    Günzler WA, Steffens GJ, Otting F, Buse G, Flohe L (1982) Structural relationship between human high and low molecular mass urokinase. Hoppe Seylers Z Physiol Chem 363:133–141PubMedCrossRefGoogle Scholar
  31. 31.
    Günzler WA, Steffens GJ, Otting F, Kim SMA, Frankus E, Flohe L (1982) The primary, structure of high molecular mass urokinase from human urine. Hoppe-Seylers Z Physiol Chem 363:1155–1165PubMedCrossRefGoogle Scholar
  32. 32.
    Heyneker HL, Holmes WE, Vehar GA (1983) Preparation of functional human urokinase proteins. European Patent Application Nr. 83103629.8, Publication Nr.0092182A2, European Patent Office, MünchenGoogle Scholar
  33. 33.
    Holmes WE, Pennica D, Blaber H, Rey MW, Günzler AW, Steffens FJ, Heyneker HL (1985) Cloning and expression of the gene for pro-urokinase in Escherichia coli. Biotechnology 3:923–929CrossRefGoogle Scholar
  34. 34.
    Yerstraete M (1980) A far-reaching program: rapid, safe and predictable thrombolysis in man. In: Kline DL, Reddy NN (eds) Fibrinolysis. CRC Press, Boca Raton/Florida pp 129— 149Google Scholar
  35. 35.
    Müllertz S, Lassen M (1953) An activator system in blood indispensable for the formation of plasmin by streptokinase. Proc Soc Exp Biol Med 82:264–268PubMedGoogle Scholar
  36. 36.
    Kosow DP (1975) Kinetic mechanism of the activation of human plasminogen by streptokinase. Biochemistry 14:4459–4465PubMedCrossRefGoogle Scholar
  37. 37.
    Gonzales-Gronow M, Siefring GE Jr, Castellino FJ (1978) Mechanism of activation of human plasminogen by the activator complex, streptokinase-plasmin. J Biol Chem 253:1090–1094Google Scholar
  38. 38.
    Pennica D, Holmes WE, Kohr WJ et al. (1983) Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature (Lond) 301:214–221CrossRefGoogle Scholar
  39. 39.
    Rijken DC, Collen D (1981) Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J Biol Chem 256:7035–7041PubMedGoogle Scholar
  40. 40.
    Banyai L, Varadi A, Patthy L (1983) Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator. FEBS Lett 163:37–41PubMedCrossRefGoogle Scholar
  41. 41.
    Ny T, Backman A, Elgh F, Enquist K, Fredrikson C, Jarvinen S (1984) Isolation and characterization of the genomic region carrying the human tissue plasminogen activator gene. Haemostasis 14:56 (abstr)Google Scholar
  42. 42.
    Ranby M, Bergsdorf N, Nilsson T (1982) Enzymatic properties of one-chain and two-chain forms of tissue plasminogen activator. Thromb Res 27:175–183PubMedCrossRefGoogle Scholar
  43. 43.
    Loskutoff DJ, Edgington T (1977) Synthesis of a fibrinolytic activator and inhibitor by endothelial cells. Proc Natl Acad Sci USA 74:3903–3907PubMedCrossRefGoogle Scholar
  44. 44.
    Levin EG, Loskutoff DJ (1983) Cultured bovine endothelial cells produce both urokinase and tissue-type plasminogen activators. J Cell Biol 94:631–636CrossRefGoogle Scholar
  45. 45.
    Rijken DC, Wijngaards G, Welbergen J (1980) Relationship between tissue plasminogen activator and the activators in blood and vascular wall. Thromb Res 18:815–830PubMedCrossRefGoogle Scholar
  46. 46.
    Loskutoff DJ, van Mourik JA, Erickson LA, Lawrence D (1984) Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells. Proc Natl Acad Sci 80:2956–2960CrossRefGoogle Scholar
  47. 47.
    Christensen U, Holmberg L, Bladh B, Astedt B (1982) Kinetics between urokinase and an inhibitor of fibrinolysis from placental tissue. Thromb Haemost 48:24–26PubMedGoogle Scholar
  48. 48.
    Kruithof EK, Ransijn A, Bachman F (1983) Inhibition of tissue plasminogen activator by human plasma. In: Davidson JF, Bachmann F, Bouvier CA, Kruithof EKO (eds) Progress in fibrinolysis, vol VI. Churchill Livingstone, Edinburgh, pp 362–366Google Scholar
  49. 49.
    Chmielewska J, Ranby M, Wiman B (1983) Evidence for a rapid inhibitor to tissue plasminogen activator in plasma. Thromb Res 31:427–436PubMedCrossRefGoogle Scholar
  50. 50.
    Juhan-Vague I, Moerman B, De Cock F, Aillaud MF, Collen D (1984) Plasma levels of a specific inhibitor of tissue-type plasminogen activator (and urokinase) in normal and pathological conditions. Thromb Res 33:523–530PubMedCrossRefGoogle Scholar
  51. 51.
    Korninger C, Stassen JM, Collen D (1981) Turnover of human extrinsic (tissue-type) plasminogen activator in rabbits. Thromb Haemost 46:658–661PubMedGoogle Scholar
  52. 52.
    Holvoet P, Lijnen HR, Collen D (1986) Characterization of functional domains in human tissue-type plasminogen activator with the use of monoclonal antibodies. Eur J Biochem 158:173–177PubMedCrossRefGoogle Scholar
  53. 53.
    Bernik MB (1973) Increased plasminogen activator (urokinase) in tissue culture after fibrin deposition. J Clin Invest 52:823–834PubMedCrossRefGoogle Scholar
  54. 54.
    Nolan C, Hall L, Barlow G, Tribby HE (1977) Plasminogen activator from human embryonic kidnex cell cultures. Evidence for a proactivator. Biochim Biophys Acta 496–384-400PubMedGoogle Scholar
  55. 55.
    Husain S, Gurewich V, Lipinski B (1983) Purification and partial characterization of a single-chain high-molecular-weight form of urokinase from human urine. Arch Biochim Biophys 220:31–38CrossRefGoogle Scholar
  56. 56.
    Stump DC, Thienpont M, Collen D (1986) Urokinase-related proteins in human urine. Isolation and characterization of single-chain urokinase (pro-urokinase) and urokinase-inhibitor complex. J Biol Chem 261:1267–1273PubMedGoogle Scholar
  57. 57.
    Wun TC, Schleuning WD, Reich E (1982) Isolation and characterization of urokinase from human plasma. J Biol Chem 257:3276–3283PubMedGoogle Scholar
  58. 58.
    Sumi H, Maruyama M, Matsuo O, Mihara H, Toki N (1982) Higher fibrin-binding and thrombolytic properties of single polypeptide chain-high molecular weight urokinase. Thromb Haemost 47:297PubMedGoogle Scholar
  59. 59.
    Kohno T, Hopper P, Lillquist JS, Suddith RL, Greenlee R, Moir DT (1984) Kidney plasminogen activator: a precursor form of human urokinase with high fibrin affinity. Biotechnology 2:628–635CrossRefGoogle Scholar
  60. 60.
    Kasai S, Arimura H, Nishida M, Suyama T (1985) Proteolytic cleavage of single-chain prourokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin. J Biol Chem 260:12377–12381PubMedGoogle Scholar
  61. 61.
    Stump DC, Lijnen HR, Collen D (1986) Purification and characterization of single-chain urokinase-type plasminogen activator (scu-PA) from human cell cultures. J Biol Chem 261:1274–1278PubMedGoogle Scholar
  62. 62.
    Stump DC, Lijnen HR, Collen D (1986) Purification and characterization of a novel low molecular weight form of single chain urokinase-type plasminogen activator. J Biol Chem 261:17120–17126PubMedGoogle Scholar
  63. 63.
    Lijnen HR, Zamarron C, Collen D (1985) Characterization of the high-affinity interaction between human plasminogen and pro-urokinase. Eur J Biochem 150:141–144PubMedCrossRefGoogle Scholar
  64. 64.
    Zamarron C, Lijnen HR, van Hoef B, Collen D (1984) Biological and thrombolytic properties of proenzyme and active forms of urokinase. I. Fibrinolytic and flbrinogenolytic properties in human plasma in vitro of urokinases obtained from human urine or by recombinant DNA technology. Thromb Haemost 52:19–23PubMedGoogle Scholar
  65. 65.
    Norman PS (1958) Studies of the plasmin system. II. Inhibition of plasmin by serum or plasma. J Exp Med 108:53–68PubMedCrossRefGoogle Scholar
  66. 66.
    Schwick HG, Heimburger N, Haut H (1966) Antiproteasen des Humanserums. Z Inn Med 21:1–6Google Scholar
  67. 67.
    Collen D (1976) Identification and some properties of a new fast-reacting plasmin inhibitor in human plasma. Eur J Biochem 69:209–216PubMedCrossRefGoogle Scholar
  68. 68.
    Moroi M, Aoki N (1976) Isolation and characterization of a2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J Biol Chem 251:5956–5965PubMedGoogle Scholar
  69. 69.
    Mullertz S, Clemmensen I (1976) The primary inhibitor of plasmin in human plasma. Biochem J 159:545–553PubMedGoogle Scholar
  70. 70.
    Bagge L, Bjork I, Saldeen T, Wallin R (1976) Purification and characterization of an inhibitor of plasminogen activation from posttraumatic patients. Forensic Sci 7:83–86CrossRefGoogle Scholar
  71. 71.
    Holmes WE, Nelles L, Lijnen HR, Collen D (1987) Primary structure of human a2-antiplasmin, a serine protease inhibitor (serpin). J Biol Chem 262:1659–1664PubMedGoogle Scholar
  72. 72.
    Wiman B, Collen D (1977) Purification and characterization of human antiplasmin, the fastacting plasmin inhibitor in plasma. Eur J Biochem 78:19–26PubMedCrossRefGoogle Scholar
  73. 73.
    Edy J, De Cock F, Collen D (1976) Inhibition of plasmin by normal and antiplasmindepleted human plasma. Thromb Res 8:513–518PubMedCrossRefGoogle Scholar
  74. 74.
    Christensen U, Clemmensen I (1978) Purification and reaction mechanisms of the primary inhibitor of plasmin from human plasma. Biochem J 175:635–641PubMedGoogle Scholar
  75. 75.
    Christensen U, Clemmensen I (1977) Kinetic properties of the primary inhibitor of plasmin from human plasma. Biochem J 163:389–391PubMedGoogle Scholar
  76. 76.
    Wiman B, Collen D (1978) On the kinetics of the reaction between human antiplasmin and plasmin. Eur J Biochem 84:573–578PubMedCrossRefGoogle Scholar
  77. 77.
    Wiman B, Boman L, Collen D (1978) On the kinetics of the reaction between human antiplasmin and a low-molecular-weight form of plasmin. Eur J Biochem 87:143–146PubMedCrossRefGoogle Scholar
  78. 78.
    Verheijen JH, Chang GIC, Kluft C (1984) Evidence for the occurrence of a fast-acting inhibitor for tissue-type plasminogen activator in human plasma. Thromb Haemost 51:392–395PubMedGoogle Scholar
  79. 79.
    Wijngaards G, Groeneveld E (1982) Temporarily increased inhibition by plasma of plasminogen activator activity in severely ill patients. Haemostasis 12:571 (abstr 188)Google Scholar
  80. 80.
    Erickson LA, Ginsberg MH, Loskutoff DJ (1984) Detection and partial characterization of an inhibitor of plasminogen activator in human platelets. J Clin Invest 74:1465–1472PubMedCrossRefGoogle Scholar
  81. 81.
    Astedt B, Lecander I, Brodin T, Lundblad A, Low K (1985) Purification of a specific placental plasminogen activator inhibitor by monoclonal antibody and its complex formation with plasminogen activator. Thromb Haemost 53:122PubMedGoogle Scholar
  82. 82.
    Collen D, Bounameaux H, De Cock F, Lijnen HR, Verstraete M (1986) Analysis of coagulation and fibrinolysis during intravenous infusion of recombinant human tissue-type plasminogen activator (t-PA) in patients with acute myocardial infarction. Circulation 73:511— 517PubMedCrossRefGoogle Scholar
  83. 83.
    Holvoet P, Lijnen HR, Collen D (1986) A monoclonal antibody preventing binding of tissue-type plasminogen activator (t-PA) to fibrin, useful to monitor fibrinogen breakdown during t-PA infusion. Blood 67:1482–1487PubMedGoogle Scholar
  84. 84.
    Van de Werf F, Nobuhara M, Collen D (1986) Coronary thrombolysis with human single chain urokinase-type plasminogen activator (scu-PA) in patients with acute myocardial infarction. Ann Int Med 104:345–348PubMedGoogle Scholar
  85. 85.
    Van de Werf F, Vanhaecke J, de Geest H, Verstraete M, Collen D (1986) Coronary thrombolysis with recombinant single chain urokinase-type plasminogen activator (rscu-PA) in patients with acute myocardial infarction. Circulation 74:1066–1070PubMedCrossRefGoogle Scholar
  86. 86.
    Collen D, De Cock F, Demarsin E, Lijnen HR, Stump DC (1986) Absence of synergism between tissue-type plasminogen activator (t-PA), single chain urokinase-type plasminogen activator (scu-PA) and urokinase on clot lysis in a plasma milieu in vitro. Thromb Haemost 56:35–39PubMedGoogle Scholar
  87. 87.
    Collen D, Stassen JM, Stump DC, Verstraete M (1986) In vivo synergism of thrombolytic agents. Circulation 74:35–39CrossRefGoogle Scholar
  88. 88.
    Collen D, Stump DC, van de Werf F (1986) Coronary thrombolysis in patients with acute myocardial infarction by intravenous infusion of synergic thrombolytic agents. Am Heart J 112:1083–1084PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • D. Collen

There are no affiliations available

Personalised recommendations