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Thromb Haemost 1980; 43(02): 077-089
DOI: 10.1055/s-0038-1650023
DOI: 10.1055/s-0038-1650023
Original Article
On the Regulation and Control of Fibrinolysis[*]
Edward Kowalski Memorial LectureFurther Information
Publication History
Publication Date:
13 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198001/lookinside/thumbnails/10-1055-s-0038-1650023-1.jpg)
* Presented at VIIth International Congress on Thrombosis and Haemostasis, London, July 15-20, 1979
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References
- 1 Morgagni JB. In: "The seats and causes of diseases",. 1769; vol: 3 book 4, London, p. 173 Cited by Fearnley G R (ref 8)
- 2 Hunter J. In: "A treatise on blood, inflammation and gunshot wounds". 1794 J. Richardson for G. Nicol, London, p. 26. Cited by Fearnley GR (ref 8)
- 3 Morawitz P. Beitr Chem Physiol Pathol 8, 1. Cited by Fearnley G R (ref 8)
- 4 Macfarlane RG. Fibrinolysis following operation. Lancet I 1937 10-12. Cited by Fearnley G R (ref 8)
- 5 Denys J, de Marbaix H. La Cellule. Adv Drug Res 1889; 5: 197 Cited by Fearnley G R (ref 8)
- 6 Tillett WS, Garner RL. Fibrinolytic activity of hemolytic streptococci. J Exper Med 1933; 58: 485-502
- 7 Astrup T. Fibrinolysis in the organism. Blood 1956; 11: 781-806
- 8 Fearnley GR. Fibrinolysis. Adv Drug Res 1973; 7: 107-163
- 9 Milstone H. Factor in normal blood which participates in streptococcal fibrinolysis. J Immunol 1941; 42: 109-116
- 10 Kaplan MH. Nature and role of the lytic factor in hemolytic streptococcal fibrinolysis. Proc Soc Exper Biol Med 1944; 57: 40-43
- 11 Christensen LR. Streptococcal fibrinolysis: proteolytic reaction due to serum enzyme activated by streptococcal fibrinolysin. J Gen Physiol 1945; 28: 363-383
- 12 Christensen LR, Macleod CM. Proteolytic enzyme of serum: characterization, activation, and reaction with inhibitors. J Gen Physiol 1945; 28: 559-583
- 13 Astrup T, Permin PM. Fibrinolysis in animal organism. Nature 1947; 159: 681-682
- 14 Macfarlane RG, Pilling J. Fibrinolytic activity of normal urine. Nature 1947; 159: 779
- 15 Williams JR B. The fibrinolytic activity of urine. Brit J Exper Pathol 1951; 32: 530-537
- 16 Mullertz S. Plasminogen activator in spontaneously active human blood. Proc Soc Exper Biol Med 1953; 82: 291-295
- 17 Wallen P. Activation of plasminogen with urokinase and tissue activator. In: "Thrombosis and urokinase". Paoletti R, Sherry S. Academic Press, London: 1977. p 91-102
- 18 Thorsen S. Human urokinase and porcine tissue plasminogen activator. Thesis, University of Copenhagen, Laegeforeningens Forlag, Copenhagen 1977
- 19 Rijken DC, Wijngaards G, Zaal-de Jong M, Welbergen J. Purification and partial characterization of plasminogen activator from human uterine tissue. Biochim Biophys Acta 1979; 580: 140-153
- 20 Cash JD. A new approach to the studies of the fibrinolytic enzyme system in man. Amer Heart J 1968; 75: 424-428
- 21 Chakrabarti R, Fearnley GR, Hocking ED, Delitheos A, Clarke GM. Fibrinolytic activity related to age in survivors of myocardial infarction. Lancet 1966; I: 573-574
- 22 Pandolfi M, Isacson S, Nilsson IM. Low fibrinolytic activity in the walls of veins of patients with thrombosis. Acta Med Scand 1969; 186: 1-5
- 23 Rosing DR, Redwood DR, Brakman P, Astrup T. Impairment of the diurnal fibrinolytic response in man. Effects of aging, type IV hyperlipoproteinemia, and coronary artery disease. Circ Res 1973; 32: 752-758
- 24 Peabody RA, Tsapogas MJ, Wu KT. Altered endogenous fibrinolysis and biochemical factors in atherosclerosis. Arch Surg 1974; 109: 309-313
- 25 Pilgeram LO. Abnormalities in clotting and thrombolysis as a risk factor for stroke. Thromb Diath haemorrh 1974; 31: 245-264
- 26 Clayton JK, Anderson JA, McNicol GP. Preoperative prediction of postoperative deep vein thrombosis. Br Med J 1976; 2: 910-912
- 27 Niewiarowski S, Prou-Wartelle O. Role of the contact factor (Hageman factor) in fibrinolysis. Thromb Diath haemorrh 1959; 3: 593-603
- 28 Ogston D, Ogston CM, Ratnoff OD, Forbes CD. Studies on a complex mechanism for the activation of plasminogen by kaolin and by chloroform: the participation of Hageman factor and additional cofactors. J Clin Invest 1969; 48: 1786-1801
- 29 Griffin JH. New hypothesis for the molecular mechanism of surface-dependent activation of Hageman factor (factor XII). Thromb Haemost 1977; 38: 50 (Abstr.)
- 30 Griffin JH. Role of surface in surface-dependent activation of Hageman factor (blood coagulation factor XII). Proc Natl Acad Sci 1978; 75: 1998-2002
- 31 Kaplan AP, Castellino FJ, Collen D, Wiman B, Taylor FB. Molecular mechanisms of fibrinolysis in man. Thromb Haemost 1978; 39: 263-283
- 32 Kluft C. An inventory of plasminogen activators in human plasma. Thromb Haemost 1978; 38: 134
- 33 Hedner U, Nilsson IM. Acquired anticoagulants against factors XI and XII in patients with severe thrombotic disease. 16th Internat Congr of Haematology Kyoto, Japan 1976 (Abstract no 8-88) p 341
- 34 Kluft C. Elimination of inhibition in euglobulin fibrinolysis by use of flufenamate: involvement of C1-inactivator. Haemostasis 1977; 6: 351-369
- 35 Hedner U. Studies on an inhibitor of plasminogen activation in human serum. Thromb Diath haemorrh 1973; 30: 414-424
- 36 Hedner U, Martinsson G. Inhibition of activated Hageman factor (factor XIIa) by an inhibitor of plasminogen activation (PA-inhibitor). Thromb Res 1978; 12: 1015-1023
- 37 Stead N, Kaplan AP, Rosenberg RD. Inhibition of activated factor XII by antithrombin-heparin cofactor. J Biol Chem 1976; 251: 6481-6488
- 38 McConnell DJ. Inhibitors of kallikrein in human plasma. J Clin Invest 1972; 51: 1611-1623
- 39 Müllertz S. Mechanism of activation and effect of plasmin in blood. Ph D Thesis, Eijnar Munksgaard, Copenhagen 1956
- 40 Gurewich V, Hyde E, Lipinski B. The resistance of fibrinogen and soluble fibrin monomer in blood to degradation by a potent plasminogen activator from cadaver limbs. Blood 1975; 46: 555-565
- 41 Collen D. α2-Antiplasmin inhibitor deficiency. Lancet 1979; I: 1039-1040
- 42 Collen D. Identification and some properties of a new fast-reacting plasmin inhibitor in human plasma. Eur J Biochem 1976; 69: 209-216
- 43 Moroi M, Aoki N. Isolation and characterization of alpha 2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J Biol Chem 1976; 251: 5956-5965
- 44 Müllertz S, Clemmensen I. The primary inhibitor of plasmin in human plasma. Biochem J 1976; 159: 545-553
- 45 Hedner U, Abildgaard U. Report on the joint Meeting of the task forces on nomenclature and standards of inhibitors of coagulation and fibrinolysis. Thromb Haemostas 1978; 39: 524-525
- 46 Bagge L, Björk I, Saldeen T, Wallin R. Purification and characterization of an inhibitor of plasminogen activation from posttraumatic patients. Forensic Sci 1976; 7: 83-86
- 47 Müllertz S. Different molecular forms of plasminogen and plasmin produced by urokinase in human plasma and their relation to protease inhibitors and lysis of fibrinogen and fibrin. Biochem J 1974; 143: 273-283
- 48 Nilehn J-E, Ganrot PO. Plasmin, plasmin inhibitors and degradation products of fibrinogen in human serum during and after intravenous infusion of streptokinase. Scand J Clin Lab Invest 1967; 20: 113-121
- 49 Collen D, Wiman B. Fast-acting plasmin inhibitor in human plasma. Blood 1978; 51: 563-569
- 50 Astrup T. Fibrinolysis – An overview. In: "Progress in chemical fibrinolysis and thrombolysis, vol 3". Davidson JF, Rowan RM, Samama MM, Desnoyers PC. Raven Press, New York: 1978. p 1-57
- 51 Reich E. Plasminogen activator: secretion by neoplastic cells and macrophages. In: "Proteases and biological control". Reich E, Rifkin DB, Shaw E. eds) Cold Spring Harbor Laboratory: 1975. p 333-341
- 52 Strickland S. Studies on the role of plasminogen activator in ovulation and early embryogenesis. In: "Regulatory proteolytic enzymes and their inhibitors". Magnusson S, Ottesen M, Foltman B, Danø K, Neurath H. eds) Pergamon Press, Oxford: 1978. p. 181-185
- 53 Sottrup-Jensen L, Claeys H, Zajdel M, Petersen TE, Magnusson S. The primary structure of human plasminogen: isolation of two lysine-binding fragments and one "mini"-plasminogen (M. W. 38,000) by elastase-catalyzed-specific limited proteolysis. In: "Progress in chemical fibrinolysis and thrombolysis, vol 3". Davidson JF, Rowan RM, Samama MM, Desnoyers PC. eds) Raven Press, New York: 1978. p 191-209
- 54 Sottrup-Jensen L, Petersen TE, Magnusson S. In: "Atlas of protein sequence and structure". 1978 Vol 5. suppl 3, p 91
- 55 Wiman B. Biochemistry of the plasminogen to plasmin conversion. In: "Fibrinolysis. Current fundamental and clinical aspects". Gaffney PJ, Balkuv-Ulutin S. eds) Academic Press, London: 1978. p 47-60
- 56 Wallen P, Wiman B. Characterization of human plasminogen. I. On the relationship between different molecular forms of plasminogen demonstrated in plasma and found in purified preparations. Biochim Biophys Acta 1970; 221: 20-30
- 57 Wallén P, Wiman B. Characterization of human plasminogen. II. Separation and partial characterization of different molecular forms of human plasminogen. Biochim Biophys Acta 1972; 257: 122-134
- 58 Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science 1970; 170: 1095-1096
- 59 Brockway WJ, Castellino FJ. Measurement of the binding of antifibrinolytic amino acids to various plasminogens. Arch Biochem Biophys 1972; 151: 194-199
- 60 Collen D, De Maeyer L. Molecular biology of human plasminogen. I. Physicochemical properties and microheterogeneity. Thromb Diath haemorrh 1975; 34: 396-402
- 61 Castellino FJ, Siefring Jr GE, Sodetz IM, Bretthauer RK. Amino terminal amino acid sequences and carbohydrate of the two major forms of rabbit plasminogen. Biochem Biophys Res Commun 1973; 53: 845-851
- 62 Summaria L, Arzadon L, Bernabe P, Robbins KC. Studies on the isolation of the multiple molecular forms of human plasminogen and plasmin by isoelectric focusing methods. J Biol Chem 1972; 247: 4691-4702
- 63 Collen D. Plasminogen and prothrombin metabolism in man. Thesis, University of Leuven, Belgium 1974
- 64 Collen D, Verstraete M. Molecular biology of human plasminogen. II. Metabolism in physiological and some pathological conditions in man. Thromb Diath haemorrh 1975; 34: 403-408
- 65 Robbins KC, Summaria L, Hsieh B, Shah RJ. The peptide chains of human plasmin. Mechanism of activation of human plasminogen to plasmin. J Biol Chem 1967; 242: 2333-2342
- 66 Groskopf WR, Summaria L, Robbins KC. Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue. J Biol Chem 1969; 244: 3590-3597
- 67 Claeys H, Vermylen J. Physico-chemical and proenzyme properties of NH2-terminal glutamic acid and NH2-terminal lysine human plasminogen. Influence of 6-aminohexanoic acid. Biochim Biophys Acta 1974; 342: 351-359
- 68 Wallen P, Wiman B. On the generation of intermediate plasminogen and its significance for activation. In: "Proteases and biological control". Reich E, Rifkin DB, Shaw E. eds) Cold Spring Harbor Laboratory: p 291-303
- 69 Thorsen S, Kok P, Astrup T. Reversible and irreversible alterations of human plasminogen indicated by changes in susceptibility to plasminogen activators and in response to epsilon-aminocaproic acid. Thromb Diath haemorrh 1974; 32: 325-340
- 70 Rickli EE, Otavsky WI. Release of an N-terminal peptide from human plasminogen during activation with urokinase. Biochim Biophys Acta 1973; 295: 381-384
- 71 Wiman B, Wallen P. 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 1973; 36: 25-31
- 72 Summaria L, Arzadon L, Bernabe P, Robbins KC. The activation of plasminogen to plasmin by urokinase in the presence of the plasmin inhibitor trasylol. The preparation of plasmin with the same NH2-terminal heavy (A) chain sequence as the parent zymogen. J Biol Chem 1975; 250: 3988-3995
- 73 Violand BN, Castellino FJ. Mechanism of the urokinase-catalyzed activation of human plasminogen. J Biol Chem 1976; 251: 3906-3912
- 74 Wiman B, Collen D. On the mechanism of the reaction between human a2-antiplasmin and plasmin. J Biol Chem 1979 (in press)
- 75 Thorsen S, Müllertz S. Reaction sequences and the mechanism of plasminogen activation in urokinase-activated plasma. Effects of fibrin and 6-aminohexanoic acid. In: "Progress in chemical fibrinolysis and thrombolysis 1979 Vol: 4" (in press)
- 76 Christensen U. Kinetic studies of the urokinase-catalysed conversion of NH2-terminal glutamic acid plasminogen to plasmin. Biochim Biophys Acta 1977; 481: 638-647
- 77 Wohl RC, Summaria L, Arzadon L, Robbins KC. Steady state kinetics of activation of human and bovine plasminogens by streptokinase and its equimolar complexes with various activated forms of human plasminogen. J Biol Chem 1978; 253: 1402-1407
- 78 Camiolo SM, Thorsen S, Astrup T. Fibrinogenolysis and fibrinolysis with tissue plasminogen activator, urokinase, streptokinase-activated human globulin, and plasmin. Proc Soc Exper Biol Med 1971; 138: 277-280
- 79 Markus G, De Pasquale JL, Wissler FC. Quantitative determination of the binding of epsilon-aminocaproic acid to native plasminogen. J Biol Chem 1978; 253: 727-732
- 80 Rickli EE, Otavsky WI. A new method of isolation and some properties of heavy chain of human plasmin. Eur J Biochem 1975; 9: 441-447
- 81 Thorsen S. Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-amino-carboxylic acids. Biochim Biophys Acta 1975; 393: 55-65
- 82 Rakoczi I, Wiman B, Collen D. On the biological significance of the specific interaction between fibrin, plasminogen and antiplasmin. Biochim Biophys Acta 1978; 540: 295-300
- 83 Wiman B, Wallen P. Structural relationship between "glutamic acid" and "lysine" forms of human plasminogen and their interaction with the NH2-terminal activation peptide as studied by affinity chromatography. Eur J Biochem 1975; 50: 489-494
- 84 Wiman B, Wallén P. The specific interaction between plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen. Thromb Res 1977; 10: 213-222
- 85 Ratnoff OD. The surface-mediated initiation of blood coagulation and related phenomena. In: "Haemostasis: biochemistry, physiology and pathology". Ogston D, Bennett B. eds) John Wiley & Sons, London: 1977. p 25-55
- 86 Ogston D, Bennett B. Surface-mediated reactions in the formation of thrombin, plasmin and kallikrein. Br Med Bull 1978; 34: 107-112
- 87 Astrup T. Tissue activators of plasminogen. Fed Proc 1966; 25: 42-51
- 88 Cole ER, Bachmann FW. Purification and properties of a plasminogen activator from pig heart. J Biol Chem 1977; 252: 3729-3737
- 89 Wallen P, Kok P, Rånby M. The tissue activator of plasminogen. In: "Regulatory enzymes and their control". Magnusson S, Ottesen M, Foltman B, Danø K, Neurath H. eds) Pergamon Press, Oxford: 1978. p 127-135
- 90 Rickli EE, Zaugg G. Isolation and purification of highly enriched tissue plasminogen activator from pig heart. Thromb Diath haemorrh 1970; 23: 64-76
- 91 Kok P, Astrup T. Isolation and purification of a tissue plasminogen activator and its comparison with urokinase. Biochemistry 1969; 8: 79-86
- 92 Aoki N, von Kaulla KN. The extraction of vascular plasminogen activator from human cadavers and a description of some of its properties. Am J Clin Pathol 1971; 55: 171-179
- 93 Pepper DS, Allen R. Isolation and characterization of human cadaver vascular endothelial activator. In: "Progress in chemical fibrinolysis and thrombolysis 1978 Vol 3". Davidson JF, Rowan RM, Samama MM, Desnoyers PC. eds) Raven Press, New York: p 91-98
- 94 Radcliffe R, Heinze T. Isolation of plasminogen activator from human plasma by chromatography on lysine-Sepharose. Arch Biochem Biophys 1978; 189: 185-194
- 95 Fletcher AP, Biederman O, Moore D, Alkjaersig N, Sherry S. Abnormal plasminogen-plasmin system activity (fibrinolysis) in patients with hepatic cirrhosis: its cause and consequences. J Clin Invest 1964; 43: 681-695
- 96 Tytgat G, Collen D, De Vreker RA. Investigations on the fibrinolytic system in liver cirrhosis. Acta Haematol 1968; 40: 265-274
- 97 Fletcher AP, Alkjaersig N, Sherry S, Genton E, Hirsh J, Bachmann F. The development of urokinase as a thrombolytic agent. Maintenance of a sustained thrombolytic state in man by its intravenous infusion. J Lab Clin Med. 1965; 65: 713-731
- 98 Kakkar VV, Scully MF. Thrombolytic therapy. Br Med Bull 1978; 34: 191-199
- 99 Paoletti R, Sherry S. (eds) Thrombosis and urokinase. Academic Press, London: 1977
- 100 Verstraete M. A far stretched program: rapid, safe and predictable thrombolysis in man. In: "Fibrinolysis". Kline DL, Reddy NN. eds) CRC Press, Cleveland: 1979. (in press)
- 101 Mullertz S, Lassen M. An activator system in blood indispensable for the formation of plasmin by streptokinase. Proc Soc Exper Biol Med 1953; 82: 264-268
- 102 Brogden RN, Speight TM, Avery GS. Streptokinase: a review of its clinical pharmacology, mechanism of action and therapeutic uses. Drugs 1973; 5: 357-445
- 103 Cederholm-Williams SA, De Cock F, Lijnen HR, Collen D. Kinetics of the reactions between streptokinase, plasmin and α2-antiplasmin. Eur J Biochem 1979; 100: 125-132
- 104 Wiman B, Collen D. Molecular mechanism of physiological fibrinolysis. Nature 1978; 272: 549-550
- 105 Verstraete M, Vermylen J, Amery A, Vermylen C. Thrombolytic therapy with streptokinase using a standard dosage scheme. Brit Med J 1966; 5485: 454-456
- 106 Johnson AJ, McCarty WR. The lysis of artificially induced intravascular clots in man by intravenous infusions of streptokinase. J Clin Invest 1959; 38: 1627-1643
- 107 Ogston D, Bennett B, Herbert RJ, Douglas AS. The inhibition of urokinase by α2-macroglobulin. Clin Sci 1973; 44: 73-79
- 108 Clemmensen I, Christensen F. Inhibition of urokinase by complex formation with human alpha 1-antitrypsin. Biochim Biophys Acta 1976; 249: 591-599
- 109 Clemmensen I. Inhibition of urokinase by complex formation with human antithrombin III in absence and presence of heparin. Thromb Haemost 1978; 39: 616-623
- 110 Collen D, De Cock F, Verstraete M. Immunochemical distinction between antiplasmin and α1-antitrypsin. Thromb Res 1975; 7: 245-249
- 111 Wiman B, Collen D. Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur J Biochem 1977; 78: 19-26
- 112 Hedner U, Collen D. Immunochemical distinction between the inhibitors of plasminogen activation and antiplasmin in human plasma. Thromb Res 1976; 8: 875-879
- 113 Edy J, Collen D. The interaction in human plasma of antiplasmin, the fast-reacting plasmin inhibitor with plasmin, thrombin, trypsin and chymotrypsin. Biochim Biophys Acta 1977; 484: 423-432
- 114 Ohlsson K, Collen D. Comparison of the reactions of neutral granulocyte proteases with the major plasma protease inhibitors and with antiplasmin. Scand J Clin Lab Invest 1977; 37: 345-350
- 115 Christensen U, Clemmensen I. Kinetic properties of the primary inhibitor of plasmin from human plasma. Biochem J 1977; 163: 389-391
- 116 Wiman B, Collen D. On the kinetics of the reaction between human antiplasmin and plasmin. Eur J Biochem 1978; 84: 573-578
- 117 Collen D, Wiman B. Turnover of antiplasmin, the fast-acting plasmin inhibitor of plasma. Blood 1979; 53: 313-324
- 118 Edy J, Collen D, Verstraete M. Quantitation of the plasma protease inhibitor antiplasmin with the chromogenic substrate S-2251. In: "Progress in chemical fibrinolysis and thrombolysis, Vol 3". Davidson JF, Rowan RM, Samama MM, Desnoyers PC. eds) Raven Press, New York: 1978. p 315-322
- 119 Teger-Nilsson AC, Friberger P, Gyzander E. Determination of a new rapid plasmin inhibitor in human blood by means of a plasmin specific tripeptide substrate. Scand J Clin Lab Invest 1977; 37: 403-409
- 120 Aoki N. Natural inhibitors of fibrinolysis. Progr. Cardiovasc Dis 1979; 21: 267-286
- 121 Verstraete M, Vermylen J, Schetz J. Biochemical changes noted during intermittent administration of streptokinase. Thromb Haemostas 1978; 39: 61-68
- 122 Barrett AJ, Starkey PM, Munn EA. The unique nature of the interaction of α2-macroglobulin with proteinases. In: "Proteinase inhibitors". Fritz H, Tschesche H, Greene LJ, Truscheit E. eds) Springer Verlag, Berlin: 1974. p 72-77
- 123 Laurell CB, Jeppsson JO. Protease inhibitors in plasma. In: "The plasma proteins" second edition, vol 1. Putnam FW. eds) Academic Press, New York: 1975. chapter 5
- 124 Harpel PC. Human alpha 2-macroglobulin. Methods Enzymol 1976; 45: 639-652
- 125 Sawyer WD, Fletcher AP, Alkjaersig N, Sherry S. Studies on the thrombolytic activity of human plasma. J Clin Invest 1960; 39: 426-434
- 126 McNicol GP, Fletcher AP, Alkjaersig N, Sherry S. Impairment of hemostasis in the urinary tract: the role of urokinase. J Lab Clin Med 1961; 58: 34-46
- 127 Nilsson L, Rybo G. Treatment of menorrhagia with an antifibrinolytic agent, tranexamic acid (AMCA). A double-blind investigation. Acta Obstet Gynec Scand 1967; 46: 572-580
- 128 Nilsson IM, Krook H, Sternby NH, Söderberg E, Soderström N. Severe thrombotic disease in a young man with bone marrow and skeletal changes and with a high content of an inhibitor of the fibrinolytic system. Acta Med Scand 1961; 169: 323-337
- 129 Brakman P, Albrechtsen OK, Astrup T. A comparative study of coagulation and fibrinolysis in blood from normal men and women. Brit. J Haemat 1966; 12: 74-85
- 130 Koie K, Kamiya T, Ogata K, Takamatsu J. α2-Plasmin-inhibitor deficiency (Miyasato disease). Lancet 1978; ii: 1334-1336
- 131 Aoki N, Moroi M, Sakata Y, Yoshida N. Abnormal plasminogen. A hereditary molecular abnormality found in a patient with recurrent thrombosis. J Clin Invest 1978; 61: 1186-1195
- 132 Collen D, Tytgat GN, Claeys H, Piessens R. Metabolism and distribution of fibrinogen. I. Fibrinogen turnover in physiological conditions in humans. Brit J Haemat 1972; 22: 681-700
- 133 Cash JD. Control mechanisms of activator release. In: "Progress in chemical fibrinolysis and thrombolysis, Vol 3". Davidson JF, Rowan RM, Samama MM, Desnoyers PC. eds) Raven Press, New York: 1978. p 65-75
- 134 Cash JD. Platelet, fibrinolysis and stress. In: "Thrombosis-risk factors and diagnostic approaches". Brinkhous KM. Schattauer Verlag, Stuttgart: 1972. p 93
- 135 Markwardt F, Klocking HP. Studies on the release of plasminogen activator. Thromb Res 1976; 8: 217-223
- 136 Barker JL, Crayton JW, Nicoll RA. Supraoptic neurosecretory cells: adrenergic and cholinergic sensitivity. Science 1972; 171: 208-210
- 137 Hawkey CM, Britton BJ, Wood WG, Peele M, Irving MH. Changes in blood catecholamine levels and blood coagulation and fibrinolytic-activity in response to graded exercise in man. Br J Haematol 1975; 29: 377-384
- 138 Pina-Cabral JM, Rodrigues C. Blood catecholamine levels, factor VIII and fibrinolysis after therapeutic electroshock. Br J Haematol 1974; 28: 371-380
- 139 Nilsson IM. Effect of drugs on activator synthesis and release. In: "Progress in chemical fibrinolysis and thrombolysis, Vol 3". Davidson JF, Rowan RM, Samama MM, Desnoyers PC. eds) Raven Press, New York: 1978. p 77-89
- 140 Davidson JF, Lochhead M, McDonald GA, McNicol GP. Fibrinolytic enhancement by stanazolol: a double blind trial. Br J Haematol 1972; 22: 543-559
- 141 Nilsson IM. Phenformin and ethylestrenol in recurrent venous thrombosis. In: "Progress in chemical fibrinolysis and thrombolysis, Vol 1". Davidson JF, Samama MM, Desnoyers PC. eds) Raven Press, New York: 1975. p 1-12
- 142 Alkjaersig N, Fletcher AP, Sherry S. The mechanism of clot dissolution by plasmin. J Clin Invest 1959; 38: 1086-1095
- 143 Ambrus CM, Markus G. Plasmin-antiplasmin complex as a reservoir of fibrinolytic enzyme. Amer J Physiol 1960; 199: 491-494
- 144 Chesterman CN, Allington MJ, Sharp AA. Relationship of plasminogen activator to fibrin. Nature 1972; 238: 15-17
- 145 Wiman B, Lijnen HR, Collen D. On the specific interaction between the lysine-binding sites in plasmin and complementary sites in α2-antiplasmin and in fibrinogen. Biochim Biophys Acta 1979; 579: 142-159
- 146 Wiman B, Collen D. On the role of α2-antiplasmin in the regulation of fibrinolysis. In: "The physiological inhibitors of coagulation and fibrinolysis". Collen D, Wiman B, Verstraete M. eds) Elsevier/North Holland: 1979. p 177-185
- 147 Collen D, Verstraete M. α2-Antiplasmin consumption and fibrinogen breakdown during thrombolytic therapy. Thromb Res 1979; 14: 631-639
- 148 Thorsen S, Müllertz S. Rate of activation and electrophoretic mobility of unmodified and partially degraded plasminogen. Effects of 6-aminohexanoic acid and related compounds. Scand J Clin Lab Invest 1974; 34: 167
- 149 Collen D, Semeraro N, Tricot JP, Vermylen J. Turnover of fibrinogen, plasminogen, and prothrombin during exercise in man. J Appl Physiol 1977; 42: 865-873
- 150 Collen D, Vermylen J. Metabolism of iodine-labeled plasminogen during streptokinase and reptilase therapy in man. Thromb Res 1973; 2: 239-250
- 151 Collen D, Verstraete M. Plasmin-antiplasmin complex formation during defibrase infusion in man. Thromb Res 1977; 11: 417-420
- 152 Collen D, Tytgat G, Claeys H, Verstraete M, Wallen P. Metabolism of plasminogen in healthy subjects: effect of tranexamic acid. J Clin Invest 1972; 51: 1310-1318
- 153 Collen D, Rouvier J, Chamone DF, Verstraete M. Turnover of radiolabeled plasminogen and prothrombin in cirrhosis of the liver. Eur J Clin Invest 1978; 8: 185-188
- 154 Kakkar VV, Sagar S, Lewis M. Treatment of deep-vein thrombosis with intermittent streptokinase and plasminogen infusion. Lancet 1975; ii: 674-676
- 155 Brochier M, Planiol T, Griguer P, Raynaud Ph, Fauchier JP, Charbonnier B, Latour F, Pellois A. Intérêt du traitement séquentiel lysyl-plasminogène-urokinase et thérapeutique thrombolytique. Coeur Med Interne 1977; 16: 513-521
- 156 Marbet GA, Walter M, Six P, Nyman D, Rüst O, Biland L, Duckert F, Madar G, Da SilvaA, Widmer LK, Schmitt HE, Vokal J. Vergleich verschiedener fibrinolytischer Methoden zur Behandlung venöser Thrombosen. In: "Blutgerinnung und Antikoagulation. Neuhaus K, Duckert F. eds) Schattauer Verlag, Stuttgart: 1976. p 87
- 157 Latallo ZS, Lopaciuk S, Meissner J. A combined treatment with Defibrase and streptokinase. Akt Probl Angiol 1975; 26: 181
- 158 Collen D, De Cock F. Emergence in plasma during activation of the coagulation or fibrinolytic systems of neoantigens, associated with the complexes of thrombin or plasmin with their inhibitors. Thromb Res 1974; 5: 777-779
- 159 Collen D, De Cock F. A tanned red cell hemagglutination inhibition immunoassay (TRCHII) for the quantitative estimation of thrombin-antithrombin III and plasmin-α1-antiplasmin complexes in human plasma. Thromb Res 1975; 7: 235-238
- 160 Collen D, De Cock F, Cambiaso CL, Masson P. A latex agglutination test for rapid quantitative estimation of the plasmin-antiplasmin complex in human plasma. Eur J Clin Invest 1977; 7: 21-26
- 161 Collen D, De Cock F, Verstraete M. Quantitation of thrombin-antithrombin III complexes in human blood. Eur J Clin Invest 1977; 7: 407-411
- 162 Plow EF, De Cock F, Collen D. Immunochemical characterization of the plasmin-antiplasmin system. Basis for the specific detection of the plasmin-antiplasmin complex by latex agglutination assay. J Lab Clin Med 1979; 93: 199-209