Hypofibrinolyse und venöse Thromboembolie

• Literatur

• 1 Sottrup-Jensen L, Claeys H, Zajdel M, Petersen T. E, 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-spezific limited proteolysis. In: Progress in Chemical Fibrinolysis and Thrombolysis. Vol. 3. Davidson J. F, Rowan R. M, Samama M. M, Desnoyers P. C. (Eds.) Raven Press; New York: 1978: 191-209.
• 2 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. 221: 20-30 1970;
• 3 Collen D, Verstraete M. Molecular biology of human plasminogen. II. Metabolism in physiological and some pathological conditions in man. Thromb. Diath. Haemorrh. 34: 403-408 1975;
• 4 Robbins K. C, Summaria L, Hsieh B, Shah R. J. The peptide chains of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue. J. Biol. Chem. 244: 3590-3597 1969;
• 5 Claeys H, Vermylen J. Physiochemical and proenzyme properties of NH₂-terminal glutamic acid and NH₂-terminal lysine human plasminogen. Influence of 6-aminohexanoic acid. Biochim. Biophys. Acta. 342: 351-359 1974;
• 6 Collen D. On the regulation and control of fibrinolysis. Thromb. Haemostas. 43: 77-89 1980;
• 7 Pennica D, Holmes W. E, Kohr W. J, Harkins R. N, Vehar G. A, Ward C. A, Bennett W. F, Ylverton E, Seeburg P. H, Heyneker H. L, Goeddel D. V, Collen D. Cloning and expression of human tissuetpye plasminogen activator cDNA in E. coli. Nature. 301: 214-221 1983;
• 8 Ranby M. Tissue plasminogen activator. Isolation, enzymatic properties and assay procedure. Thesis, Umea University Medical Dissertation; New Series, No. 70, Umea 1982
• 9 Albrechtsen O. K. The fibrinolytic activity of human tissues. Brit. J. Haematol. 03: 284-291 1957;
• 10 Larsson A, Astedt B. Immunohistochemical localisation of tissue plasminogen activator and urokinase in the vessel wall. J. Clin. Pathol. 38: 140-145 1985;
• 11 Korninger C, Stassen J. M, Collen D. Turnover of human extrinsic (tissue-type) plasminogen activator in rabbits. Thromb. Haemostas. 46: 658-661 1981;
• 12 Binder B. R, Spragg J. The effect of fibrin on the activity of purified human vascular plasminogen activator. In: Protides of the Biological Fluids. Vol. 28. Peeters H. (Ed.) Pergamon Press; Oxford: 1980: 391-394.
• 13 Hoylaerts M, Rijken D. C, Lijnen H. R, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J. Biol. Chem. 257: 2912-2919 1982;
• 14 Ranby M, Bergsdorf N, Nilsson T. Enzymatic properties of the oneand two-chain form of tissue plasminogen activator. Thromb. Res. 27: 175-183 1982;
• 15 Beckmann R, Binder B. R. Generation of a high affinity t-PA binding site in FCB-2 fibrinogen fragments by limited proteolysis. Thromb. Haemostas. 54: 60 1985;
• 16 Nieuwenhuizen W, Verheijen J. H, Vermond A, Chang G. T. G. Plasminogen activation by tissue activator is accelerated in the presence of fibrin(ogen) cyanogen bromide fragment FBB-2. Biochim. Biophys. Acta. 755: 531-533 1983;
• 17 Marsh N, Gaffney P. Some observations on the release of extrinsic plasminogen activators during exercise in man. Haemostasis 09: 238-247 1980;
• 18 Clarke R. L, Orandi A, Cliffton E. E. Induction of fibrinolysis by venous obstruction. Angiology 11: 367-370 1960;
• 19 Prowse C. V, Cash J. D. Physiologic and pharmacologic enhancement of fibrinolysis. Sem. Thromb. Hemostas. 10: 51-60 1984;
• 20 Korninger C, Niessner H, Thaler E, Lechner K. Wirkung von DDAVP auf Fibrinolyseund Gerinnungsparameter Untersuchungen an Normalpersonen, Haemophilen und Patienten mit von-WillebrandJürgens-Syndrom. In: DDAVP in Bleeding Disorders. Sutor A. H. (Ed.) Schattauer; Stuttgart New York: 1980: 55-64.
• 21 Manucci P. M, Rota L. Plasminogen activator response after DDAVP: A clinicopharmacological study. Thromb. Res. 20: 69-76 1980;
• 22 Collen D. Identification and some properties of a new fast-acting plasmin inhibitor in human plasma. Eur. J. Biochem. 69: 209-216 1976;
• 23 Moroi M, Aoki N. Isolation and charakterization of alpha-2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J. Biol. Chem. 251: 5956-5965 1976;
• 24 Wiman B, Collen D. Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur. J. Biochem. 78: 19-26 1977;
• 25 Sataka Y, Aoki N. Cross-linking of alpha-2-plasmin inhibitor to fibrin by fibrin stabilizing factor. J. Clin. Invest. 65: 290-297 1980;
• 26 Kruithof E. K. O, Tran-Thang C, Ransijn A, Bachmann F. Demonstration of a fast-acting inhibitor of plasminogen activators in human plasma. Blood. 64: 907-913 1984;
• 27 Thorsen S, Philips M. Isolation of tissuetype plasminogen activator-inhibitor complexes from human plasma. Evidence for a rapid plasminogen activator inhibitor. Biochim. Biophys. Acta. 802: 111-118 1984;
• 28 Wiman B, Chmielewska J, Ranby M. Inactivation of tissue plasminogen activator in plasma. J. Biol. Chem. 259: 3644-3647 1984;
• 29 Philips M, Juul A-G, Thorsen S. Human endothelial cells produce a plasminogen activator inhibitor and a tissue-type plasminogen activator-inhibitor complex. Biochim. Biophys. Acta. 802: 99-110 1984;
• 30 Erickson L. A, Ginsberg M. H, Loskutoff D. J. Detection and partial characterization of an inhibitor of plasminogen activator in human platelets. J. Clin. Invest. 74: 1465-1472 1984;
• 31 Friberger P, Knös M. Plasminogen determination in human plasma. In: Chromogenic Peptide Substrates. Scully M. F, Kakar V. V. (Eds.) Churchill Livingstone; Edinburgh: 1979: 128-140.
• 32 Laurell C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal. Biochem. 15: 45-52 1969;
• 33 Verheijen J. H, Mullaart E, Chang G. T. G, Kluft C, Wijngaards G. A simple, sensitive spectrophotometric assay for extrinsic (tissue-type) plasminogen activator applicable to measurements in plasma. Thromb. Haemostas 48: 266-269 1982;
• 34 Wiman B, Mellbring G, Ranby M. Plasminogen activator release during venous stasis and exercise as determined by a new specific assay. Clin. Chim. Acta. 127: 279-288 1983;
• 35 Korninger C, Wagner O, Binder B. R. Tissue plasminogen activator inhibitor (antiactivator) in human plasma: development of a functional assay system and demonstration of a correlating M_r = 50,000 antiactivator. J. Lab. Clin. Med. 105: 718-724 1985;
• 36 Holmberg L, Kristoffersson A, Lecander I, Wallen P, Astedt B. Immuneradiometric quantification of tissue plasminogen activator secreted by fetal organs. Comparison with urokinase. Scand. J. Clin. Lab. Invest. 42: 347-354 1982;
• 37 Rijken D. C, Juhan-Vague I, De Cock F, Collen D. Measurement of human tissuetype plasminogen activator by a two-site immuneradiometric assay. J. Lab. Clin. Med. 42: 347-354 1982;
• 38 MacGregor I. R, Prowse C. V. Tissue plasminogen activator in human plasma measured by radioimmunoassay. Thromb. Res. 31: 461-474 1983;
• 39 Bergsdorf N, Nilsson T, Wallen P. An enzyme linked immunosorbent assay for determination of t-PA applied to patients with thromboembolic disease. Thromb. Haemostas. 50: 740-744 1983;
• 40 Rijken D. C, Hinsbergh V. W. M, Sens E. H. C. Quantitation of tissue-type plasminogen activator in human endothelial cell cultures by use of an enzyme immunoassay. Thromb. Res. 33: 145-153 1984;
• 41 Korninger C, Speiser W, Wojta J, Binder B. R. Sandwich ELISA for t-PA antigen employing a monoclonal antibody. Thromb. Res. (im Druck, 1985).
• 42 Edy J, De Cock F, Collen D. Inhibition of plasmin by normal and antiplasmin-depleted plasma. Thromb. Res. 08: 513-518 1976;
• 43 Chmielewska J. H, Ranby M, Wiman B. Evidence for a rapid inhibitor to tissue plasminogen activator in plasma. Thromb. Res. 31: 427-436 1983;
• 44 Verheijen J. H, Chang G. T. G, Kluft C. Evidence for the occurrence of a fast acting inhibitor for tissue-type plasminogen activator in human plasma. Thromb. Haemostas. 51: 392-395 1984;
• 45 Nilsson I. M, Olow R. Fibrinolysis induced by Streptokinase in man. Acta Chir. Scand. 123: 247-266 1962;
• 46 Astrup T, Miillertz S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. 39: 346-350 1952;
• 47 Levin R. I, Harpel P. C, Well D, Chang T-S, Rifkin D. B. Aspirin inhibits vascular plasminogen activator activity in vivo. Studies utilizing a new assay to quantify plasminogen activator activity. J. Clin. Invest. 74: 571-580 1984;
• 48 Jacobsen C. D. A family with low proteolytic capacity in plasma, probably related to a low plasminogen content. Scand. J. Clin. Lab. Invest. 18: 359-365 1966;
• 49 Aoki N, Moroi M, Sakata Y, Yoshida N, Matsuda M. Abnormal plasminogen. A hereditary molecular abnormality found in a patient with recurrent thrombosis. J. Clin. Invest. 61: 1186-1195 1978;
• 50 Wohl R. C, Summaria L, Robbins K. C. Physiological activation of the fibrinolytic system. Isolation and characterization of human plasminogen variants, Chicago I and II. J. Biol. Chem. 254: 9063-9069 1979;
• 51 Kazama M, Tahara C, Suzuki Z, Gohchi K, Abe T. Abnormal plasminogen, a case of recurrent thrombosis. Thromb. Res. 21: 517-522 1981;
• 52 Wohl R. C, Summaria L, Chediak J, Rosenfeld S, Robbins K. C. Human plasminogen variant Chicago III. Thromb. Haemostas 48: 146-152 1982;
• 53 Scharrer I, Robbins K. C, Wohl R. C, Hach V, Maas C. Investigations on 2 congenital abnormal plasminogens (Frankfurt I, II) and its relationship to thrombosis. Thromb. Haemostas 50: 257 1983;
• 54 Kwaan H. C, Astrup T. Fibrinolytic activity in thrombosed veins. Circ. Res. 17: 477-484 1965;
• 55 Kwaan H. C. The role of fibrinolysis in disease processes. Sem. Thromb. Haemostas. 10: 71-79 1984;
• 56 Vermylen D. G, Chamone D. A. F. The role of the fibrinolytic system in thromboembolism. Prog. Cardiovasc. Dis. 21: 255-266 1979;
• 57 Isacson S, Nilsson I. M. Defective fibrinolysis in blood and vein walls in recurrent »idiopathic« venous thrombosis. Acta Chir. Scand. 138: 313-319 1972;
• 58 Browse N. L, Gray L, Jarrett P. E. M, Morland M. Blood and vein-wall fibrinolytic activity in health and vascular disease. Brit. Med. J. 01: 478-481 1977;
• 59 Pandolfi M, Isacson S, Nilsson I. M. Low fibrinolytic activity in the walls of veins in patients with trombosis. Acta Med. Scand. 186: 1-5 1969;
• 60 Korninger C, Haubenstock A, Lechner K, Niessner H, Thaler E. Verminderte fibrinolytische Aktivität als Risikofaktor bei Patienten mit venösen Thromboembolien. In: Haemostase, Thrombophilie und Arteriosklerose. Van de Loo J, Asbeck F. (Hrsg.) Schattauer; Stuttgart New York: 1982: 136-154.
• 61 Andersen P. Hyperlipidaemia and reduced fibrinolytic activity associated with thromboembolic complications in a family. Acta Med. Scand 200: 289-291 1976;
• 62 Johansson L, Hedner U, Nilsson I. M. A family with thromboembolic disease associated with deficient fibrinolytic activity in the vessel wall. Acta Med. Scand 203: 477-480 1978;
• 63 Jorgensen M, Mortensen J. Z, Madsen A. G, Thorsen S, Jacobsen B. A family with reduced plasminogen activator activity in blood associated with recurrent venous thrombosis. Scand. J. Haematol. 29: 217-223 1982;
• 64 Korninger C. Der Plasminogenaktivator vom Gewebetyp. Physiologie, Pathophysiologie und klinische Bedeutung. Wien. Klin. Wschr. (im Druck, 1985).
• 65 Korninger C, Wagner O, Speiser W, Binder B. R. Levels of tissue plasminogen activator inhibitor (antiactivator, A A) in patients with a history of deep venous thrombosis. Isolation and partial characterization of A A from two patients. In: VI II. Int. Congress on Thrombosis; Abstract Book, Istanbul: 1984: 340.
• 66 Wiman B, Ljungberg B, Chmielewska J, Urden G, Blombach B, Johnsson H. The role of the fibrinolytic system in deep vein thrombosis. J. Lab. Clin. Med. 105: 265-270 1985;
• 67 Korninger C, Lechner K, Niessner H, Gössinger H, Kundi M. Impaired fibrinolytic capacity predisposes for recurrence of venous thrombosis. Thromb. Haemostas. 52: 127-130 1984;
• 68 Clayton J. K, Anderson J. A, McNicol G. P. Preoperative prediction of postoperative deep vein thrombosis. Brit. Med. J. 02: 910-912 1976;
• 69 Rakoczi I, Chamone D, Verstraete M, Collen D. The relevance of clinical and hemostasis parameters for the prediction of postoperative thrombosis of the deep veins of the lower extremity in gynecologic patients. Surg. Gynec. Obstet. 151: 225-231 1980;
• 70 Lowe G. D. O, Osborne D. H, McArdle B. M, Smith A, Carter D. C, Forbes C. D, McLaren D, Prentice C. R. M. Prediction and selective prophylaxis of venous thrombosis in elective gastrointestinal surgery. Lancet I: 409-412 1982;
• 71 Dhall T. Z, Shah G. A, Ferguson I. A, Ardlie N. G, Dhall D. P. Preoperative blood tests in prediction of postoperative deep vein thrombosis. Thromb. Res. 27: 143-153 1982;
• 72 Mellbring G, Nilsson T, Bergsdorf N, Wallen P. Tissue plasminogen activator concentration in major abdominal surgery. Thromb. Res. 36: 331-334 1984;
• 73 Mellbring G, Dahlgren S, Reiz S, Wiman B. Fibrinolytic activity in plasma and deep vein thrombosis after major abdominal surgery. Thromb. Res. 32: 575-584 1983;
• 74 Gallus A. S, Hirsh J, Gent M. Relevance of preoperative and postoperative blood tests to postoperative leg-vein thrombosis. Lancet II: 805-809 1973;
• 75 Smokovitis A, Binder B. R. The effect of the anabolic steroid stanazolol on tissue plasminogen activator activity and plasmin inhibition in the rat. Experientia. 36: 2624-2630 1980;
• 76 Davidson J. F, Lockhead M, McDonald G. A, McNicol G. P. Fibrinolytic enhancement by stanazolol. Brit. J. Haematol. 22: 543 1972;
• 77 Blarney S. L, McArdle B. M, Burns P, Lowe F. D. O, Forbes C. D, Carter D. C, Prentice C. R. M. Prevention of fibrinolytic shutdown after major surgery by intramuscular stanazolol. Thromb. Res. 31: 451-459 1983;
• 78 Verheijen J. H, Rijken D. C, Chang G. T. G, Preston F. E, Kluft C. Modulation of rapid plasminogen activator inhibitor in plasma by stanazolol. Thromb. Haemostas. 51: 396-397 1984;
• 79 Desnoyers P. C. Indirect fibrinolytic agents. In: Handbook of Experimental Pharmacology 46. Markwardt F. (Hrsg.) Springer; Berlin Heidelberg New York: 1978: 273.