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Hamostaseologie 1983; 03(02): 45-51
DOI: 10.1055/s-0038-1656615
DOI: 10.1055/s-0038-1656615
Originalarbeiten
Grundlagen der fibrinolytischen Therapie
Further Information
Publication History
Publication Date:
22 June 2018 (online)
Zusammenfassung
Aufklärung von Struktur und Funktion der an der Fibrinolyse beteiligten Komponenten läßt erkennen, daß der Körper in der Lage ist, Fibrinolyse und Fibrinogenolyse unabhangig voneinander einzusetzen. Da das therapeutische Ziel entweder die Verbesserung der Fibrinolyse oder die Unterdriickung einer Fibrinogenolyse ist, reicht es nicht aus, nach Möglichkeiten zu suchen, urn die Plasminaktivierungskaskade an- oder abzuschalten. Vielmehr gilt es die Steuermoglichkeiten auszunutzen, urn eine erforderliche Fibrinolyse bei gleichzeitig verhinderter Fibrinogenolyse therapeutisch auszulösen.
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LITERATUR
- 1 Hoylaerts M, Dingeman C. R, Lijnen H. R, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. J. Biol. Chem 1982; 257: 2912-2919.
- 2 Taylor F. B, Caroll R. C, Gerard J, Esmon C. T, Radcliffe R. D. Lysis of clots prepared from whole blood and plasma. Fed. Proc 1981; 40: 2092-2098.
- 3 Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim. Biophys. Acta: 1982; 704: 461-469.
- 4 Reddy K. N. N, Kline D. L. Plasminogen Activators. Aus: Fibrinolysis, CRC-Press; 1980
- 5 Smokovitis A. A new hypothesis: possible mechanisms in the involvement of the increased plasminogen activator acitivity in branching regions of the aorta in the initiation of atherosclerosis. Thromb. Haemost 1980; 43: 141-146.
- 6 Opdenakker G, Wenning H, Collen D, Billiau A, de Somer P. Messenger RNA for human tissue plasminogen activator. Eur. J. Biochem 1982; 121: 269-274.
- 7 Bernik M. B, Wijngaards G, Rijken D. C. Production by human tissue in culture of immunologically distinct, multiple molecular weight forms of plasminogen activators. Ann. NY Acad. Sci 1981; 370: 592-608.
- 8 Haverkate F, Brakman P, Kluft C, Rijken und D. C, Wijngaards G. Physiologische Aktivatoren der Fibrinolyse. Fibrinolyse, Thrombose, Hämostase; Schattauer-Verlag Stuttgart: 1980
- 9 Rijken D. C, Collen D. Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J. Biol. Chem 1981; 256: 7035-7041.
- 10 Deutsch E, Eisner P. The mechanism of fibrinolysis induced by bacterial pyrogens. Thromb. Diath. Haemorrh 1959; III Nr. 2 (03) 286-295.
- 11 Small M, McArdle B. M, Lowe G. D. O, Forbes C. D, Prentice C. R. M. The effect of intramuscular stanozolol on fibrinolysis and blood lipids. Thromb. Res 1982; 28: 27-36.
- 12 Marsh N. A, Gaffney P. J. Exercise-induced fibrinolysis-fact or fiction? Thromb. Haemostas 1982; 48 (02) 201-203.
- 13 Holmberg L, Nilsson I. M, Wallen P, Astedt B. Studies on the blood plasminogen activator induced by l-Desamino-8-D-arginine Vasopressin with Observations in v. Willebrand’s Disease (41407). Proc. Soc. Exp. Biol. Med 1982; 170: 126-132.
- 14 Keber D, Stegnar M. Exhaustion of arm fibrinolytic potential after repeated venous occlusions and local exercise. Thromb. Res 1982; 28: 693-704.
- 15 Korninger Ch, Niessner H, Lechner K. Impaired fibrinolytic response to DDAVP and venous occlusion in a sub-group of patients with v. Willebrand’s Disease. Thromb. Res 1981; 23: 365-374.
- 16 Heimburger N. Biochemie des Plasminogens und der Plasminogen-Aktivierung. aus: Fibrinolyse, Thrombose, Hämostase. Schattauer-Verlag; 1980: 3-13.
- 17 Collen D, Verstraete M. Molecular biology of human plasminogen. II. Metabolism in physiological and some pathological conditions in man. Thrombos. Diathes. Haemorrh 1975; 34: 403-408.
- 18 Wieman B. Primary structure of the C-chain of human plasmin. Eur. J. Biochem 1977; 76: 129-137.
- 19 Magnusson S. Thrombin and prothrombin. Blombäck, B., L. A. Hanson: Plasma proteins. J. Wiley, Chichester.
- 20 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 (mol wt, 38000) by elastase-catalyzed-specific limited proteolysis. In Davidson J. F, Rowan R. M, Samama M. M, Desnoyers P. C. (eds.) Progress in chemical fibrinolysis and thrombolysis, Vol. 3 1st. ed Raven Press; New York: 191-209.
- 21 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.
- 22 Wiman B, Collen D. Molecular mechanism of physiological fibrinolysis. Nature. 1978: 272.
- 23 Hayes M. L, Castellino F. J. Carbohydrate of the human plasminogen variants. J. Biol. Chem 1979; 254: 8768-8780.
- 24 Collen D. On the regulation and control of Fibrinolysis. VIIth Int. Congr. Thromb. Haemost. London: 1979
- 25 Korninger C, Collen D. Neutralization of human extrinsic (tissue-type) plasminogen activator in human plasma: no evidence for a specific inhibitor. Thromb. Haemostas 1981; 46: 662-665.
- 26 Chang M. L, Bang N. U. Biological behavior of higher molecular weight products of fibrinolysis. J. Lab. Clin. Med., Vol 1977; 90: 216-226.
- 27 Wallin R, Belew M, Gerdin B, Saldeen T. Differential degradation by plasmin of fragment E derived from fibrin and fibrinogen. Thromb. Res 1980; 19: 441-445.
- 28 Francis C. W, Marder V. J. A molecular model of plasmatic degradation of cross-linked fibrin. Semin. Thrombos. Haemostas 1982; 8: 25-35.
- 29 Lijnen H. R, Hoylaerts M, Collen D. Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. J. Biolog. Chem 1980; 255: 10214-10222.
- 30 Wiman B, Collen D. Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur. J. Biochem 1977; 78: 19-26.
- 31 Tamaki T, Sakata Y, Aoki N. Survival of transfused a2-plasmin inhibitor in a patient with its congenital deficiency. Thromb. Res 1981; 22: 281-286.
- 32 Clemmensen I, Thorsen S, Müllertz S, Petersen L. C. Properties of three different molecular forms of a2-plasmin inhibitor. Eur. J. Biochem 1981; 120: 105-112.
- 33 Lijnen H. R, Collen D. Interaction of plasminogen activators and inhibitors with plasminogen and fibrin. Semin. Thrombos. and Hemostas 1982; 8: 2-10.
- 34 Lünen H. R, Maes M, Castel M, Samama M, Collen D. Kinetics of the inhibition of plasmin in acidified human plasma. Thromb. Haemostas 1982; 48: 257-259.
- 35 Matsuo O. Turnover of tissue plasminogen activator in man. Thromb. Haemostas 1982; 48: 242.
- 36 Fletcher A. P, 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.
- 37 Harpel P. C. a2-Plasmin Inhibitor and a2-Macroglobulin-Plasmin complexes in plasma. J. Clin. Invest 1981; 68: 46-55.
- 38 Wohl R. C, Sinio L, Robbins K. C. Methods for studying fibrinolytic pathway components in human plasma. Thromb. Res 1982; 27: 523-535.
- 39 Wohl R. C, Summaria L, Chediak J, Rosenfeld S, Robbins K. C. Human plasminogen variant Chicago III. J. Biol. Chem 1979; 254: 6.
- 40 Sueishi K, Nanno S, Tanaka K. Permeability enhancing and chemotactic acitivities of lower molecular weight degradation products of human fibrinogen. Thrombos. Haemostas 1981; 45: 90-94.
- 41 Verstraete M, Collen D. Thrombolyse mit Gewebeaktivator. aus: Verhandl. 88. Tg. Dtsch. Ges. Inn. Med. Springer: S. 1288-1291. 1982
- 42 v. Kaulla K. N. Synthetic Fibrinolytic Agents. In Kline D. L, Reddy K. N. N. (Hrsg.) Fibrinolysis: CRC Press; 1980: 95-128.
- 43 Halse Th. Enzymologie der spontanen und therapeutisch induzierten Fibrinolyse. Ztschr. f. Vitamin, Hormonund Fermentforschung, Sonderdruck aus Bd. XI. 1960 Heft 1
- 44 Marx R, Schmidt H. Über den Einfluß von Anticoagulantien auf die Fibrinolyse im menschlichen Serum. Angewandte Medizin I. 192-200. Heft 6, Jhrg. 5
- 45 Sandritter W, Bergenhof H. D, Kroker R. Morphologische Untersuchungen zur Wirkung des Heparins auf experimentellen Abscheidungsthromben. Frankf. Ztschr. f. Pathologie 1954; 65: 342-349.
- 46 Carlin G, Bang N. U. Enhancement of plasminogen activation and hydrolysis of purified fibrinogen and fibrin by dextran 70. Thromb. Res 1980; 19: 535-546.
- 47 Paar D, Maruhn D. Spectrometric determination of urokinase in urine after gel filtration, using the chromogenic substrat S 2444. J. Clin. Chem. Clin. Biochem 1980; 18: 557-562.
- 48 Tissor J. D, Schneider P, Hauert J, Ruegg M, Kruithof E. K. O, Bachmann F. Isolation from human plasma of a plasminogen activator identical to urinary high molecular weight urokinase. J. Clin. Invest 1982; 70: 1320-1323.
- 49 Sumi H. Enzymatic modifications of fibrinolytic enzyme and inhibitor molecules. Thrombos. Haemostas 1982; 48: 342.
- 50 Jackson K. W, Tang J. Complete amino sequence of streptokinase and its homology with serine proteases. Biochemistry 1982; 21: 6620-6625.
- 51 Jackson K. W, Tang J. The amino-terminal sequence of streptokinase and its functional implications in plasminogen activation. Thromb. Res 1978; 13: 693-699.
- 52 Koide A, Suzuki S, Kobayashi S. Preparation of polyethylene glycolmodified streptokinase with disappearance of binding ability towards anti-serum and retention of acticity. FEBS letters 1982; 143: 73.
- 53 Brunisholz R. A, Lerch P. G, Schaller J, Rickli E. E, Lergier W, Manneberg M, Gillessen D. Comparison of the primary structure of the N-terminal CNBr fragments of human bovine and porcine plasminogen. Eur. J. Biochem 1981; 114: 465-470.
- 54 Smith R. A. G, Dupe R. J, English P. D, Green J. Fibrinolysis with acylenzymes: a new approach to thrombolytic therapy. Nature 1981; 290: 505-507.