Download PDF
Hamostaseologie 1983; 03(02): 45-51
DOI: 10.1055/s-0038-1656615
Originalarbeiten
Schattauer GmbH

Grundlagen der fibrinolytischen Therapie

L. Róka
1   Institut für Klinische Chemie und Pathobiochemie der Justus-Liebig-Universität Gießen
› Author Affiliations
Further Information

Publication History

Publication Date:
22 June 2018 (online)

Also available at
    Permissions and Reprints

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.

 

  • 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.
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 3 Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim. Biophys. Acta: 1982; 704: 461-469.
    CrossrefPubMedGoogle Scholar
  • 4 Reddy K. N. N, Kline D. L. Plasminogen Activators. Aus: Fibrinolysis, CRC-Press; 1980
    Google Scholar
  • 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.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 8 Haverkate F, Brakman P, Kluft C, Rijken und D. C, Wijngaards G. Physiologische Aktivatoren der Fibrinolyse. Fibrinolyse, Thrombose, Hämostase; Schattauer-Verlag Stuttgart: 1980
    Google Scholar
  • 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.
    PubMedGoogle Scholar
  • 10 Deutsch E, Eisner P. The mechanism of fibrinolysis induced by bacterial pyrogens. Thromb. Diath. Haemorrh 1959; III Nr. 2 (03) 286-295.
    PubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 12 Marsh N. A, Gaffney P. J. Exercise-induced fibrinolysis-fact or fiction? Thromb. Haemostas 1982; 48 (02) 201-203.
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 14 Keber D, Stegnar M. Exhaustion of arm fibrinolytic potential after repeated venous occlusions and local exercise. Thromb. Res 1982; 28: 693-704.
    CrossrefPubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 16 Heimburger N. Biochemie des Plasminogens und der Plasminogen-Aktivierung. aus: Fibrinolyse, Thrombose, Hämostase. Schattauer-Verlag; 1980: 3-13.
    Google Scholar
  • 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.
    PubMedGoogle Scholar
  • 18 Wieman B. Primary structure of the C-chain of human plasmin. Eur. J. Biochem 1977; 76: 129-137.
    CrossrefPubMedGoogle Scholar
  • 19 Magnusson S. Thrombin and prothrombin. Blombäck, B., L. A. Hanson: Plasma proteins. J. Wiley, Chichester.
    PubMedGoogle Scholar
  • 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.
    Google Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 22 Wiman B, Collen D. Molecular mechanism of physiological fibrinolysis. Nature. 1978: 272.
    Google Scholar
  • 23 Hayes M. L, Castellino F. J. Carbohydrate of the human plasminogen variants. J. Biol. Chem 1979; 254: 8768-8780.
    PubMedGoogle Scholar
  • 24 Collen D. On the regulation and control of Fibrinolysis. VIIth Int. Congr. Thromb. Haemost. London: 1979
    Google Scholar
  • 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.
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 28 Francis C. W, Marder V. J. A molecular model of plasmatic degradation of cross-linked fibrin. Semin. Thrombos. Haemostas 1982; 8: 25-35.
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 33 Lijnen H. R, Collen D. Interaction of plasminogen activators and inhibitors with plasminogen and fibrin. Semin. Thrombos. and Hemostas 1982; 8: 2-10.
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 35 Matsuo O. Turnover of tissue plasminogen activator in man. Thromb. Haemostas 1982; 48: 242.
    PubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 37 Harpel P. C. a2-Plasmin Inhibitor and a2-Macroglobulin-Plasmin complexes in plasma. J. Clin. Invest 1981; 68: 46-55.
    CrossrefPubMedGoogle Scholar
  • 38 Wohl R. C, Sinio L, Robbins K. C. Methods for studying fibrinolytic pathway components in human plasma. Thromb. Res 1982; 27: 523-535.
    CrossrefPubMedGoogle Scholar
  • 39 Wohl R. C, Summaria L, Chediak J, Rosenfeld S, Robbins K. C. Human plasminogen variant Chicago III. J. Biol. Chem 1979; 254: 6.
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 41 Verstraete M, Collen D. Thrombolyse mit Gewebeaktivator. aus: Verhandl. 88. Tg. Dtsch. Ges. Inn. Med. Springer: S. 1288-1291. 1982
    Google Scholar
  • 42 v. Kaulla K. N. Synthetic Fibrinolytic Agents. In Kline D. L, Reddy K. N. N. (Hrsg.) Fibrinolysis: CRC Press; 1980: 95-128.
    Google Scholar
  • 43 Halse Th. Enzymologie der spontanen und therapeutisch induzierten Fibrinolyse. Ztschr. f. Vitamin, Hormonund Fermentforschung, Sonderdruck aus Bd. XI. 1960 Heft 1
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    PubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 49 Sumi H. Enzymatic modifications of fibrinolytic enzyme and inhibitor molecules. Thrombos. Haemostas 1982; 48: 342.
    PubMedGoogle Scholar
  • 50 Jackson K. W, Tang J. Complete amino sequence of streptokinase and its homology with serine proteases. Biochemistry 1982; 21: 6620-6625.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar
  • 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.
    CrossrefPubMedGoogle Scholar