Skip to main content
NCBI home page
Journal of Clinical Pathology. Supplement (Royal College of Pathologists) logoLink to Journal of Clinical Pathology. Supplement (Royal College of Pathologists)
. 1980;14:24–30.

Natural inhibitors of fibrinolysis

D Collen 1
PMCID: PMC1347101  PMID: 6448870

Full text

PDF
24

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abiko Y., Iwamoto M., Tomikawa M. Plasminogen-plasmin system. V. A stoichiometric equilibrium complex of plasminogen and a synthetic inhibitor. Biochim Biophys Acta. 1969;185(2):424–431. doi: 10.1016/0005-2744(69)90435-5. [DOI] [PubMed] [Google Scholar]
  2. Alkjaersig N. The purification and properties of human plasminogen. Biochem J. 1964 Oct;93(1):171–182. doi: 10.1042/bj0930171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Aoki N. Natural inhibitors of fibrinolysis. Prog Cardiovasc Dis. 1979 Jan-Feb;21(4):267–286. doi: 10.1016/0033-0620(79)90014-8. [DOI] [PubMed] [Google Scholar]
  4. Camiolo S. M., Thorsen S., Astrup T. Fibrinogenolysis and fibrinolysis with tissue plasminogen activator, urokinase, streptokinase-activated human globulin, and plasmin. Proc Soc Exp Biol Med. 1971 Oct;138(1):277–280. doi: 10.3181/00379727-138-35878. [DOI] [PubMed] [Google Scholar]
  5. Christensen U., Clemmensen I. Kinetic properties of the primary inhibitor of plasmin from human plasma. Biochem J. 1977 May 1;163(2):389–391. doi: 10.1042/bj1630389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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 Apr 11;342(2):351–359. doi: 10.1016/0005-2795(74)90090-7. [DOI] [PubMed] [Google Scholar]
  7. Clemmensen I., Christensen F. Inhibition of urokinase by complex formation with human alpha1-antitrypsin. Biochim Biophys Acta. 1976 Apr 8;429(2):591–599. doi: 10.1016/0005-2744(76)90307-7. [DOI] [PubMed] [Google Scholar]
  8. Clemmensen I. Inhibition of urokinase by complex formation with human antithrombin III in absence and presence of heparin. Thromb Haemost. 1978 Jun 30;39(3):616–623. [PubMed] [Google Scholar]
  9. Collen D. Identification and some properties of a new fast-reacting plasmin inhibitor in human plasma. Eur J Biochem. 1976 Oct 1;69(1):209–216. doi: 10.1111/j.1432-1033.1976.tb10875.x. [DOI] [PubMed] [Google Scholar]
  10. Collen D., Semeraro N., Telesforo P., Verstraete M. Inhibition of plasmin by antithrombin-heparin complex. II. During thrombolytic therapy in man. Br J Haematol. 1978 May;39(1):101–110. doi: 10.1111/j.1365-2141.1978.tb07132.x. [DOI] [PubMed] [Google Scholar]
  11. Collen D., Wiman B. Turnover of antiplasmin, the fast-acting plasmin inhibitor of plasma. Blood. 1979 Feb;53(2):313–324. [PubMed] [Google Scholar]
  12. Collen D. alpha2-Antiplasmin inhibitor deficiency. Lancet. 1979 May 12;1(8124):1039–1040. doi: 10.1016/s0140-6736(79)92800-9. [DOI] [PubMed] [Google Scholar]
  13. Den Ottolander G. J., Leijnse B., Cremer-Elfrink H. M. Plasmatic and platelet anti-plasmins and anti-activators. Thromb Diath Haemorrh. 1967 Dec 31;18(3-4):404–415. [PubMed] [Google Scholar]
  14. 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 Oct 13;484(2):423–432. doi: 10.1016/0005-2744(77)90098-5. [DOI] [PubMed] [Google Scholar]
  15. Ekert H., Friedlander I., Hardisty R. M. The role of platelets in fibrinolysis. Studies on the plasminogen activator and anti-plasmin activity of platelets. Br J Haematol. 1970 May;18(5):575–584. doi: 10.1111/j.1365-2141.1970.tb00779.x. [DOI] [PubMed] [Google Scholar]
  16. FLETCHER A. P., 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 May;65:713–731. [PubMed] [Google Scholar]
  17. 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 Apr;43:681–695. doi: 10.1172/JCI104953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ganguly P. A low molecular weight antiplasmin of human blood platelets. Clin Chim Acta. 1972 Jul;39(2):466–468. doi: 10.1016/0009-8981(72)90068-x. [DOI] [PubMed] [Google Scholar]
  19. Gurewich V., Hyde E., Lipinski B. The resistance of fibrinogen and soluble fibrin monomer in blood to degradation by a potent plasminogen activator derived from cadaver limbs. Blood. 1975 Oct;46(4):555–565. [PubMed] [Google Scholar]
  20. Harpel P. C. Human alpha2-macroglobulin. Methods Enzymol. 1976;45:639–652. doi: 10.1016/s0076-6879(76)45055-3. [DOI] [PubMed] [Google Scholar]
  21. Hedner U., Abildgaard U. Report on the joint meeting of the task forces on nomenclature and standards of inhibitors of coagulation and fibrinolysis. Thromb Haemost. 1978 Apr 30;39(2):524–525. [PubMed] [Google Scholar]
  22. Hedner U., Martinsson G. Inhibition of activated Hageman factor (factor XIIa) by an inhibitor of the plasminogen activation (PA inhibitor). Thromb Res. 1978 Jun;12(6):1015–1023. doi: 10.1016/0049-3848(78)90057-9. [DOI] [PubMed] [Google Scholar]
  23. Hedner U. Studies on an inhibitor of plasminogen activation in human serum. Thromb Diath Haemorrh. 1973 Nov;30(2):414–424. [PubMed] [Google Scholar]
  24. Highsmith R. F., Rosenberg R. D. The inhibition of human plasmin by human antithrombin-heparin cofactor. J Biol Chem. 1974 Jul 25;249(14):4335–4338. [PubMed] [Google Scholar]
  25. Iwamoto M. Plasminogen-plasmin system IX. Specific binding of tranexamic acid to plasmin. Thromb Diath Haemorrh. 1975 Jun 30;33(3):573–585. [PubMed] [Google Scholar]
  26. JOHNSON A. J., McCARTY W. R. The lysis of artificially induced intravascular clots in man by intravenous infusions of streptokinase. J Clin Invest. 1959 Sep;38:1627–1643. doi: 10.1172/JCI103941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. JOHNSON S. A., SCHNEIDER C. L. The existence of antifibrinolysin activity in platelets. Science. 1953 Feb 27;117(3035):229–230. [PubMed] [Google Scholar]
  28. Kluft C. Elimination of inhibition in euglobulin fibrinolysis by use of flufenamate: involvement of C1-inactivator. Haemostasis. 1977;6(6):351–369. doi: 10.1159/000214202. [DOI] [PubMed] [Google Scholar]
  29. MULLERTZ S. A plasminogen activator in spontaneously active human blood. Proc Soc Exp Biol Med. 1953 Feb;82(2):291–295. doi: 10.3181/00379727-82-20097. [DOI] [PubMed] [Google Scholar]
  30. Markus G., DePasquale J. L., Wissler F. C. Quantitative determination of the binding of epsilon-aminocaproic acid to native plasminogen. J Biol Chem. 1978 Feb 10;253(3):727–732. [PubMed] [Google Scholar]
  31. McConnell D. J. Inhibitors of kallikrein in human plasma. J Clin Invest. 1972 Jul;51(7):1611–1623. doi: 10.1172/JCI106962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. McDonagh J., Kiesselbach T. H., Wagner R. H. Factor 13 and antiplasmin activity in human platelets. Am J Physiol. 1969 Mar;216(3):508–513. doi: 10.1152/ajplegacy.1969.216.3.508. [DOI] [PubMed] [Google Scholar]
  33. Moore S., Pepper D. S., Cash J. D. The isolation and characterisation of a platelet-specific beta-globulin (beta-thromboglobulin) and the detection of antiurokinase and antiplasmin released from thrombin-aggregated washed human platelets. Biochim Biophys Acta. 1975 Feb 27;379(2):360–369. doi: 10.1016/0005-2795(75)90143-9. [DOI] [PubMed] [Google Scholar]
  34. Moroi M., Aoki N. Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J Biol Chem. 1976 Oct 10;251(19):5956–5965. [PubMed] [Google Scholar]
  35. Mui P. T., James H. L., Ganguly P. Isolation and properties of a low molecular weight antiplasmin of human blood platelets and serum. Br J Haematol. 1975 Apr;29(4):627–637. doi: 10.1111/j.1365-2141.1975.tb02749.x. [DOI] [PubMed] [Google Scholar]
  36. Murray J., Crawford G. P., Ogston D., Douglas A. S. Studies on an inhibitor of plasminogen activators in human platelets. Br J Haematol. 1974 Apr;26(4):661–668. doi: 10.1111/j.1365-2141.1974.tb00509.x. [DOI] [PubMed] [Google Scholar]
  37. Müllertz S., Clemmensen I. The primary inhibitor of plasmin in human plasma. Biochem J. 1976 Dec 1;159(3):545–553. doi: 10.1042/bj1590545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. 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 Nov;143(2):273–283. doi: 10.1042/bj1430273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Ogston D., Bennett B., Herbert R. J., Douglas A. S. The inhibition of urokinase by alpha 2 -macroglobulin. Clin Sci. 1973 Jan;44(1):73–79. doi: 10.1042/cs0440073. [DOI] [PubMed] [Google Scholar]
  40. 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 Jun;37(4):345–350. doi: 10.3109/00365517709092640. [DOI] [PubMed] [Google Scholar]
  41. Okamoto S., Oshiba S., Mihara H., Okamoto U. Synthetic inhibitors of fibrinolysis: in vitro and in vivo mode of action. Ann N Y Acad Sci. 1968 Jun 28;146(2):414–429. doi: 10.1111/j.1749-6632.1968.tb20303.x. [DOI] [PubMed] [Google Scholar]
  42. Rákóczi I., Wiman B., Collen D. On the biological significance of the specific interaction between fibrin, plasminogen and antiplasmin. Biochim Biophys Acta. 1978 May 3;540(2):295–300. doi: 10.1016/0304-4165(78)90142-3. [DOI] [PubMed] [Google Scholar]
  43. Semeraro N., Colucci M., Telesforo P., Collen D. The inhibition of plasmin by antithrombin-heparin complex. I. In human plasma in vitro. Br J Haematol. 1978 May;39(1):91–99. doi: 10.1111/j.1365-2141.1978.tb07131.x. [DOI] [PubMed] [Google Scholar]
  44. Sjöholm I. Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid. Eur J Biochem. 1973 Nov 15;39(2):471–479. doi: 10.1111/j.1432-1033.1973.tb03146.x. [DOI] [PubMed] [Google Scholar]
  45. Stead N., Kaplan A. P., Rosenberg R. D. Inhibition of activated factor XII by antithrombin-heparin cofactor. J Biol Chem. 1976 Nov 10;251(21):6481–6488. [PubMed] [Google Scholar]
  46. Teger-Nilsson A. C., 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 Sep;37(5):403–409. [PubMed] [Google Scholar]
  47. Thorsen S. Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-aminocarboxylic acids. Biochim Biophys Acta. 1975 May 30;393(1):55–65. doi: 10.1016/0005-2795(75)90216-0. [DOI] [PubMed] [Google Scholar]
  48. Thorsen S., Glas-Greenwalt P., Astrup T. Differences in the binding to fibrin of urokinase and tissue plasminogen activator. Thromb Diath Haemorrh. 1972 Aug 31;28(1):65–74. [PubMed] [Google Scholar]
  49. Tytgat G., Collen D., De Vreker R., Verstraete M. Investigations on the fibrinolytic system in liver cirrhosis. Acta Haematol. 1968;40(5):265–274. doi: 10.1159/000208914. [DOI] [PubMed] [Google Scholar]
  50. Verstraete M., Vermylen J., Amery A., Vermylen C. Thrombolytic therapy with streptokinase using a standard dosage scheme. Br Med J. 1966 Feb 19;1(5485):454–456. doi: 10.1136/bmj.1.5485.454. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Verstraete M., Vermylen J., Schetz J. Biochemical changes noted during intermittent administration of streptokinase. Thromb Haemost. 1978 Feb 28;39(1):61–68. [PubMed] [Google Scholar]
  52. Wiman B., Collen D. Molecular mechanism of physiological fibrinolysis. Nature. 1978 Apr 6;272(5653):549–550. doi: 10.1038/272549a0. [DOI] [PubMed] [Google Scholar]
  53. Wiman B., Collen D. On the kinetics of the reaction between human antiplasmin and plasmin. Eur J Biochem. 1978 Mar 15;84(2):573–578. doi: 10.1111/j.1432-1033.1978.tb12200.x. [DOI] [PubMed] [Google Scholar]
  54. Wiman B., Collen D. On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin. J Biol Chem. 1979 Sep 25;254(18):9291–9297. [PubMed] [Google Scholar]
  55. Wiman B., Collen D. Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur J Biochem. 1977 Aug 15;78(1):19–26. doi: 10.1111/j.1432-1033.1977.tb11709.x. [DOI] [PubMed] [Google Scholar]
  56. Wiman B., Wallén 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 Jan 15;50(3):489–494. doi: 10.1111/j.1432-1033.1975.tb09887.x. [DOI] [PubMed] [Google Scholar]
  57. Wiman B., Wallén P. The specific interaction between plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen. Thromb Res. 1977 Feb;10(2):213–222. doi: 10.1016/0049-3848(77)90003-2. [DOI] [PubMed] [Google Scholar]
  58. den Ottolander G. J., Leijnse B., Cremer-Elfrink H. M. Plasmatic and thrombocytic anti-plasmins and anti-activators. II. Thromb Diath Haemorrh. 1969 Feb 28;21(1):26–34. [PubMed] [Google Scholar]

Articles from Journal of Clinical Pathology. Supplement (Royal College of Pathologists). are provided here courtesy of BMJ Publishing Group

RESOURCES