Download PDF
Thromb Haemost 1966; 15(03/04): 413-419
DOI: 10.1055/s-0038-1649442
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Some Effects of Fibrinogen Degradation Products (FDP) on Blood Platelets[*]

Z Jerushalmy
1   American National Red Cross Research Laboratory, Eastern Division, New York; and the Department of Pathology, New York University Medical Center, New York
,
M. B Zucker
1   American National Red Cross Research Laboratory, Eastern Division, New York; and the Department of Pathology, New York University Medical Center, New York
› Author Affiliations
Further Information

Publication History

Publication Date:
24 July 2018 (online)

Also available at
    Permissions and Reprints

Summary

“Early” fibrinogen degradation products are more potent inhibitors of thrombin-induced clotting than “late” products and also interfere with the ability of thrombin to release serotonin from platelets. “Early” and “intermediate” FDP cause moderate inhibition of platelet aggregation induced by adenosine diphosphate or connective tissue particles. Serotonin release by connective tissue particles is probably not inhibited by FDP.

* This study was partially supported by Grant# HE-0500:3-06, National Institutes of Health, U.S. Public Health Service.


 

  • References

  • 1 Niewiarowski S, Kowalski E. Un nouvel anticoagulant dérivé du fibrinogène. Rev. Hémat 13: 320 1958;
    PubMedGoogle Scholar
  • 2 Triantaphyllopoulos D. G. Nature of the thrombin-inhibiting effect of incubated fibrinogen. Amer. J. Physiol 197: 575 1959;
    PubMedGoogle Scholar
  • 3 Fletcher A. P, Alkjaersig N, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (‘‘fibrinolytic”) states. I. The significance of fibrinogen proteolysis and circulating fibrinogen breakdown products. J. clin. Invest 41: 896 1962;
    CrossrefPubMedGoogle Scholar
  • 4 Latallo Z. S, Fletcher A. P, Alkjaersig N, Sherry S. Inhibition of fibrin polymerization by fibrinogen proteolysis products. Amer. J. Physiol 202: 681 1962;
    PubMedGoogle Scholar
  • 5 Alkjaersig N, Fletcher A. P, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (“fibrinolytic”) states. II. The significance, mechanism and consequences of defective fibrin polymerization. J. clin. Invest 41: 917 1962;
    CrossrefPubMedGoogle Scholar
  • 6 Bang N. U, Fletcher A. P, Alkjaersig N, Sherry S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic (“fibrinolytic”) states. III. Demonstration of abnormal clot structure by electron microscopy. J. clin. Invest 41: 935 1962;
    PubMedGoogle Scholar
  • 7 Latallo Z. S, Budzynski A. Z, Lipinski B, Kowalski E. Inhibition of thrombin and of fibrin polymerization, two activities derived from plasmin-digested fibrinogen. Nature (Lond) 203: 1184 1964;
    CrossrefPubMedGoogle Scholar
  • 8 Kowalski E, Kopec M, Wegrzynowicz Z. Influence of fibrinogen degradation products (FDP) on platelet aggregation, adhesiveness and viscous metamorphosis. Thrombos. Diathes. haemorrh. (Stuttg) 10: 406 1964;
    PubMedGoogle Scholar
  • 9 Johnson A. J, McCarty W. R, Titlet W. S, Tse A. O, Skoza L, Newmcm J, Semar M. Fibrinolytic, caseinolytic and biochemical methods for the study of thrombolysis in man: Application and standardization. In: Blood Coagulation, Hemorrhage & Thrombosis. Eds. Tocantins L. M, Kazal L. A. 449 Grune & Stratton; New York: 1964
    Google Scholar
  • 10 Spaet T. H, Zucker M. B. Mechanism of platelet plug formation and role of adenosine diphosphate. Amer. J. Physiol 206: 1267 1964;
    PubMedGoogle Scholar
  • 11 Kowalski E, Budzynski A. Z, Kopec N, Latallo Z. S, Lipinski B, Wegrzynowicz Z. Studies on the molecular pathology and pathogenesis of bleeding in severe fibrinolytic states in dogs. Thrombos. Diathes. haemorrh. (Stuttg) 12: 69 1964;
    PubMedGoogle Scholar
  • 12 Bray G. A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Ann. Biochem 01: 279 1960;
    CrossrefPubMedGoogle Scholar
  • 13 Triantaphyllopoulos D. G, Triantaphyllopoulos E. Anticoagulants derived from plasmino- lysed fibrinogen. 13th Annual Symposium on Blood. Wayne State University School of Medicine. Thrombos. Diathes. haemorrh. (Stuttg) 13: 585 1965;
    PubMedGoogle Scholar
  • 14 Wallén P, Bergström K. Action of thrombin on plasmin digested fibrinogen. Acta chem. scand 12: 594 1958;
    CrossrefPubMedGoogle Scholar
  • 15 Salmon J, Bounameaux Y. Etude des antigènes des plaquettes et en particulier du fibrinogène. Thrombos. Diathes. haemorrh. (Stuttg) 02: 93 1958;
    PubMedGoogle Scholar
  • 16 Nachman R. L. Immunologie studies of platelet protein. Blood 25: 703 1965;
    PubMedGoogle Scholar
  • 17 Born G. V. R, Gross M. J. The aggregation of blood platelets. J. Physiol. (Lond) 168: 178 1963;
    CrossrefPubMedGoogle Scholar
  • 18 Hovig T. Release of platelet - aggregating substance (adenosine diphosphate) from rabbit blood platelets induced by saline “extracts” of tendons. Thrombos. Diathes. haemorrh. (Stuttg) 09: 264 1963;
    PubMedGoogle Scholar
  • 19 Salzman E. W, Chambers D. A. Inhibition of ADP-induced platelet aggregation by substituted amino acids. Nature (Lond) 204: 698 1964;
    PubMedGoogle Scholar
  • 20 Zucker M. B, Jerushalmy Z. Effects of inhibitors of platelet aggregation on platelet degranulation and release. Blood 25: 603 1965;
    PubMedGoogle Scholar
  • 21 Jerushalmy Z, Skoza L, Zucker M. B. Inhibition of ADP-induced platelet clumping. Fed. Proc. 24/402 1965
    PubMedGoogle Scholar
  • 22 Hawk P. B, Oser B. L, son Summer W. H. Practical Physiological Chemistry. 122 McGraw-Hill Book Co; New York: 1954
    Google Scholar
  • 23 Sherry S, Fletcher A. P, Alkjaersig N. Fibrinolysis and fibrinolytic activity in man. Physiol. Rev 39: 343 1959;
    CrossrefPubMedGoogle Scholar