Thromb Haemost 1980; 44(03): 146-149
DOI: 10.1055/s-0038-1650106
Original Article
Schattauer GmbH Stuttgart

Catabolism of Human Fibrinogen Fragment D in Normal Subjects and Patients with Liver Cirrhosis

Nicole Ardaillou
The Department of Coagulation INSERM U. 143, Institut de Pathologie Cellulaire and from the Department of Nuclear Medicine and of Internal Medicine, Hôpital Bicêtre, Kremlin-Bicêtre, France
,
Jeannine Yvart
The Department of Coagulation INSERM U. 143, Institut de Pathologie Cellulaire and from the Department of Nuclear Medicine and of Internal Medicine, Hôpital Bicêtre, Kremlin-Bicêtre, France
,
Philippe Le Bras
The Department of Coagulation INSERM U. 143, Institut de Pathologie Cellulaire and from the Department of Nuclear Medicine and of Internal Medicine, Hôpital Bicêtre, Kremlin-Bicêtre, France
,
Marie-José Larrieu
The Department of Coagulation INSERM U. 143, Institut de Pathologie Cellulaire and from the Department of Nuclear Medicine and of Internal Medicine, Hôpital Bicêtre, Kremlin-Bicêtre, France
› Author Affiliations
Further Information

Publication History

Received 04 August 1980

Accepted 29 September 1980

Publication Date:
13 July 2018 (online)

Summary

The catabolism of human fragment D, (FgD), obtained by plasmin digestion of fibrinogen has been investigated in normal subjects and patients with liver cirrhosis and the results compared with those obtained for fibrinogen (Fg). Fg was labelled with I-125 and Fg D with I-131 using the chloramine T method. The plasma disappearance curves of both labelled proteins fitted a two exponential curve. In controls the plasma clearance rate of Fg D was greater than that of Fg as shown by the marked difference between the half-lives of these two tracers: 8,9 and 83,5 hours for Fg D and Fg respectively. The fractional catabolic rate of Fg D was 3.38 times the plasma pool per day. In nine patients with liver cirrhosis, catabolism of Fg was not modified. In contrast, catabolism of Fg D was significantly reduced with a half life of 13.0 hours and a low fractional catabolic rate. These results suggest the role of the liver in the catabolism of Fg D in man.

 
  • References

  • 1 McFarlane AS, Todd D, Cromwell S. Fibrinogen catabolism in human. Clin Sci 1964; 26: 415-420
  • 2 Blomback B, Carlson LA, Franzen S, Zetterqvist E. Turnover of 131I-labelled fibrinogen in man. Studies in normal subjects in congenital coagulation factor deficiency states, in liver cirrhosis, in polycytemia vera and in epidermolysis bullosa. Acta Med Scand 1966; 179: 557-574
  • 3 Collen D, Tytgat GN, Claeys H, Piessens R. Metabolism and distribution of fibrinogen. I. Fibrinogen turnover in physiological conditions in humans. Br J Haematol 1972; 22: 681-700
  • 4 Tytgat GN, Collen D, Verstraete M. Metabolism of fibrinogen in cirrhosis of the liver. J Clin Invest 1971; 50: 1690-1701
  • 5 Tytgat GN, Collen D, Vermylen J. Metabolism and distribution of fibrinogen. II. Fibrinogen turnover in polycythaemia, thrombocytosis, haemophilia A, congenital afibrinogemia and during streptokinase therapy. Br J Haematol 1972; 22: 701-717
  • 6 Ardaillou N, Sraer JD, Beaufils P. Fibrinogen kinetics in chronic renal failure of various causes. Biomedicine (Express) 1974; 21: 49-56
  • 7 Hayne OA, Sherman LA. In vivo behavior of fragment D in experimental renal, hepatic and reticulo endothelial dysfunction. Am J Pathol 1973; 71: 219-236
  • 8 Catanzaro A, Edgington TS. The in vivo behavior of the terminal derivatives of fibrinogen and fibrin cleaved by plasmin. J Lab Clin Med 1974; 83: 458-466
  • 9 Ardaillou N, Dray L, Budzynski AZ, Marder VJ, Larrieu MJ. The half-life of plasmic degradation products of human fibrinogen in rabbits. Throm Haemostas 1977; 37: 201-209
  • 10 Lattalo ZS, Budzynski AZ, Lipinski B, Kowalski E. Inhibition of thrombin and fibrin polymerization. Two activities derived from plasmin digested fibrinogen. Nature 1964; 203: 1184-1185
  • 11 Larrieu MJ, Dray L, Ardaillou N. Biological effects of fibrinogen fibrin degradation products. Thromb Diath Haemmorrh 1975; 34: 686-692
  • 12 Barnhart MI, Cress DC, Noonan SH, Walsh RT. Influence of fibrinolytic products on hepatic release and synthesis of fibrinogen. Thromb Diath Haemorrh suppl 1970; 39: 143-159
  • 13 Kessler CM, Bell WR. The effect of homologous thrombin and fibrinogen degradation products on fibrinogen synthesis in rabbit. J Lab Clin Med 1979; 93: 768-782
  • 14 Kessler CM, Bell WR. Stimulation of fibrinogen synthesis: A possible functional role for fibrinogen degradation products. Blood 1980; 55: 40-47
  • 15 Ittyerah TR, Weidner N, Wochner RD, Sherman LA. Effect of fibrin degradation products and thrombin on fibrinogen synthesis. Br J Haematol 1979; 43: 661-668
  • 16 Ahlgren T, Berghem L, Lahnborg G. Phagocytic and catabolic function of the reticulo-endothelial system in dogs subjected to defrinogenation: Kupffer cells and other liver sinusoidal cells. Wisse E, Knook DL. ed. North Holland Biomedical Press Amsterdam: 1977: 373-378
  • 17 Scheidegger JJ. Une microméthode de l'immunoélectrophorèse. Int Arch Allergy Appl Immunol 1955; 7: 103-110
  • 18 Weber K, Osborn M. The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis:. J Biol Chem 1969; 244: 4406-4412
  • 19 Caen J, Larrieu MJ, Samama M. L'Hémostase. Méthodes d'exploration et diagnostic pratique. Expansion Scientifique 2ème édition 1975
  • 20 Gordon YB, Martin MJ, Landon J, Chard T. The development of radioimmunoassays for fibrinogen degradation products: fragments D and E. Br J Haematol 1975; 29: 109-119
  • 21 Bradley J, Hickman JA. Behaviour of commercially prepared I-125 fibrinogen in metabolic studies. J Clin Pathol 1975; 28: 487-493
  • 22 Marder VJ, James HL, Sherry S. The purification of fibrinogen degradation products by Pevikon block electrophoresis. Thromb Diath Haemorrh 1969; 22: 234-239
  • 23 Hunter WM, Greenwood FC. Preparation of iodine 131 labelled human growth hormone of high specific activity. Nature 1962; 194: 495-496
  • 24 Regoeczi E. Iodine labelled fibrinogen: a review:. Br J Haematol 1971; 20: 649-662
  • 25 Iio A, Rutherford EW, Wochner DR, Spilberg I, Sherman LA. The roles of renal catabolism and uremia in modifying the clearance of fibrinogen and its degradation fragments D and E. J Lab Clin Med 1976; 87: 934-946
  • 26 Sherman LA, Lee J. Specific binding of soluble fibrin to macrophages. J Exp Med 1977; 145: 76-85