Download PDF
Thromb Haemost 1981; 45(01): 090-094
DOI: 10.1055/s-0038-1650136
Original Article
Schattauer GmbH Stuttgart

Permeability Enhancing and Chemotactic Activities of Lower Molecular Weight Degradation Products of Human Fibrinogen

Katsuo Sueishi
The Department of Pathology, Faculty of Medicine, Kyushu University, Fukuoka, Japan
,
Shigeru Nanno
The Department of Pathology, Faculty of Medicine, Kyushu University, Fukuoka, Japan
,
Kenzo Tanaka
The Department of Pathology, Faculty of Medicine, Kyushu University, Fukuoka, Japan
› Author Affiliations
Further Information

Publication History

Received 05 May 1980

Accepted 20 October 1980

Publication Date:
04 July 2018 (online)

Also available at
  PDF Download  Permissions and Reprints

Summary

Fibrinogen degradation products were investigated for leukocyte chemotactic activity and for enhancement of vascular permeability. Both activities increased progressively with plasmin digestion of fibrinogen. Active fragments were partially purified from 24 hr-plasmin digests. Molecular weights of the permeability increasing and chemotactic activity fractions were 25,000-15,000 and 25,000 respectively. Both fractions had much higher activities than the fragment X, Y, D or E. Electron microscopic observation of the small blood vessels in rabbit skin correlated increased permeability with the formation of characteristic gaps between adjoining endothelial cells and their contraction.

These findings suggest that lower molecular weight degradation products of fibrinogen may be influential in contributing to granulocytic infiltration and enhanced permeability in lesions characterized by deposits of fibrin and/or fibrinogen.

Keywords

Lower molecular weight FDP - Permeability - Chemotactic activity
 

  • References

  • 1 Godal HC, Helle I. The influence of fibrinogenolytic and fibrinolytic split products on the last stage of coagulation. Scand J Clin Lab Invest 1963; 15: 327-338
    CrossrefPubMedGoogle Scholar
  • 2 Kowalski E. Fibrinogen derivatives and their biological activities. Semin Hematol 1968; 5: 45-59
    PubMedGoogle Scholar
  • 3 Marder VJ, Shulman NR. High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity. J Biol Chem 1969; 244: 2120-2124
    PubMedGoogle Scholar
  • 4 Mitchell PS, Beller FK. Quantitation of the coagulation inhibition in vivo due to breakdown products of fibrin. Thromb Diath Haemorrh 1970; 23: 477-485
    PubMedGoogle Scholar
  • 5 Larrieu MJ, Rigollot C, Marder VJ. Comparative effects of fibrinogen degradation fragments D and E on coagulation. Br J Haematol 1972; 22: 719-733
    CrossrefPubMedGoogle Scholar
  • 6 Arnesen H. The effect of products D and E on the thrombin induced conversion of fibrinogen to fibrin. Scand J Haematol 1974; 12: 165-172
    PubMedGoogle Scholar
  • 7 Niewiarowski S, Gurewich V. Laboratory identification of intravascular coagulation. The serial dilution protamine sulfate test for the detection of fibrin monomer and fibrin degradation products. J Lab Clin Med 1971; 77: 665-676
    PubMedGoogle Scholar
  • 8 Clarkson AR, MacDonald MK, Cash JD, Robson JS. Modification by drugs of urinary fibrin/fibrinogen degradation products in glomerulonephritis. Br Med J 1972; 3: 255-260
    CrossrefPubMedGoogle Scholar
  • 9 Marder VJ, Cruz GO, Schumer BR. Evaluation of a new antifibrinogen-coated latex particle agglutination test in the measurement of serum fibrin degradation products. Thromb Haemostas 1977; 37: 183-191
    PubMedGoogle Scholar
  • 10 Stachurska J, Latallo Z, Kopeé M. Inhibition of platelet aggregation by dialysable fibrinogen degradation products (FDP). Thromb Diath Haemorrh 1970; 23: 91-98
    PubMedGoogle Scholar
  • 11 Buczko W, De GaetanoG, Franco R, Donati MB. Biological properties of dialysable peptides derived from plasmin digestion of bovine fibrinogen preparations. Thromb Haemostas 1976; 35: 651-657
    PubMedGoogle Scholar
  • 12 Takaki A, Ishiguro M, Funatsu M. Anticoagulant peptide obtained from fibrinogen degradation products by plasmin. Proc Japan Acad 1972; 48: 528-533
    CrossrefPubMedGoogle Scholar
  • 13 McKenzie R, Pepper DS, Kay AB. The generation of chemotactic activity for human leukocytes by the action of plasmin on human fibrinogen. Thromb Res 1975; 6: 1-8
    CrossrefPubMedGoogle Scholar
  • 14 Richardson DL, Pepper DS, Kay AB. Chemotaxis for human monocytes by fibrinogen-derived peptides. Br J Haematol 1976; 32: 507-513
    CrossrefPubMedGoogle Scholar
  • 15 Malofiejew M. The biological and pharmacological properties of some fibrinogen degradation products. Scand J Haematol 1971; Suppl. 13: 303-308
    PubMedGoogle Scholar
  • 16 Solum NO, Rigollot C, Budzyñski AZ, Marder VJ. A quantitative evaluation of the inhibition of platelet aggregation by low molecular weight degradation products of fibrinogen. Br J Haematol 1973; 24: 419-434
    CrossrefPubMedGoogle Scholar
  • 17 Mosseson MW, Sherry S. The preparation of properties of human fibrinogen of relatively high solubility. Biochemistry 1966; 5: 2829-2835
    CrossrefPubMedGoogle Scholar
  • 18 Marder VJ, James HL, Sherry S. The purification of fibrinogen degradation products by pevikon block electrophoresis. Thromb Diath Haemorrh 1969; 22: 234-239
    PubMedGoogle Scholar
  • 19 Fairbanks G, Steck TL, Wallach DFH. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 1971; 10: 2606-2617
    CrossrefPubMedGoogle Scholar
  • 20 Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265-275
    PubMedGoogle Scholar
  • 21 Ward PA, Cochrane CG, Müller-Eberhard HJ. The role of serum complement in chemotaxis of leukocytes in vitro. J Exp Med 1965; 122: 327-346
    CrossrefPubMedGoogle Scholar
  • 22 Nitta R, Hayashi H, Norimatsu K. Quantitative extraction of pontamine blue from skin; Its application for measurement of increased capillary permeability. Proc Soc exp Biol Med 1963; 113: 185-187
    CrossrefPubMedGoogle Scholar
  • 23 Luft JH. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol 1961; 9: 409-414
    CrossrefPubMedGoogle Scholar
  • 24 Henry RL. Leykocytes and thrombosis. Thromb Diath Haemorrh 1965; 13: 35-46
    PubMedGoogle Scholar
  • 25 Koga M. Experimental study on resolution and organization of thrombi in pulmonary arteries of rabbits. Fukuoka Igaku Zasshi 1971; 62: 525-540
    PubMedGoogle Scholar
  • 26 Hisano S, Sueishi K, Ishii Y, Tanaka K. Immunohistochemical and histochemical investigations on in vivo thrombosis with urokinase in rabbits. Thromb Haemostas 1979; 41: 796-803
    PubMedGoogle Scholar
  • 27 Barnhart MI, Sulisz L, Bluhm GB. Role for fibrinogen and its derivatives in acute inflammation. In Forscher BK, Houck JC. (ed) Immunopathology of Inflammation (Excerpta Medica. International congress series, No 229). Amsterdam: 1971: 59-65
    Google Scholar
  • 28 Tanaka K. Role of fibrinolysis in various pathological conditions. Tr Soc Path Jap 1977; 66: 03-26
    PubMedGoogle Scholar
  • 29 Stewart GJ. The intravascular generation of fibrinogen derivatives and the blood vessel wall in venous thrombosis and disseminated intravascular coagulation. Thromb Haemostas 1977; 38: 831-849
    PubMedGoogle Scholar
  • 30 Barnhart MI. Role of blood coagulation in acute inflammation. In Houck JC, Forscher BK. (ed) Brook Lodge Conference on Inflammation, Augusta, Mich., 1967. Chemical Biology of Inflammation. Pergamon Press; Oxford: 1968: 205-218
    Google Scholar
  • 31 Stecher VJ, Sorkin E. The chemotactic activity of fibrin lysis products. Int Arch Allergy Appl Immunol 1972; 43: 879-886
    CrossrefPubMedGoogle Scholar
  • 32 Wilhelm DL. Increased vascular permeability in acute inflammation. Rev Can Biol 1971; 30: 153-172
    PubMedGoogle Scholar
  • 33 Wilhelm DL. Inflammation and healing. In Anderson WAD, Kissane JM. (ed) Pathology: Mosby Co, St Louis; 1977: 25-89
    Google Scholar
  • 34 Majno G, Shea SM, Leventhal M. Endothelial contraction induced by histamine-type mediators. An electron microscopic study. J Cell Biol 1969; 42: 647-672
    CrossrefPubMedGoogle Scholar