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Thromb Haemost 1978; 39(01): 109-121
DOI: 10.1055/s-0038-1646661
Original Article
Schattauer GmbH Stuttgart

Enhancement of Fibrinolysis in Rabbits Exposed to Low and Moderate Levels of Carbon Monoxide Inhibited by Epsilon Amino Caproic Acid

Ekrem V Kalmaz
The Oklahoma Medical Research Foundation, Hematology Research Laboratories, Oklahoma City, Oklahoma 73104, and the NASA – Lyndon B. Johnson Space Center, Biomedical Research Division, DB-7, Houston, Texas 77058, U.S.A.
,
Larry W Canter
The Oklahoma Medical Research Foundation, Hematology Research Laboratories, Oklahoma City, Oklahoma 73104, and the NASA – Lyndon B. Johnson Space Center, Biomedical Research Division, DB-7, Houston, Texas 77058, U.S.A.
,
Robert L Coleman
The Oklahoma Medical Research Foundation, Hematology Research Laboratories, Oklahoma City, Oklahoma 73104, and the NASA – Lyndon B. Johnson Space Center, Biomedical Research Division, DB-7, Houston, Texas 77058, U.S.A.
,
James W Hampton
The Oklahoma Medical Research Foundation, Hematology Research Laboratories, Oklahoma City, Oklahoma 73104, and the NASA – Lyndon B. Johnson Space Center, Biomedical Research Division, DB-7, Houston, Texas 77058, U.S.A.
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Publikationsverlauf

Received 06. Juni 1976

Accepted 25. Mai 1977

Publikationsdatum:
12. Juli 2018 (online)

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Summary

The first (control) group of rabbits breathed ambient air whereas the second was exposed to low level carbon monoxide (CO, 50 ppm by volume) for 24 hr continuously for 8 weeks. The third group was exposed to 300 ppm CO for 4 weeks. The fourth group was exposed to 300 ppm CO for the same period of time as the third group but in addition they were also given epsilon amino caproic acid (EACA) orally, and the results compared to Group III. Per cent oxyhemoglobin (HbO2), per cent hemoglobin (Hb) and per cent carboxyhemoglobin (HbCO) were monitored in all groups. Tests of fibrinolysis were monitored and showed acceleration of the whole blood clot lysis and euglobulin lysis times (ELT). A fibrin plate test confirmed the increased lysis and serum fibrin and/or fibrinogen degradation products (FDP) were elevated in the CO exposed animals. No changes were observed in the same tests in the rabbits exposed to ambient air. The fourth group of animals receiving EACA showed inhibition of lysis and decrease in serum FDP. Alpha-1-antitrypsin and alpha-2-macroglobulin assays in all groups showed no change. Microscopic examination of the large vessels in these test groups showed endothelial damage which indicates a possible source for a plasminogen activator release, or lead to activation of Hageman factor and activated plasma plasminogen proactivator.

 

  • References

  • 1 Alkjaersig N, Fletcher AP, Sherry S. 1959; Epsilon aminocaproic acid. an inhibitor of plasminogen activation. The Journal of Biological Chemistry 234: 832
    PubMedGoogle Scholar
  • 2 Astrup P, Kjeldson K, Wanstrup J. 1967; Enhancing influence of carbon monoxide on the development of atheromatosis in cholesterol-fed rabbits. Journal of Altheroseclerosis Research 7: 343
    PubMedGoogle Scholar
  • 3 Astrup T. 1952. Physiology of fibrinolysis. Koller and Strembi (eds.), Thrombolytic Activity and Related Phenomenon . Schattauer, Stuttgart; New York:
    Google Scholar
  • 4 Astrup T, Möllertz S. 1952; The fibrin plate method for estimating fibrinolytic activity. Archives of Biochemistry and Biophysics 40: 346
    CrossrefPubMedGoogle Scholar
  • 5 Barnhart MI, Cress DC, Henry RL, Riddle JN. 1952; Influence of fibrinogen split products on platelets. Thrombosis et Diathesis Haemorrhagica 17: 78
    PubMedGoogle Scholar
  • 6 Brackman P. 1952. Fibrinolysis, a Standardized Fibrin Plate and a Fibrinolytic Assay of Plasminogen. Thesis University of Amsterdam, Scheltema and Holkema, N. V
    Google Scholar
  • 7 Brackman P, Astrup T. 1952. The fibrin plate method and fibrinolytic agents. In: Bang NU, Beller FK, Deutsch E, Mammen EF. (eds.) Thrombosis and Bleeding Disorders. Academic Press; London: 332
    Google Scholar
  • 8 Bruckner J, Desmond F. 1952; Spectrophotometric methods for the estimation of carbon monoxide hemoglobin in blood. Clinica Chimica Acta 3: 173
    PubMedGoogle Scholar
  • 9 Deutsch DG, Mertz ET. 1952; Plasminogen. purification from human plasma by affinity chromatography. Science(Washington D. C.) 170: 1095
    PubMedGoogle Scholar
  • 10 Duckert F, Jung E, Shmerling DE. 1952; A hitherto undescribed congenital haemorrhagic diathesis probably due to fibrin stabilizing factor deficiency. Thrombosis et Diathesis Haemorrhagica 5: 179
    PubMedGoogle Scholar
  • 11 Fati S, Mole R, Pecora L. 1952; Blood enzyme change during carbon monoxide exposure. Folia Medica 43: 1092
    PubMedGoogle Scholar
  • 12 Fearnley GR. 1952. Fibrinolysis. Edward Arnold Lts; London:
    Google Scholar
  • 13 Finlayson JS, Mosesson MW. 1952; Heterogeneity of human fibrinogen. Biochemistry 2: 42
    PubMedGoogle Scholar
  • 14 Gigli I, Mason JW, Colman RW. Austen 1952; Interactions of plasma kallikrein with CI inhibitor. Journal of Immunology 104: 558
    PubMedGoogle Scholar
  • 15 Grannis GF. 1952; Plasma fibrinogen. determination normal values physiopathologic shifts and fluctuations. Clinical Chemistry 16: 486
    PubMedGoogle Scholar
  • 16 Haagen-Smith AJ. 1952; Carbon monoxide levels in city driving. Archives of Environmental Health 12: 548
    PubMedGoogle Scholar
  • 17 Halperin MH, McFarland RA, Niven JI, Roughton FJW. 1952; The time course of the effect of carbon monoxide on visual thresholds. The Journal of Physiology 146: 583
    PubMedGoogle Scholar
  • 18 Johnson AJ, Semar M, Newman J. 1952. Estimation of fibrinolytic activity by whole blood eu-globulin clot lysis. In: Tocantins LM, Kazau LA. Blood Coagulation, Hemorrhage and Thrombosis. Grune and Stratton; New York: 465
    Google Scholar
  • 19 Kollias J, Jordan P. 1952; An improved system for prolonged exposure of small animals to artificial low pressure. Journal of Applied Physiology 20: 742
    PubMedGoogle Scholar
  • 20 Kowalski E, Budzynski AZ, Kopec M, Latallo ZS, Lipinski B, Wegrzynowicz Z. 1952; Studies on the molecular pathology and pathogenesis of bleeding in servere fibrinolytic states in dogs. Thrombosis et Diathesis Haemorrhagica 12: 69
    PubMedGoogle Scholar
  • 21 Kwaan HC, LO R. McFadzean 1952; Plasma fibrinolytic activity induced by ischaemia. Clinical Science 15: 245
    PubMedGoogle Scholar
  • 22 Larrieu MJ. 1952; Action of fibrinogen degradation products and fibrin monomer soluble complexes on platelet aggregation. Scandinavian Journal of Haematology suppl 13: 273
    PubMedGoogle Scholar
  • 23 Larrieu MJ, Marder VJ, Inceman S. 1952; “Effects of fibrinogen degradation products on platelets and coagulation” in Diffuse Intravascular Clotting. Transactions of the International Committee on Haemostasis and Thrombosis. 1965; Koller F, Streuli JP. 215
    PubMedGoogle Scholar
  • 24 Latallo ZS, Fletcher AP, Alkjaersig N, Sherry S. 1952; Inhibition of fibrin polymerization by fibrinogen proteolysis products. American Journal of Physiology 202: 681
    PubMedGoogle Scholar
  • 25 Lee RI, White PD. 1952; A clinical study of the coagulation time in blood. The American Journal of the Medical Sciences 145: 495
    PubMedGoogle Scholar
  • 26 Mallory FB. 1952. Pathological Techniques. W. B. Saunders; Philadelphia PA: 154
    Google Scholar
  • 27 Mancini G, Carbonaro AO, Heremans JF. 1952; Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 2: 235
    PubMedGoogle Scholar
  • 28 Marder VJ, Shulman NR. 1952; High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity. Journal of Biological Chemistry 244: 2120
    PubMedGoogle Scholar
  • 29 Marder VJ, Shulman NR, Carroll WR. 1952; The importance of intermediate degradation products of fibrinogen in fibrinolytic haemorrhage. Transactions of the Association of American Physicians 80: 156
    PubMedGoogle Scholar
  • 30 Merskey C, Lalezari P, Johnson AH. 1952; A rapid, simple, sensitive method for measuring fibrinolytic split products in human serum. Proceedings of the Society for Experimental Biology and Medicine. 131: 871
    PubMedGoogle Scholar
  • 31 Mertens BF, McDuffle FC, Bowie EJ W, Owen CA. 1952; Rapid, sensitive method for measuring fibrinogen split products in human serum. Mayo Clinic Proceedings 44: 114
    PubMedGoogle Scholar
  • 32 Miesch F, Bieth J, Metais P. 1952; The alpha-1-anti trypsin and alpha-2-macroglobulin and protease inhibiting capacity of normal and pathological sera. Clinica Chimica Acta 31: 231
    PubMedGoogle Scholar
  • 33 Niewiarowski S, Kowalski E. 1952; Anti thrombin formation during proteolysis of fibrinogen. Transactions Vlth Conference of the European Society of Haematology. 560
    PubMedGoogle Scholar
  • 34 Niewiarowski S, Kowalski E. 1952; Un nouvel anticoagulant derive du fibrinogene. Revue Hematologie 13: 320
    PubMedGoogle Scholar
  • 35 Rainoff OD, Menzie C. 1952; A new method for the determination of fibrinogen in small samples of plasma. The Journal of Laboratory and Clinical Medicine 37: 316
    PubMedGoogle Scholar
  • 36 Ratnoff OD, Pensky J, Ogston D, Naff GB. 1952; The inhibition of plasmin, plasma kalli-krein, plasma permeability factor and the C’ lr subcomponent of the first component of complement by the serum C’l esterase inhibitor. Journal of Experimental Medicine 129: 315
    PubMedGoogle Scholar
  • 37 Rozeno G, Fati S. 1952; Acid and alkaline intra-erythrocytic and serous phosphatases in chronic carbon monoxide poisoning. Folia Medica 42: 1204
    PubMedGoogle Scholar
  • 38 Sairo O, El-Attar A. 1952; Effect of carbon monoxide on the whole fibrinolytic activity. Industrial Medicine and Surgery 37: 774
    PubMedGoogle Scholar
  • 39 Triantaphyllopoulos DC. 1952; Anticoagulant effect of incubated fibrinogen. Canadian Journal of Biochemistry 36: 249
    PubMedGoogle Scholar
  • 40 Kaulla von KN. 1952. Chemistry of thrombosis. Human Fibrinolytic Enzymes. Charles C. Thomas Publisher; Springfield: Illinois 352
    Google Scholar
  • 41 Kaulla von KN. Swan 1952; Clotting deviation in man during cardiac by-pass fibrinolysis and circulating anti-coagulant. The Journal of Thoracic Surgery 26: 517
    PubMedGoogle Scholar
  • 42 Wilson PA, Mcnicol GP, Douglas AS. 1952; The effects of fibrinogen degradation products on platelet aggregation. Journal of Clinical Pathology 21: 147
    PubMedGoogle Scholar
  • 43 Winer BJ. 1952. Statistical Principles in Experimental Design. McGraw-Hill; New York: 20
    Google Scholar
  • 44 Wintrobe MM, Lee GR, Boggs DR, Bithell TC, Athens JW, Foerster J. 1952. Clinical Hematology. Lea and Febiger; Philadelphia PA: 1061
    Google Scholar