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Thromb Haemost 1984; 52(03): 343-346
DOI: 10.1055/s-0038-1661210
Original Article
Schattauer GmbH Stuttgart

Defective Fibrin Crosslinking in Acute Leukemia

F Rodeghiero
1   The Divisione di Ematologia, Ospedale Regionale Vicenza, Italy
,
T Barbui
2   The Divisione di Ematologia, Ospedali Riuniti, Bergamo, Italy
,
A Dal Belin-Peruffo
3   The Università di Padova, Facoltà di Agraria, Italy
,
E Dini
1   The Divisione di Ematologia, Ospedale Regionale Vicenza, Italy
› Author Affiliations
Further Information

Publication History

Received 18 June 1984

Accepted 03 October 1984

Publication Date:
19 July 2018 (online)

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Summary

Fibrin crosslinking was assayed in 22 patients with acute leukemia showing secondary coagulation abnormalities of variable severity. In 9 patients fibrin crosslinking was found to be normal, whereas 10 patients presented impaired polymerization of α-chains and 3 of both α- and γ-chains.

Only a rough correlation was found between transamidating activity of factor XIII and the fibrin crosslinking pattern in these patients. Moreover, incomplete fibrin crosslinkage occurred at levels of factor XIII far in excess of that required for full polymerization of fibrin in “normal” plasma. This latter finding suggests that, in addition to factor XIII deficiency, other causes are responsible for thehigh rate of fibrin crosslinking impairment in acute leukemia.

Key words

Factor XIII - Fibrin crosslinking - Acute leukemia - Disseminated intravascular coagulation
 

  • References

  • 1 Schwartz ML, Pizzo SU, Hill RL, McKee PA. Human Factor XIII from plasma and platelets. J Biol Chem 1973; 248: 1395-1407
    PubMedGoogle Scholar
  • 2 Chen R, Doolittle RF. Identification of the polypeptide chains involved in the cross-linking of fibrin. Proc Natl Acad Sei USA 1969; 63: 420-427
    CrossrefPubMedGoogle Scholar
  • 3 McKee PA, Mattock P, Hill RL. Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc Natl Acad Sei USA 1970; 66: 738-744
    CrossrefPubMedGoogle Scholar
  • 4 Gaffney PJ, Whitaker AN. Fibrin crosslinks and lysis rates. Thromb Res 1979; 14: 85-94
    CrossrefPubMedGoogle Scholar
  • 5 Shen L, Lorand L. Contribution of fibrin stabilization to clot strength. J Clin Invest 1983; 71: 1336-1341
    CrossrefPubMedGoogle Scholar
  • 6 Lorand L, Losowski MS, Miloszewski KG M. Human Factor XIII: Fibrin stabilizing factor. In: Progress in Haemostasis and Thrombosis. Spaet TN. (Ed) Grune & Stratton Inc; New York: 1980. 5 245-290
    Google Scholar
  • 7 Barbui T, Rodeghiero F, Dini E. Factor XIII subunits -A and -S in congenital deficiency and in acute myeloblastic leukaemia. Haematologica 1974; 59: 458-466
    PubMedGoogle Scholar
  • 8 Havemann K, Egbring R, Gropp C, Schmidt M, Sodomann CP. Factor-XIII-Mangel bei akuter Leukämie des Erwachsenen. Ergebnisse einer Substitution mit Faktor XIII Klin Wochenschr 1977; 55: 801-809
    CrossrefPubMedGoogle Scholar
  • 9 Kreissei M, Oehme J. Faktor-XIII-Aktivität im Plasma bei akuter Leukämie im Kindesalter. Klin Paediatr 1973; 185: 267-270
    PubMedGoogle Scholar
  • 10 Rasche M, Dietrich M, Hiemeyer V. Untersuchungen über die Faktor-XIII-Aktivität im Plasma bei akuter Leukämie. Klin Wochenschr 1972; 50: 1017-1019
    CrossrefPubMedGoogle Scholar
  • 11 Bennet JM, Catowski B, Daniel MT, Flandrin G, Galton DA G, Gralnick HR, Sultan C. Proposals for the classification of the acute leukaemias. Br J Haematol 1976; 33: 451-458
    CrossrefPubMedGoogle Scholar
  • 12 Rodeghiero F, Barbui T, Dal Belin A. Simplified method for the polyacrilamide gel electrophoresis of fibrin. Giornale Arteriosclerosi 1977; 2: 23-29
    PubMedGoogle Scholar
  • 13 Rodeghiero F, Barbui T. Fibrin cross-linking in congenital factor XIII deficiency. J Clin Pathol 1980; 33: 434-437
    CrossrefPubMedGoogle Scholar
  • 14 Finlayson GS, Morton RO. Gel electrophoresis for assessing fibrin cross-linking: a precaution. Clin Chim Acta 1972; 36: 254-256
    CrossrefPubMedGoogle Scholar
  • 15 Barbui T, Rodeghiero F, Dini E, Mariani G, Papa ML, De Biasi R, Cordero Murillo R, Montero Umana C. Subunit -A and -S inheritance in four families with congenital factor XIII deficiency. Br J Haematol 1978; 38: 267-271
    CrossrefPubMedGoogle Scholar
  • 16 Rodeghiero F, Barbui T, Battista R, Chisesi T, Rigoni E, Dini E. Molecular subunits and transamidase activity of factor XIII during disseminated intravascular coagulation in acute leukaemia. Thromb Haemostas 1980; 43: 6-9
    PubMedGoogle Scholar
  • 17 Egbring R, Schmidt W, Fuchs G, Havemann K. Demonstration of granulocyte proteases in plasma of patients with acute leukaemia and septicaemia with coagulation defects. Blood 1977; 49: 219-231
    PubMedGoogle Scholar
  • 18 Rasche M, Dietrich M, Gaus W, Schleyer M. Factor-XIII-activity and fibrin structure in acute leukaemia. Biomedicine 1974; 21: 61-66
    PubMedGoogle Scholar
  • 19 Bohn M. Immunologische Untersuchungen über Faktor XIII und das FSF-bindende Globulin. Blut 1974; 28: 81-89
    CrossrefPubMedGoogle Scholar
  • 20 Rodeghiero F, Morbin M, Barbui T. Subunit A of factor XIII regulates subunit B plasma concentration. Thromb Haemostas 1981; 46: 621-622
    PubMedGoogle Scholar
  • 21 Niewiarowski S, Stewart GJ, Marder VJ. Formation of highly ordered polymers from fibrinogen and fibrin degradation products. Biochim Biophys Acta 1970; 221: 326-341
    CrossrefPubMedGoogle Scholar
  • 22 Schwartz ML, Pizzo SU, Hill RL, McKee PA. The effect of fibrin stabilizing factor on the subunit structure of human fibrin. J Clin Invest 1971; 50: 1506-1513
    CrossrefPubMedGoogle Scholar
  • 23 Duckert F. Documentation of the plasma factor XIII deficiency in man. Ann NY Acad Sei 1972; 202: 190-199
    CrossrefPubMedGoogle Scholar
  • 24 Lisiewicz G. Mechanisms of hemorrage in leukemias. Semin Thromb Haemostas 1978; 4: 241-267
    Article in Thieme ConnectPubMedGoogle Scholar
  • 25 Mosesson MW, Finlayson JS, Umfleet RA, Galanakis D. Human fibrinogen heterogeneties. 1.Structural and related studies of plasma fibrinogens which are high solubility catabolic intermediates. J Biol Chem 1972; 247: 5210-5219
    PubMedGoogle Scholar