Thromb Haemost 1988; 60(02): 293-297
DOI: 10.1055/s-0038-1647047
Original Article
Schattauer GmbH Stuttgart

Fibrinolysis Resistant Fibrin Deposits in Lymph Nodes with Hodgkin's Disease

Róza Ádány
1   The Department of Clinical Chemistry, University School of Medicine, Debrecen, Hungary and
,
Andrea Szegedi
1   The Department of Clinical Chemistry, University School of Medicine, Debrecen, Hungary and
,
Richard J Ablin
2   The Department of Urology, School of Medicine, SUNY, Stony Brook, NY, USA
,
László Muszbek
1   The Department of Clinical Chemistry, University School of Medicine, Debrecen, Hungary and
› Author Affiliations
Further Information

Publication History

Received 30 March 1988

Accepted after revision 24 June 1988

Publication Date:
28 June 2018 (online)

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Summary

Extravasal fibrin deposition is frequently observed within and around tumorous tissues and has been implicated in various aspects of tumor growth. However, no adequate information has been available on the mechanism how intratumoral interstitial fibrin deposits escape a prompt elimination by the fibrinolytic system. In this study we provide immunomorphological evidence showing that fibrin deposits in lymph nodes with Hodgkin's disease are stabilized and made resistant to fibrinolysis by factor XIII (FXIII) of blood coagulation. By double immuno- fluorescent labelling systems fibrin deposits were simultaneously stained for α2-antiplasmin (α2-AP), the main physiological inhibitor of fibrinolysis and in a number of nodular areas they were also labelled for plasmin (ogen). The detection of α2-antiplasmin-plasmin complex-neoantigen (α2-AP-P-Neo) revealed that α2-AP reacted with plasmin, i.e., α2-AP covalently linked to fibrin indeed inhibited intratumoral fibrinolysis. In addition to fibrin deposits FXIII was also found in cellular elements characterized earlier as tumor associated macrophages. These cells were attached to fibrin strands suggesting that they are involved in the intratumoral fibrin formation and might be a source of fibrin stabilizing factor in the tumor stroma.