Fibrinolysis resistant fibrin deposits in lymph nodes with Hodgkin's disease
Adány, R.; Szegedi, A.; Ablin, R.J.; Muszbek, L.
Thrombosis and Haemostasis 60(2): 293-297
1988
ISSN/ISBN: 0340-6245 PMID: 3064359 Document Number: 309606
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 immunofluorescent labelling systems fibrin deposits were simultaneously stained for .alpha.2-antiplasmin (.alpha.2-AP), the main physiological inhibitor of fibrinolysis and a number of nodular areas they were also labelled for plasmin(ogen). The detection of .alpha.2-antiplasmin-plasmin complex-neoantigen (.alpha.2-AP-P-Neo) revealed that .alpha.2-AP reacted with plasmin, i.e., .alpha.2-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.