TY - JOUR
T1 - Fibrinolysis resistant fibrin deposits in lymph nodes with Hodgkin's disease
AU - Adany, R.
AU - Szegedi, A.
AU - Ablin, R. J.
AU - Muszbek, L.
PY - 1988
Y1 - 1988
N2 - 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 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.
AB - 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 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.
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U2 - 10.1055/s-0038-1647047
DO - 10.1055/s-0038-1647047
M3 - Article
C2 - 3064359
AN - SCOPUS:0023798810
SN - 0340-6245
VL - 60
SP - 293
EP - 297
JO - Thrombosis and Haemostasis
JF - Thrombosis and Haemostasis
IS - 2
ER -