FIBRONECTIN-FIBRIN-COMPLEXES : AN IMMUNOASSAY TO EVALUATE THEIR FUNCTION IN COAGULATION DISORDERS AND TUMOR SITUATION

O Wilhelm, R Hafter, H Graeff
1987 DIABETES   unpublished
Fibronectin and fibronectin degradation products interact with fibrin(ogen) by non-covalent and by factor XIII catalyzed covalent binding. In certain physiological or pathophysiological situations these complexes may be of considerable importance. It was the aim of this study to accumulate more information of the function of this proteininteraction. Immunoadsorption in combination with Westernblotting with different monoclonal and polyclonal antibodies demonstrate several
more » ... )-complexes in tumor ascites. For further information we established an immunoassay to measure these complexes. As the capture antibody we used a polyclonal fibronectin antibody and as the tag antibody a monoclonal fibrin(ogen) antibody. In this immunoassay we observed a decrease of these complexes from very high values during the therapy of disseminated intra-vascular coagulation besides also a decrease of high molecular weight fibrin derivatives and fibronectin split products. We also found elevated levels in ascitic fluid and plasma of patients with advanced ovarian cancer (x=202,3± SD 45.1 ng/ml fibrinogen equivalent) in comparison to a control group with benign gynecological diseases (X= 102,9± SD 14,9 ng/ml fibrinogen equivalent). In conclusion we suggest that during intravascular coagulation fibronectin binds fibrin derivatives for elimination from plasma. In the tumor situation these complexes may stem from the fibronectin-fibrin-gel-matrix surrounding the tumor by proteolytical degradation and subsequent release into the ascites, (supported by Deutsche Forschungsgemeinschaft, SFB207, A2).
doi:10.1055/s-0038-1643194 fatcat:qqlh7xduy5c73pqx6af6b4viym