Oxidized fibrin(ogen) derivatives enhance the activity of tissue type plasminogen activator

Oxidation of fibrinogen degradation products (FDP) with chloramines, results in a five- fold increase of their property to stimulate plasminogen activation by tissue type plasminogen activator (t-PA). Binding studies with immobilized stimulators demonstrated greater affinity of t-PA to oxidized than to unmodified FDP. The fibrin (ogen) domain responsible for this oxidant mediated increase in t-PA stimulation is localized in the D- subunit of fibrin(ogen). Thus, experimental data with (oxidized) I-labelled fibrin(ogen) should be interpreted with caution: the oxidized product might behave in a distinct manner than the unoxidized, native, one. As activated leukocytes release large amounts of oxidants of the chloramine type (Weiss et al., Science 222, 625-628, 1983), oxidation of fibrin might contribute significantly to fibrinolysis and proteolysis in areas of inflammation. The data give further evidence for an involvement of physiological components of haemostasis in non haemostasis but inflammation related processes.