Plasminogen (PLG) and Fibrin (FBN) (PLG/FBN)

Plasminogen and fibrin are the primary protein components of the endogenous fibrinolytic system, which maintains vascular patency by dissolving blood clots (Weisel & Litvinov, 2017). Plasminogen is a proenzyme that, upon binding to fibrin, is activated into plasmin, a serine protease that degrades the fibrin matrix (Cellai et al., 2004). In pathological environments characterized by high levels of reactive oxygen species (ROS), such as myocardial infarction or chronic inflammation, these proteins undergo oxidative modifications (Standeven et al., 2005). Oxidative stress can lead to the formation of carbonylated fibrinogen, which polymerizes into a dense, lysis-resistant fibrin network (Undas et al., 2009). Furthermore, ROS can directly damage plasminogen and its activators, significantly reducing the efficiency of clot dissolution (Whittington et al., 2012). This modified state is a major contributor to thrombolytic resistance, where standard fibrinolytic drugs fail to effectively clear occlusions. Therapeutic strategies often involve using recombinant tissue plasminogen activators to overcome this resistance, though the oxidative environment remains a challenge. Understanding the interaction between ROS and the fibrinolytic machinery is crucial for developing more effective treatments for thrombotic disorders.

Other names

Oxidized fibrinOxidized fibrinogenROS-modified fibrinolytic systemCarbonylated fibrinogenNitrated fibrinogen

Activation of the zymogen plasminogen into the active serine protease plasmin, which subsequently cleaves fibrin polymers into soluble degradation products; oxidative modification of these components typically impairs this process (Cellai et al., 2004; Standeven et al., 2005).