The excess thrombin cleaves fibrinogen, which ultimately leaves behind multiple fibrin clots in the circulation. CD44 glycosylation also directly controls its binding capacity to fibrin and immobilized fibrinogen. The alpha angle represents the thrombin burst and conversion of fibrinogen to fibrin. Platelet activation in turn degranulates and releases factor V and fibrinogen, potentiating the coagulation cascade. It is a receptor for fibrinogen and von Willebrand factor and aids platelet activation. The remaining amount consists mainly of albumin, globulins, fibrinogen and coagulation factors. The result is influenced by coagulation factors, platelets, fibrinogen and heparin. The deficiency may be caused by adhesion of platelets with immobilised fibrinogen. These include antifibrinolytics, blood coagulation factors, fibrinogen, and vitamin K. The fibrinolytic system then functions to break down fibrinogen and fibrin. Thrombin triggers the binding of the adhesive platelets with vWF and fibrinogen. PLA then modifies the integrin membrane glycoprotein IIb/IIIa, increasing its affinity to bind fibrinogen. Findings may include low platelets, low fibrinogen, high INR, or high D-dimer. When GPIIb/IIIa receptor is dysfunctional, fibrinogen cannot cross-link platelets, which inhibits primary hemostasis. "S. aureus" expresses surface receptors for fibrinogen, fibronectin, and vitronectin.