An alternative pathway for fibrinolysis is activated in patients who have undergone cardiopulmonary bypass surgery and major abdominal surgery.

Introduction: We conducted this prospective study in order to investigate the hypotheses that an alternative pathway for fibrinolysis is activated in patients who have undergone cardiopulmonary bypass (CPB) surgery and major abdominal surgery and that the levels of fibrin degradation products digested by polymorphonuclear neutrophil elastase (elastase-XDP) and the D-dimer increase in the patients plasma. Materials and methods: We studied a total of 77 patients who were scheduled to undergo either CPB surgery (36 patients) or major abdominal surgery (41 patients) and then measured the elastase-XDP and D-dimer levels at several time points both during and after the surgeries. The CPB surgery was divided into surgery for aortic dissection (AD) and cardiac surgery. The major abdominal surgery consists of hepatic resection and esophagectomy. Results: The elastase-XDP and D-dimer levels significantly increased in the patients who underwent both CPB surgery and major abdominal surgery. The elastase-XDP levels in AD surgery showed highest values at the end of the CPB, while the levels in the other surgeries reached their peak on the day after the surgery. Statistical difference was seen in the levels of elastase-XDP among the three subgroups undergoing a hepatic resection. While we found significant correlations between the levels of elastase-XDP and D-dimer in patients undergoing CPB surgery and a subsegmentectomy of a cirrhotic liver, the correlation coefficients were markedly low in comparison to those of the other surgeries. Conclusions: Our findings demonstrated that the elastase-mediated pathway of fibrinolysis is activated to varying degrees depending on the surgery performed. Variations in the correlation coefficients between the levels of elastase-XDP and D-dimer may suggest that elastase-Mediated fibrinolysis play a different rote from the physiological fibrinolysis mediated by plasmin. (c) 2006 Elsevier Ltd. All rights reserved.