Pancreatic Phospholipase A₂ Induces Bacterial Translocation In Rats

Abstract

The importance of pancreatic enzymes, particularly phospholipase A₂ (PLA₂), for bacterial translocation, which is considered to be one of the aggravating causes of acute pancreatitis, was investigated. Male rats were administered an intraperitoneal or intravenous injection of normal saline, PLA₂, or amylase. Four days later, the mesenteric lymph nodes (MLNs) and portal blood of the animals were cultured. None of the animals had a positive portal blood culture. The MLNs contained enteric bacteria in 78 % of the animals given 50 mg/kg of PLA₂ intraperitoneally. 5 mg/kg of PLA₂ intraperitoneally, 50 mg/kg of amylase intraperitoneally, or 50 mg/kg of PLA₂ intravenously showed positive cultures in 25 %, 20 %, and 11 %, respectively. None of the animals given intraperitoneal or intravenous normal saline had positive cultures of their MLNs. Intraperitoneal injection of 25mg/kg of nafamostat mesilate just before intraperitoneal PIA₂ (50 mg/kg) resulted in a reduction of positive MLNs from 70 % to 30 %. The cecal myeroperoxidase (MPO) activity of animals administered 50 mg/kg of PIA₂ intraperitoneally was significantly higher compared with animals administered saline intraperitoneally. These results indicate that intraperitoneal leakage of PLA₂ plays an important role in bacterial translocation during acute pancreatitis and that administration of a protease inhibitor may be effective against the bacterial translocation.