title: Enhanced endothelial cell injury by activated neutrophils in patients with obstructive jaundice.
abstract: OBJECTIVE
  A high incidence of complications has been documented in patients with obstructive jaundice after operations. Recent reports have revealed that neutrophils are involved in the mechanism causing postoperative complications. However, there are few reports investigating the interaction between neutrophils and endothelial cells in obstructive jaundice. The aim of this study was to evaluate neutrophil-mediated endothelial cell injury in patients with obstructive jaundice.
  
  
  METHODS
  Patients were divided into three groups: those with normal liver, obstructive jaundice, and relief of obstructive jaundice. Neutrophils were isolated from patients individually. Human umbilical vein endothelial cells and neutrophils were co-cultured after addition of phorbol myristate acetate. The release of lactate dehydrogenase and thrombomodulin was measured in the medium.
  
  
  RESULTS
  Lactate dehydrogenase and thrombomodulin were released in the co-culture medium, and Eglin C, which is an elastase inhibitor, reduced the release of lactate dehydrogenase and thrombomodulin in a dose-dependent manner. The release of lactate dehydrogenase and thrombomodulin in the group with relief of obstructive jaundice was significantly higher than in the group with normal liver. There was no significant difference between the group with obstructive jaundice and the group with normal liver. The elastase activity in neutrophil suspension was similarly higher in the group with relief of obstructive jaundice than in the group with normal liver.
  
  
  CONCLUSIONS
  This study suggests that neutrophils in patients with obstructive jaundice are not activated before its relief. After relief of obstructive jaundice, neutrophils are strongly primed and have the potential to cause endothelial cell injury. The neutrophil "priming" in patients with obstructive jaundice may be associated with the frequent occurrence of postoperative complications.
authors.affiliation: First Department of Surgery, School of Medicine, Chiba University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Shimizu
authors.forename: M
authors.initials: M
authors.lastname: Miyazaki
authors.forename: H
authors.initials: H
authors.lastname: Ito
authors.forename: K
authors.initials: K
authors.lastname: Nakagawa
authors.forename: S
authors.initials: S
authors.lastname: Ambiru
authors.forename: H
authors.initials: H
authors.lastname: Shimizu
authors.forename: N
authors.initials: N
authors.lastname: Nakajima
mesh_terms: D000328:Adult; D000368:Aged; D002478:Cells, Cultured; D002779:Cholestasis / Q000503:physiopathology*; D018920:Coculture Techniques; D016207:Cytokines / Q000097:blood; D004730:Endothelium, Vascular / Q000378:metabolism*; D004731:Endotoxins / Q000097:blood; D005260:Female; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D019272:Leukocyte Elastase / Q000378:metabolism; D008297:Male; D008875:Middle Aged; D009504:Neutrophils / Q000187:drug effects / Q000473:pathology*; D011506:Proteins; D015843:Serpins / Q000494:pharmacology; D013482:Superoxide Dismutase / Q000494:pharmacology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D018180:Thrombomodulin / Q000378:metabolism; D013997:Time Factors
chemical_list: D016207:Cytokines; D004731:Endotoxins; D011506:Proteins; D015843:Serpins; D018180:Thrombomodulin; C028656:eglin proteinase inhibitors; D007770:L-Lactate Dehydrogenase; D013482:Superoxide Dismutase; D019272:Leukocyte Elastase; D013755:Tetradecanoylphorbol Acetate