title: Possible role of heat shock protein 60 in reducing ischemic-reperfusion injury in canine pancreas grafts after preservation by the two-layer method.
abstract: BACKGROUND
  Recently, results of the clinical application of the two-layer method have shown the morphologic quality of the human pancreas grafts after reperfusion to be excellent, although ischemia-reperfusion injury is related to early graft loss in pancreas transplantation. However, some reports have indicated that heat shock proteins (HSPs) have important functions in response to the stress-related events.
  
  
  OBJECTIVE
  To examine whether the two-layer method reduced ischemia-reperfusion injury in a canine pancreas autotransplantation model by investigating the expression of HSPs.
  
  
  METHODS
  There were three experimental groups in which dogs received segmental autografts after preservation by the two-layer method using University of Wisconsin solution (UW) (group 1), simple storage in UW (group 2) for 24 hours, or no preservation (group 3).
  
  
  RESULTS
  In group 1, pancreatic tissue perfusions were high, and pancreatic exocrine functions were well preserved after 1, 2, and 4 hours of reperfusion with low incidence of graft pancreatitis or vessel thrombosis compared with that in group 2. Moreover, ATP rapidly recovered, and HSP 60 was strongly enhanced after reperfusion in group 1. On the other hand, ATP recovery and the enhancement of HSP 60 were weak after reperfusion in group 2.
  
  
  CONCLUSIONS
  The two-layer method reduced ischemia-reperfusion injury compared with UW simple storage in canine pancreas autotransplantation with a strong expression of HSP 60.
authors.affiliation: First Department of Surgery, Kobe University Faculty of Medicine, 7-5-2 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan. yasu120@med.kobe-u.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Fujino
authors.forename: Y
authors.initials: Y
authors.lastname: Suzuki
authors.forename: T
authors.initials: T
authors.lastname: Tsujimura
authors.forename: T
authors.initials: T
authors.lastname: Takahashi
authors.forename: Y
authors.initials: Y
authors.lastname: Tanioka
authors.forename: M
authors.initials: M
authors.lastname: Tominaga
authors.forename: Y
authors.initials: Y
authors.lastname: Ku
authors.forename: Y
authors.initials: Y
authors.lastname: Kuroda
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000681:Amylases / Q000097:blood; D000818:Animals; D018834:Chaperonin 60 / Q000032:analysis / Q000502:physiology*; D004285:Dogs; D005260:Female; D006085:Graft Survival; D018841:HSP90 Heat-Shock Proteins / Q000032:analysis; D007150:Immunohistochemistry; D008049:Lipase / Q000097:blood; D008297:Male; D010179:Pancreas / Q000098:blood supply* / Q000737:chemistry / Q000201:enzymology; D016035:Pancreas Transplantation; D015427:Reperfusion Injury / Q000517:prevention & control*; D014182:Transplantation, Autologous
chemical_list: D018834:Chaperonin 60; D018841:HSP90 Heat-Shock Proteins; D000255:Adenosine Triphosphate; D008049:Lipase; D000681:Amylases