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Glycohydrolases are a group of enzymes contained predominantly within lysosomes, which are released during Kupffer cell activation or death. One of these, beta-galactosidase, has been proposed as a marker of ischemia-reperfusion injury in the liver because Kupffer cell activation represents a primary event in the injurious reperfusion cascade. In this study, we compared B-galactosidase with more traditional indicators of liver injury and function in a porcine model of liver preservation. Porcine livers were allocated into two groups: group C (n = 5), preserved in University of Wisconsin solution by standard cold storage for 24 hours, and group W (n = 5), perfused with oxygenated autologous blood on an extracorporeal circuit for 24 hours. Both groups were subsequently tested on the circuit during a 24-hour reperfusion phase. The perfusate was sampled for levels of beta-galactosidase, as well as traditional markers of liver injury and function. A sharp increase in beta-galactosidase levels was seen on reperfusion of cold preserved livers to a level of 1,900 IU/mL. This contrasted dramatically with normothermically preserved livers, in which the level never exceeded 208 IU/mL (P =.002). beta-Galactosidase levels showed much earlier and greater increases compared with transaminase levels in livers injured by ischemia. A rapid elevation in beta-galactosidase levels corresponded well with poor liver function and more liver injury. Measurement of beta-galactosidase is a simple test that quantifies ischemia-reperfusion injury of preserved livers. It is more sensitive than transaminases, with faster and larger increases in levels after ischemic injury. It can be useful in assessing the viability of a liver during machine preservation.

Original publication

DOI

10.1053/jlts.2002.30344

Type

Journal article

Journal

Liver Transpl

Publication Date

01/2002

Volume

8

Pages

21 - 26

Keywords

Animals, Extracorporeal Circulation, Liver, Liver Transplantation, Models, Animal, Organ Preservation, Reperfusion Injury, Swine, beta-Galactosidase