Glutathione peroxidase, superoxide dismutase and catalase activities in hepatic tissue from children with glycogen storage disease

Introduction: The glycogen storage diseases are caused by inherited deficiencies of enzymes that regulate the synthesis or degradation of glycogen. The most common forms of glycogen storage disease (GSD) are types I, II, III, and IV, which may account for more than 90% of all cases. The most common form is type I, or von Gierke’s disease, which occurs in one out of every 100,000 births. Intracellular antioxidant defence is primarily provided by antioxidant enzymes, which catalyse decomposition of reactive oxygen species. To study the oxidative stress status in children with glycogen storage disease by determining activities of glutathione peroxidase, superoxide dismutase and catalase in liver tissue.
Material and methods: Nine children suffering from glycogen storage diseases types I and III were studied. They were selected from the Hepatology Clinic, Cairo University and compared with children who happened to have incidental normal liver biopsy. Glutathione peroxidase (GPX), superoxide dismutase (SOD) and catalase (CAT) levels were measured in fresh liver tissue using ELISA.
Results: Glycogen storage disease patients showed significant increases in SOD and GPX, and there were significant correlations between SOD and both direct bilirubin and prothrombin concentration, and between GPX activity and both ALT and AST.
Conclusions: Oxidative stress could play a role in the pathogenesis of glycogen storage disease. These preliminary results are encouraging to conduct more extensive clinical studies using adjuvant antioxidant therapy.