Activities of Lysosomal Enzymes in Alloxan-Induced Diabetes in the Mouse.

Abstract

The study investigated a panel of lysosomal enzymes in the liver and kidney tissues in alloxan-induced diabetes in the mouse. The mice were divided into six experimental groups receiving 10% alloxan at a dose of 50 and 75 mg/kg over a period of four, eight, and twelve days; each group was compared with controls receiving 0.9% NaCl. The findings were that diabetes induced by both doses of alloxan was accompanied by significant increases in the lysosomal activities of acid phosphatase and the glycosidases investigated: β-glucuronidase, β-galactosidase, β-glucosidase, and N-acetyl-hexosaminidase. The lysosomal enzyme activity in both liver and kidney cells peaked 12 days after onset of diabetes for most enzymes, at the time when hyperglycemia and hyperinsulinemia already started abating after their peak at 8 days into the course of diabetes. The enzyme activity was in most cases higher with the higher dose of alloxan and thus higher level of glycemia. Lysosomal enzymes degrade glycoconjugates, the molecules that are present in the basement membrane of endothelial cells where they contribute to capillary wall stability. Thus, enhanced activity of these enzymes could presage the progression of diabetic microangiopathy, atherosclerosis, and the development of microvascular complications.