Aldehyde dehydrogenase activities in hepatocyte nodules and hepatocellular carcinomas from Wistar rats

Abstract

The activities of aldehyde dehydrogenases using benzaldehyde and propionaldehyde as substrates and NADP and NAD as coenzymes were determined in normal liver, hepatocyte nodules and hepatocellular carcinomas from male Wistar rats. Hepatocyte nodules were produced by intermittent exposure of rats to 0.05% 2-acetylaminofluorene or by initiation with diethylnitrosamine followed by selection using 2 weeks of dietary exposure to 0.02% 2-acetylaminofluorene and partial hepatectomy. The activities of propionaldehyde: NAD and benzaldehyde: NADP aldehyde dehydrogenases were increased in hepatocyte nodules of all types as well as in most hepatocellular carcinomas. The most prominent elevation of enzyme activity was found in the cytosol of persistent hepatocyte nodules (35–60 times) and some hepatocellular carcinomas (92 times) using benzaldehyde and NADP. The benzaldehyde: NADP aldehyde dehydrogenase activity varied considerably between different nodules suggesting the existence of a subpopulation of hepatocyte nodules with very high enzymatic activities. The activity of propionaldehyde: NAD aldehyde dehydrogenase activity as well as of γ-glutamyltransferase did not show substantial internodular variations. The activity of benzaldehyde: NADP aldehyde dehydrogenase in individual carcinomas investigated in these experiments varied extensively. The data did not support the idea that all hepatomas had been developed from pre-neoplastic nodules with very high activity of this enzyme.