Abstract
The metabolism of acetaldehyde was studied in isolated dog, rat and guinea-pig kidney-cortex tubules. In contrast with previous observations of Cederbaum and Rubin in rat kidney mitochondria ( Archs Biochem. Biophys. 179, 46–66 1977) acetaldehyde was found to be metabolized by the tubules at high rates and in a dose-dependent manner at concentrations up to 5–10 mM. At high acetaldehyde concentrations (1–10 mM) acetaldehyde removal was accompanied by a high rate of acetate accumulation which explained most of the acetaldehyde metabolized in dog and guinea-pig but not in rat kidney tubules. These species differences in acetaldehyde metabolism can be explained by the differences in activities of aldehyde dehydrogenase (EC 1.2.1.3) and acetyl-CoA synthetase (EC 6.2.1.1), the enzymes involved in renal acetaldehyde metabolism which were measured in the renal cortex of the three species. The acetaldehyde carbon removed and not accounted for by acetate accumulation was completely oxidized to CO 2 as demonstrated by the measurement of [U- 14C]-acetaldehyde conversion into 14CO 2. At “physiological” acetaldehyde concentrations (0.1 and 0.2 mM) acetaldehyde utilization was also concentration-dependent but no acetate accumulation was observed.
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