Abstract
Alcohol dehydrogenase (ADH) is expressed in a tissue-specific fashion and its activity is modulated by several hormones. Class I ADH activity is largely confined to the liver, with considerably smaller levels in the kidney. Experiments with intact animals indicate that thyroid hormone and testosterone reduce the activity of the enzyme in liver (Mezey and Potter, 1981; Rachamin et al., 1980), and that estrogen and growth hormone increase the activity (Teschke et al., 1986; Mezey and Potter, 1979). In primary hepatocyte cultures, growth hormone produced an increase in ADH activity and mRNA levels, and dihydrotestosterone reduced the activity (Mezey et al., 1986a, 1986b; Potter et al., 1989). Certain hepatoma cell lines express low levels of ADH activity and mRNA, and these can be induced by exposure to glucocorticoids (Wolfla et al., 1988; Dong et al., 1988). The enzyme activity in the kidney is induced by androgens in the mouse (Felder et al., 1988) and by estrogen in the rat (Dembic and Sabolic, 1982). Although the effect of androgens in mouse kidney is known to be mediated by an increase in the transcription of the gene, the mechanism of the effect of estrogens in rat kidney has not been reported.
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© 1990 Plenum Press, New York
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Crabb, D.W., Qulali, M., Dipple, K.M. (1990). Endocrine Regulation and Methylation Patterns of Rat Class I Alcohol Dehydrogenase in Liver and Kidney. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_30
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DOI: https://doi.org/10.1007/978-1-4684-5901-2_30
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