Treatment of mallard ducks with estradiol, or a combination of estradiol and thyroxine, has been shown to result in the proliferation of peroxisomes and production of diesters of 3‐hydroxy fatty acids, the female pheromones, in the uropygial gland of male and female mallard ducks. Such a treatment results in the induction of a unique set of proteins. A cDNA library enriched in hormone‐induced transcripts was subjected to differential screening. The nucleotide sequence of one of the two unique cDNA clones, DGH1, had high similarity to the Human class I alcohol dehydrogenase (ADH) gamma subunit and represented the carboxy‐terminus of the protein from amino acid 190–374. SDS/PAGE and Western blot analysis of the proteins indicated that the level of a 38‐kDa protein that cross‐reacted with antibodies prepared against the chicken ADH was increased 5–7‐fold by hormone treatment. Assays for ADH activity in the uropygial gland extracts of male mallards showed a 5–7‐fold induction of the enzyme by hormone treatment. The 1.9‐kb ADH mRNA levels were increased 12–14‐fold under these conditions. Of all the tissues tested, the uropygial gland had the highest levels of ADH mRNA. Induction of ADH by estradiol treatment occurred only in this tissue. Elevated levels of ADH were also observed in the glands of male mallards in eclipse, the post‐nuptial condition when the hormonal balance is shifted to higher estrogen levels, suggesting that this enzyme is regulated by estrogens in this period. Estradiol treatment caused an 80% decrease in the NAD+/NADH ratio in the uropygial gland and a twofold increase in the fatty alcohol oxidation rate catalyzed by the gland extract. These observations could help explain how increased levels of ADH could contribute to the production of the diesters. Copyright © 1992, Wiley Blackwell. All rights reserved
CITATION STYLE
HIREMATH, L. S., KESSLER, P. M., SASAKI, G. C., & KOLATTUKUDY, P. E. (1992). Estrogen induction of alcohol dehydrogenase in the uropygial gland of mallard ducks. European Journal of Biochemistry, 203(3), 449–457. https://doi.org/10.1111/j.1432-1033.1992.tb16569.x
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