Alcohol intake may increase aromatization of androgens

[mewalrus]

Toxicology. 1990 Jun;62(3):285-95.
Effects of chronic ethanol intake on aromatization of androgens and concentration of estrogen and androgen receptors in rat liver.
Chung KW.

Abstract
The present study was carried out to investigate if ethanol alters aromatization of androgens and concentrations of hepatic estrogen and androgen receptors. Hepatic aromatization of androgen to estrogen was significantly increased by ethanol administration. There was a significant increase in serum estrogen level but a decreased circulating testosterone level in alcohol-fed rats. Furthermore, the concentration of estrogen receptors in liver cytosol was significantly higher in alcohol-fed rats (37 +/- 5.3 fmol/mg protein), as compared to the intact control value (21 +/- 4.8 fmol/mg protein). However, hepatic androgen receptor levels were much lower (4.4 +/- 0.5) in alcohol-fed rats than those (10.2 +/- 1.4 fmol/mg protein) in control animals. Similarly, castration increased hepatic aromatization of androgens and concentrations of serum estrogen and hepatic estrogen receptors, but it decreased contents of circulating androgen and hepatic androgen receptors. These findings indicate that alcohol administration is considered a chemical form of castration, altering the hepatic steroid metabolism and sex hormone receptor contents and contributing to the pathogenesis of feminization. A combination of alcohol-feeding and castration has no synergistic effect on the hepatic steroid receptors and aromatization, but this combination does have a more profound effect in lowering the concentration of circulating androgen.

 

[mewalrus]

Alcohol Clin Exp Res. 1981 Spring;5(2):183-7.
Effect of ethanol feeding upon levels of a male-specific hepatic estrogen-binding protein: a possible mechanism for feminization.
Eagon PK, Porter LE, Gavaler JS, Egler KM, Van Thiel DH.

Abstract
Male, but not female, rat liver cytosol contains an estrogen-binding protein with unique properties: rapid binding of estradiol, high binding capacity, moderate affinity for estradiol, and specificity for steroidal estrogens and weak androgens, but not for nonsteroidal estrogens or other steroids. The estradiol-binding activity of this protein is reduced in cytosol from livers of alcohol-fed rats as compared to that from their isocalorically fed controls. The properties of this male-specific hepatic estrogen-binding protein suggest a role for this protein in the regulation of estrogen levels in the male animal. Moreover, the reduction in activity of this unique protein in the liver of alcohol-fed animals may explain, at least in part, the feminization commonly seen in chronic alcoholic men.