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Regulation of the androgen and glucocorticoid receptors in rat and mouse skeletal muscle cytosol.
Endocrinology. 1981 Apr; 108(4):1431-40.E

Abstract

Using a charcoal technique, we determined the relative binding affinity of some anabolic compounds for the androgen and glucocorticoid receptors in cytosol from rat skeletal muscle. Only a few of the compounds analyzed competed for the receptor-binding sites. The androgen and glucocorticoid receptors were analyzed in rat and mouse skeletal muscle cytosols by Scatchard analysis. In rats grouped according to sex and age, the cytosolic protein content was about the same in all groups, but the DNA content decreased with increased weight of the animal regardless of sex (male, female, or castrated male). The glucocorticoid receptor did not differ in concentration (2-3 pmol/g tissue) or ligand affinity (Kd, 10-40 nM) among the groups, but the androgen receptor concentration decreased with increased weight and age of the animals, more in the case of males than in the case of females or castrates. The Kd for the androgen receptor increased with age in males but was constantly about 0.2 nM for castrates or females. In adult intact rats, the androgen and glucocorticoid receptor concentrations in muscle cytosol from females were about 100 and 3000 fmol/g tissue, respectively, the corresponding values for males being about 50 and 2000 fmol/g tissue, respectively. Short term castration or adrenalectomy increased the concentration of and ligand affinity for the androgen and glucocorticoid receptors, respectively. After long term castration of male rats, the concentration of both receptors increased during 5 weeks to about the female level, only to decrease later. Neonatally castrated male rats had about the same androgen receptor concentrations and Kd values as female rats. Female mice had higher androgen receptor concentrations (approximately 700 fmol/g tissue) than rats. Intact male mice had about 200 fmol androgen receptor-binding sites/g tissue, and the same amount was found in mice bearing the testicular feminization (Tfm) mutant gene. In summary, the concentrations of androgen and glucocorticoid receptors in rat skeletal muscle are regulated at least by the testes. The presence of androgen receptors in skeletal muscle from Tfm mice is surprising and may motivate a reinvestigation of the regulation of androgen receptors in Tfm animals.

Authors

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Pub Type(s)

Journal Article

Language

eng

PubMed ID

6970661

Citation

Dahlberg, E, et al. "Regulation of the Androgen and Glucocorticoid Receptors in Rat and Mouse Skeletal Muscle Cytosol." Endocrinology, vol. 108, no. 4, 1981, pp. 1431-40.
Dahlberg E, Snochowski M, Gustafsson JA. Regulation of the androgen and glucocorticoid receptors in rat and mouse skeletal muscle cytosol. Endocrinology. 1981;108(4):1431-40.
Dahlberg, E., Snochowski, M., & Gustafsson, J. A. (1981). Regulation of the androgen and glucocorticoid receptors in rat and mouse skeletal muscle cytosol. Endocrinology, 108(4), 1431-40.
Dahlberg E, Snochowski M, Gustafsson JA. Regulation of the Androgen and Glucocorticoid Receptors in Rat and Mouse Skeletal Muscle Cytosol. Endocrinology. 1981;108(4):1431-40. PubMed PMID: 6970661.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of the androgen and glucocorticoid receptors in rat and mouse skeletal muscle cytosol. AU - Dahlberg,E, AU - Snochowski,M, AU - Gustafsson,J A, PY - 1981/4/1/pubmed PY - 1981/4/1/medline PY - 1981/4/1/entrez SP - 1431 EP - 40 JF - Endocrinology JO - Endocrinology VL - 108 IS - 4 N2 - Using a charcoal technique, we determined the relative binding affinity of some anabolic compounds for the androgen and glucocorticoid receptors in cytosol from rat skeletal muscle. Only a few of the compounds analyzed competed for the receptor-binding sites. The androgen and glucocorticoid receptors were analyzed in rat and mouse skeletal muscle cytosols by Scatchard analysis. In rats grouped according to sex and age, the cytosolic protein content was about the same in all groups, but the DNA content decreased with increased weight of the animal regardless of sex (male, female, or castrated male). The glucocorticoid receptor did not differ in concentration (2-3 pmol/g tissue) or ligand affinity (Kd, 10-40 nM) among the groups, but the androgen receptor concentration decreased with increased weight and age of the animals, more in the case of males than in the case of females or castrates. The Kd for the androgen receptor increased with age in males but was constantly about 0.2 nM for castrates or females. In adult intact rats, the androgen and glucocorticoid receptor concentrations in muscle cytosol from females were about 100 and 3000 fmol/g tissue, respectively, the corresponding values for males being about 50 and 2000 fmol/g tissue, respectively. Short term castration or adrenalectomy increased the concentration of and ligand affinity for the androgen and glucocorticoid receptors, respectively. After long term castration of male rats, the concentration of both receptors increased during 5 weeks to about the female level, only to decrease later. Neonatally castrated male rats had about the same androgen receptor concentrations and Kd values as female rats. Female mice had higher androgen receptor concentrations (approximately 700 fmol/g tissue) than rats. Intact male mice had about 200 fmol androgen receptor-binding sites/g tissue, and the same amount was found in mice bearing the testicular feminization (Tfm) mutant gene. In summary, the concentrations of androgen and glucocorticoid receptors in rat skeletal muscle are regulated at least by the testes. The presence of androgen receptors in skeletal muscle from Tfm mice is surprising and may motivate a reinvestigation of the regulation of androgen receptors in Tfm animals. SN - 0013-7227 UR - https://www.unboundmedicine.com/medline/citation/6970661/Regulation_of_the_androgen_and_glucocorticoid_receptors_in_rat_and_mouse_skeletal_muscle_cytosol_ L2 - https://academic.oup.com/endo/article-lookup/doi/10.1210/endo-108-4-1431 DB - PRIME DP - Unbound Medicine ER -