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Skeletal muscle cytosol [3H]methyltrienolone receptor binding and serum androgens: effects of hypertrophy and hormonal state.
J Steroid Biochem. 1983 Dec; 19(6):1705-12.JS

Abstract

Normal, castrated, and hypophysectomized male rats underwent compensatory hypertrophy of plantaris muscles following surgical removal of their synergistic gastrocnemius muscles. The increases in muscle wet weights above control values, determined when the muscles were in stable-state hypertrophy, were as follows: normal 50%, castrated 50%, and hypophysectomized 32%. There were marked differences in concentration of serum androgens between surgical groups, yet no increases in testosterone or 5 alpha-dihydrotestosterone were observed as a result of hypertrophy. The amount of testosterone binding to serum proteins (approx 94%) was reduced only in hypophysectomized animals that underwent muscle growth. Cytosol androgen receptor specific binding (fmol/mg protein), measured using saturating concentrations of [3H]methyltrienolone (R1881) at 4 degrees C for 20 h for exchange with endogenous steroid, was significantly increased in hypertrophied muscles of normal, (1.77 +/- 0.17 vs 1.16 +/- 0.21), castrated (2.27 +/- 0.20 vs 1.46 +/- 0.03) and hypophysectomized (6.23 +/- 0.56 vs 3.64 +/- 0.30) animals. Receptor dissociation constants (Kd) were approx 10(-10) M in all groups and were not altered by the hypertrophy. These findings show that a major adaptation to skeletal muscle enlargement is an augmentation of cytosol [3H]methyltrienolone receptor binding capacity. This effect occurs in a normal or androgen deficient state.

Authors

Hickson RC
No affiliation info available
Galassi TM
No affiliation info available
Kurowski TT
No affiliation info available
Daniels DG
No affiliation info available
Chatterton RT
No affiliation info available

MeSH

AndrogensAnimalsCastrationCytosolEstrenesHypertrophyHypophysectomyMaleMetriboloneMusclesRatsRats, Inbred StrainsReceptors, AndrogenReceptors, SteroidTestosterone

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

6608632

Citation

Hickson, R C., et al. "Skeletal Muscle Cytosol [3H]methyltrienolone Receptor Binding and Serum Androgens: Effects of Hypertrophy and Hormonal State." Journal of Steroid Biochemistry, vol. 19, no. 6, 1983, pp. 1705-12.
Hickson RC, Galassi TM, Kurowski TT, et al. Skeletal muscle cytosol [3H]methyltrienolone receptor binding and serum androgens: effects of hypertrophy and hormonal state. J Steroid Biochem. 1983;19(6):1705-12.
Hickson, R. C., Galassi, T. M., Kurowski, T. T., Daniels, D. G., & Chatterton, R. T. (1983). Skeletal muscle cytosol [3H]methyltrienolone receptor binding and serum androgens: effects of hypertrophy and hormonal state. Journal of Steroid Biochemistry, 19(6), 1705-12.
Hickson RC, et al. Skeletal Muscle Cytosol [3H]methyltrienolone Receptor Binding and Serum Androgens: Effects of Hypertrophy and Hormonal State. J Steroid Biochem. 1983;19(6):1705-12. PubMed PMID: 6608632.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Skeletal muscle cytosol [3H]methyltrienolone receptor binding and serum androgens: effects of hypertrophy and hormonal state. AU - Hickson,R C, AU - Galassi,T M, AU - Kurowski,T T, AU - Daniels,D G, AU - Chatterton,R T,Jr PY - 1983/12/1/pubmed PY - 2001/3/28/medline PY - 1983/12/1/entrez SP - 1705 EP - 12 JF - Journal of steroid biochemistry JO - J Steroid Biochem VL - 19 IS - 6 N2 - Normal, castrated, and hypophysectomized male rats underwent compensatory hypertrophy of plantaris muscles following surgical removal of their synergistic gastrocnemius muscles. The increases in muscle wet weights above control values, determined when the muscles were in stable-state hypertrophy, were as follows: normal 50%, castrated 50%, and hypophysectomized 32%. There were marked differences in concentration of serum androgens between surgical groups, yet no increases in testosterone or 5 alpha-dihydrotestosterone were observed as a result of hypertrophy. The amount of testosterone binding to serum proteins (approx 94%) was reduced only in hypophysectomized animals that underwent muscle growth. Cytosol androgen receptor specific binding (fmol/mg protein), measured using saturating concentrations of [3H]methyltrienolone (R1881) at 4 degrees C for 20 h for exchange with endogenous steroid, was significantly increased in hypertrophied muscles of normal, (1.77 +/- 0.17 vs 1.16 +/- 0.21), castrated (2.27 +/- 0.20 vs 1.46 +/- 0.03) and hypophysectomized (6.23 +/- 0.56 vs 3.64 +/- 0.30) animals. Receptor dissociation constants (Kd) were approx 10(-10) M in all groups and were not altered by the hypertrophy. These findings show that a major adaptation to skeletal muscle enlargement is an augmentation of cytosol [3H]methyltrienolone receptor binding capacity. This effect occurs in a normal or androgen deficient state. SN - 0022-4731 UR - https://www.unboundmedicine.com/medline/citation/6608632/Skeletal_muscle_cytosol_[3H]methyltrienolone_receptor_binding_and_serum_androgens:_effects_of_hypertrophy_and_hormonal_state_ DB - PRIME DP - Unbound Medicine ER -