Skeletal muscle cytosol [3H]methyltrienolone receptor binding and serum androgens: Effects of hypertrophy and hormonal state

R. C. Hickson*, T. M. Galassi, T. T. Kurowski, D. G. Daniels, R. T. Chatterton

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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 5α-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°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.

Original languageEnglish (US)
Pages (from-to)1705-1712
Number of pages8
JournalJournal of Steroid Biochemistry
Issue number6
StatePublished - Dec 1983

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology


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