Short-Term Oxandrolone Administration Stimulates Net Muscle Protein Synthesis in Young Men1
Abstract
Short term administration of testosterone stimulates net protein synthesis in healthy men. We investigated whether oxandrolone[ Oxandrin (OX)], a synthetic analog of testosterone, would improve net muscle protein synthesis and transport of amino acids across the leg. Six healthy men [22 ± 1 (±se) yr] were studied in the postabsorptive state before and after 5 days of oral OX (15 mg/day). Muscle protein synthesis and breakdown were determined by a three-compartment model using stable isotopic data obtained from femoral arterio-venous sampling and muscle biopsy. The precursor-product method was used to determine muscle protein fractional synthetic rates. Fractional breakdown rates were also directly calculated. Total messenger ribonucleic acid (mRNA) concentrations of skeletal muscle insulin-like growth factor I and androgen receptor (AR) were determined using RT-PCR. Model-derived muscle protein synthesis increased from 53.5 ± 3 to 68.3 ± 5 (mean ± se) nmol/min·100 mL/leg (P < 0.05), whereas protein breakdown was unchanged. Inward transport of amino acids remained unchanged with OX, whereas outward transport decreased (P < 0.05). The fractional synthetic rate increased 44% (P < 0.05) after OX administration, with no change in fractional breakdown rate. Therefore, the net balance between synthesis and breakdown became more positive with both methodologies (P < 0.05) and was not different from zero. Further, RT-PCR showed that OX administration significantly increased mRNA concentrations of skeletal muscle AR without changing insulin-like growth factor I mRNA concentrations. We conclude that short term OX administration stimulated an increase in skeletal muscle protein synthesis and improved intracellular reutilization of amino acids. The mechanism for this stimulation may be related to an OX-induced increase in AR expression in skeletal muscle.
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Testosterone and IGF-1 positively regulate muscle protein anabolism by promoting muscle protein synthesis and repressing genes that activate muscle protein degradation.
“Testosterone and IGF‐1 positively regulate muscle protein anabolism by promoting muscle protein synthesis (Sheffield‐Moore et al., 1999; Urban et al., 1995), while repressing the genes that activate muscle protein degradation (Zhao et al., 2008).”
From The effect of acute sleep deprivation on skeletal muscle protein synthesis and the hormonal environment (2021) · cites this paper as Sheffield‐Moore et al., 1999
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- Authors
- Sheffield-Moore, M., Urban, R. J., Wolf, S. E., Jiang, J., Catlin, D. H., Herndon, D. N., Wolfe, R. R., & Ferrando, A. A.
- Affiliations
- Departments of Surgery (M.S.-M., S.E.W., D.N.H., R.R.W., A.A.F.), Texas 77550
- The University of Texas Medical Branch at Galveston (US)
- University of California, Los Angeles (US)
- Shriners Hospitals for Children - Galveston (US)
- Venue
- The Journal of Clinical Endocrinology & Metabolism
- Publisher
- The Endocrine Society
- Published
- 1999-08-01
- Volume
- 84
- Issue
- 8
- Pages
- 2705-2711
- ISSN
- 0021-972X (ISSN-L)
- 1945-7197
- OpenAlex
- W2127475498
- Cited by
- 199
- References
- 3
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 5 · 2023: 2 · 2022: 7 · 2021: 9 · 2020: 1 · 2019: 8 · 2018: 3 · 2017: 5 · 2016: 4 · 2015: 4 · 2014: 2 · 2013: 7 · 2012: 5
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Clinical Endocrinology & Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (M01-00073)
- National Institute on Aging (AG-11000, R01AG011000)
- National Institute of Diabetes and Digestive and Kidney Diseases (5-R01-DK-38010-11, R01DK038010)
- NIH Clinical Center
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal and reproductive studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- oxandrolone, muscle protein synthesis, muscle protein degradation, androgen receptor, insulin-like growth factor I, amino acid transport, skeletal muscle, anabolic steroids, fractional synthesis rate, mRNA expression
- MeSH terms
- Adult, Amino Acids, Humans, Insulin-Like Growth Factor I, Male, Muscle Proteins, Muscles, Oxandrolone, Receptors, Androgen, RNA, Messenger, Anabolic Agents
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