Cited by 442Muscle metabolism and nutritionMetabolism, Diabetes, and CancerMuscle Physiology and Disorders

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Physiologic hyperinsulinemia stimulates protein synthesis and enhances transport of selected amino acids in human skeletal muscle

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Biolo, G, Declan Fleming, R Y, Wolfe, R R·1995·Journal of Clinical Investigation

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Abstract

We have investigated the mechanisms of the anabolic effect of insulin on muscle protein metabolism in healthy volunteers, using stable isotopic tracers of amino acids. Calculations of muscle protein synthesis, breakdown, and amino acid transport were based on data obtained with the leg arteriovenous catheterization and muscle biopsy. Insulin was infused (0.15 mU/min per 100 ml leg) into the femoral artery to increase femoral venous insulin concentration (from 10 +/- 2 to 77 +/- 9 microU/ml) with minimal systemic perturbations. Tissue concentrations of free essential amino acids decreased (P < 0.05) after insulin. The fractional synthesis rate of muscle protein (precursor-product approach) increased (P < 0.01) after insulin from 0.0401 +/- 0.0072 to 0.0677 +/- 0.0101%/h. Consistent with this observation, rates of utilization for protein synthesis of intracellular phenylalanine and lysine (arteriovenous balance approach) also increased from 40 +/- 8 to 59 +/- 8 (P < 0.05) and from 219 +/- 21 to 298 +/- 37 (P < 0.08) nmol/min per 100 ml leg, respectively. Release from protein breakdown of phenylalanine, leucine, and lysine was not significantly modified by insulin. Local hyperinsulinemia increased (P < 0.05) the rates of inward transport of leucine, lysine, and alanine, from 164 +/- 22 to 200 +/- 25, from 126 +/- 11 to 221 +/- 30, and from 403 +/- 64 to 595 +/- 106 nmol/min per 100 ml leg, respectively. Transport of phenylalanine did not change significantly. We conclude that insulin promoted muscle anabolism, primarily by stimulating protein synthesis independently of any effect on transmembrane transport.

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Authors: Biolo, G., Declan Fleming, R. Y., & Wolfe, R. R.
Affiliations: The University of Texas Medical Branch at Galveston (US)
Shriners Hospitals for Children - Galveston (US)
ORCID: Biolo, G
Wolfe, R R
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1995-02-01
Volume: 95
Issue: 2
Pages: 811-819
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci117731
PMC: PMC295560
OpenAlex: W2041707781
Cited by: 442
References: 46
Citations by year: 2026: 3 · 2025: 10 · 2024: 13 · 2023: 11 · 2022: 24 · 2021: 16 · 2020: 7 · 2019: 10 · 2018: 4 · 2017: 11 · 2016: 18 · 2015: 11 · 2014: 13 · 2013: 11 · 2012: 13
FWCI: 3.78
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion)
Funders: University of Texas Medical Branch
Shriners Hospitals for Children
National Institutes of Health (5r01dk033952-14)
U.S. Public Health Service (00074)
National Institute of Diabetes and Digestive and Kidney Diseases (DK 33952, DK-38010, R01DK038010)
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords: insulin, hyperinsulinemia, skeletal muscle, muscle protein synthesis, muscle protein degradation, amino acid transport, muscle anabolism, essential amino acids, phenylalanine, leucine, lysine, alanine
MeSH terms: Adult, Alanine, Amino Acids, Biological Transport, Femoral Vein, Humans, Hyperinsulinism, Insulin, Kinetics, Leucine, Lysine, Male, Mathematics, Models, Biological, Phenylalanine, Reference Values, Protein Biosynthesis, Muscle, Skeletal

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Physiologic hyperinsulinemia stimulates protein synthesis and enhances transport of selected amino acids in human skeletal muscle

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