Cited by 382Metabolism, Diabetes, and CancerMuscle metabolism and nutritionDiabetes, Cardiovascular Risks, and Lipoproteins

Insulin signaling and insulin sensitivity after exercise in human skeletal muscle

Wojtaszewski, J F, Hansen, B F, Gade, Kiens, B, Markuns, J F, Goodyear, L J, Richter, E A·2000·Diabetes

Abstract

Muscle glucose uptake, glycogen synthase activity, and insulin signaling were investigated in response to a physiological hyperinsulinemic (600 pmol/l)-euglycemic clamp in young healthy subjects. Four hours before the clamp, the subjects performed one-legged exercise for 1 h. In the exercised leg, insulin more rapidly activated glucose uptake (half activation time [t1/2] = 11 vs. 34 min) and glycogen synthase activity (t1/2 = 8 vs. 17 min), and the magnitude of increase was two- to fourfold higher compared with the rested leg. However, prior exercise did not result in a greater or more rapid increase in insulin-induced receptor tyrosine kinase (IRTK) activity (t1/2 = 50 min), serine phosphorylation of Akt (t1/2 = 1-2 min), or serine phosphorylation of glycogen synthase kinase-3 (GSK-3) (t1/2 = 1-2 min) or in a larger or more rapid decrease in GSK-3 activity (t1/2 = 3-8 min). Thirty minutes after cessation of insulin infusion, glucose uptake, glycogen synthase activity, and signaling events were partially reversed in both the rested and the exercised leg. We conclude the following: 1) physiological hyperinsulinemia induces sustained activation of insulin-signaling molecules in human skeletal muscle; 2) the more distal insulin-signaling components (Akt, GSK-3) are activated much more rapidly than the proximal signaling molecules (IRTK as well as insulin receptor substrate 1 and phosphatidylinositol 3-kinase [Wojtaszewski et al., Diabetes 46:1775-1781, 1997]); and 3) prior exercise increases insulin stimulation of both glucose uptake and glycogen synthase activity in the absence of an upregulation of signaling events in human skeletal muscle.

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Crossref · 10.2337/diabetes.49.3.325

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  • Even a single bout of exercise can enhance insulin-stimulated glucose uptake in whole muscle tissue and individual muscle fibers.

    “In fact, even a single bout of exercise can enhance insulin-stimulated glucose uptake in whole muscle tissue 103-105 and individual muscle fibers.106, 107”

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Authors
Wojtaszewski, J. F., Hansen, B. F., Gade, Kiens, B., Markuns, J. F., Goodyear, L. J., & Richter, E. A.
Affiliations
Brigham and Women's Hospital (US)
Venue
Diabetes
Published
2000-03-01
Volume
49
Issue
3
Pages
325-331
ISSN
  • 0012-1797 (ISSN-L)
  • 1939-327X
OpenAlex
W2112396418
Cited by
382
References
15
Citations by year
2026: 3 · 2025: 5 · 2024: 8 · 2023: 7 · 2022: 17 · 2021: 19 · 2020: 20 · 2019: 10 · 2018: 19 · 2017: 19 · 2016: 20 · 2015: 17 · 2014: 16 · 2013: 18 · 2012: 19
FWCI
5.29
Type
journal article
Language
en
Open access
closed
Locations
  • Diabetes (publishedVersion)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Funders
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR45670, AR-42238, R01AR045670)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
Keywords
insulin signaling, insulin sensitivity, physical activity, skeletal muscle, muscle glucose uptake, glycogen synthase, hyperinsulinemic-euglycemic clamp, insulin receptor tyrosine kinase, Akt, glycogen synthase kinase-3, IRS-1, phosphatidylinositol 3-kinase, signal transduction
MeSH terms
Adult, Amino Acid Sequence, Glucose, Glycogen, Humans, Insulin, Insulin Resistance, Leg, Male, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Glucose Clamp Technique, Signal Transduction, Exercise, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Muscle, Skeletal, Glycogen Synthase Kinases, Glycogen Synthase Kinase 3, Proto-Oncogene Proteins c-akt

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