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Cited by 492Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismCellular transport and secretion

Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin

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Lund, S, Holman, G D, Schmitz, O, Pedersen, O·1995·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.92.13.5817PMC PMC41592
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Abstract

The acute effects of contraction and insulin on the glucose transport and GLUT4 glucose transporter translocation were investigated in rat soleus muscles by using a 3-O-methylglucose transport assay and the sensitive exofacial labeling technique with the impermeant photoaffinity reagent 2-N-4-(1-azi-2,2,2-trifluoroethyl)benzoyl-1,3-bis(D-mannose-4-y loxy)-2- propylamine (ATB-BMPA), respectively. Addition of wortmannin, which inhibits phosphatidylinositol 3-kinase, reduced insulin-stimulated glucose transport (8.8 +/- 0.5 mumol per ml per h vs. 1.4 +/- 0.1 mumol per ml per h) and GLUT4 translocation [2.79 +/- 0.20 pmol/g (wet muscle weight) vs. 0.49 +/- 0.05 pmol/g (wet muscle weight)]. In contrast, even at a high concentration (1 microM), wortmannin had no effect on contraction-mediated glucose uptake (4.4 +/- 0.1 mumol per ml per h vs. 4.1 +/- 0.2 mumol per ml per h) and GLUT4 cell surface content [1.75 +/- 0.16 pmol/g (wet muscle weight) vs. 1.52 +/- 0.16 pmol/g (wet muscle weight)]. Contraction-mediated translocation of the GLUT4 transporters to the cell surface was closely correlated with the glucose transport activity and could account fully for the increment in glucose uptake after contraction. The combined effects of contraction and maximal insulin stimulation were greater than either stimulation alone on glucose transport activity (11.5 +/- 0.4 mumol per ml per h vs. 5.6 +/- 0.2 mumol per ml per h and 9.0 +/- 0.2 mumol per ml per h) and on GLUT4 translocation [4.10 +/- 0.20 pmol/g (wet muscle weight) vs. 1.75 +/- 0.25 pmol/g (wet muscle weight) and 3.15 +/- 0.18 pmol/g (wet muscle weight)]. The results provide evidence that contraction stimulates translocation of GLUT4 in skeletal muscle through a mechanism distinct from that of insulin.

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Authors
Lund, S., Holman, G. D., Schmitz, O., & Pedersen, O.
Affiliations
Aarhus University Hospital (DK)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1995-06-20
Volume
92
Issue
13
Pages
5817-5821
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.92.13.5817
PMC
PMC41592
OpenAlex
W2019691564
Cited by
492
References
36
Citations by year
2026: 5 · 2025: 5 · 2024: 4 · 2023: 12 · 2022: 10 · 2021: 15 · 2020: 15 · 2019: 20 · 2018: 15 · 2017: 11 · 2016: 17 · 2015: 16 · 2014: 15 · 2013: 11 · 2012: 19
FWCI
7.56
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
glucose transporter translocation, skeletal muscle, muscle contraction, insulin, glucose transport, phosphatidylinositol 3-kinase, wortmannin, soleus muscle, glucose uptake, cell surface
MeSH terms
Wortmannin, Affinity Labels, Androstadienes, Animals, Azides, Biological Transport, Cell Membrane, Disaccharides, Glycosides, Insulin, Kinetics, Methylglucosides, Monosaccharide Transport Proteins, Muscle Contraction, Muscle Proteins, Propylamines, Sensitivity and Specificity, Rats, Wistar, Phosphotransferases (Alcohol Group Acceptor), Muscle, Skeletal, 3-O-Methylglucose, Phosphatidylinositol 3-Kinases, Glucose Transporter Type 4, Rats, In Vitro Techniques

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