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Rac1 is a novel regulator of contraction-stimulated glucose uptake in skeletal muscle

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Authors:
  • Sylow, Lykke ;
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    Orcid logo0000-0003-0905-5932
    PhD, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Jensen, Thomas Elbenhardt ;
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    Orcid logo0000-0001-6139-8268
    Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Kleinert, Maximilian ;
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    PhD, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Mouatt, Joshua Roger ;
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    PhD, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Maarbjerg, Stine Just ;
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    Diabetes Research Unit, Novo Nordisk A/S
  • Jeppesen, Jacob Fuglsbjerg ;
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    Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
  • Prats Gavalda, Clara ;
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    Systems Biology Research, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, Københavns Universitet
  • Chiu, Tim T ;
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    Program in Cell Biology, The Hospital for Sick Children, Toronto, Ontario
  • Boguslavsky, Shlomit ;
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    Program in Cell Biology, The Hospital for Sick Children, Toronto, Ontario
  • Klip, Amira ;
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    Program in Cell Biology, The Hospital for Sick Children, Toronto, Ontario
  • Schjerling, Peter ;
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    Department of Clinical Medicine, Faculty of Health and Medical Sciences, Københavns Universitet
  • Richter, Erik
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    Orcid logo0000-0002-6850-3056
    Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, Københavns Universitet
DOI:
10.2337/db12-0491
Abstract:
In skeletal muscle, the actin cytoskeleton-regulating GTPase, Rac1, is necessary for insulin-dependent GLUT4 translocation. Muscle contraction increases glucose transport and represents an alternative signaling pathway to insulin. Whether Rac1 is activated by muscle contraction and regulates contraction-induced glucose uptake is unknown. Therefore, we studied the effects of in vivo exercise and ex vivo muscle contractions on Rac1 signaling and its regulatory role in glucose uptake in mice and humans. Muscle Rac1-GTP binding was increased after exercise in mice (~60-100%) and humans (~40%), and this activation was AMP-activated protein kinase independent. Rac1 inhibition reduced contraction-stimulated glucose uptake in mouse muscle by 55% in soleus and by 20-58% in extensor digitorum longus (EDL; P <0.01). In agreement, the contraction-stimulated increment in glucose uptake was decreased by 27% (P = 0.1) and 40% (P <0.05) in soleus and EDL muscles, respectively, of muscle specific inducible Rac1 knockout mice. Furthermore, depolymerization of the actin cytoskeleton decreased contraction-stimulated glucose uptake by 100% and 62% (P <0.01) in soleus and EDL muscles, respectively. These are the first data to show that Rac1 is activated during muscle contraction in murine and human skeletal muscle and suggest that Rac1 and possibly the actin cytoskeleton are novel regulators of contraction-stimulated glucose uptake.
Type:
Journal article
Language:
English
Published in:
Diabetes, 2013, Vol 62, Issue 4, p. 1139-1151
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2013
Scientific Level:
Scientific
ID:
239957987

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