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Copenhagen Muscle Research Centre, August Krogh Institute, University of Copenhagen, DK-2100 Copenhagen; Hagedorn Research Center, Gentofte, DK-2820 Copenhagen; and Diabetes Research, Novo Nordisk, DK-2880 Bagsvaerd, Denmark
Received 22 February 1996; accepted in final form 13 May 1996.
Wojtaszewski, Jørgen F. P., Bo F. Hansen, Birgitte
Ursø, and Erik A. Richter. Wortmannin inhibits both insulin-
and contraction-stimulated glucose uptake and transport in rat skeletal muscle. J. Appl. Physiol. 81(4):
1501-1509, 1996.
The role of phosphatidylinositol (PI) 3-kinase
for insulin- and contraction-stimulated muscle glucose transport was
investigated in rat skeletal muscle perfused with a cell-free
perfusate. The insulin receptor substrate-1-associated PI 3-kinase
activity was increased sixfold upon insulin stimulation but was
unaffected by contractions. In addition, the insulin-stimulated PI
3-kinase activity and muscle glucose uptake and transport in individual
muscles were dose-dependently inhibited by wortmannin with one-half
maximal inhibition values of ~10 nM and total inhibition at 1 µM.
This concentration of wortmannin also decreased the
contraction-stimulated glucose transport and uptake by ~30-70%
without confounding effects on contractility or on muscle ATP and
phosphocreatine concentrations. At higher concentrations
(3 and 10 µM), wortmannin completely blocked the
contraction-stimulated glucose uptake but also decreased the
contractility. In conclusion, inhibition of PI 3-kinase with wortmannin
in skeletal muscle coincides with inhibition of insulin-stimulated glucose uptake and transport. Furthermore, in contrast to recent findings in incubated muscle, wortmannin also inhibited
contraction-stimulated glucose uptake and transport. The inhibitory
effect of wortmannin on contraction-stimulated glucose uptake may be
independent of PI 3-kinase activity or due to inhibition of a
subfraction of PI 3-kinase with low sensitivity to wortmannin.
hindlimb; signaling; phosphatidylinositol 3-kinase
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