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1 Department of Internal Medicine, Division of Endocrinology, Metabolism, Pathobiochemistry and Clinical Chemistry, University of Tuebingen, Tuebingen, Germany
* To whom correspondence should be addressed. E-mail: enschlei{at}med.uni-tuebingen.de.
Previous studies showed an insulin-"desensitizing" action of interleukin-6 (IL-6) on glycogen synthesis in hepatocytes. We found recently no inhibition of the proximal steps of the insulin signal cascade in human skeletal muscle cells. Since these data indicate a possible tissue-specific effect of IL-6 we investigated the influence of IL-6 on insulin-stimulated glycogen synthesis in these cells. At first, we found that incubation of the cells with 20 ng/ml IL-6 alone induced phosphorylation of Ser-473 of Akt, but not of Thr-308 time-dependently and we observed that IL-6 augments insulin-induced Ser-473 and Thr-308 phosphorylation in the low nanomolar range of insulin. Moreover, IL-6 increased insulin-stimulated phosphorylation of glycogen synthase kinase-3. Accordingly, IL-6 enhanced glycogen synthesis in the presence of 3 and 10 nM insulin, while IL-6 alone had only a marginal effect. IL-6 treatment of C57Bl/6 mice readily stimulated phosphorylation of Ser-473 in skeletal muscle. Our result that IL-6 did not induce Ser-473 phosphorylation in the liver of these mice suggests a tissue-specific effect. Together, our data demonstrate a novel insulin sensitizing function of IL-6 on glycogen synthesis in skeletal muscle cells and indicate that IL-6 exerts cell/tissue-specific effects on insulin action.
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