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Medientyp:
E-Artikel
Titel:
Interleukin-6 acts as insulin sensitizer on glycogen synthesis in human skeletal muscle cells by phosphorylation of Ser473 of Akt
Beteiligte:
Weigert, Cora;
Hennige, Anita M.;
Brodbeck, Katrin;
Häring, Hans U.;
Schleicher, Erwin D.
Erschienen:
American Physiological Society, 2005
Erschienen in:American Journal of Physiology-Endocrinology and Metabolism
Sprache:
Englisch
DOI:
10.1152/ajpendo.00448.2004
ISSN:
0193-1849;
1522-1555
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p> Previous studies showed an insulin-“desensitizing” action of IL-6 on glycogen synthesis in hepatocytes. We recently found no inhibition of the proximal steps of the insulin signal cascade in human skeletal muscle cells. Because 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<jats:sup>473</jats:sup> of Akt, but not of Thr<jats:sup>308</jats:sup> time dependently and we observed that IL-6 augments insulin-induced Ser<jats:sup>473</jats:sup> and Thr<jats:sup>308</jats:sup> 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, whereas IL-6 alone had only a marginal effect. IL-6 treatment of C57Bl/6 mice readily stimulated phosphorylation of Ser<jats:sup>473</jats:sup> in skeletal muscle. Our result that IL-6 did not induce Ser<jats:sup>473</jats:sup> 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. </jats:p>