PMID: 9003374Dec 15, 1996Paper

Insulin action in cultured human myoblasts: contribution of different signalling pathways to regulation of glycogen synthesis

The Biochemical Journal
S J HurelS J Yeaman

Abstract

A key metabolic action of insulin is the stimulation of non-oxidative glucose utilization in skeletal muscle, by increasing both glucose uptake and glycogen synthesis. The molecular mechanism underlying this process has been investigated using a variety of experimental systems. We report here the use of cultured human myoblasts to study insulin control of glycogen synthesis in humans. In these cells insulin stimulates glycogen synthesis approx. 2.2-fold, associated with a similar activation of glycogen synthase (GS) which occurs within 5-10 min of the addition of insulin. Insulin also causes inactivation of glycogen synthase kinase-3 (GSK-3) and activation of protein kinase B, both processes being sufficiently rapid to account for the effects of insulin on GS. Activation by insulin of the protein kinases p70s6K, p90s6K and extracellular signal-regulated kinase 2 (ERK2) is observed, but is significantly slower than the activation of GS. Selective inhibitors of the p70s6K pathway (rapamycin), the ERK2/p90s6K pathway (PD98059) and phosphatidylinositol 3-kinase (wortmannin) have been used to probe the contribution of these components to insulin signalling in human muscle. Wortmannin blocks activation of both glycogen synthesis and ...Continue Reading

Citations

Apr 21, 2009·Biochimie·Luisa Helena CazarolliFátima Regina Mena Barreto Silva
Jan 24, 2009·Computer Methods and Programs in Biomedicine·A CutroneG Vozzi
Jul 10, 2003·Molecular and Cellular Endocrinology·A RedondoMaría L Villanueva-Peñacarrillo
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