Human skeletal muscle cell differentiation is associated with changes in myogenic markers and enhanced insulin-mediated MAPK and PKB phosphorylation
Article first published online: 17 MAR 2004
DOI: 10.1111/j.1365-201X.2004.01259.x
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How to Cite
Al-Khalili, L., Krämer, D., Wretenberg, P. and Krook, A. (2004), Human skeletal muscle cell differentiation is associated with changes in myogenic markers and enhanced insulin-mediated MAPK and PKB phosphorylation. Acta Physiologica Scandinavica, 180: 395–403. doi: 10.1111/j.1365-201X.2004.01259.x
Publication History
- Issue published online: 17 MAR 2004
- Article first published online: 17 MAR 2004
- Received 29 April 2003, accepted 19 December 2003
- Abstract
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Keywords:
- Akt/protein kinase B;
- cell culture;
- ERK mitogen-activated protein kinase
Abstract
Aim: We hypothesized that myogenic differentiation of HSMC would yield a more insulin responsive phenotype.
Methods: We assessed expression of several proteins involved in insulin action or myogenesis during differentiation of primary human skeletal muscle cultures (HSMC).
Results: Differentiation increased creatine kinase activity and expression of desmin and myocyte enhancer factor (MEF)2C. No change in expression was observed for big mitogen-activated protein kinase (BMK1/ERK5), MEF2A, insulin receptor (IR), hexokinase II, and IR substrates 1 and 2, while expression of glycogen synthase, extracellular signal-regulated kinase 1 and 2 (ERK1/2 MAP kinase) and the insulin responsive aminopeptidase increased after differentiation. In contrast to protein kinase B (PKB)a, expression of (PKB)b increased, with differentiation. Both basal and insulin-stimulated PI 3-kinase activity increased with differentiation. Insulin-mediated phosphorylation of PKB and ERK1/2 MAP kinase increased after differentiation.
Conclusion: Components of the insulin-signalling machinery are expressed in myoblast and myotube HSMC; however, insulin responsiveness to PKB and ERK MAP kinase phosphorylation increases with differentiation.

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