These authors contributed equally to this work.
Intracellular signal transduction pathways induced by leptin in C2C12 cells
Article first published online: 2 JAN 2013
© The Author(s) Journal compilation © 2005 International Federation for Cell Biology
Cell Biology International
Volume 29, Issue 7, pages 542–550, July 2005
How to Cite
Maroni, P., Bendinelli, P. and Piccoletti, R. (2005), Intracellular signal transduction pathways induced by leptin in C2C12 cells. Cell Biology International, 29: 542–550. doi: 10.1016/j.cellbi.2005.03.008
- Issue published online: 2 JAN 2013
- Article first published online: 2 JAN 2013
- Received 2 September 2004; revised 23 January 2005; accepted 15 March 2005
- C2C12 cells;
- Signal transduction
As experimental evidence suggests that leptin may have direct effects on peripheral tissues, we investigated some of the transductional molecules induced by leptin in C2C12 cells. In immunoprecipitation experiments using anti-p85 antibodies (a regulatory subunit of phosphatidylinositol-3-kinase; PI3K), we observed a significant increase in PI3K activity. Immunoblot analyses showed that Akt, GSK3, ERK1, ERK2, and p38 mitogen-activated protein kinase (p38 MAPK) phosphorylation significantly increased after leptin treatment. Protein kinase C (PKC)-ζ was also activated by leptin, as documented by an immunocomplex kinase assay and immunoblotting experiments. The treatment of C2C12 cells with Wortmannin before leptin administration inhibited induction of the phosphorylation of ERKs (extracellular signal-regulated kinases) but not that of p38 MAPK, whereas pre-treatment with a PKC-ζ inhibitor partially decreased ERK phosphorylation. Taken together, our in vitro results further support the hypothesis that leptin acts acutely on skeletal muscle tissue through some of the components of insulin signalling, including PKC-ζ.