The effect of estrogen on Akt signalling and protein synthesis in C2C12 mouse skeletal myotubes

Stefanetti, R., Turner, A., Quick, M., Snow, R. and Russell, A. 2008, The effect of estrogen on Akt signalling and protein synthesis in C2C12 mouse skeletal myotubes, in AuPS 2008 : Proceedings of the Australian Physiological Society Meeting, Australian Physiological Society, [Melbourne, Vic.].

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Title The effect of estrogen on Akt signalling and protein synthesis in C2C12 mouse skeletal myotubes
Author(s) Stefanetti, R.
Turner, A.ORCID iD for Turner, A.
Quick, M.
Snow, R.ORCID iD for Snow, R.
Russell, A.ORCID iD for Russell, A.
Conference name Australian Physiological Society Meeting (2008 : Melbourne, Vic.)
Conference location Melbourne, Vic.
Conference dates 30 Nov.-3rd Dec. 2008
Title of proceedings AuPS 2008 : Proceedings of the Australian Physiological Society Meeting
Publication date 2008
Publisher Australian Physiological Society
Place of publication [Melbourne, Vic.]
Summary The maintenance of skeletal muscle mass is a critical component of health in both chronic wasting diseases and aging. A considerable amount of progress has been made in the understanding of the signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Akt is seen as a key molecular protein involved in the maintenance of skeletal muscle mass as it has the dual ability to positively influence protein syntheses and negatively regulate protein degradation in its active state (Glass, 2003). Potential mechanisms which may assist with maintaining skeletal muscle mass are the estrogen hormones. Estrogens increase the proliferation of mouse and rat myoblasts and can also attenuate immobilization-induced skeletal muscle atrophy in rats in vivo (Kahlert et al., 1997). No studies have investigated the effect of estrogens on the activation of skeletal muscle hypertrophy and atrophy signalling pathways. Estrogens may contribute to maintaining skeletal muscle mass via their activation of the Akt signalling pathways. Therefore, the aims of the present study were to determine if treatment of C2C12 myotubes with either 17β-estrodiol or estrone increases the activity of Akt and its downstream anabolic signalling proteins, GSK, p70s6k and 4E-BP1 and decreases its catabolic stimulating targets, FOXO, atrogin-1 and MuRF-1. A secondary aim was to determine if this was associated with an increased rate of protein synthesis.

C2C12 myotubes were incubated at 37°C in serum free DMEM without phenol red containing 10 000 units/ml penicillin, 10 000 μg/ml streptomycin, and 250μg/ml amphotericin B for 24h. Myotubes were then stimulated with 17-β estradiol (10nM) for 24h. Phosphorylated and total proteins for Akt, p70S6k, GSK3β, 4E-BP1, FOXO and atrogin-1 were measured using western blotting techniques. Atrogin-1 and MuRF1 mRNA levels were measured using real time-PCR. Protein synthesis rates were measured by incorporation of [3H]-tyrosine into the myotubes during the last hour of treatment.

Compared to control myotubes, treatment with 17β-estradiol increased the ratio of phosphorylated to total protein contents for Akt, GSK-3β and P70s6k by, 1.62, 1.53 and 2.2 fold, respectively (n=6 per group; p < 0.05). There was, however, no difference in the ratios of phosphorylated to total 4E-BP1 or Foxo3a or Atrogin-1 and MuRF1 mRNA. Protein synthesis rates remained unchanged.

This study demonstrates that in C2C12 mouse myotubes, 17β-estradiol treatment increases the phosphorylation of the hypertrophy signalling protein, Akt, and its downstream hypertrophy signalling targets, GSK-3β and P70s6k; no associated changes in protein synthesis were observed. Future studies should investigate the ability of 17β-estradiol to activate these proteins in a model of myotube catabolism and to determine if protein degradation is attenuated.
Language eng
Field of Research 110306 Endocrinology
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category E3 Extract of paper
Copyright notice ©2008, Australian Physiological Society
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