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Am J Physiol Endocrinol Metab 284: E102-E109, 2003. First published October 1, 2002; doi:10.1152/ajpendo.00028.2002
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Vol. 284, Issue 1, E102-E109, January 2003

Adrenalectomy enhances the insulin sensitivity of muscle protein synthesis

Wen Long, Eugene J. Barrett, Liping Wei, and Zhenqi Liu

Division of Endocrinology and Metabolism, Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908

After confirming that adrenalectomy per se does not affect skeletal muscle protein synthesis rates, we examined whether endogenously produced glucocorticoids modulate the effect of physiological insulin concentrations on protein synthesis in overnight-fasted rats 4 days after either a bilateral adrenalectomy (ADX), ADX with dexamethasone treatment (ADX + DEX), or a sham operation (Sham; n = 6 each). Rats received a 3-h euglycemic insulin clamp (3 mU · min-1 · kg-1). Rectus muscle protein synthesis was measured at the end of the clamp, and the phosphorylation states of protein kinase B (Akt), eukaryotic initiation factor 4E-binding protein 1 (4E-BP1), and ribosomal protein S6 kinase (p70S6K) were quantitated before and after the insulin clamp. The basal phosphorylation states of Akt, 4E-BP1, and p70S6K were similar between ADX and Sham rats. Insulin significantly enhanced the phosphorylation of Akt (P < 0.03), 4E-BP1 (P = 0.003), and p70S6K (P < 0.002) in ADX but not in Sham rats. Protein synthesis was significantly greater after insulin infusion in ADX than in Sham rats (P = 0.01). Glucocorticoid replacement blunted the effect of insulin on Akt, 4E-BP1, and p70S6K phosphorylation and protein synthesis. In conclusion, glucocorticoid deficiency enhances the insulin sensitivity of muscle protein synthesis, which is mediated by increased phosphorylation of translation initiation-regulatory proteins.

dexamethasone; translation initiation; protein kinase B; eukaryotic initiation factor 4E-binding protein-1; p70 S6 kinase


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