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J. Biol. Chem., Vol. 277, Issue 27, 23977-23980, July 5, 2002
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From the Department of Cellular and Molecular Physiology, The
Pennsylvania State University College of Medicine, Hershey,
Pennsylvania 17033
AMP-activated protein kinase (AMPK) is viewed as
an energy sensor that acts to modulate glucose uptake and fatty acid
oxidation in skeletal muscle. Given that protein synthesis is a high
energy-consuming process, it may be transiently depressed during
cellular energy stress. Thus, the intent of this investigation was to
examine whether AMPK activation modulates the translational control of protein synthesis in skeletal muscle. Injections of
5-aminoimidazole-4-carboxamide 1-
-D-ribonucleoside
(AICAR) were used to activate AMPK in male rats. The activity of
1 AMPK remained unchanged in gastrocnemius muscle from
AICAR-treated animals compared with controls, whereas 2
AMPK activity was significantly increased (51%). AICAR treatment resulted in a reduction in protein synthesis to 45% of the control value. This depression was associated with decreased activation of
protein kinases in the mammalian target of rapamycin (mTOR) signal
transduction pathway as evidenced by reduced phosphorylation of protein
kinase B on Ser473, mTOR on Ser2448, ribosomal
protein S6 kinase on Thr389, and eukaryotic initiation
factor eIF4E-binding protein on Thr37. A reduction in eIF4E
associated with eIF4G to 10% of the control value was also noted. In
contrast, eIF2B activity remained unchanged in response to AICAR
treatment and therefore would not appear to contribute to the
depression in protein synthesis. This is the first investigation to
demonstrate changes in translation initiation and skeletal muscle
protein synthesis in response to AMPK activation.
To whom correspondence should be addressed: Dept. of Cellular and
Molecular Physiology, Penn State College of Medicine, H166, 500 University Dr., Hershey, PA 17033. Tel.: 717-531-8566; Fax: 717-531-7667; E-mail: jjefferson@psu.edu.
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