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Noll Physiological Research Center and Graduate Program in Physiology, Pennsylvania State University, University Park 16802; and Department of Cellular and Molecular Physiology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033
Translational control of protein synthesis depends on
numerous eukaryotic initiation factors (eIFs) and we have previously shown (Am. J. Physiol. Endocrinol. Metab. 276:
E721-E727, 1999) that increases in one factor, eIF2B, are
associated with increases in rates of protein synthesis after
resistance exercise in rats. In the present study we investigated
whether the eIF4E family of initiation factors is also involved with an
anabolic response to exercise. Male Sprague-Dawley rats either remained
sedentary (n = 6) or performed acute resistance exercise
(n = 6), and rates of protein synthesis were assessed in vivo
16 h after the last session of resistance exercise. eIF4E complexed to
eIF4G (eIF4E · eIF4G), eIF4E binding protein 1 (4E-BP1) complexed to eIF4E, and phosphorylation state of eIF4E and
4E-BP1 (
-form) were assessed in gastrocnemius. Rates of protein
synthesis were higher in exercised rats compared with sedentary rats
[205 ± 8 (SE) vs. 164 ± 5.5 nmol phenylalanine
incorporated · g
muscle
1 · h
1,
respectively; P < 0.05]. Arterial plasma insulin
concentrations were not different between the two groups. A trend
(P = 0.09) for an increase in eIF4E · eIF4G
with exercise was noted; however, no statistically significant
differences were observed in any of the components of the eIF4E family
in response to resistance exercise. These new data, along with our
previous report on eIF2B, suggest that the regulation of peptide chain
initiation after exercise is more dependent on eIF2B than on the eIF4E system.
translation; contractions; insulin
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