Increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibers

Koopman, René; Zorenc, Antoine H. G.; Gransier, Rudy J. J.; Cameron‐Smith, David; Loon, Luc J. C. van

doi:10.1152/ajpendo.00530.2005

Cited by 161 publications

(157 citation statements)

References 41 publications

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“…Previous studies showed elevated 4E-BP1 phosphorylation after resistance exercise (4,38). However, changes in phosphorylation of 4E-BP1 and p70S6K in response to a bout of exercise do not necessarily correspond, and some previous studies have failed to find elevated phosphorylation of 4E-BP1 (9,10,23,29). We also did not detect an elevated rate of 4E-BP1 phosphorylation 24 h after exercise throughout the training and detraining periods, suggesting differential regulation of 4E-BP1 and p70S6K.…”

Section: Discussioncontrasting

confidence: 74%

mTOR signaling response to resistance exercise is altered by chronic resistance training and detraining in skeletal muscle

Ogasawara

Kobayashi

Tsutaki

et al. 2013

Journal of Applied Physiology

119

107

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Section: Discussioncontrasting

confidence: 74%

mTOR signaling response to resistance exercise is altered by chronic resistance training and detraining in skeletal muscle

Ogasawara

Kobayashi

Tsutaki

et al. 2013

Journal of Applied Physiology

119

107

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“…A single bout of resistance exercise can increase AMPK Thr 172 phosphorylation (36) and AMPK ␣2 activity (37), but using similar resistance exercise to that used in the latter studies (36,37), AS160 phosphorylation was decreased in the present study. Although a significant increase in AMPK phosphorylation and ␣2-activity with exercise was not detected in the present study, ACC Ser 79 phosphorylation, an in vivo measure of AMPK activity, increased more than threefold.…”

Section: Discussionmentioning

confidence: 48%

Resistance Exercise and Insulin Regulate AS160 and Interaction With 14-3-3 in Human Skeletal Muscle

et al. 2007

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A single bout of aerobic exercise can enhance insulin action, but whether a similar effect occurs after resistance exercise is unknown. Hyperinsulinemic-euglycemic clamps were performed on eight male subjects at rest and after a single bout and three repeated bouts of resistance exercise over 7 days. Skeletal muscle biopsies were taken before and after the clamp and immediately after a single exercise bout. Whole-body insulin action measured by glucose infusion rate decreased (P < 0.05) after a single exercise bout, whereas in response to repeated bouts of resistance exercise, the glucose infusion rate was similar to the rest trial. In skeletal muscle, Akt substrate of 160 kDa (AS160) phosphorylation, an Akt substrate implicated in the regulation of GLUT4 translocation, and its interaction with 14-3-3 was decreased (P < 0.05) only after a single exercise bout. Insulin increased (P < 0.05) phosphorylation of AS160 and its interaction with 14-3-3, but the insulin response was not influenced by resistance exercise. Phosphorylation of insulin receptor substrate-1 and Akt were similar to changes in AS160 phosphorylation after exercise and/or insulin. In conclusion, a single bout of resistance exercise impairs whole-body insulin action. Regulation of AS160 and interaction with 14-3-3 in skeletal muscle are influenced by resistance exercise and insulin but do not fully explain the effect of resistance exercise on wholebody insulin action.

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“…Indeed, both resistance-type and endurance-type exercise increase AMPK activity (Fig. 2) (13,19,32,45) and decrease 4EBP1 phosphorylation ( Fig. 1) (11, 13, 19), and resistance-exercise may actually decrease PKB activity (11) in skeletal muscle of humans.…”

Section: Discussionmentioning

confidence: 99%

Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type

Rose¹,

Bisiani²,

Vistisen³

et al. 2009

American Journal of Physiology-Regulatory, Integrative and Comp

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Rose AJ, Bisiani B, Vistisen B, Kiens B, Richter EA. Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type. Am J Physiol Regul Integr Comp Physiol 296: R326 -R333, 2009. First published November 26, 2008 doi:10.1152/ajpregu.90806.2008.-Protein synthesis in skeletal muscle is known to decrease during exercise, and it has been suggested that this may depend on the magnitude of the relative metabolic stress within the contracting muscle. To examine the mechanisms behind this, the effect of exercise intensity on skeletal muscle eukaryotic elongation factor 2 (eEF2) and eukaryotic initiation factor 4E binding protein 1 (4EBP1) phosphorylation, key components in the mRNA translation machinery, were examined together with AMP-activated protein kinase (AMPK) in healthy young men. Skeletal muscle eEF2 phosphorylation at Thr 56 increased during exercise but was not influenced by exercise intensity, and was lower than rest 30 min after exercise. On the other hand, 4EBP1 phosphorylation at Thr 37/46 decreased during exercise, and this decrease was greater at higher exercise intensities and was similar to rest 30 min after exercise. AMPK activity, as indexed by AMPK ␣-subunit phosphorylation at Thr 172 and phosphorylation of the AMPK substrate ACC␤ at Ser 221 , was higher with higher exercise intensities, and these indices were higher than rest after high-intensity exercise only. Using immunohistochemistry, it was shown that the increase in skeletal muscle eEF2 Thr 56 phosphorylation was restricted to type I myofibers. Taken together, these data suggest that the depression of skeletal muscle protein synthesis with endurance-type exercise may be regulated at both initiation (i.e., 4EBP1) and elongation (i.e., eEF2) steps, with eEF2 phosphorylation contributing at all exercise intensities but 4EBP1 dephosphorylation contributing to a greater extent at high vs. low exercise intensities. protein synthesis; translation; elongation; initiation; AMPK IT IS RECOGNIZED THAT THE understanding of the mechanisms controlling skeletal muscle protein turnover may aid in the development of novel therapies to combat skeletal muscle diseases (30). The control of protein turnover in skeletal muscle during exercise is poorly understood (30). It is known that skeletal muscle protein synthesis is blunted during exercise (2, 13). A recent study (24) demonstrated that contractile activity was a potent stimulus to blunt net protein synthesis rate of rat skeletal muscle ex vivo and can even override the anabolic effect of insulin. Studies by BylundFellenius et al. (7) in perfused rat hindquarters demonstrated that protein synthesis rates were lower in contracting compared with resting skeletal muscle, particularly in fast-twitch muscles. In that study (7), it was shown that the magnitude of the blunting of protein synthesis was related to the magnitude of changes in high-energy phosphogens, indicating that signaling downstream of metabolic stress is a likely mechanism behind the fall...

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Increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibers

Cited by 161 publications

References 41 publications

mTOR signaling response to resistance exercise is altered by chronic resistance training and detraining in skeletal muscle

mTOR signaling response to resistance exercise is altered by chronic resistance training and detraining in skeletal muscle

Resistance Exercise and Insulin Regulate AS160 and Interaction With 14-3-3 in Human Skeletal Muscle

Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type

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