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l-Alanylglutamine inhibits signaling proteins that activate protein degradation, but does not affect proteins that activate protein synthesis after an acute resistance exercise

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Abstract

Sustamine™ (SUS) is a dipeptide composed of alanine and glutamine (AlaGln). Glutamine has been suggested to increase muscle protein accretion; however, the underlying molecular mechanisms of glutamine on muscle protein metabolism following resistance exercise have not been fully addressed. In the present study, 2-month-old rats climbed a ladder 10 times with a weight equal to 75 % of their body mass attached at the tail. Rats were then orally administered one of four solutions: placebo (PLA-glycine = 0.52 g/kg), whey protein (WP = 0.4 g/kg), low dose of SUS (LSUS = 0.1 g/kg), or high dose of SUS (HSUS = 0.5 g/kg). An additional group of sedentary (SED) rats was intubated with glycine (0.52 g/kg) at the same time as the ladder-climbing rats. Blood samples were collected immediately after exercise and at either 20 or 40 min after recovery. The flexor hallucis longus (FHL), a muscle used for climbing, was excised at 20 or 40 min post exercise and analyzed for proteins regulating protein synthesis and degradation. All supplements elevated the phosphorylation of FOXO3A above SED at 20 min post exercise, but only the SUS supplements significantly reduced the phosphorylation of AMPK and NF-kB p65. SUS supplements had no effect on mTOR signaling, but WP supplementation yielded a greater phosphorylation of mTOR, p70S6k, and rpS6 compared with PLA at 20 min post exercise. However, by 40 min post exercise, phosphorylation of mTOR and rpS6 in PLA had risen to levels not different than WP. These results suggest that SUS blocks the activation of intracellular signals for MPB, whereas WP accelerates mRNA translation.

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Abbreviations

Akt:

Protein kinase B

AMPK:

5′ Adenosine monophosphate-activated protein kinase

FOXO3A:

Forkhead box O-3A

IGF-1:

Insulin-like growth factor-1

mTOR:

Mammalian target of rapamycin

NF-kB p65:

Nuclear factor kappa-light-chain-enhancer of activated B cells-p65

p70S6k:

70-kDa ribosomal S6 protein kinase

rpS6:

Ribosomal protein S6

MPS:

Muscle protein synthesis

MPB:

Muscle protein breakdown

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Acknowledgments

We would like to thank Lynne Kammer and all other colleagues in the Exercise Physiology and Metabolism Laboratory at the University of Texas at Austin for the excellent technical assistance.

Conflict of interest

This research was supported by a grant from Kyowa Hakko Bio Co., Ltd.

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Authors and Affiliations

  1. Exercise Physiology and Metabolism Laboratory, Department of Kinesiology and Health Education, University of Texas at Austin, Bellmont Hall 822E, Austin, TX, 78712-0360, USA

    Wanyi Wang, Ran Hee Choi, Geoffrey J. Solares, Zhenping Ding, Kyoungrae Kim & John L. Ivy

  2. Department of Physical Education, National Taipei University of Education, Taipei, Taiwan, Republic of China

    Hung-Min Tseng

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  1. Wanyi Wang
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  2. Ran Hee Choi
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  3. Geoffrey J. Solares
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Correspondence to John L. Ivy.

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Wang, W., Choi, R.H., Solares, G.J. et al. l-Alanylglutamine inhibits signaling proteins that activate protein degradation, but does not affect proteins that activate protein synthesis after an acute resistance exercise. Amino Acids 47, 1389–1398 (2015). https://doi.org/10.1007/s00726-015-1972-7

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