The effect of short-term heat stress on protein synthesis signaling in isolated rat skeletal muscle

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  • Goto Ayumi
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University Sportology Center, Graduate School of Medicine, Juntendo University
  • Sekine Keiichi
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Oshima Rieko
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Sakon Ichika
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Iwamoto Mayu
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Osaki Tomohiko
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Haga Kotaro
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Hayashi Tatsuya
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University
  • Egawa Tatsuro
    Laboratory of Sports and Exercise Medicine, Graduate School of Human and Environmental Studies, Kyoto University Laboratory of Health and Exercise Sciences, Graduate School of Human and Environmental Studies, Kyoto University

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<p>Heat stress (HS) is a potent stimulus for activating glucose metabolism in skeletal muscles. However, the effect of short-term HS on protein turnover in skeletal muscles is unclear. This study aimed to investigate the effect of short-term HS on protein synthesis and protein degradation in skeletal muscles. The epitrochlearis muscle was isolated from male Sprague–Dawley rats weighing 150-160 grams (g) and incubated with or without HS at 42°C for 10 or 30 min in alpha minimum essential medium. HS for 30 min significantly decreased phosphorylation of 70-kDa ribosomal protein S6 kinase at Thr389 and 4E-binding protein 1 at Thr37/46. Correspondingly, HS for 30 min decreased the rate of protein synthesis. In contrast, HS had no effect on the expression of autophagy-related proteins, including microtubule-associated protein light chain 3 and p62, or on the mRNA expression of muscle-specific ubiquitin ligases, including muscle RING-finger 1 (MuRF1) and atrogin-1/MAFbx. These findings suggested that short-term HS for approximately 30 min is a physiologically relevant stimulus that suppresses protein synthesis signaling in skeletal muscles.</p>

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