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  • 1.
    Mattsson, C. Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Flockhart, Mikael
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    Söderlund, Karin
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Hendo, Gina
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Jakobsson, Madeleine
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    Effects of prolonged low intensity exercise with energy deficit (military training operation) on markers of muscle protein turnover.2015Conference paper (Refereed)
    Abstract [en]

    Introduction

    It is well known that ultra-endurance exercise, such as Adventure racing and military operations, often induce substantial energy deficits. This suggests a catabolic state, but the exact effects on protein turnover have not yet been sufficiently investigated. The aim of this study was to examine several markers involved in muscle protein turnover before and after a multi-day physically demanding military training operation.

    Methods

    Seven female (age 21 ± 5 years, weight 71.2 ± 6.6 kg) and seventeen male (age 20 ± 1 years, weight 76.6 ± 6.2 kg) performed a 185 hours military training operation. Energy intake was estimated from food supply and energy expenditure was calculated from continuous heart rate and accelerometer recordings. Muscle biopsies were taken from M Vastus Lateralis before and after the operation.

    Results

    A negative energy balance of 1,500-2,000 kcal/24 hours was estimated. Body weight declined 3.4 (95% CI 3.0-3.8) kg and muscle explosive strength, evaluated from squad and counter movement jumps, was reduced 5 and 6 %, respectively, after the operation with no difference between genders. Muscle glycogen content was reduced from 269 ± 58 to 181 ± 44 mmol/kg dry muscle (p<0.05) with no difference between genders. Muscle content of mTOR and p70 as well as MAFbx were unchanged while the protein content of MuRF-1 was significantly down regulated in both genders.

    Discussion

    The study indicated that prolonged low intensity exercise with substantial energy deficit reduces muscle function and muscle glycogen content. Proteins for muscle synthesis mTOR and p70 were unchanged while the down regulation of MuRF-1 indicates a protection against muscle break down during the energy deficit situation, preserving the muscle mass.

  • 2.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Effects of exercise and amino acid intake on mechanisms regulating protein synthesis and breakdown in human muscle2016Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Skeletal muscle adapts differently to specific modes of exercise, where resistance training results in muscle growth and endurance training induces mitochondrial biogenesis. These are results of molecular events that occur after each exercise session, increasing the expression of specific genes and the rate of both synthesis and breakdown of protein. The rate of protein synthesis is controlled by the mTORC1 signaling pathway, which is potently stimulated by resistance exercise and amino acid, and their combined effect is needed for muscle growth. The essential amino acids (EAA) are responsible for the stimulation of protein synthesis and here leucine has been attributed specific attention, but its particular role among the EAA, and the involvement of the other branched-chain amino acids (BCAA) is unclear. Endurance exercise activates the protein AMPK which, in animal models, has been shown to inhibit mTORC1 signaling and protein synthesis.  Suggesting that concurrent endurance and resistance exercise could restrain muscle growth, but it is unknown if this mechanism is relevant in exercising human muscle. Little is known about the regulation of protein breakdown and although much attention has been given the proteins MuRF-1 and MAFbx which target proteins for degradation, their role requires further investigation. The aim of thesis was to address the mentioned uncertainties by examining how different modes of exercise and amino acids affect mTORC1 signaling, protein synthesis and markers of protein breakdown in human muscle.

    In study I, the influence of high intensity endurance exercise on subsequent resistance exercised induced mTORC1 signaling was examined. Despite robust activation of AMPK by the endurance exercise there was no inhibition of mTORC1 signaling or protein synthesis during recovery from resistance exercise. Study II utilized a similar set up, but with the difference that resistance exercise was performed with the triceps. The cycling exercise reduced the resistance exercise stimulated mTORC1 signaling immediately after the exercise, but during the recovery period mTORC1 signaling and protein synthesis was similar between trials. Concurrent exercise induced the mRNA expression of MuRF-1 and that of PGC-1α, the master regulator of mitochondrial biogenesis, in both studies, despite that the exercise modes in study II were separated between legs and arms. In study III, the effect of an EAA supplement with or without leucine, in the stimulation of mTORC1 signaling in connection with resistance exercise was examined. Intake of EAA robustly stimulated mTORC1 signaling after exercise, but this was only minor when leucine was excluded from the supplement. In study IV, subjects were supplied with leucine, BCAA, EAA or placebo in a randomized fashion during four sessions of resistance exercise. Leucine alone stimulated mTORC1 signaling after the exercise, but both the amplitude and extent of stimulation was substantially greater with EAA, an effect that was largely mediated by the BCAA as a group.

    In conclusion, endurance exercise prior to resistance exercise using the leg or arm muscles does not affect mTORC1 signaling or protein synthesis during the three hour recovery period from exercise, supporting compatibility between resistance- and endurance exercise induced signaling. Concurrent exercise increases the expression of the proteolytic marker MuRF-1 compared to resistance exercise only, which could indicate both and increased demand of cellular adaptive remodeling or a more direct detrimental proteolytic effect. Leucine is crucial among the EAA in the stimulation of mTORC1 signaling after exercise, its effect is however potentiated by intake of the remaining EAA. As a supplement a mixture of EAA must be regarded preferable, although the effect is largely mediated by the BCAA as a group.  

     

  • 3.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    Hendo, Gina
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Jakobsson, Madelene
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Mattsson, C Mikael
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Ekblom-Bak, Elin
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Flockhart, Mikael
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Research group for Mitokondriell funktion och metabolisk kontroll.
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Söderlund, Karin
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    Increased autophagy signaling but not proteasome activity in human skeletal muscle after prolonged low-intensity exercise with negative energy balance2017In: Physiological Reports, E-ISSN 2051-817X, Vol. 5, no 23, article id e13518Article in journal (Refereed)
    Abstract [en]

    Little is known about the molecular regulation of skeletal muscle protein turnover during exercise in field conditions where energy is intake inadequate. Here, 17 male and 7 female soldiers performed an 8 day long field based military operation. Vastus lateralis muscle biopsies, in which autophagy, the ubiquitin-proteasome system and the mTORC1 signaling pathway where studied, were collected before and after the operation. The 187 h long operation resulted in a 15% and 29% negative energy balance as well as a 4.1% and 4.6% loss of body mass in women and men respectively. After the operation protein levels of ULK1 as well as the phosphorylation of ULK1Ser317 and ULK1Ser555 had increased by 11%, 39% and 13%, respectively, and this was supported by a 17% increased phosphorylation of AMPKThr172 (P<0.05). The LC3b-I/II ratio was 3-fold higher after compared to before the operation (P<0.05), whereas protein levels of p62/SQSTM1 were unchanged. The β1, β2, and β5 activity of the proteasome and protein levels of MAFbx did not change, while levels of MuRF-1 were slightly reduced (6%, P<0.05). Protein levels and phosphorylation status of key components in the mTORC1 signaling pathway remained at basal levels after the operation. Muscle levels of glycogen decreased from 269±12 to 181±9 mmol ∙ kg dry muscle-1 after the exercise period (P<0.05). In conclusion, the 8 days of field based exercise resulted in induction of autophagy without any increase in proteasome activity or protein ubiquitination. Simultaneously, the regulation of protein synthesis through the mTORC1 signaling pathway was maintained.

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