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  • 1.
    Chaillou, Thomas
    et al.
    Département Environnements opérationnels, Institut de Recherche Biomédicale des Armées Antenne de la Tronche, La Tronche, France.
    Koulmann, N.
    Département Environnements opérationnels, Institut de Recherche Biomédicale des Armées Antenne de la Tronche, La Tronche, France; Ecole du Val-de-Grâce, Paris, France.
    Meunier, A.
    Département Environnements opérationnels, Institut de Recherche Biomédicale des Armées Antenne de la Tronche, La Tronche, France.
    Malgoyre, A.
    Département Environnements opérationnels, Institut de Recherche Biomédicale des Armées Antenne de la Tronche, La Tronche, France.
    Serrurier, B.
    Département Environnements opérationnels, Institut de Recherche Biomédicale des Armées Antenne de la Tronche, La Tronche, France.
    Beaudry, M.
    Laboratoire Réponses cellulaires et fonctionnelles à l'hypoxie, Université Paris, Sorbonne-Paris-Cité, France.
    Bigard, X.
    Département Environnements opérationnels, Institut de Recherche Biomédicale des Armées Antenne de la Tronche, La Tronche, France; Ecole du Val-de-Grâce, Paris, France.
    Effect of hypoxia exposure on the phenotypic adaptation in remodelling skeletal muscle submitted to functional overload2013In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 209, no 4, p. 272-282Article in journal (Refereed)
    Abstract [en]

    Aim: To determine whether hypoxia influences the phenotypic adaptation of skeletal muscle induced by mechanical overload.

    Methods: Plantaris muscles of female rats were submitted to mechanical overload following synergist ablation. After 3 days of overload, rats were exposed to either hypobaric hypoxia (equivalent to 5500 m) or normoxia. Muscles were collected after 5, 12 and 56 days of overload (i.e. after 3, 9 and 53 days of hypoxia). We determined the myosin heavy chain (MHC) distribution, mRNA levels of myocyte-enriched calcineurin-integrating protein 1 (MCIP1) to indirectly assess calcineurin activity, the changes in oxidative capacity from the activities of citrate synthase (CS) and cytochrome c oxidase (COX), and the expression of regulators involved in mitochondrial biogenesis (Pgc-1α, NRF1 and Tfam) and degradation (BNIP-3).

    Results: Hypoxia did not alter the fast-to-slow MHC shift and the increase in calcineurin activity induced by overload; it only transiently slowed down the overload-induced transition in MHC isoforms. Hypoxia similarly decreased CS and COX activities in overloaded and control muscles. Nuclear respiratory factor 1 (NRF1) and transcription factor A (Tfam) mRNA and BNIP-3 protein were not influenced by hypoxia in overloaded muscles, whereas Pgc-1α mRNA and protein contents did not correlate with changes in oxidative capacity.

    Conclusion: Hypoxia is not a critical stimulus to modulate the fast-to-slow MHC transition associated with overload. Thus, the impairment of the fast-to-slow fibre shift often observed during post-natal development in hypoxia could be explained by the lower voluntary locomotor activity associated with hypoxia. Hypoxia alters mitochondrial oxidative capacity, but this adaptive response is similar in overloaded and control muscles.

  • 2.
    Cheng, A
    et al.
    Karolinska Institutet, Stockholm, Sweden.
    Allodi, I
    Karolinska Institutet, Stockholm, Sweden.
    Chaillou, Thomas
    Karolinska Institutet, Stockholm, Sweden.
    Thams, S
    Karolinska Institutet, Stockholm, Sweden.
    Ivarsson, N
    Karolinska Institutet, Stockholm, Sweden.
    Schlittler, M
    Karolinska Institutet, Stockholm, Sweden.
    Lanner, J
    Karolinska Institutet, Stockholm, Sweden.
    Hedlund, E
    Karolinska Institutet, Stockholm, Sweden.
    Andersson, D
    Karolinska Institutet, Stockholm, Sweden.
    Increased fatigue resistance and preserved specific force in intact single muscle fibres from the SOD1G93A mouse model of ALS2017In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 219, no S710, p. 17-17, article id P-28Article in journal (Refereed)
    Abstract [en]

    Introduction: Amyotrophic lateral sclerosis (ALS) is a motor neurone disease characterized by degeneration and loss of motor neurones, leading to severe muscle weakness and paralysis. Although motor neurone degeneration is already a well-characterized symptom that contributes to muscle weakness in the SOD1G93A mouse model of ALS, the purpose of the current study was to determine whether muscle weakness in ALS can be attributed to impaired intrinsic force generation in skeletal muscles of SOD1G93A mice.

    Methods: Experiments were performed on whole muscles and mechanically dissected intact single fibres from the flexor digitorum brevis (FDB) muscle of SOD1G93A mice at three age groups of 50, 125 and 150 days of age (P50, P125 and P150). Myoplasmic free [Ca2+] ([Ca2+]i) was measured using the fluorescent indicator, indo-1.

    Results: Motor neurone loss and decreased force were evident in whole FDB muscles of P125–150 mice. In the intact single muscle fibres however, specific force, tetanic [Ca2+]iand resting [Ca2+]i were similar in single FDB fibres from symptomatic P125–150 SOD1G93A and age-matched wild-type littermates. The most intriguing finding was a markedly greater fatigue resistance in single fibres from P125–150 SOD1G93A vs. wild-type mice, which was not present in asymptomatic young P50 SOD1G93A mice. No shift in fibre-type distribution was observed in whole FDB muscles to explain the increased fatigue resistance of single fibres from P125–150 SOD1G93A mice.

    Conclusion: These results support the hypothesis that muscle weakness in ALS is not attributed to intrinsicdefects in skeletal muscle fibre force generation.

  • 3.
    Folkesson, Mattias
    et al.
    Örebro University, School of Health and Medical Sciences.
    Mackey, A. L.
    Institute of Sports Medicine, Bispebjerg Hospital and Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
    Holm, L.
    Institute of Sports Medicine, Bispebjerg Hospital and Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
    Kjaer, M.
    Institute of Sports Medicine, Bispebjerg Hospital and Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
    Paulsen, G.
    Department of Sports Medicine, Norwegian School of Sports Sciences, Oslo, Norway.
    Raastad, T.
    Department of Sports Medicine, Norwegian School of Sports Sciences, Oslo, Norway.
    Henriksson, J.
    Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
    Kadi, Fawzi
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden.
    Immunohistochemical changes in the expression of HSP27 in exercised human vastus lateralis muscle2008In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 194, no 3, p. 215-222Article in journal (Refereed)
    Abstract [en]

    Aim: The role of HSP27 in the adaptive process of skeletal muscle to exercise, especially in humans, is not well understood. The objective of this study was to investigate immunohistochemical changes in HSP27 expression in human vastus lateralis muscle following resistance and endurance exercises.

    Methods: Two different exercise protocols were used: (1) one-leg ergometer cycling (EC, n = 6) consisting of two 30-min bouts at 40% and 75% of peak oxygen uptake, respectively, and (2) leg extension resistance exercise (RE, n = 9) including 10 sets of eight repetitions at a load corresponding to 70% of one maximal repetition (1RM). Immunohistochemistry using specific monoclonal antibodies was used to determine the location of HSP27 protein in muscle biopsies from human vastus lateralis.

    Results: Our results show that RE, but not EC, induced a significant appearance of scattered accumulations of HSP27 protein in muscle fibres from five of nine subjects. The number of fibres with accumulation of HSP27 in RE ranged from 0% to 32% with a mean of 6.3% of the total number of fibres.

    Conclusion: We conclude that this rapid HSP27 protein relocation after RE is an important player in the cellular remodelling of human muscle fibres in response to exercise involving high-force contractions, but not in response to endurance exercises.

  • 4.
    Folkesson, Mattias
    et al.
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden.
    Mackey, Abigail L.
    Department of Orthopaedic Surgery M, Faculty of Health Sciences, Institute of Sports Medicine, Bispebjerg Hospital, Copenhagen, Denmark; Centre for Healthy Ageing, University of Copenhagen, Copenhagen, Denmark.
    Langberg, Henning
    Department of Orthopaedic Surgery M, Faculty of Health Sciences, Institute of Sports Medicine, Bispebjerg Hospital, Copenhagen, Denmark; Centre for Healthy Ageing, University of Copenhagen, Copenhagen, Denmark.
    Oskarsson, Eva
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden.
    Piehl-Aulin, Karin
    School of Health and Medical Sciences, Örebro University, Örebro, Sweden; Department of Clinical Sciences, Danderyds Hospital, Karolinska Institutet, Stockholm, Sweden.
    Henriksson, Jan
    Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
    Kadi, Fawzi
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden.
    The expression of heat shock protein in human skeletal muscle: effects of muscle fibre phenotype and training background2013In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 209, no 1, p. 26-33Article in journal (Refereed)
    Abstract [en]

    Aim: Exercise-induced adaptations of skeletal muscle are related to training mode and can be muscle fibre type specific. This study aimed to investigate heat shock protein expression in type I and type II muscle fibres in resting skeletal muscle of subjects with different training backgrounds.

    Methods: Three groups of subjects were included: healthy active not engaged in any training programme (ACT, n = 12), resistance trained (RES, n = 6) and endurance trained (END, n = 8). Biopsies were obtained from vastus lateralis, and immunohistochemistry was performed using monoclonal antibodies against myosin heavy chain I and IIA, αB-crystallin, HSP27, HSP60 and HSP70.

    Results: In ACT and RES, but not in END, a fibre type–specific expression with higher staining intensity in type I than type II fibres was seen for αB-crystallin. The opposite (II > I) was found for HSP27 in subjects from ACT (6 of 12 subjects) and RES (3 of 6), whereas all subjects from END displayed uniform staining. HSP60 showed no fibre-specific expression. HSP70 displayed a fibre-specific expression pattern (I > II) in ACT (4 of 12), but not in END or RES.

    Conclusion: This study shows that the level of expression of the different HSPs in human skeletal muscle is influenced by muscle fibre phenotype. The fibre type–specific expression of HSP70 is influenced by resistance and endurance training, whereas those of αB-crystallin and HSP27 is influenced only by endurance training, suggesting the existence of a training-modality-specific action on the adaptive processes including heat shock proteins in human skeletal muscle.

  • 5.
    Khanal, P.
    et al.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Axel, A. M. D.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Kongsted, A. H.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Husted, S. V.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Johnsen, L.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Pandey, Deepak
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark; School of Science and Technology, Örebro University, Örebro, Sweden.
    Pedersen, K. L.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Birtwistle, M.
    Early Life Research Unit, Academic Division of Child Health, School of Medicine, Nottingham University, Nottingham, UK.
    Markussen, B.
    Department of Mathematical Sciences, Faculty of Science, Laboratory of Applied Statistics, University of Copenhagen, Copenhagen, Denmark.
    Kadarmideen, H. N.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Nielsen, M. O.
    Department of Veterinary Clinical and Animal Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Late gestation under- and overnutrition have differential impacts when combined with a post-natal obesogenic diet on glucose-lactate-insulin adaptations during metabolic challenges in adolescent sheep2015In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 213, no 2, p. 519-536Article in journal (Refereed)
    Abstract [en]

    Aim: To determine whether late gestation under- and overnutrition programme metabolic plasticity in a similar way, and whether metabolic responses to an obesogenic diet in early post-natal life depend on the foetal nutrition history.

    Methods: In a 3x2 factorial design, twin-pregnant ewes were for the last 6weeks of gestation (term=147days) assigned to HIGH (N=13; 150 and 110% of energy and protein requirements, respectively), NORM (N=9; 100% of requirements) or LOW (N=14; 50% of requirements) diets. The twin offspring were raised on high-carbohydrate-high-fat (HCHF; N=35) or conventional (CONV; N=35) diets from 3days to 6months of age (around puberty). Then intravenous glucose (GTT; overnight fasted), insulin (ITT; fed) and propionate (gluconeogenetic precursor; PTT; both fed and fasted) tolerance tests were conducted to evaluate (hepatic) metabolic plasticity.

    Results: Prenatal malnutrition differentially impacted adaptations of particularly plasma lactate followed by glucose, cholesterol and insulin. This was most clearly expressed during PTT in fasted lambs and much less during ITT and GTT. In fasted lambs, propionate induced more dramatic increases in lactate than glucose, and HIGH lambs became more hyperglycaemic, hyperlactataemic and secreted less insulin compared to the hypercholesterolaemic LOW lambs. Propionate-induced insulin secretion was virtually abolished in fasted HCHF lambs, but upregulated in fasted compared to fed CONV lambs. HCHF lambs had the greatest glucose-induced insulin secretory responses.

    Conclusion: Prenatal malnutrition differentially programmed glucose-lactate metabolic pathways and cholesterol homeostasis. Prenatal overnutrition predisposed for hyperglycaemia and hyperlactataemia, whereas undernutrition predisposed for hypercholesterolaemia upon exposure to an obesogenic diet. Prenatal overnutrition (not undernutrition) interfered with pancreatic insulin secretion by non-glucose-dependent mechanisms.

  • 6.
    Kvorning, T
    et al.
    Team Danmark, The House of Sport, Brøndby, Denmark; Institute of Sport Science and Clinical Biomechanics, University of Southern Denmark, Odense, Denmark.
    Kadi, Fawzi
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden.
    Schjerling, P
    Institute of Sports Medicine, Department of Orthopedic Surgery, Bispebjerg Hospital, Copenhagen, Denmark; Center for Healthy Aging, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
    Andersen, M
    Department of Endocrinology, Odense University Hospital, Odense, Denmark.
    Brixen, K
    Department of Endocrinology, Odense University Hospital, Odense, Denmark.
    Suetta, C
    Division of Clinical Physiology and Nuclear Medicine, Department of Diagnostics, Glostrup University Hospital, Copenhagen, Denmark.
    Madsen, K
    Department of Food and Nutrition, and Sport Exercise, University of Gothenburg, Gothenburg, Sweden.
    The activity of satellite cells and myonuclei following 8 weeks of strength training in young men with suppressed testosterone levels2015In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 213, no 3, p. 676-687Article in journal (Refereed)
    Abstract [en]

    AIM: To investigate how suppression of endogenous testosterone during an 8-week strength training period influences the activity of satellite cells and myonuclei.

    METHODS: Twenty-two moderately trained young men participated in this randomized, placebo-controlled, and double-blinded intervention study. The participants were randomized to treatment with a GnRH analogue, goserelin (n = 12), which suppresses testosterone or placebo (n = 10) for 12 weeks. The strength training period of 8 weeks started after 4 weeks of treatment and included exercises for all major muscles. Biopsies were obtained from the mid-portion of the vastus lateralis muscle.

    RESULTS: Testosterone resting level in goserelin was 10-20 times lower compared with placebo, and the training-induced increase in the level of testosterone was abolished in goserelin. Training increased satellite cells number in type II fibres by 20% in placebo and by 52% in goserelin (P < 0.01), whereas the myonuclear number significantly increased by 12% in type II fibres in placebo and remained unchanged in goserelin (P < 0.05). No changes in satellite cells and myonuclei were seen in type I fibres in either group. Data from the microarray analysis indicated that low testosterone affects the bone morphogenetic proteins signalling, which might regulate proliferation vs. differentiation of satellite cells.

    CONCLUSION: Eight weeks of strength training enhances the myonuclear number in type II fibres, and this is largely blocked by the suppression of testosterone. The data indicate that low testosterone levels could reduce the differentiation of satellite cells to myonuclei via the bone morphogenetic proteins signalling pathway, resulting in reduced increases in lean leg mass.

  • 7.
    Malgoyre, A
    et al.
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Sanchez, H
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Tonini, J
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Serrurier, B
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Prola, A
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Chaillou, Thomas
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Simler, N
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Bigard, X
    Institut de Recherche Biomdicale de Armes, La Tronche, France.
    Aerobic performance improvment and mitochondrial adaptations after endurance training in hypoxia2011In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 202, no Suppl. 685Article in journal (Refereed)
    Abstract [en]

    Aim: The aim of the present study was to examine the effects of hypoxic endurance training on both aerobic performance and mitochondrial changes within plantaris muscle, independently of hematopoietic modifications.

    Methods: Four groups of female rats were constituted either sedentary (S) or trained (T), in either hypoxia (H) or normoxia (N). H conditions corresponded to 14% O2 and the training program to 5 running sessions/week for 5 weeks. Duration and intensity reached progressively 75Õ up to 80% of individual maximal aerobic running velocity (MAV) in either H or N. Performances of each rat were analysed through MAV values and time to exhaustion at 65% MAV (T65). Mitochondrial oxidative capacities (Vmax) for pyruvate (pyr), palmitoyl-carnitine (PC) and palmitoyl-CoA (PCoA) were measured in plantaris skinned fibers. Citrate synthase (CS) and HAD activities were also measured.

    Results: MAV increased in both TN and TH rats (respectively +52%, +39%, P<0.001) without difference between H and N, whereas hypoxia specifically increased T65 (+ 39%, P<0.05) independently of training effect. The training-induced increase in CS activity (P<0.001) was more marked in TN than in TH group (+39% vs +26%, P<0.001) whereas HAD activity rose similarly in TN and TH (respectively +83%, +64%, P<0.05). Physical training increased Vmaxpyr only in N rats (+30%, P<0.001), while VmaxPCoA decreased in hypoxia (P<0.05) without change in VmaxPC. This suggests that LCFA transport by CPT-1 was limiting in hypoxia. As expected, training improved creatine kinase efficiency in N rats (+80%, P<0.005), but no change was shown in H rats.

    Conclusion: Regarding the modest changes in mitochondrial function, it is likely that other factors contribute to explain the improvement of physical performance after an endurance training in hypoxia.

  • 8. Mascher, H
    et al.
    Andersson, Helena M
    Örebro University, School of Health and Medical Sciences.
    Nilsson, P-A
    Ekblom, B
    Blomstrand, E
    Changes in signalling pathways regulating protein synthesis in human muscle in the recovery period after endurance exercise2007In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 191, no 1, p. 67-75Article in journal (Refereed)
    Abstract [en]

    AIM: Exercise induced alterations in the rate of muscle protein synthesis may be related to activity changes in signalling pathways involved in protein synthesis. The aim of the present study was to investigate whether such changes in enzyme phosphorylation occur after endurance exercise. METHODS: Six male subjects performed ergometer cycling exercise for 1 h at 75% of the maximal oxygen uptake. Muscle biopsy samples from the vastus lateralis were taken before, immediately after, 30 min, 1 h, 2 h and 3 h after exercise for the determination of protein kinase B (PKB/Akt), mammalian target of rapamycin (mTOR), glycogen synthase 3 kinase (GSK-3), p70S6 kinase (p70(S6k)) and eukaryotic elongation factor 2 (eEF2) phosphorylation. RESULTS: The phosphorylation of Akt was unchanged directly after exercise, but two- to fourfold increased 1 and 2 h after the exercise, whereas GSK-3alpha and beta phosphorylation were two- to fourfold elevated throughout most of the 3-h recovery period. Phosphorylation of mTOR was elevated threefold directly after, 30 min and 2 h after exercise and eEF2 phosphorylation was decreased by 35-75% from 30 min to 3 h-recovery. Exercise led to a five- to eightfold increase in Ser(424)/Thr(421) phosphorylation of p70(S6k) up to 30 min after exercise, but no change in Thr(389) phosphorylation. CONCLUSIONS: The marked decrease in eEF2 phosphorylation suggests an activation of translation elongation and possibly protein synthesis in the recovery period after sustained endurance exercise. The lack of p70(S6k) activation suggests that translation initiation is activated via alternative pathways, possibly via the activation of eukaryotic initiating factor 2B.

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