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  • 1.
    Apro, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Granberg, Jonas
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Andersson, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Physical Activity and Health.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH.
    Intake Of Essential Amino Acids Stimulates Mtorc1 Signaling And Inhibits Autophagy Following Glycogen-depleted Resistance Exercise2020In: MEDICINE AND SCIENCE IN SPORTS AND EXERCISE. 52:17, Suppl. Meeting Abstract 125, Lippincott Williams & Wilkins, 2020, Vol. 52, no 17, p. 18-18Conference paper (Other academic)
  • 2.
    Apro, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    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.
    Holmberg, Hans-Christer
    Mittuniversitetet.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    High intensity interval cycling performed prior to resistance exercise stimulates autophagy signaling2016In: Conference program & abstracts, 2016, p. 84-84Conference paper (Other academic)
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  • 3.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group. Karolinska Institutet, Inst för klinisk vetenskap, intervention och teknik / Dept of Clinical Science, Intervention and Technology.
    Regulation of protein synthesis in human skeletal muscle: separate and combined effects of exercise and amino acids2014Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Skeletal muscle is a highly plastic tissue which has the ability to adapt to various forms of external stimuli such as diverse modes of contractile activity. Thus, performance of endurance exercise over several of weeks results in increased oxidative capacity. In contrast, prolonged performance of resistance exercise ultimately results in increased muscle mass. These adaptations are brought about by transient alterations in gene expression and mRNA translation which result in altered protein turnover, i.e. the balance between protein synthesis and protein breakdown. Protein synthesis is the major determinant of muscle growth, which at the molecular level, is regulated by the mTORC1 pathway. This pathway is potently activated by resistance exercise and amino acids, but the stimulatory role of individual amino acids in human skeletal muscle is unclear. Muscle adaptations in response to endurance exercise are largely dependent on the PGC-1 α pathway, which regulates mitochondrial biogenesis. Given the different training adaptations after resistance and endurance exercise, it has been suggested that these exercise modalities may be incompatible when combined. Such potential interference could be exerted at the molecular level between the pathways responsible for each adaptive response. AMPK, an enzyme usually activated by endurance exercise and, when pharmacologically activated in cell culture and rodent models, has been shown to inhibit mTORC1 and protein synthesis. However, it is not known if activation of AMPK by endurance exercise inhibits resistance exercise induced signaling through the mTORC1 pathway in human skeletal muscle.

    Thus, the main objective of this thesis was to examine the molecular mechanisms regulating protein synthesis in response to amino acids and various modes of exercise in human skeletal muscle.

    In study I, the role of BCAAs in stimulating the mTORC1 pathway was examined in both resting and exercising muscle. BCAA increased mTORC1 activity, as assessed by S6K1 phosphorylation, in both resting and exercising muscle, but more so when exercise and BCAA were combined. In study II, the effect of leucine was compared to that of essential amino acids with or without leucine. It was found that when leucine was combined with the remaining essential amino acids, S6K1 phosphorylation was more pronounced than when leucine was provided alone. Furthermore, when leucine was removed from the essential amino acids, the effect was equal to that of placebo. In study III, the impact of endurance exercise on resistance exercise induced mTORC1 signaling was examined. When performed after resistance exercise, endurance exercise did not inhibit S6K1 phosphorylation compared to when single mode resistance exercise was performed. In study IV, performance of high intensity endurance exercise prior to resistance exercise did not inhibit S6K1 phosphorylation compared to single mode resistance exercise, despite prior activation of AMPK.

    In conclusion, amino acids and resistance exercise activate mTORC1 signaling, as assessed by S6K1 phosphorylation, in a synergistic manner. Leucine is crucial in mediating the amino acid response, however, additional amino acids appear to be required to induce a maximal response downstream of mTORC1. Activation of the mTORC1 pathway in response to heavy resistance exercise is robust and this activation does not appear to be inhibited by prior or by subsequent endurance exercise. As such, these results do not lend support to the existence of molecular interference when resistance and endurance exercise are combined acutely.

    Download full text (pdf)
    fulltext
  • 4.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Influence of supplementation with branched-chain amino acids in combination with resistance exercise on p70S6 kinase phosphorylation in resting and exercising human skeletal muscle.2010In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 200, no 3, p. 237-48Article in journal (Refereed)
    Abstract [en]

    AIM: Skeletal muscle growth is thought to be regulated by the mammalian target of rapamycin (mTOR) pathway, which can be activated by resistance exercise and branched-chain amino acids (BCAA). The major aim of the present study was to distinguish between the influence of resistance exercise and BCAA on key enzymes considered to be involved in the regulation of protein synthesis, including p70(S6) kinase (p70(S6k)). METHODS: Nine healthy subjects (four men and five women) performed unilateral resistance exercise on two occasions separated by 1 month. Subjects were randomly supplied either a mixture of BCAA or flavoured water. Muscle biopsies were taken from both resting and exercising muscle before, after and 1 h after exercise. RESULTS: Phosphorylation of Akt was unaltered by either resistance exercise and/or BCAA supplementation whereas mTOR phosphorylation was enhanced (P<0.05) to a similar extent in both exercising and resting muscle following exercise in the absence (70-90%) and presence of BCAA supplementation (80-130%). Phosphorylation of p70(S6k) was unaffected by resistance exercise alone; however, BCAA intake increased (P<0.05) this phosphorylation in both legs following exercise. In resting muscle, a 5- and 16-fold increase in p70(S6k) was observed immediately after and 1 h after exercise, respectively, as compared to 11- and 30-fold increases in the exercising muscle. Phosphorylation of eukaryotic elongation factor 2 was attenuated 1 h after exercise (P<0.05) in both resting (10-40%) and exercising muscle (30-50%) under both conditions. CONCLUSION: The present findings indicate that resistance exercise and BCAA exert both separate and combined effects on the p70(S6k) phosphorylation in an Akt-independent manner.

  • 5.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH.
    Holmberg, Hans-Christer
    Mittuniversitetet.
    Rooyackers, Olav
    Karolinska universitetssjukhuset, Huddinge.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Is leucine induced p70S6 kinase phosphorylation following resistance exercise dependent on elevated phenylalanine levels in human skeletal muscle?2010Conference paper (Other academic)
  • 6.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's and Mats Börjesson's research group.
    Rooyackers, O
    Holmberg, HC
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Leucine does not affect mTORC1 assembly but is required for maximal S6K1 activity in human skeletal muscle following resistance exerciseManuscript (preprint) (Other academic)
  • 7.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    Hamilton, D Lee
    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.
    Rooyackers, Olav
    Holmberg, Hans-Christer
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Leucine does not affect mechanistic target of rapamycin complex 1 assembly but is required for maximal ribosomal protein s6 kinase 1 activity in human skeletal muscle following resistance exercise.2015In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 29, no 10, p. 4358-4373Article in journal (Refereed)
    Abstract [en]

    We examined how the stimulatory effect of leucine on the mechanistic target of rapamycin complex 1 (mTORC1) pathway is affected by the presence of the remaining essential amino acids. Nine male subjects performed resistance exercise on 4 occasions and were randomly supplied essential amino acids (EAAs) with or without leucine (EAA-Leu), leucine alone, or flavored water (placebo; control). Muscle biopsies were taken from the vastus lateralis before and 60 and 90 min after exercise. Biopsies were analyzed for protein phosphorylation, kinase activity, protein-protein interactions, amino acid concentrations, and tracer incorporation. Leucine alone stimulated ribosomal protein s6 kinase 1 (S6K1) phosphorylation ∼280% more than placebo and EAA-Leu after exercise. Moreover, this response was enhanced by 60-75% after intake of EAAs compared with that of leucine alone (P < 0.05). Kinase activity of S6K1 reflected that of S6K1 phosphorylation; 60 min after exercise, the activity was elevated 3.3- and 4.2-fold with intake of leucine alone and with EAAs, respectively (P < 0.05). The interaction between mammalian target of rapamycin and regulatory-associated protein of mammalian target of rapamycin was unaltered in response to both resistance exercise and amino acid provision. Leucine alone stimulates mTORC1 signaling, although this response is enhanced by other EAA and does not appear to be caused by alterations in mTORC1 assembly.-Apró, W., Moberg, M., Hamilton, D. L., Ekblom, B., Rooyackers, O., Holmberg, H.-C., Blomstrand, E. Leucine does not affect mechanistic target of rapamycin complex 1 assembly but is required for maximal ribosomal protein s6 kinase 1 activity in human skeletal muscle following resistance exercise.

  • 8.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    Hamilton, L.
    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.
    van Hall, G.
    Holmberg, HC
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Resistance exercise induced S6K1 kinase activity is not inhibited in human skeletal muscle despite prior activation of AMPK by high intensity interval cycling.2015In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 308, no 6, p. E470-E481Article in journal (Refereed)
    Abstract [en]

    Combining endurance and strength training in the same session has been reported to reduce the anabolic response to the latter form of exercise. The underlying mechanism, based primarily on results from rodent muscle, is proposed to involve AMPK-dependent inhibition of mTORC1 signaling. This hypothesis was tested in eight trained male subjects who in a randomized order performed either resistance exercise only (R) or interval cycling followed by resistance exercise (ER). Biopsies taken from the vastus lateralis before and after endurance exercise and repeatedly after resistance exercise were assessed for glycogen content, kinase activity, protein phosphorylation and gene expression. Mixed muscle fractional synthetic rate was measured at rest and during 3h of recovery using the stable isotope technique. In ER, AMPK activity was elevated immediately after both endurance and resistance exercise (~90%, P<0.05) but was unchanged in R. Thr389 phosphorylation of S6K1 was increased several-fold immediately after exercise (P<0.05) in both trials and increased further throughout recovery. After 90 and 180 min recovery, S6K1 activity was elevated (~55% and ~110%, respectively, P<0.05) and eEF2 phosphorylation was reduced (~55%, P<0.05) with no difference between trials. In contrast, markers for protein catabolism were differently influenced by the two modes of exercise; ER induced a significant increase in gene and protein expression of MuRF1 (P<0.05), which was not observed following R exercise only. In conclusion, cycling-induced elevation in AMPK activity does not inhibit mTORC1 signaling after subsequent resistance exercise, but may instead interfere with the hypertrophic response by influencing key components in protein breakdown.

  • 9.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    Holmberg, Hans-Christer
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Amino Acid-induced S6K1 Activity In Human Skeletal Muscle Is Mediated By Increased mTor/Rheb Interaction: 128 June 1, 11: 15 AM - 11: 30 AM.2016In: Medicine And Science In Sports And Exercise 2016 May; Vol. 48 (5S Suppl 1), pp. 17., 2016, Vol. 48, no 5S Suppl 1, p. 17-17Conference paper (Refereed)
    Abstract [en]

    Cell culture studies have shown that amino acids activate mTORC1 signaling by increasing the interaction between mTOR and its essential activator Rheb. However, the existence of this mechanism in human skeletal muscle remains to be determined.

    PURPOSE: To determine if increased mTORC1 signaling in response to amino acids in human skeletal muscle is due to an increased interaction between mTOR and Rheb.

    METHODS: Eight well trained men performed resistance exercise on two separate occasions. In connection with the exercise, subjects were supplemented with flavored water (Pla) and essential amino acids (EAA) in a double-blind, randomized cross-over design. Muscle biopsies were taken in the vastus lateralis muscle before, immediately after and 90 and 180 min post exercise. Activity of the mTORC1 pathway was assessed by a radiolabeled in-vitro kinase assay for its immediate downstream target S6K1. Protein-protein interactions were determined by western blot following co-immunoprecipitation of mTOR with Rheb. Co-immunoprecipitation was performed on pooled muscle samples from three of the eight subjects.

    RESULTS: Activity of S6K1 remained unchanged immediately after exercise in both trials. However, at 90 min post exercise, S6K1 activity increased by approximately 2- and 8-fold (p<0.05) from baseline the Pla and EAA trials, respectively. At the 180 min time point, S6K1 activity remained elevated in both trials being approx. 3-fold higher in the Pla trial and 5-fold higher (p<0.05) in the EAA trial. The fold-change in mTOR and Rheb interaction largely resembled the activity pattern of S6K1 in both trials; in the Pla trial the fold-change was 0.9, 1.3 and 1.4 while in the EAA trial the fold-change was 1.6, 2.9 and 1.9 immediately after, 90 min after and 180 min after exercise, respectively.

    CONCLUSIONS: The large increase in S6K1 activity following EAA intake appears to be mediated by an increased interaction between mTOR and its proximal activator Rheb. This is the first time this mechanism has been demonstrated in human skeletal muscle.

  • 10.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Wang, Li
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Research group for Mitokondriell funktion och metabolisk kontroll.
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Sahlin, Kent
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Research group for Mitokondriell funktion och metabolisk kontroll.
    Endurance Exercise Does Not Impair mTOR Signalling After Resistance Exercise: D-58 Thematic Poster - Skeletal Muscle Cell Signaling: JUNE 2, 2011 3:15 PM - 5:15 PM: ROOM: 3042011In: Medicine & Science in Sports & Exercise, ISSN 0195-9131, E-ISSN 1530-0315, Vol. 43, no 5, p. 52-Article in journal (Other academic)
    Abstract [en]

    Resistance exercise is known to stimulate muscle hypertrophy and this effect is mainly mediated by the mammalian target of rapamycin (mTOR) pathway. In contrast, endurance exercise results in a divergent phenotypic response which to a large extent is mediated by adenosine monophosphate-activated protein kinase (AMPK). Research indicates that molecular interference may exist, possibly through an inhibitory effect on mTOR signalling by AMPK, when these two modes of exercise are combined.

    PURPOSE: To investigate the impact of subsequent endurance exercise on resistance exercise induced mTOR signalling.

    METHODS: In a randomized and cross-over fashion, ten male subjects performed either heavy resistance exercise (R) or heavy resistance exercise followed by endurance exercise (RE) on two separate occasions. The R protocol consisted of thirteen sets of leg press exercise with 3 minutes of recovery allowed between each set. In the RE session, resistance exercise was followed by 15 minutes recovery after which 30 min of cycling was initiated at an intensity equal to 70 % of the subjects' maximal oxygen consumption. Muscle biopsies were collected before, 1 and 3 hours after resistance exercise in both trials. Samples were analyzed for several signalling proteins in the mTOR pathway using western blot technique.

    RESULTS: Phosphorylation of mTOR increased approx. twofold at 1 h post resistance exercise and remained elevated at the 3 h time point (p< 0.01) with no difference between the two trials. Phosphorylation of p70S6k, a downstream target of mTOR, was increased about 6-and18-fold at 1 h and 3 h post resistance exercise (p< 0.01). There was no difference in p70S6k phosphorylation at any time point between the two trials. Phosphorylation of the eukaryotic elongation factor eEF2 was decreased 3- to 4-fold at both time points post resistance exercise (p< 0.01) with no difference between trials. Phosphorylation of AMPK was unchanged at the 1 h time point but decreased approximately 30 % from pre-exercise values in both trials at 3 h post resistance exercise (p< 0.01).

    CONCLUSIONS: The signalling response following heavy resistance exercise is not blunted by subsequent endurance exercise. Supported by the Swedish National Centre for Research in Sports.

  • 11.
    Apró, William
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Wang, Li
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Research group for Mitokondriell funktion och metabolisk kontroll.
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Research group for Mitokondriell funktion och metabolisk kontroll.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Sahlin, Kent
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Research group for Mitokondriell funktion och metabolisk kontroll.
    Resistance exercise induced mTORC1 signaling is not impaired by subsequent endurance exercise in human skeletal muscle.2013In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 305, no 1, p. E22-32Article in journal (Refereed)
    Abstract [en]

    The current dogma is that the muscle adaptation to resistance exercise is blunted when combined with endurance exercise. The suggested mechanism (based on rodent experiments) is that activation of adenosine monophosphate-activated protein kinase (AMPK) during endurance exercise impairs muscle growth through inhibition of the mechanistic target of rapamycin complex 1 (mTORC1). The purpose of this study was to investigate potential interference of endurance training on the signaling pathway of resistance training [mTORC1 phosphorylation of ribosomal protein S6 kinase 1 (S6K1)] in human muscle. Ten healthy and moderately trained male subjects performed on two separate occasions either acute high-intensity and high-volume resistance exercise (leg press, R) or R followed by 30 min of cycling (RE). Muscle biopsies were collected before and 1 and 3 h post resistance exercise. Phosphorylation of mTOR (Ser(2448)) increased 2-fold (P < 0.05) and that of S6K1 (Thr(389)) 14-fold (P < 0.05), with no difference between R and RE. Phosphorylation of eukaryotic elongation factor 2 (eEF2, Thr(56)) was reduced ∼70% during recovery in both trials (P < 0.05). An interesting finding was that phosphorylation of AMPK (Thr(172)) and acetyl-CoA carboxylase (ACC, Ser(79)) decreased ∼30% and ∼50%, respectively, 3 h postexercise (P < 0.05). Proliferator-activated receptor-γ coactivator-1 (PGC-1α) mRNA increased more after RE (6.5-fold) than after R (4-fold) (RE vs. R: P < 0.01) and was the only gene expressed differently between trials. These data show that the signaling of muscle growth through the mTORC1-S6K1 axis after heavy resistance exercise is not inhibited by subsequent endurance exercise. It is also suggested that prior activation of mTORC1 signaling may repress subsequent phosphorylation of AMPK.

  • 12.
    Blackwood, Sarah J
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Stockholm, Sweden..
    Ekblom, Maria
    Swedish School of Sport and Health Sciences, GIH, Department of Physical Activity and Health. Department of Neuroscience, Karolinska Institutet, Stockholm, Sweden..
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Extreme Variations in Muscle Fiber Composition Enable Detection of Insulin Resistance and Excessive Insulin Secretion.2022In: Journal of Clinical Endocrinology and Metabolism, ISSN 0021-972X, E-ISSN 1945-7197, Vol. 107, no 7, p. e2729-e2737, article id dgac221Article in journal (Refereed)
    Abstract [en]

    CONTEXT: Muscle fiber composition is associated with peripheral insulin action.

    OBJECTIVE: We investigated whether extreme differences in muscle fiber composition are associated with alterations in peripheral insulin action and secretion in young, healthy subjects who exhibit normal fasting glycemia and insulinemia.

    METHODS: Relaxation time following a tetanic contraction was used to identify subjects with a high or low expression of type I muscle fibers: group I (n=11), area occupied by type I muscle fibers = 61.0 ± 11.8%; group II (n=8), type I area = 36.0 ± 4.9% (P<0.001). Biopsies were obtained from the vastus lateralis muscle and analyzed for mitochondrial respiration on permeabilized fibers, muscle fiber composition and capillary density. An intravenous glucose tolerance test was performed and indices of glucose tolerance, insulin sensitivity and secretion were determined.

    RESULTS: Glucose tolerance was similar between groups, whereas whole-body insulin sensitivity was decreased by ~50% in group II vs group I (P=0.019). First phase insulin release (area under the insulin curve during 10 min after glucose infusion) was increased by almost 4-fold in group II vs I (P=0.01). Whole-body insulin sensitivity was correlated with % area occupied by type I fibers (r=0.54; P=0.018) and capillary density in muscle (r=0.61; P=0.005), but not with mitochondrial respiration. Insulin release was strongly related to % area occupied by type II fibers (r=0.93; P<0.001).

    CONCLUSIONS: Assessment of muscle contractile function in young healthy subjects may prove useful in identifying individuals with insulin resistance and enhanced glucose stimulated insulin secretion prior to onset of clinical manifestations.

  • 13.
    Blackwood, Sarah J
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden..
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Stockholm, Sweden.
    Ekblom, Maria
    Swedish School of Sport and Health Sciences, GIH, Department of Physical Activity and Health. Department of Neuroscience, Karolinska Institutet, Stockholm, Sweden..
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Insulin resistance after a 3-day fast is associated with an increased capacity of skeletal muscle to oxidize lipids.2023In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 324, no 5, p. E390-E401Article in journal (Refereed)
    Abstract [en]

    There is a debate on whether lipid-mediated insulin resistance derives from an increased or decreased capacity of muscle to oxidize fats. Here we examine the involvement of muscle fiber composition in the metabolic responses to a 3-day fast (starvation, which results in increases in plasma lipids and insulin resistance) in two groups of healthy young subjects: 1, area occupied by type I fibers = 61.0 ± 11.8%; 2, type I area = 36.0 ± 4.9% (P<0.001). Muscle biopsies and intravenous glucose tolerance tests were performed after an overnight fast and after starvation. Biopsies were analyzed for muscle fiber composition and mitochondrial respiration. Indices of glucose tolerance and insulin sensitivity were determined. Glucose tolerance was similar in both groups after an overnight fast and deteriorated to a similar degree in both groups after starvation. In contrast, whole-body insulin sensitivity decreased markedly after starvation in group 1 (P<0.01), whereas the decrease in group 2 was substantially smaller (P=0.06). Non-esterified fatty acids and β-hydroxybutyrate levels in plasma after an overnight fast were similar between groups and increased markedly and comparably in both groups after starvation, demonstrating similar degrees of lipid load. The capacity of permeabilized muscle fibers to oxidize lipids was significantly higher in group 1 vs. 2, whereas there was no significant difference in pyruvate oxidation between groups. The data demonstrate that loss of whole-body insulin sensitivity after short-term starvation is a function of muscle fiber composition and is associated with an elevated rather than a diminished capacity of muscle to oxidize lipids.

  • 14.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Det viktigaste du behöver veta om protein och träning2018In: Idrottsforskning.se, ISSN 2002-3944, article id 30 majArticle in journal (Other (popular science, discussion, etc.))
  • 15.
    Borgenvik, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Supplementation with BCAA Reduces MAFbx Expression and Phenylalanine Concentration in Rested and Exercised Human Muscle2011In: Medicine & Science in Sports & Exercise, 2011, Vol. 43, no 5, p. 419-419Conference paper (Refereed)
  • 16.
    Borgenvik, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Intake of branched-chain amino acids influences the levels of MAFbx mRNA and MuRF-1 total protein in resting and exercising human muscle.2012In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 302, no 5, p. E510-21Article in journal (Refereed)
    Abstract [en]

    Resistance exercise and amino acids are two major factors that influence muscle protein turnover. Here, we examined the effects of resistance exercise and branched-chain amino acids (BCAA), individually and in combination, on the expression of anabolic and catabolic genes in human skeletal muscle. Seven subjects performed two sessions of unilateral leg press exercise with randomized supplementation with BCAA or flavored water. Biopsies were collected from the vastus lateralis muscle of both the resting and exercising legs before and repeatedly after exercise to determine levels of mRNA, protein phosphorylation, and amino acid concentrations. Intake of BCAA reduced (P < 0.05) MAFbx mRNA by 30 and 50% in the resting and exercising legs, respectively. The level of MuRF-1 mRNA was elevated (P < 0.05) in the exercising leg two- and threefold under the placebo and BCAA conditions, respectively, whereas MuRF-1 total protein increased by 20% (P < 0.05) only in the placebo condition. Phosphorylation of p70(S6k) increased to a larger extent (∼2-fold; P < 0.05) in the early recovery period with BCAA supplementation, whereas the expression of genes regulating mTOR activity was not influenced by BCAA. Muscle levels of phenylalanine and tyrosine were reduced (13-17%) throughout recovery (P < 0.05) in the placebo condition and to a greater extent (32-43%; P < 0.05) following BCAA supplementation in both resting and exercising muscle. In conclusion, BCAA ingestion reduced MAFbx mRNA and prevented the exercise-induced increase in MuRF-1 total protein in both resting and exercising leg. Further-more, resistance exercise differently influenced MAFbx and MuRF-1 mRNA expression, suggesting both common and divergent regulation of these two ubiquitin ligases.

  • 17.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Flockhart, Mikael
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Need for Speed: Human fast-twitch mitochondria favor power over efficiency.2024In: Molecular Metabolism, ISSN 2212-8778, Vol. 79, article id 101854Article in journal (Refereed)
    Abstract [en]

    OBJECTIVE: Human skeletal muscle consists of a mixture of slow- and fast-twitch fibers with distinct capacities for contraction mechanics, fermentation, and oxidative phosphorylation (OXPHOS). While the divergence in mitochondrial volume favoring slow-twitch fibers is well established, data on the fiber type-specific intrinsic mitochondrial function and morphology are highly limited with existing data mainly being generated in animal models. This highlights the need for more human data on the topic.

    METHODS: Here, we utilized THRIFTY, a rapid fiber type identification protocol to detect, sort, and pool fast- and slow-twitch fibers within six hours of muscle biopsy sampling. Respiration of permeabilized fast- and slow-twitch fiber pools was then analyzed with high-resolution respirometry. Using standardized western blot procedures, muscle fiber pools were subsequently analyzed for control proteins and key proteins related to respiratory capacity.

    RESULTS: Maximal complex I CI+II respiration was 25% higher in human slow-twitch fibers compared to fast-twitch fibers. However, per volume, the respiratory rate of mitochondria in fast-twitch fibers was approximately 50% higher for CI+II, which was primarily mediated through elevated CII respiration, but not CI or. Furthermore, the abundance of CII protein and proteins regulating cristae structure were disproportionally elevated in mitochondria of the fast-twitch fibers. The difference in intrinsic respiratory rate was not reflected in fatty acid- or complex I respiration.

    CONCLUSION: Mitochondria of human fast-twitch muscle fibers compensate for their lack of volume by substantially elevating intrinsic respiratory rate through increased reliance on complex II.

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  • 18.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Flockhart, Mikael
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Need for Speed: Human fast-twitch mitochondria favour power over efficiencyManuscript (preprint) (Other academic)
  • 19.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Andersson, Alva
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    THRIFTY; A Novel Method For Rapid Fiber Type Identification Of Isolated Skeletal Muscle Fibers2022In: Medicine & Science in Sports & Exercise 54(2022);Suppl. 2, Lippincott Williams & Wilkins, 2022, Vol. 54, no 9, p. 109-109, article id 457Conference paper (Other academic)
  • 20.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    THRIFTY - A High-throughput Single Muscle Fiber Typing Method Based on Immunofluorescence Detection2023In: Bio-protocol, E-ISSN 2331-8325, Vol. 13, no 10, article id e4678Article in journal (Refereed)
    Abstract [en]

    Skeletal muscle consists of a mixture of fiber types with different functional and metabolic characteristics. The relative composition of these muscle fiber types has implications for muscle performance, whole-body metabolism, and health. However, analyses of muscle samples in a fiber type-dependent manner are very time consuming. Therefore, these are often neglected in favor of more time-efficient analyses on mixed muscle samples. Methods such as western blot and myosin heavy chain separation by SDS-PAGE have previously been utilized to fiber type-isolated muscle fibers. More recently, the introduction of the dot blot method significantly increased the speed of fiber typing. However, despite recent advancements, none of the current methodologies are feasible for large-scale investigations because of their time requirements. Here, we present the protocol for a new method, which we have named THRIFTY (high-THRoughput Immunofluorescence Fiber TYping), that enables rapid fiber type identification using antibodies towards the different myosin heavy chain (MyHC) isoforms of fast and slow twitch muscle fibers. First, a short segment (<1 mm) is cut off from isolated muscle fibers and mounted on a customized gridded microscope slide holding up to 200 fiber segments. Second, the fiber segments attached to the microscope slide are stained with MyHC-specific antibodies and then visualized using a fluorescence microscope. Lastly, the remaining pieces of the fibers can either be collected individually or pooled together with fibers of the same type for subsequent analyses. The THRIFTY protocol is approximately three times as fast as the dot blot method, which enables not only time-sensitive assays to be performed but also increases the feasibility to conduct large-scale investigations into fiber type specific physiology.

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  • 21.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Strömlind, Henrik
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Fiber type-specific signaling responses to nutritional and contractile stimuli in young and aged human skeletal muscleManuscript (preprint) (Other academic)
  • 22.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Söderlund, Karin
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    mTORC1 Signaling in Individual Human Muscle Fibers Following Resistance Exercise in Combination With Intake of Essential Amino Acids2019In: Frontiers in Nutrition, E-ISSN 2296-861X, Vol. 6, article id 96Article in journal (Refereed)
    Abstract [en]

    Human muscles contain a mixture of type I and type II fibers with different contractile and metabolic properties. Little is presently known about the effect of anabolic stimuli, in particular nutrition, on the molecular responses of these different fiber types. Here, we examine the effect of resistance exercise in combination with intake of essential amino acids (EAA) on mTORC1 signaling in individual type I and type II human muscle fibers. Five strength-trained men performed two sessions of heavy leg press exercise. During exercise and recovery, the subjects ingested an aqueous solution of EAA (290 mg/kg) or flavored water (placebo). Muscle biopsies were taken from the vastus lateralis before and 90 min after exercise. The biopsies were freeze-dried and single fibers dissected out and weighed (range 0.95-8.1 mu g). The fibers were homogenized individually and identified as type I or II by incubation with antibodies against the different isoforms of myosin. They were also analyzed for both the levels of protein as well as phosphorylation of proteins in the mTORC1 pathway using Western blotting. The levels of the S6K1 and eEF2 proteins were similar to 50% higher in type II than in type I fibers (P < 0.05), but no difference was found between fiber types with respect to the level of mTOR protein. Resistance exercise led to non-significant increases (2-3-fold) in mTOR and S6K1 phosphorylation as well as a 50% decrease (P < 0.05) in eEF2 phosphorylation in both fiber types. Intake of EAA caused a 2 and 6-fold higher (P < 0.05) elevation of mTOR and S6K1 phosphorylation, respectively, in both type I and type II fibers compared to placebo, with no effect on phosphorylation of eEF2. In conclusion, protein levels of S6K1 and eEF2 were significantly higher in type II than type I fibers suggesting higher capacity of the mTOR pathway in type II fibers. Ingestion of EAA enhanced the effect of resistance exercise on phosphorylation of mTOR and S6K1 in both fiber types, but with considerable variation between single fibers of both types.

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  • 23.
    Flockhart, Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Nilsson, Lina
    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.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    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.
    Larsen, Filip J
    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.
    Dose-response relationship between exercise load and mitochondrial function2019Conference paper (Other academic)
    Abstract [en]

    Dose-response relationship between exercise load and mitochondrial function

    Flockhart M, Nilsson L, Bergman K, Apro W, Ekblom B, Larsen FJ

    A dose-dependent relationship exists between exercise load and muscular adaptation. Mitochondria adapt to the increased ATP-demand by alterations in mass and/or quality. How mitochondrial mass and quality changes as a function of exercise load is not well investigated and we have previously found mitochondrial dysfunction after short-term intensive exercise. We therefore aimed to study mitochondrial function by altering exercise load during a three week interval training regimen to understand the dose-response relationship between exercise load and mitochondrial function. We took four muscle biopsies throughout the study, and as expected, mitochondrial function was positively affected during the first two weeks. After the third week, a dramatic mitochondrial dysfunction was evident as mitochondrial intrinsic respiration was reduced by 26% despite a 32% increase in mitochondrial yield. We hereby present evidence of a striking exercise-induced reduction in mitochondrial function after a period of very intense interval training.

  • 24.
    Flockhart, Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nilsson, Lina C.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Tais, Senna
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Karolinska Institutet, Stockholm, Sweden.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Excessive exercise training causes mitochondrial functional impairment and decreases glucose tolerance in healthy volunteers.2021In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 33, no 5, p. 957-970, article id S1550-4131(21)00102-9Article in journal (Refereed)
    Abstract [en]

    Exercise training positively affects metabolic health through increased mitochondrial oxidative capacity and improved glucose regulation and is the first line of treatment in several metabolic diseases. However, the upper limit of the amount of exercise associated with beneficial therapeutic effects has not been clearly identified. Here, we used a training model with a progressively increasing exercise load during an intervention over 4 weeks. We closely followed changes in glucose tolerance, mitochondrial function and dynamics, physical exercise capacity, and whole-body metabolism. Following the week with the highest exercise load, we found a striking reduction in intrinsic mitochondrial function that coincided with a disturbance in glucose tolerance and insulin secretion. We also assessed continuous blood glucose profiles in world-class endurance athletes and found that they had impaired glucose control compared with a matched control group.

  • 25.
    Flockhart, Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nilsson, Lina
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Tillqvist, E N
    Linnaeus University, Kalmar, Sweden..
    Vinge, Fredrik
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Millbert, F
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Lännerström, Johan
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nilsson, P H
    Linnaeus University, Kalmar, Sweden..
    Samyn, D
    Örebro University, Örebro, Sweden.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Sundqvist, Michaela L
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Glucosinolate-rich broccoli sprouts protect against oxidative stress and improve adaptations to intense exercise training.2023In: Redox Biology, E-ISSN 2213-2317, Vol. 67, article id 102873Article in journal (Refereed)
    Abstract [en]

    Oxidative stress plays a vital role for the adaptive responses to physical training. However, excessive oxidative stress can precipitate cellular damage, necessitating protective mechanisms to mitigate this effect. Glucosinolates, found predominantly in cruciferous vegetables, can be converted into isothiocyanates, known for their antioxidative properties. These compounds activate crucial antioxidant defence pathways and support mitochondrial function and protein integrity under oxidative stress, in both Nrf2-dependent and independent manners. We here administered glucosinolate-rich broccoli sprouts (GRS), in a randomized double-blinded cross-over fashion to 9 healthy subjects in combination with daily intense exercise training for 7 days. We found that exercise in combination with GRS significantly decreased the levels of carbonylated proteins in skeletal muscle and the release of myeloperoxidase into blood. Moreover, it lowered lactate accumulation during submaximal exercise, and attenuated the severe nocturnal hypoglycaemic episodes seen during the placebo condition. Furthermore, GRS in combination with exercise improved physical performance, which was unchanged in the placebo condition.

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  • 26.
    Flockhart, Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Tischer, Dominik
    School of Health Sciences, Örebro University, Örebro, Sweden.
    Nilsson, Lina
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Blackwood, Sarah J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physical Activity and Health.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    THREE HOURS OF MODERATE INTENSITY EXERCISE TRAINING REDUCES GLUCOSE TOLERANCE IN ENDURANCE TRAINED ATHLETES2022Conference paper (Other academic)
    Abstract [en]

    BACKGROUND

    It is well accepted that exercise training improves glucose uptake and insulin sensitivity, and that endurance trained athletes in general show a high capacity for these parameters and excellent metabolic control. However, some studies fail to observe positive effects on glucose regulation in healthy, trained subjects the day after exercise. These, often unexpected, results have been postulated to be caused by excessive training loads, muscle damage, energy deficit, differences in glucose uptake in the exercised and non-exercised musculature and a metabolic interaction through increased fatty acid metabolism which suppresses glucose oxidation and uptake. The mode or volume of exercise that can lead to glucose intolerance in trained athletes as well as mechanistic insights and its relevance for health and performance are, however, not fully understood.

    AIM

    We studied the metabolic response to a glucose load the day after a session of high intensity interval training (HIIT) or three hours of continuous exercise (3h) in endurance trained athletes and compared the results with measurements during rest.

    METHOD

    Nine endurance trained athletes (5 females, 4 males) underwent oral glucose tolerance tests (OGTT) after rest and ~14 hours after exercise on a cycle ergometer (HIIT 5x4 minutes at ~95% of VO2max or 3h at 65% of VO2max). Venous blood was sampled at 15-minute intervals for 120 minutes and concentrations of glucose, insulin, free fatty acids (FFA) and ketones (β-hydroxybutyrate) were measured. Statistical analysis was performed using a RM one-way ANOVA with the Giesser-Greenhouse correction and Dunnett’s test was used to compare the exercise conditions to the resting condition.

    RESULTS

    The area under the curve (AUC) during the OGTT increased greatly after 3h (668±124 mM · min) (p<0.01) compared to rest (532±89) but was found to be unchanged after HIIT (541±96). Resting values of FFA and ketones were increased after 3h (p<0.01 and p<0.05, respectively) but not after HIIT. Insulin was found to be unaltered during all conditions.

    CONCLUSIONS AND RELEVANCE

    Here, we show manifestation of glucose intolerance in endurance trained athletes together with concomitant increases in plasma concentrations of FFA and ketones the day after a session of prolonged exercise training but not after HIIT. This could be a protective response for securing glucose delivery to the brain and therefore have a positive effect on endurance. It also has the potential to reduce the recovery of glycogen depots, glucose uptake during exercise and performance at higher work rates.

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    THREE HOURS OF MODERATE INTENSITY EXERCISE TRAINING REDUCES GLUCOSE TOLERANCE IN ENDURANCE TRAINED ATHLETES
  • 27.
    Flockhart, Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Tischer, Dominik
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nilsson, Lina
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Blackwood, Sarah J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Three hours of moderate intensity exercise training reduces glucose tolerance in endurance trained athletes2022In: Svensk idrottsmedicin 2022:2, Svensk förening för fysisk aktivitet och idrottsmedicin , 2022, p. 28-Conference paper (Other academic)
  • 28.
    Flockhart, Mikael
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Tischer, Dominik
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nilsson, Lina C.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Blackwood, Sarah J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Sciences, Intervention and Technology, Karolinska Institutet, Stockholm, Sweden.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Reduced glucose tolerance and insulin sensitivity after prolonged exercise in endurance athletes.2023In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 238, no 4, article id e13972Article in journal (Refereed)
    Abstract [en]

    AIM: The purpose of this study was to 1. investigate if glucose tolerance is affected after one acute bout of different types of exercise; 2. assess if potential differences between two exercise paradigms are related to changes in mitochondrial function; and 3. determine if endurance athletes differ from nonendurance-trained controls in their metabolic responses to the exercise paradigms.

    METHODS: Nine endurance athletes (END) and eight healthy nonendurance-trained controls (CON) were studied. Oral glucose tolerance tests (OGTT) and mitochondrial function were assessed on three occasions: in the morning, 14 h after an overnight fast without prior exercise (RE), as well as after 3 h of prolonged continuous exercise at 65% of VO2 max (PE) or 5 × 4 min at ~95% of VO2 max (HIIT) on a cycle ergometer.

    RESULTS: Glucose tolerance was markedly reduced in END after PE compared with RE. END also exhibited elevated fasting serum FFA and ketones levels, reduced insulin sensitivity and glucose oxidation, and increased fat oxidation during the OGTT. CON showed insignificant changes in glucose tolerance and the aforementioned measurements compared with RE. HIIT did not alter glucose tolerance in either group. Neither PE nor HIIT affected mitochondrial function in either group. END also exhibited increased activity of 3-hydroxyacyl-CoA dehydrogenase activity in muscle extracts vs. CON.

    CONCLUSION: Prolonged exercise reduces glucose tolerance and increases insulin resistance in endurance athletes the following day. These findings are associated with an increased lipid load, a high capacity to oxidize lipids, and increased fat oxidation.

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  • 29.
    Hammarström, Daniel
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group. Section for Health and Exercise Physiology, Department of Public Health and Sport Sciences, Inland Norway.
    Øfsteng, Sjur
    Section for Health and Exercise Physiology, Department of Public Health and Sport Sciences, Inland Norway.
    Koll, Lise
    Innlandet Hospital Trust, Lillehammer, Norway.
    Hanestadhaugen, Marita
    Innlandet Hospital Trust, Lillehammer, Norway.
    Hollan, Ivana
    Hospital for Rheumatic Diseases, Lillehammer, Norway.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Whist, Jon Elling
    Innlandet Hospital Trust, Lillehammer, Norway.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Rønnestad, Bent R
    Section for Health and Exercise Physiology, Department of Public Health and Sport Sciences, Inland Norway.
    Ellefsen, Stian
    Section for Health and Exercise Physiology, Department of Public Health and Sport Sciences, Inland Norway.
    Benefits of higher resistance-training volume are related to ribosome biogenesis.2020In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 598, no 3, p. 543-565Article in journal (Refereed)
    Abstract [en]

    KEY POINTS: For individuals showing suboptimal adaptations to resistance training, manipulation of training volume is a potential measure to facilitate responses. This remains unexplored. Here, 34 untrained individuals performed contralateral resistance training with moderate and low volume for 12 weeks. Moderate volume led to larger increases in muscle cross-sectional area, strength and type II fibre-type transitions. These changes coincided with greater activation of signalling pathways controlling muscle growth and greater induction of ribosome synthesis. Thirteen and sixteen participants, respectively, displayed clear benefits of moderate-volume training on muscle hypertrophy and strength. This coincided with greater total RNA accumulation in the early-phase of the training period, suggesting that ribosomal biogenesis regulates the dose-response relationship between training volume and muscle hypertrophy. These results demonstrate that there is a dose-dependent relationship between training volume and outcomes. On the individual level, benefits of higher training volume were associated with increased ribosomal biogenesis.

    ABSTRACT: Resistance-exercise volume is a determinant of training outcomes. However not all individuals respond in a dose-dependent fashion. In this study, 34 healthy individuals (males n = 16, 23.6 (4.1) years; females n = 18, 22.0 (1.3)) performed moderate- (3 sets per exercise, MOD) and low-volume (1 set, LOW) resistance training in a contralateral fashion for 12 weeks (2-3 sessions × week-1 ). Muscle cross-sectional area (CSA) and strength were assessed at weeks 0 and 12, along with biopsy sampling (m. Vastus lateralis). Muscle biopsies were also sampled before and one hour after the fifth session (Week 2). MOD resulted in larger increases in muscle CSA (5.2 (3.8)% versus 3.7 (3.7)%, P < 0.001) and strength (3.4-7.7% difference, all P < 0.05. This coincided with greater reductions in type IIX fibres from week 0 to 12 (MOD, -4.6; LOW -3.2%-point), greater phosphorylation of S6-kinase 1 (p85 S6K1Thr412 , 19%; p70 S6K1Thr389 , 58%) and ribosomal protein S6Ser235/236 (37%), greater rested-state total RNA (8.8%) and greater exercise-induced c-Myc mRNA expression (25%; Week 2, all P < 0.05). Thirteen and sixteen participants, respectively, displayed clear benefits in response to MOD on muscle hypertrophy and strength. Benefits were associated with greater accumulation of total RNA at Week 2 in the MOD leg, with every 1% difference increasing the odds of MOD benefit by 7.0% (P = 0.005) and 9.8% (P = 0.002). In conclusion, MOD led to greater functional and biological adaptations than LOW. Associations between dose-dependent total RNA accumulation and increases in muscle mass and strength points to ribosome biogenesis as a determinant of dose-dependent training responses. This article is protected by copyright. All rights reserved.

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  • 30.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    Godhe, Manne
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    Helge, Torbjörn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's research group.
    Ekblom, Maria
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Laboratory for Biomechanics and Motor Control.
    Lindén Hirschberg, Angelica
    Karolinska institutet.
    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.
    Fiber type-specific hypertrophy and increased capillarization in skeletal muscle following testosterone administration of young women.2020In: Journal of applied physiology, ISSN 8750-7587, E-ISSN 1522-1601, Vol. 128, no 5, p. 1240-1250Article in journal (Refereed)
    Abstract [en]

    It is well established that testosterone administration induces muscle fiber hypertrophy and myonuclear addition in men, however, it remains to be determined whether similar morphological adaptations can be achieved in women. The aim of the present study was therefore to investigate whether exogenously administered testosterone alters muscle fiber morphology in skeletal muscle of young healthy, physically active women. Thirty-five young (20-35 years), recreationally trained women were randomly assigned to either 10-week testosterone administration (10 mg daily) or placebo. Before and after the intervention, hormone concentrations and body composition were assessed, and muscle biopsies were obtained from the vastus lateralis. Fiber type composition, fiber size, satellite cell- and myonuclei content, as well as muscle capillarization were assessed in a fiber type-specific manner using immunohistochemistry. Following the intervention, testosterone administration elevated serum testosterone concentration (5.1-fold increase, P=0.001), and induced significant accretion of total lean mass (+1.9%, P=0.002) and leg lean mass (+2.4%, P=0.001). On the muscle fiber level, testosterone increased mixed fiber cross-sectional area (+8.2%, P=0.001), an effect primarily driven by increases in type II fiber size (9.2%, P=0.006). Whereas myonuclei content remained unchanged, a numerical increase (+30.8%) was found for satellite cells associated with type II fibers in the Testosterone group. In parallel with fiber hypertrophy, testosterone significantly increased capillary contacts (+7.5%, P=0.015) and capillary-to-fiber ratio (+9.2%, P=0.001) in type II muscle fibers. The current study provides novel insight into fiber type-specific adaptations present already after 10 weeks of only moderately elevated testosterone levels in women.

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  • 31.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Edman, Sebastian
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Åstrand Laboratory.
    Andersson, Alva
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Stockholm, Sweden..
    THRIFTY: a novel high-throughput method for rapid fibre type identification of isolated skeletal muscle fibres.2022In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 600, no 20, p. 4421-4438Article in journal (Refereed)
    Abstract [en]

    Fibre type-specific analyses are required for broader understanding of muscle physiology, but such analyses are difficult to conduct due to the extreme time requirements of dissecting and fibre typing individual fibres. Investigations are often confined to a small number of fibres from few participants with low representativeness of the entire fibre population and the participant population. To increase the feasibility of conducting large-scale fibre type-specific studies, a valid and rapid method for high-throughput fibre typing of individually dissected fibres was developed and named THRIFTY (for high-THRoughput Immunofluorescence Fibre TYping). Employing THRIFTY, 400 fibre segments were fixed onto microscope slides with a pre-printed coordinated grid system, probed with antibodies against myosin heavy chain (MyHC)-I and MyHC-II and classified using a fluorescence microscope. The validity and speed of THRIFTY was compared to a previously validated protocol (dot blot) on a fibre-to-fibre basis. Fibre pool purity was evaluated using 'gold standard' SDS-PAGE and silver staining. A modified THRIFTY-protocol using fluorescence western blot equipment was also validated. THRIFTY displayed excellent agreement with the dot blot protocol, κ = 0.955 (95% CI: 0.928, 0.982), P < 0.001. Both the original and modified THRIFTY protocols generated type I and type II fibre pools of absolute purity. Using THRIFTY, 400 fibres were typed just under 11 h, which was approximately 3 times faster than dot blot. THRIFTY is a novel and valid method with high versatility for very rapid fibre typing of individual fibres. THRIFTY can therefore facilitate the generation of large fibre pools for more extensive mechanistic studies into skeletal muscle physiology. KEY POINTS: Skeletal muscle is composed of different fibre types, each with distinct physiological properties. To fully understand how skeletal muscle adapts to external cues such as exercise, nutrition and ageing, fibre type-specific investigations are required. Such investigations are very difficult to conduct due to the extreme time requirements related to classifying individually isolated muscle fibres. To bypass this issue, we have developed a rapid and reliable method named THRIFTY which is cheap as well as versatile and which can easily be implemented in most laboratories. THRIFTY increases the feasibility of conducting larger fibre type-specific studies and enables time-sensitive assays where measurements need to be carried out in close connection with tissue sampling. By using THRIFTY, new insights into fibre type-specific muscle physiology can be gained which may have broad implications in health and disease.

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  • 32.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Envall, Helena
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Student.
    Röja, Julia
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Student.
    Emanuelsson, Eric Bengt
    Karolinska Institute, Sweden.
    Sanz, Gema
    Karolinska Institute, Sweden.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Karolinska Institute, Sweden.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Karolinska Institute, Sweden.
    Variablity in vastus lateralis fiber type distribution, fiber size and myonuclear content along and between the legs.2021In: Journal of applied physiology, ISSN 8750-7587, E-ISSN 1522-1601, Vol. 131, no 1, p. 158-173Article in journal (Refereed)
    Abstract [en]

    Human skeletal muscle characteristics such as fiber type composition, fiber size and myonuclear content are widely studied in clinical and sports related contexts. Being aware of the methodological and biological variability of the characteristics is a critical aspect in study design and outcome interpretation, but comprehensive data on the variability of morphological features in human skeletal muscle is currently limited. Accordingly, in the present study, m. vastus lateralis biopsies (10 per subject) from young and healthy individuals, collected in a systematic manner, were analyzed for various characteristics using immunohistochemistry (n=7) and SDS-PAGE (n=25). None of the analyzed parameters; fiber type % (FT%), type I and II CSA (fCSA), percentage fiber type area (fCSA%), myosin heavy chain composition (MyHC%), type IIX content, myonuclear content or myonuclear domain varied in a systematic manner longitudinally along the muscle or between the two legs. The average within subject coefficient of variation for FT%, fCSA, fCSA%, and MyHC% ranged between 13-18%, but was only 5% for fiber specific myonuclear content, which reduced the variability for myonuclear domain size to 11-12%. Pure type IIX fibers and type IIX MyHC were randomly distributed and present in <24% of the analyzed samples, with the average content being 0.1 and 1.1%, respectively. In conclusion, leg or longitudinal orientation does not seem to be an important aspect to consider when investigating human vastus lateralis characteristics. However, single muscle biopsies should preferably not be used when studying fiber type and fiber size related aspects given the notable sample to sample variability.

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  • 33.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Granberg, Jonas
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Low Glycogen Availability Increases Autophagy Signalling Following Resistance Exercise2019Conference paper (Other academic)
  • 34.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
    Hirschberg, Angelica Lindén
    Department of Women´s and Children´s Health, Division of Neonatology, Obstetrics and Gynaecology, Karolinska Institutet, Stockholm, Sweden; Department of Gynaecology and Reproductive Medicine, Karolinska University Hospital, Stockholm, Sweden..
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Stockholm, Sweden..
    Molecular Regulators of Muscle Mass and Mitochondrial Remodeling Are Not Influenced by Testosterone Administration in Young Women.2022In: Frontiers in Endocrinology, E-ISSN 1664-2392, Vol. 13, article id 874748Article in journal (Refereed)
    Abstract [en]

    Testosterone (T) administration has previously been shown to improve muscle size and oxidative capacity. However, the molecular mechanisms underlying these adaptations in human skeletal muscle remain to be determined. Here, we examined the effect of moderate-dose T administration on molecular regulators of muscle protein turnover and mitochondrial remodeling in muscle samples collected from young women. Forty-eight healthy, physically active, young women (28 ± 4 years) were assigned in a random double-blind fashion to receive either T (10 mg/day) or placebo for 10-weeks. Muscle biopsies collected before and after the intervention period were divided into sub-cellular fractions and total protein levels of molecular regulators of muscle protein turnover and mitochondrial remodeling were analyzed using Western blotting. T administration had no effect on androgen receptor or 5α-reductase levels, nor on proteins involved in the mTORC1-signaling pathway (mTOR, S6K1, eEF2 and RPS6). Neither did it affect the abundance of proteins associated with proteasomal protein degradation (MAFbx, MuRF-1 and UBR5) and autophagy-lysosomal degradation (AMPK, ULK1 and p62). T administration also had no effect on proteins in the mitochondria enriched fraction regulating mitophagy (Beclin, BNIP3, LC3B-I, LC3B-II and LC3B-II/I ratio) and morphology (Mitofilin), and it did not alter the expression of mitochondrial fission- (FIS1 and DRP1) or fusion factors (OPA1 and MFN2). In summary, these data indicate that improvements in muscle size and oxidative capacity in young women in response to moderate-dose T administration cannot be explained by alterations in total expression of molecular factors known to regulate muscle protein turnover or mitochondrial remodeling.

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  • 35.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Larsen, Filip J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Philp, Andrew
    Garvan Institute of Medical Research, Darlinghurst, Sydney, New South Wales, Australia.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Karolinska institutet, Sweden.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Influence of sex- and fiber type on the satellite cell pool in human skeletal muscle.2021In: Scandinavian Journal of Medicine and Science in Sports, ISSN 0905-7188, E-ISSN 1600-0838, Vol. 31, no 2, p. 303-312Article in journal (Refereed)
    Abstract [en]

    The repair, remodeling and regeneration of myofibers is dependent on satellite cells (SCs), although, the distribution of SCs in different fiber types of human muscle remains inconclusive. There is also a paucity of research comparing muscle fiber characteristics in a sex-specific manner. Therefore, the aim of this study was to investigate fiber type-specific SC content in men and women. Muscle biopsies from vastus lateralis were collected from 64 young (mean age 27 ± 5), moderately trained men (n=34) and women (n=30). SCs were identified by Pax7-staining together with immunofluorescent analyses of fiber type composition, fiber size and myonuclei content. In a mixed population, comparable number of SCs were associated to type I and type II fibers (0.07 ± 0.02 vs 0.07 ± 0.02 SCs per fiber, respectively). However, unlike men, women displayed a fiber type-specific distribution, with SC content being lower in type II than type I fibers (P=0.041). Sex-based differences were found specifically for type II fibers, where women displayed lower SC content compared to men (P<0.001). In addition, positive correlations (r-values between 0.36-0.56) were found between SC content and type I and type II fiber size in men (P=0.03 and P<0.01, respectively), whereas similar relationships could not be detected in women. Sex-based differences were also noted for fiber type composition and fiber size, but not for myonuclei content. We hereby provide evidence for sex-based differences present at the myocellular level, which may have important implications when studying exercise- and training induced myogenic responses in skeletal muscle.

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  • 36.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nordström, Fabian
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Satellite cell pool expansion induced by resistance exercise is not altered by acute normobaric hypoxia2022In: Svensk idrottsmedicin 2022:2, Svensk förening för fysisk aktivitet och idrottsmedicin , 2022, Vol. 41, p. 30-Conference paper (Other academic)
  • 37.
    Horwath, Oscar
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Nordström, Fabian
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    von Walden, Ferdinand
    Division of Pediatric Neurology, Department of Women's and Children's Health, Karolinska Institutet, Stockholm, Sweden..
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Solna, Sweden..
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Physiology and Pharmacology, Karolinska Institutet, Solna, Sweden..
    Acute hypoxia attenuates resistance exercise-induced ribosome signaling but does not impact satellite cell pool expansion in human skeletal muscle.2023In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 37, no 3, article id e22811Article in journal (Refereed)
    Abstract [en]

    Cumulative evidence supports the hypothesis that hypoxia acts as a regulator of muscle mass. However, the underlying molecular mechanisms remain incompletely understood, particularly in human muscle. Here we examined the effect of hypoxia on signaling pathways related to ribosome biogenesis and myogenic activity following an acute bout of resistance exercise. We also investigated whether hypoxia influenced the satellite cell response to resistance exercise. Employing a randomized, crossover design, eight men performed resistance exercise in normoxia (FiO2 21%) or normobaric hypoxia (FiO2 12%). Muscle biopsies were collected in a time-course manner (before, 0, 90, 180 min and 24 h after exercise) and were analyzed with respect to cell signaling, gene expression and satellite cell content using immunoblotting, RT-qPCR and immunofluorescence, respectively. In normoxia, resistance exercise increased the phosphorylation of RPS6, TIF-1A and UBF above resting levels. Hypoxia reduced the phosphorylation of these targets by ~37%, ~43% and ~ 67% throughout the recovery period, respectively (p < .05 vs. normoxia). Resistance exercise also increased 45 S pre-rRNA expression and mRNA expression of c-Myc, Pol I and TAF-1A above resting levels, but no differences were observed between conditions. Similarly, resistance exercise increased mRNA expression of myogenic regulatory factors throughout the recovery period and Pax7+ cells were elevated 24 h following exercise in mixed and type II muscle fibers, with no differences observed between normoxia and hypoxia. In conclusion, acute hypoxia attenuates ribosome signaling, but does not impact satellite cell pool expansion and myogenic gene expression following a bout of resistance exercise in human skeletal muscle.

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  • 38. Kazior, Zuzanna
    et al.
    Willis, Sarah J
    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.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Calbet, José A L
    Holmberg, Hans-Christer
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Endurance Exercise Enhances the Effect of Strength Training on Muscle Fiber Size and Protein Expression of Akt and mTOR.2016In: PLOS ONE, E-ISSN 1932-6203, Vol. 11, no 2, article id e0149082Article in journal (Refereed)
    Abstract [en]

    Reports concerning the effect of endurance exercise on the anabolic response to strength training have been contradictory. This study re-investigated this issue, focusing on training effects on indicators of protein synthesis and degradation. Two groups of male subjects performed 7 weeks of resistance exercise alone (R; n = 7) or in combination with preceding endurance exercise, including both continuous and interval cycling (ER; n = 9). Muscle biopsies were taken before and after the training period. Similar increases in leg-press 1 repetition maximum (30%; P<0.05) were observed in both groups, whereas maximal oxygen uptake was elevated (8%; P<0.05) only in the ER group. The ER training enlarged the areas of both type I and type II fibers, whereas the R protocol increased only the type II fibers. The mean fiber area increased by 28% (P<0.05) in the ER group, whereas no significant increase was observed in the R group. Moreover, expression of Akt and mTOR protein was enhanced in the ER group, whereas only the level of mTOR was elevated following R training. Training-induced alterations in the levels of both Akt and mTOR protein were correlated to changes in type I fiber area (r = 0.55-0.61, P<0.05), as well as mean fiber area (r = 0.55-0.61, P<0.05), reflecting the important role played by these proteins in connection with muscle hypertrophy. Both training regimes reduced the level of MAFbx protein (P<0.05) and tended to elevate that of MuRF-1. The present findings indicate that the larger hypertrophy observed in the ER group is due more to pronounced stimulation of anabolic rather than inhibition of catabolic processes.

  • 39.
    Liegnell, Rasmus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology. Karolinska Institute, Sweden.
    Danielsson, Sebastian
    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.
    van Hall, Gerrit
    University of Copenhagen, Denmark.
    Holmberg, Hans-Christer
    Mid Sweden University, Sweden.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Elevated plasma lactate levels via exogenous lactate infusion do not alter resistance exercise-induced signaling or protein synthesis in human skeletal muscle.2020In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 319, p. E792-E804Article in journal (Refereed)
    Abstract [en]

    Lactate has been implicated as a potential signaling molecule. In myotubes, lactate incubation increases mTORC1- and ERK-signaling and induces hypertrophy, indicating that lactate could be a mediator of muscle adaptations to resistance exercise. However, the potential signaling properties of lactate, at rest or with exercise, have not been explored in human tissue. In a cross-over design study, 8 men and 8 women performed one-legged resistance exercise while receiving venous infusion of saline or sodium lactate. Blood was sampled repeatedly, and muscle biopsies were collected at rest and at 0, 90,180 min and 24 h after exercise. The primary outcomes examined were intracellular signaling, fractional protein synthesis rate (FSR), and blood/muscle levels of lactate and pH. Post-exercise blood lactate concentrations were 130% higher in the Lactate trial (3.0 vs 7.0 mmol×l-1, p<0.001) whereas muscle levels were only marginally higher (27 vs 32 mmol×kg-1 d.w., p=0.003) compared to the Saline-trial. Post-exercise blood pH was higher in the Lactate-trial (7.34 vs 7.44, p<0.001), with no differences in intramuscular pH. Exercise increased the phosphorylation of mTORS2448 (~40%), S6K1T389 (~3-fold), and p44T202/T204 (~80%) during recovery, without any differences between trials. FSR over the 24-h recovery period did not differ between the Saline (0.067 %/h) and Lactate (0.062 %/h) trials. This study does not support the hypothesis that blood lactate levels can modulate anabolic signaling in contracted human muscle. Further in vivo research investigating the impact of exercised versus rested muscle and the role of intramuscular lactate is needed to elucidate its potential signaling properties.

  • 40.
    Lilja, Mats
    et al.
    Karolinska institutet.
    Mandić, Mirko
    Karolinska institutet.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Melin, Michael
    Karolinska institutet.
    Olsson, Karl
    Karolinska institutet.
    Rosenborg, Staffan
    Karolinska institutet.
    Gustafsson, Thomas
    Karolinska institutet.
    Lundberg, Tommy R
    Karolinska institutet.
    High-doses of anti-inflammatory drugs compromise muscle strength and hypertrophic adaptations to resistance training in young adults.2018In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 222, no 2, article id e12948Article in journal (Refereed)
    Abstract [en]

    AIMS: This study tested the hypothesis that high doses of anti-inflammatory drugs would attenuate the adaptive response to resistance training compared with low doses.

    METHODS: Healthy men and women (aged 18-35 years) were randomly assigned to daily consumption of ibuprofen (IBU; 1200 mg; n=15) or acetylsalicylic acid (ASA; 75 mg; n=16) for 8 weeks. During this period, subjects completed supervised knee-extensor resistance training where one leg was subjected to training with maximal volitional effort in each repetition using a flywheel ergometer (FW), while the other leg performed conventional (work-matched across groups) weight-stack training (WS). Before and after training, muscle volume (MRI) and strength were assessed, and muscle biopsies were analysed for gene and protein expression of muscle growth regulators.

    RESULTS: The increase in m. quadriceps volume was similar between FW and WS, yet was (averaged across legs) greater in ASA (7.5%) compared with IBU (3.7%, group difference 34 cm(3) ; P=0.029). In the WS leg, muscle strength improved similarly (11-20%) across groups. In the FW leg, increases (10-23%) in muscle strength were evident in both groups yet they were generally greater (interaction effects P<0.05) for ASA compared with IBU. While our molecular analysis revealed several training effects, the only group interaction (P<0.0001) arose from a down-regulated mRNA expression of IL-6 in IBU.

    CONCLUSION: Maximal over-the-counter doses of ibuprofen attenuate strength and muscle hypertrophic adaptations to 8 weeks of resistance training in young adults. Thus, young individuals using resistance training to maximise muscle growth or strength should avoid excessive intake of anti-inflammatory drugs. This article is protected by copyright. All rights reserved.

  • 41.
    Lilja, Mats
    et al.
    Department of Laboratory Medicine, Division of Clinical Physiology, Karolinska Institutet, Stockholm, Sweden ; Unit of Clinical Physiology, Karolinska University Hospital, Stockholm, Sweden..
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Martínez-Aranda, Luis Manuel
    Movement Analysis Laboratory for Sport and Health (MALab), Faculty of Sport, Catholic University of Murcia, Spain..
    Rundqvist, Håkan
    Department of Laboratory Medicine, Division of Clinical Physiology, Karolinska Institutet, Stockholm, Sweden ; Unit of Clinical Physiology, Karolinska University Hospital, Stockholm, Sweden..
    Langlet, Billy
    Department of Neurobiology, Karolinska Institutet, Stockholm, Sweden..
    Gustafsson, Thomas
    Department of Laboratory Medicine, Division of Clinical Physiology, Karolinska Institutet, Stockholm, Sweden ; Unit of Clinical Physiology, Karolinska University Hospital, Stockholm, Sweden..
    Lundberg, Tommy R
    Department of Laboratory Medicine, Division of Clinical Physiology, Karolinska Institutet, Stockholm, Sweden ; Unit of Clinical Physiology, Karolinska University Hospital, Stockholm, Sweden..
    Limited effect of over-the-counter doses of ibuprofen on mechanisms regulating muscle hypertrophy during resistance training in young adults.2023In: Journal of applied physiology, ISSN 8750-7587, E-ISSN 1522-1601, Vol. 134, no 3, p. 753-765Article in journal (Refereed)
    Abstract [en]

    We have previously shown that maximal over-the-counter doses of ibuprofen, compared with low doses of acetylsalicylic acid, reduce muscle hypertrophy in young individuals after 8 weeks of resistance training. Because the mechanism behind this effect has not been fully elucidated, we here investigated skeletal muscle molecular responses and myofiber adaptations in response to acute and chronic resistance training with concomitant drug intake. Thirty-one young (aged 18-35 years) healthy men (n=17) and women (n=14) were randomized to receive either ibuprofen (IBU;1200mg daily; n=15) or acetylsalicylic acid (ASA; 75mg daily; n=16) while undergoing 8 weeks of knee extension training. Muscle biopsies from the vastus lateralis were obtained before, at week 4 after an acute exercise session, and after 8 weeks of resistance training and analyzed for mRNA markers and mTOR signaling, as well as quantification of total RNA content (marker of ribosome biogenesis) and immunohistochemical analyzes of muscle fiber size, satellite cell content, myonuclear accretion, and capillarization. There were only two treatment ´ time interaction in selected molecular markers after acute exercise (atrogin-1 and MuRF1 mRNA), but several exercise effects. Muscle fiber size, satellite cell and myonuclear accretion, and capillarization were not affected by chronic training or drug intake. RNA content increased comparably (~14%) in both groups. Collectively, these data suggest that established acute and chronic hypertrophy regulators (including mTOR signaling, ribosome biogenesis, satellite cell content, myonuclear accretion, and angiogenesis) were not differentially affected between groups and therefore do not explain the deleterious effects of ibuprofen on muscle hypertrophy in young adults.

  • 42.
    Mascher, Henrik
    et al.
    Swedish School of Sport and Health Sciences, GIH.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH.
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH.
    Effects of essential amino acid supplementation on markers for anabolic and catabolic response to resistance exercise in female subjects2010Conference paper (Other academic)
  • 43.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Karolinska Institutet, Stockholm, Sweden..
    Cervenka, Igor
    Karolinska Institutet, Stockholm, Sweden..
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    van Hall, Gerrit
    University of Copenhagen, Copenhagen, Denmark..
    Holmberg, Hans-Christer
    Karolinska Institutet, Stockholm, Sweden..
    Ruas, Jorge L
    Karolinska Institutet, Stockholm, Sweden..
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Karolinska Institutet, Stockholm, Sweden..
    High-intensity leg cycling alters the molecular response to resistance exercise in the arm muscles.2021In: Scientific Reports, E-ISSN 2045-2322, Vol. 11, no 1, article id 6453Article in journal (Refereed)
    Abstract [en]

    This study examined acute molecular responses to concurrent exercise involving different muscles. Eight men participated in a randomized crossover-trial with two sessions, one where they performed interval cycling followed by upper body resistance exercise (ER-Arm), and one with upper body resistance exercise only (R-Arm). Biopsies were taken from the triceps prior to and immediately, 90- and 180-min following exercise. Immediately after resistance exercise, the elevation in S6K1 activity was smaller and the 4E-BP1:eIF4E interaction greater in ER-Arm, but this acute attenuation disappeared during recovery. The protein synthetic rate in triceps was greater following exercise than at rest, with no difference between trials. The level of PGC-1α1 mRNA increased to greater extent in ER-Arm than R-Arm after 90 min of recovery, as was PGC-1α4 mRNA after both 90 and 180 min. Levels of MuRF-1 mRNA was unchanged in R-Arm, but elevated during recovery in ER-Arm, whereas MAFbx mRNA levels increased slightly in both trials. RNA sequencing in a subgroup of subjects revealed 862 differently expressed genes with ER-Arm versus R-Arm during recovery. These findings suggest that leg cycling prior to arm resistance exercise causes systemic changes that potentiate induction of specific genes in the triceps, without compromising the anabolic response.

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  • 44.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Holmberg, Hans-Christer
    Swedish Winter Sports Res Ctr, Östersund, Sweden..
    van Hall, Gerrit
    Clin Metabol Core Facil, Copenhagen, Denmark..
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH.
    Effects Of Lactate Infusion On Resistance Exericse Induced MTORC1-signaling And Protein Synthesis In Human Muscle2020In: MEDICINE AND SCIENCE IN SPORTS AND EXERCISE. 52:17. Suppl. Meeting Abstract: 128, Lippincott Williams & Wilkins, 2020, Vol. 52, no 17, p. 19-19Conference paper (Other academic)
  • 45.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Physiology and Pharmacology, Karolinska Institute, Sweden.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institute, Sweden.
    Horwath, Oscar
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    van Hall, Gerrit
    University of Copenhagen, Denmark.; Rigshospitalet, Copenhagen, Denmark..
    Blackwood, Sarah J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Acute normobaric hypoxia blunts contraction-mediated mTORC1- and JNK-signaling in human skeletal muscle.2022In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 234, no 2, article id e13771Article in journal (Refereed)
    Abstract [en]

    AIM: Hypoxia has been shown to reduce resistance exercise-induced stimulation of protein synthesis and long-term gains in muscle mass. However, the mechanism whereby hypoxia exerts its effect is not clear. Here we examine the effect of acute hypoxia on the activity of several signaling pathways involved in regulation of muscle growth following a bout of resistance exercise.

    METHODS: Eight men performed two sessions of leg resistance exercise in Normoxia or Hypoxia (12% O2 ) in a randomized crossover fashion. Muscle biopsies were obtained at rest and at 0, 90,180 min after exercise. Muscle analyses included levels of signaling proteins and metabolites associated with energy turnover.

    RESULTS: Exercise during Normoxia induced a 5-10-fold increase of S6K1Thr389 phosphorylation throughout the recovery period, but Hypoxia blunted the increases by ~50%. Phosphorylation of JNKThr183/Tyr185 and the JNK target SMAD2Ser245/250/255 was increased by 30-40-fold immediately after exercise in Normoxia, but Hypoxia blocked almost 70% of the activation. Throughout recovery, phosphorylation of JNK and SMAD2 remained elevated following exercise in Normoxia, but the effect of Hypoxia was lost at 90-180 min post-exercise. Hypoxia had no effect on exercise induced Hippo- or autophagy-signaling and ubiquitin-proteasome related protein levels. Nor did Hypoxia alter the changes induced by exercise in high energy phosphates, glucose 6-P, lactate, or phosphorylation of AMPK or ACC.

    CONCLUSION: We conclude that acute severe hypoxia inhibits resistance exercise induced mTORC1- and JNK signaling in human skeletal muscle, effects that do not appear to be mediated by changes in the degree of metabolic stress in the muscle.

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  • 46.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Aminosyror ökar träningseffekten2013In: Svensk Idrottsforskning: Organ för Centrum för Idrottsforskning, ISSN 1103-4629, Vol. 22, no 1, p. 45-49Article in journal (Other academic)
    Abstract [sv]

    Kostens sammansättning är viktig för prestation och återhämtning. Dess innehåll av protein och essentiella aminosyror kan påverka musklernas anpassning till träning. Ny forskning visar att vissa aminosyror har en viktigare roll än att enbart agera som byggstenar eller energigivande näringsämnen.

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  • 47.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's and Mats Börjesson's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    High-intensity cycling performed prior to resistance exercise does not influence mTORC1-signaling and the rate of muscle protein synthesis in the triceps brachii2014Conference paper (Other academic)
    Abstract [en]

    Introduction

    Endurance exercise can influence strength training adaptations when performed concurrently, with both inhibition (Kreamer 1995) and augmentation (Lundberg 2012) of muscular hypertrophy being reported. Our lab has set out to conduct a series of studies to examine the influence of endurance exercise on the acute stimulatory effect of resistance exercise on anabolic processes. In the present study, the effect of endurance exercise on a previously inactive muscle was investigated. The aim was to examine the influence of resistance exercise on mTORC1-signaling and rate of protein synthesis in the triceps brachii muscle with or without preceding intervals of high-intensity cycling. 

     

    Methods

    Eight trained males performed, in a randomized fashion, two sessions of heavy resistance exercise (RE) with the triceps muscles, where one session was preceded by intervals of high-intensity cycling (E+RE), 5 x 4 min at 85% of VO2 peak. Mixed muscle protein fractional synthetic rate (FSR) was measured at rest, prior to exercise, and during a 3 hour recovery period following exercise by continuous infusion of L-[ring-13C6] phenylalanine. Muscle biopsies from the triceps brachii was collected twice at rest separated by three hours, directly after resistance exercise and following 90 and 180 min of recovery. Signalling in the mTORC1-and AMPK-pathway was assessed using western blot technique.

     

    Results

    The same amount of work with regard to load, total number of repetitions and total time under tension was performed in the two trials. Muscle protein FSR increased from 0.050 ± 0.006 %/h at rest to 0.078 ± 0.008 and 0.082 ± 0.0016 %/h following E+RE and RE, respectively, with no difference between trials. Phosphorylation (P) of AMPKT172 was increased by 45-65% directly after exercise, similarly in both conditions, and regressed to a level approx. 20% lower than baseline following 180 min of recovery. P-mTORS2448 was increased 76 and 108% above rest directly after the E+RE and RE, respectively, and remained elevated in both trials during the entire recovery period. P-eEF2T56 was 20-36% higher directly after exercise but fell to a level that was 30-36% lower than pre-exercise and remained reduced during the entire recovery, with no difference between trials.

     

    Conclusion

    High-intensity endurance cycling does not influence the acute stimulation of anabolic signalling and muscle protein synthesis in the triceps brachii following resistance exercise.

     

     

    References

    Kreamer WJ et al. (1995) J Appl Physiol 78(3):976-989

    Lundberg T et al. (2013) J Appl Physiol 114: 81-89

  • 48.
    Moberg, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Apró, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Ohlsson, Inger
    Pontén, Marjan
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Villanueva, Antonio
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom's and Mats Börjesson's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Absence of leucine in an essential amino acid supplement reduces activation of mTORC1 signalling following resistance exercise in young females.2014In: Applied Physiology, Nutrition and Metabolism, ISSN 1715-5312, E-ISSN 1715-5320, Vol. 39, no 2, p. 183-94Article in journal (Refereed)
    Abstract [en]

    The purpose of the study was to investigate the specific effect of leucine on mTORC1 signalling and amino acid metabolism in connection with resistance exercise. Comparisons were made between ingestion of supplements with and without leucine. Eight young women performed leg press exercise on 2 occasions. In randomized order they received either an aqueous solution of essential amino acids with leucine (EAA) or without leucine (EAA-Leu), given as small boluses throughout the experiment. Muscle biopsies were taken after an overnight fast before exercise and 1 and 3 h postexercise and samples of blood were taken repeatedly during the experiment. Plasma and muscle concentrations of leucine rose 60%-140% (p < 0.05) with EAA and fell 35%-45% (p < 0.05) with the EAA-Leu supplement. In the EAA-trial, plasma and muscle levels of tyrosine (not present in the supplement) and the sum of the EAA were 15%-25% (p < 0.05) lower during recovery. Phosphorylation of mTOR and p70S6k was elevated to a larger extent following 1 h of recovery with leucine in the supplement (120% vs. 49% (p < 0.05) and 59- vs. 8-fold (p < 0.05) for EAA and EAA-Leu, respectively). The levels of MAFbx and MuRF-1 mRNA and of the corresponding proteins were not significantly altered after 3 h recovery from exercise. In conclusion, the presence of leucine in the supplement enhances the stimulatory effect on mTORC1 signalling and reduces the level of tyrosine and the sum of the EAA in muscle and plasma, suggesting a stimulation of protein synthesis and (or) inhibition of breakdown, leading to improvement in net protein balance.

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  • 49.
    Nilsson, Lina
    et al.
    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.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    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.
    Larsen, Filip J
    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.
    Biphasic relationship between training load and glucose tolerance2019Conference paper (Other academic)
    Abstract [sv]

    Biphasic relationship between training load and glucose tolerance

    Nilsson, L, Flockhart M, Bergman K, Apro W, Ekblom B, Larsen FJ

     

    There is a well-established construct regarding the positive effects of exercise on glucose tolerance and insulin sensitivity, as well as muscle glycogen storage. In insulin resistance, physical activity is an essential part of the treatment. However, the optimal dose is unknown. Reduced muscular glycogen stores, resulting from exercise, should stimulate an increased uptake of blood glucose. In this study we investigated the relation between training load, glucose tolerance and insulin sensitivity during three weeks of increasing interval training. Three times during the intervention, oral glucose tests were conducted to investigate the rate of glucose uptake. We found a biphasic dose-response relationship between training load and glucose tolerance, where an excessive training load led to a paradoxical reduction in glucose tolerance and impaired insulin release despite an unchanged amount of muscle glycogen. In light of these results, an upper limit of physical exercise exist where the negative effects overpowers the positive.

  • 50.
    Nordström, Fabian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Liegnell, Rasmus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Apro, William
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Clinical Science, Intervention and Technology, Karolinska Institute, Sweden.
    Blackwood, Sarah J
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Katz, Abram
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Physiology, Nutrition and Biomechanics. Department of Physiology and Pharmacology, Karolinska Institute, Sweden.
    The lactate receptor GPR81 is predominantly expressed in type II human skeletal muscle fibers: potential for lactate autocrine signaling.2023In: American Journal of Physiology - Cell Physiology, ISSN 0363-6143, E-ISSN 1522-1563, Vol. 324, no 2, p. C477-C487Article in journal (Refereed)
    Abstract [en]

    GPR81 was first identified in adipocytes as a receptor for L-lactate, which upon binding inhibits cAMP-PKA-CREB signaling. Moreover, incubation of myotubes with lactate augments expression of GPR81 and genes and proteins involved in lactate- and energy metabolism. However, characterization of GPR81 expression and investigation of related signaling in human skeletal muscle under conditions of elevated circulating lactate levels are lacking. Muscle biopsies were obtained from healthy men and women at rest, after leg extension exercise, with or without venous infusion of sodium lactate, and 90 and 180 min after exercise (8 men and 8 women). Analyses included protein and mRNA levels of GPR81, as well as GPR81-dependent signaling molecules. GPR81 expression was 2.5-fold higher in type II glycolytic compared with type I oxidative muscle fibers, and the expression was inversely related to the percentage of type I muscle fibers. Muscle from women expressed about 25% more GPR81 protein than from men. Global PKA-activity increased by 5-8% after exercise, with no differences between trials. CREBS133 phosphorylation was reduced by 30% after exercise and remained repressed during the entire trials, with no influence of the lactate infusion. The mRNA expression of VEGF and PGC-1α were increased by 2.5 - 6-fold during recovery, and that of LDH reduced by 15% with no differences between trials for any gene at any time point. The high expression of GPR81-protein in type II fibers suggests that lactate functions as an autocrine signaling molecule in muscle; however, lactate does not appear to regulate CREB signaling during exercise.

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