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  • 1. Andersson, Ulrika
    et al.
    Leighton, Brendan
    Young, Martin E
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Newsholme, Eric A
    Inactivation of aconitase and oxoglutarate dehydrogenase in skeletal muscle in vitro by superoxide anions and/or nitric oxide.1998In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 249, no 2, p. 512-6Article in journal (Refereed)
    Abstract [en]

    Strips of rat soleus muscle were incubated in media containing a superoxide generating system and/or the nitric oxide donor sodium nitroprusside (SNP) before the maximal catalytic activities of aconitase, citrate synthase, and oxoglutarate dehydrogenase were measured. The maximal activities of aconitase and oxoglutarate dehydrogenase were both decreased by 25-30% by superoxide anions; however, only the maximal activity of aconitase was decreased, by approximately 50%, by incubation of muscles with SNP. Furthermore, when both superoxide and NO were present in the medium, aconitase activity was decreased by 70%. The maximal activity of citrate synthase was not affected by any of the treatments. This is the first time that superoxide anions or NO has been shown to inactivate aconitase and oxoglutarate dehydrogenase in skeletal muscle. It is suggested that these effects may be responsible for some alterations in skeletal muscle metabolism, and these possibilities are discussed.

  • 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)
  • 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.

  • 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 and Mats Börjesson'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 and Mats Börjesson'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.
    Bermon, Stephane
    et al.
    Monaco Inst Sports Med & Surg, Monaco.
    Castell, Lindy M
    Univ Oxford, Green Templeton Coll, Oxford, England.
    Calder, Philip C
    Bishop, Nicolette C
    Univ Southampton, Fac Med, Human Dev & Hlth Acad Unit, Southampton, Hants, England.
    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.
    Mooren, Frank C
    Justus Liebig Univ, Dept Sports Med, Giessen, Germany.
    Krüger, Karsten
    Justus Liebig Univ, Dept Sports Med, Giessen, Germany.
    Kavazis, Andreas N
    Auburn Univ, Sch Kinesiol, Auburn, AL 36849 USA.
    Quindry, John C
    Univ Montana, Hlth & Human Performance, Missoula, MT 59812 USA.
    Senchina, David S
    Drake Univ, Dept Biol, Kinesiol Program, Des Moines, IA 50311 USA.
    Nieman, David C
    Appalachian State Univ, Human Performance Lab, North Carolina Res Campus, Kannapolis, NC USA.
    Gleeson, Michael
    Univ Loughborough, Sch Sport Exercise & Hlth Sci, Loughborough, Leics, England.
    Pyne, David B
    Australian Inst Sport, Bruce, Australia.
    Kitic, Cecilia M
    Univ Tasmania, Sch Hlth Sci, Sport Performance Optimisat Res Team, Launceston, Tas, Australia.
    Close, Graeme L
    Liverpool John Moores Univ, Res Inst Sport & Exercise Sci, Liverpool, Merseyside, England.
    Larson-Meyer, D Enette
    Univ Wyoming, Dept Family & Consumer Sci, Nutr & Exercise Lab, Laramie, WY 82071 USA.
    Marcos, Ascension
    CSIC, Spanish Natl Res Council, Inst Food Sci Technol & Nutr ICTAN, Madrid, Spain.
    Meydani, Simin N
    Tufts Univ, Jean Mayer USDA Human Nutr Res Ctr Aging, Boston, MA 02111 USA.
    Wu, Dayong
    Tufts Univ, Jean Mayer USDA Human Nutr Res Ctr Aging, Boston, MA 02111 USA.
    Walsh, Neil P
    Bangor Univ, Sch Sport Hlth & Exercise Sci, Bangor, Gwynedd, Wales.
    Nagatomi, Ryochi
    Tohoku Univ, Grad Sch Biomed Engn, Lab Hlth & Sports Sci, Sendai, Miyagi, Japan.
    Consensus Statement Immunonutrition and Exercise.2017In: Exercise immunology review, ISSN 1077-5552, Vol. 23, p. 8-50Article, review/survey (Refereed)
    Abstract [en]

    In this consensus statement on immunonutrition and exercise, a panel of knowledgeable contributors from across the globe provides a consensus of updated science, including the background, the aspects for which a consensus actually exists, the controversies and, when possible, suggested directions for future research.

  • 13.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    A role for branched-chain amino acids in reducing central fatigue.2006In: Journal of Nutrition, ISSN 0022-3166, E-ISSN 1541-6100, Vol. 136, no 2, p. 544S-547SArticle in journal (Refereed)
    Abstract [en]

    Several factors have been identified to cause peripheral fatigue during exercise, whereas the mechanisms behind central fatigue are less well known. Changes in the brain 5-hydroxytryptamine (5-HT) level is one factor that has been suggested to cause fatigue. The rate-limiting step in the synthesis of 5-HT is the transport of tryptophan across the blood-brain barrier. This transport is influenced by the fraction of tryptophan available for transport into the brain and the concentration of the other large neutral amino acids, including the BCAAs (leucine, isoleucine, and valine), which are transported via the same carrier system. Studies in human subjects have shown that the plasma ratio of free tryptophan (unbound to albumin)/BCAAs increases and that tryptophan is taken up by the brain during endurance exercise, suggesting that this may increase the synthesis of 5-HT in the brain. Ingestion of BCAAs increases their concentration in plasma. This may reduce the uptake of tryptophan by the brain and also 5-HT synthesis and thereby delay fatigue. Accordingly, when BCAAs were supplied to human subjects during a standardized cycle ergometer exercise their ratings of perceived exertion and mental fatigue were reduced, and, during a competitive 30-km cross-country race, their performance on different cognitive tests was improved after the race. In some situations the intake of BCAAs also improves physical performance. The results also suggest that ingestion of carbohydrates during exercise delays a possible effect of BCAAs on fatigue since the brain's uptake of tryptophan is reduced.

  • 14.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Amino acids and central fatigue.2001In: Amino Acids, ISSN 0939-4451, E-ISSN 1438-2199, Vol. 20, no 1, p. 25-34Article in journal (Refereed)
    Abstract [en]

    There is an increasing interest in the mechanisms behind central fatigue, particularly in relation to changes in brain monoamine metabolism and the influence of specific amino acids on fatigue. Several studies in experimental animals have shown that physical exercise increases the synthesis and metabolism of brain 5-hydroxytryptamine (5-HT). Support for the involvement of 5-HT in fatigue can be found in studies where the brain concentration of 5-HT has been altered by means of pharmacological agents. When the 5-HT level was elevated in this way the performance was impaired in both rats and human subjects, and in accordance with this a decrease in the 5-HT level caused an improvement in running performance in rats. The precursor of 5-HT is the amino acid tryptophan and the synthesis of 5-HT in the brain is thought to be regulated by the blood supply of free tryptophan in relation to other large neutral amino acids (including the branched-chain amino acids, BCAA) since these compete with tryptophan for transport into the brain. Studies in human subjects have shown that the plasma ratio of free tryptophan/BCAA increases during and, particularly, after sustained exercise. This would favour the transport of tryptophan into the brain and also the synthesis and release of 5-HT which may lead to central fatigue. Attempts have been made to influence the 5-HT level by giving BCAA to human subjects during different types of sustained heavy exercise. The results indicate that ingestion of BCAA reduces the perceived exertion and mental fatigue during exercise and improves cognitive performance after the exercise. In addition, in some situations ingestion of BCAA might also improve physical performance; during exercise in the heat or in a competitive race when the central component of fatigue is assumed to be more pronounced than in a laboratory experiment. However, more experiments are needed to further clarify the effect of BCAA and also of tryptophan ingestion on physical performance and mental fatigue.

  • 15.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Branched-chain Amino Acids and Central Fatigue: Implications for Diet and Behavior2011In: Handbook of Behavior, Food and Nutrition / [ed] V.R. Preedy et al., Springer Science + Business Media , 2011, p. 865-877Chapter in book (Other academic)
  • 16.
    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.
    Fysiologisk forskning åren 1997-20132014In: Från Kungl. Gymnastiska Centralinstitutet till Gymnastik- och idrottshögskolan: en betraktelse av de senaste 25 åren som del av en 200-årig historia / [ed] Suzanne Lundvall, Stockholm: Gymnastik- och idrottshögskolan, GIH , 2014, p. 200-206Chapter in book (Other (popular science, discussion, etc.))
  • 17.
    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.
    Maximera träningen med fokus på kosten2018In: Idrottsmedicin, ISSN 2001-3302, Vol. 37, no 3, p. 6-7Article in journal (Other academic)
    Abstract [sv]

    Med fokus på kosten kan idrottare maximera träningens effekter. Genom att träna med låga glykogendepåer kan den aeroba prestationsförmågan öka och intag av essentiella aminosyror i samband med styrketräning kan stimulera tillväxt av muskelmassa.

  • 18.
    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.
    Utilisation of different energy sources during exercise and nutritional strategies for effective recovery2014In: Women and sport, Stockholm: SISU idrottsböcker , 2014Chapter in book (Other academic)
    Abstract [en]

    In this text, we will examine how the body uses the nutrients in food to produce energy during exercise, and whether these processes differ between the sexes. If they do, does this mean that the nutritional requirements should be different for men and women? We will also present current knowledge on the effects of nutrition on recovery after physical activity, a topic that has attracted much interest in the sports world. finally, we will briefl y discuss the nutritional requirements of physically active women and the common nutritional problems they encounter.

  • 19.
    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.))
  • 20.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Celsing, F
    Newsholme, E A
    Changes in plasma concentrations of aromatic and branched-chain amino acids during sustained exercise in man and their possible role in fatigue.1988In: Acta Physiologica Scandinavica, ISSN 0001-6772, E-ISSN 1365-201X, Vol. 133, no 1, p. 115-21Article in journal (Refereed)
    Abstract [en]

    The plasma concentrations of branched-chain and aromatic amino acids have been measured in two different types of sustained dynamic exercise. Twenty-two subjects participated in the 1986 Stockholm Marathon and eight subjects took part in an army training programme of approximately 1.5-h duration. Both types of exercise caused a significant decrease in the plasma concentration of branched-chain amino acids, while there was no change in the concentration of total (free plus bound to albumin) tryptophan. The plasma concentration of free tryptophan, which was measured in the marathon runners, was found to increase 2.4-fold during the race. This increase is probably caused by a pronounced elevation in the concentration of plasma free fatty acids during exercise, since these are known to displace tryptophan from albumin. The observed increase in plasma free tryptophan concentration, together with the decrease in plasma concentration of branched-chain amino acids, gives rise to a marked increase in the plasma concentration ratio of free tryptophan/branched-chain amino acids. This should lead to an increase in the rate of transport of tryptophan across the blood-brain barrier and hence to an increase in the rate of synthesis of 5-hydroxytryptamine (5-HT) in the brain. An elevated concentration of 5-HT in specific areas of the brain may be responsible, at least in part, for the development of physical, and/or mental fatigue during prolonged exercise.

  • 21.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Ek, Sonja
    Newsholme, Eric A
    Influence of ingesting a solution of branched-chain amino acids on plasma and muscle concentrations of amino acids during prolonged submaximal exercise.1996In: Nutrition (Burbank, Los Angeles County, Calif.), ISSN 0899-9007, E-ISSN 1873-1244, Vol. 12, no 7-8, p. 485-90Article in journal (Refereed)
    Abstract [en]

    On two occasions, seven male endurance-trained cyclists performed sustained exhaustive exercise with reduced muscle glycogen stores. During exercise, the subjects were supplied in random order with an aqueous solution of branched-chain amino acids (BCAA) or flavored water (placebo). Ingestion of BCAA caused the concentration of these amino acids to increase by 135% in the plasma and by 57% in muscle tissue during exercise, whereas in the placebo trial there was no change or a slight decrease in the concentration in plasma and a decrease of 18% in the muscle. The plasma concentration of alanine increased by 48% during exercise when BCAA were ingested, and the increase in the muscle concentration of alanine during exercise was larger (70% versus 31% in the placebo trial), suggesting an increased rate of alanine production. Also, the plasma concentration of arginine increased by 14% during exercise when BCAA were ingested, whereas there was no change during exercise in the placebo trial. There was a smaller decrease in the muscle glutamate concentration during exercise in the BCAA trial (32% versus 47% in the placebo trial; p < 0.05), but, for the remaining amino acids, there was no difference between the BCAA and placebo trials. There was a significant decrease in the muscle glycogen concentration during exercise in the placebo trial, whereas only a small decrease was found in the BCAA trial (28 and 9 mmol/kg wet wt [p < 0.05] in the placebo and BCAA trial, respectively). This might indicate that an increased supply of BCAA has a sparing effect on muscle glycogen degradation during exercise.

  • 22.
    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.
    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.
    Hedman, Rune
    Schantz, Peter
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, The Research Unit for Movement, Health and Environment.
    Irma Åstrand: Nekrolog2016Other (Other (popular science, discussion, etc.))
  • 23.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Eliasson, Jörgen
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Karlsson, Håkan K R
    Köhnke, Rickard
    Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise2006In: Journal of Nutrition, ISSN 0022-3166, E-ISSN 1541-6100, Vol. 136, no 1 Suppl, p. 269S-273SArticle in journal (Refereed)
  • 24.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Essén-Gustavsson, B
    Influence of reduced muscle temperature on metabolism in type I and type II human muscle fibres during intensive exercise.1987In: Acta Physiologica Scandinavica, ISSN 0001-6772, E-ISSN 1365-201X, Vol. 131, no 4, p. 569-74Article in journal (Refereed)
    Abstract [en]

    Six male subjects performed intensive cycle exercise to exhaustion after cooling their legs in water at 10-12 degrees C (muscle temperature (Tm) 28 +/- 2.6 degrees C, mean +/- SD). Exercise at exactly the same rate and duration (370 +/- 34 W, 1.5 +/- 0.2 min) was then repeated by each subject 2-5 weeks later at normal Tm (35 +/- 1.0 degrees C). Muscle biopsies were taken from the vastus lateralis muscle at rest and after exercise. The muscle tissue was freeze-dried and fragments of single fibres were dissected out. The fibres were classified and pooled into groups of type I and type II. Analyses of glycogen, glucose 6-phosphate, lactate and phosphagens were performed on pools of type-identified fibres. After exercise at reduced Tm, all subjects had higher concentrations of glucose 6-phosphate and lactate in both type I and type II fibres, and in most subjects the concentrations of ATP and phosphocreatine were lower as compared with the findings after exercise at normal Tm. During exercise the glycogen content of both fibre types decreased to a greater extent at reduced than at normal Tm in most subjects. The results suggest that during intensive dynamic exercise at reduced Tm there is a higher degree of glycolysis from glycogen in the muscle than in the normal situation. In some subjects the cause of fatigue may be related to a more rapid accumulation of lactate in the cold muscle, while in others fatigue may be related to alternative factors, e.g. low levels of ATP and phosphocreatine.

  • 25.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Essén-Gustavsson, Birgitta
    Changes in amino acid concentration in plasma and type I and type II fibres during resistance exercise and recovery in human subjects.2009In: Amino Acids, ISSN 0939-4451, E-ISSN 1438-2199, Vol. 37, no 4, p. 629-36Article in journal (Refereed)
    Abstract [en]

    Eight male subjects performed leg press exercise, 4 x 10 repetitions at 80% of their maximum. Venous blood samples were taken before, during exercise and repeatedly during 2 h of recovery. From four subjects, biopsies were taken from the vastus lateralis muscle prior to, immediately after and following one and 2 h of recovery. Samples were freeze-dried, individual muscle fibres were dissected out and identified as type I or type II. Resistance exercise led to pronounced reductions in the glutamate concentration in both type I (32%) and type II fibres (70%). Alanine concentration was elevated 60-75% in both fibre types and 29% in plasma. Glutamine concentration remained unchanged after exercise; although 2 h later the concentrations in both types of fibres were reduced 30-35%. Two hours after exercise, the plasma levels of glutamate and six of the essential amino acids, including the branched-chain amino acids were reduced 5-30%. The data suggest that glutamate acts as an important intermediate in muscle energy metabolism during resistance exercise, especially in type II fibres.

  • 26.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Hassmén, Peter
    Ek, S
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Newsholme, E A
    Influence of ingesting a solution of branched-chain amino acids on perceived exertion during exercise.1997In: Acta Physiologica Scandinavica, ISSN 0001-6772, E-ISSN 1365-201X, Vol. 159, no 1, p. 41-9Article in journal (Refereed)
    Abstract [en]

    On two occasions, seven male endurance-trained cyclists performed exhaustive exercise on a cycle ergometer in the morning after they had performed a bout of exercise the preceding evening in an attempt to lower the muscle glycogen stores. The subjects exercised at a work rate corresponding to approximately 70% of their maximal oxygen uptake for 60 min, followed by another 20 min of maximal exercise. During exercise the subjects were given either a solution of branched-chain amino acids (BCAAs) or flavoured water (placebo). Every 10 min during exercise the subjects rated their perceived exertion and mental fatigue on two different Borg scales. During the 60 min exercise at a given work rate the subjects ratings of perceived exertion when they were given BCAAs were 7% lower, and their ratings of mental fatigue were 15% lower than when they were given placebo. In addition, the performance in the colour task of Stroops Colour Word Test performed after exercise was improved when BCAAs had been ingested during exercise, compared with the results from the placebo trial. There was no difference in the physical performance between the two trials measured as the amount of work done during the last 20 min of exercise when the subjects performed at their maximum. The plasma concentration ratio of free tryptophan/BCAAs, which increased by 45% during exercise and by 150% 5 min after exercise in the placebo trial, remained unchanged or even decreased when BCAAs were ingested.

  • 27.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Krustrup, Peter
    Søndergaard, Hans
    Rådegran, Göran
    Calbet, José A L
    Saltin, Bengt
    Exercise training induces similar elevations in the activity of oxoglutarate dehydrogenase and peak oxygen uptake in the human quadriceps muscle.2011In: Pflügers Archiv: European Journal of Physiology, ISSN 0031-6768, E-ISSN 1432-2013, Vol. 462, no 2, p. 257-65Article in journal (Refereed)
    Abstract [en]

    During exercise involving a small muscle mass, peak oxygen uptake is thought to be limited by peripheral factors, such as the degree of oxygen extraction from the blood and/or mitochondrial oxidative capacity. Previously, the maximal activity of the Krebs cycle enzyme oxoglutarate dehydrogenase has been shown to provide a quantitative measure of maximal oxidative metabolism, but it is not known whether the increase in this activity after a period of training reflects the elevation in peak oxygen consumption. Fourteen subjects performed one-legged knee extension exercise for 5-7 weeks, while the other leg remained untrained. Thereafter, the peak oxygen uptake by the quadriceps muscle was determined for both legs, and muscle biopsies were taken for assays of maximal enzyme activities (at 25°C). The peak oxygen uptake was 26% higher in the trained than in the untrained muscle (395 vs. 315 ml min(-1) kg(-1), respectively; P<0.01). The maximal activities of the Krebs cycle enzymes in the trained and untrained muscle were as follows: citrate synthase, 22.4 vs. 18.2 μmol min(-1) g(-1) (23%, P<0.05); oxoglutarate dehydrogenase, 1.88 vs. 1.54 μmol min(-1) g(-1) (22%, P<0.05); and succinate dehydrogenase, 3.88 vs. 3.28 μmol min(-1) g(-1) (18%, P<0.05). The difference between the trained and untrained muscles with respect to peak oxygen uptake (80 ml min(-1) kg(-1)) corresponded to a flux through the Krebs cycle of 1.05 μmol min(-1) g(-1), and the corresponding difference in oxoglutarate dehydrogenase activity (at 38°C) was 0.83 μmol min(-1) g(-1). These parallel increases suggest that there is no excess mitochondrial capacity during maximal exercise with a small muscle mass.

  • 28.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Møller, K
    Secher, N H
    Nybo, L
    Effect of carbohydrate ingestion on brain exchange of amino acids during sustained exercise in human subjects.2005In: Acta Physiologica Scandinavica, ISSN 0001-6772, E-ISSN 1365-201X, Vol. 185, no 3, p. 203-9Article in journal (Refereed)
    Abstract [en]

    AIM: This study investigated the effect of prolonged exercise with and without carbohydrate intake on the brain exchange of amino acids, especially focussing on tryptophan and branched-chain amino acids (BCAA). METHODS: Five male subjects exercised for 3 h on a cycle ergometer at 200 +/- 7 W on two occasions; either supplemented with a 6% carbohydrate solution or with flavoured water (placebo). Catheters were inserted into the right internal jugular vein and the radial artery of the non-dominant arm. The brain exchange of amino acids during exercise was calculated from the arterial-jugular venous concentration difference multiplied by plasma flow. RESULTS: About 106 micromol (22 mg) of tryptophan was taken up by the brain during exercise in the placebo trial, whereas no significant uptake was observed in the carbohydrate trial. In accordance, the arterial concentration of free tryptophan increased from 12 +/- 1 to 20 +/- 2 micromol L(-1) during the placebo trial and was significantly higher compared with the glucose trial (14 +/- 1 micromol L(-1) at the end of exercise). Also, the arterial concentration of total tryptophan (free and albumin-bound) increased during the first 30 min of exercise in both trials, but returned to the basal level at 180 min of exercise. In both trials, BCAA were taken up by the brain while glutamine was released. CONCLUSION: The present data show that both tryptophan and BCAA are taken up by the brain during prolonged exercise, and we suggest that the cerebral uptake of tryptophan may relate to increased synthesis of serotonin (5-HT) in the brain.

  • 29.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Rådegran, Göran
    Saltin, Bengt
    Maximum rate of oxygen uptake by human skeletal muscle in relation to maximal activities of enzymes in the Krebs cycle.1997In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 501 ( Pt 2), p. 455-60Article in journal (Refereed)
    Abstract [en]

    1. Ten subjects performed incremental exercise up to their maximum work rate with the knee extensors of one leg. Measurements of leg blood flow and femoral arteriovenous differences of oxygen were made in order to be able to calculate oxygen uptake of the leg. 2. The volume of the quadriceps muscle was determined from twenty-one to twenty-five computer tomography section images taken from the patella to the anterior inferior iliac spine of each subject. 3. The maximal activities of three enzymes in the Krebs cycle, citrate synthase, oxoglutarate dehydrogenase and succinate dehydrogenase, were measured in biopsy samples taken from the vastus lateralis muscle. 4. The average rate of oxygen uptake over the quadriceps muscle at maximal work, 353 ml min-1 kg-1, corresponded to a Krebs cycle rate of 4.6 mumol min-1 g-1. This was similar to the maximal activity of oxoglutarate dehydrogenase (5.1 mumol min-1 g-1), whereas the activities of succinate dehydrogenase and citrate synthase averaged 7.2 and 48.0 mumol min-1 g-1, respectively. 5. It is suggested that of these enzymes, only the maximum activity of oxoglutarate dehydrogenase can provide a quantitative measure of the capacity of oxidative metabolism, and it appears that the enzyme is fully activated during one-legged knee extension exercise at the maximal work rate.

  • 30.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Saltin, Bengt
    BCAA intake affects protein metabolism in muscle after but not during exercise in humans.2001In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 281, no 2, p. E365-74Article in journal (Refereed)
    Abstract [en]

    Branched-chain amino acids (BCAA) or a placebo was given to seven subjects during 1 h of ergometer cycle exercise and a 2-h recovery period. Intake of BCAA did not influence the rate of exchange of the aromatic amino acids, tyrosine and phenylalanine, in the legs during exercise or the increase in their concentration in muscle. The increase was approximately 30% in both conditions. On the other hand, in the recovery period after exercise, a faster decrease in the muscle concentration of aromatic amino acids was found in the BCAA experiment (46% compared with 25% in the placebo condition). There was also a tendency to a smaller release (an average of 32%) of these amino acids from the legs during the 2-h recovery. The results suggest that BCAA have a protein-sparing effect during the recovery after exercise, either that protein synthesis has been stimulated and/or protein degradation has decreased, but the data during exercise are too variable to make any conclusions about the effects during exercise. The effect in the recovery period does not seem to be mediated by insulin.

  • 31.
    Blomstrand, Eva
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Saltin, Bengt
    Effect of muscle glycogen on glucose, lactate and amino acid metabolism during exercise and recovery in human subjects.1999In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 514 ( Pt 1), p. 293-302Article in journal (Refereed)
    Abstract [en]

    1. Eight subjects performed two-legged exercise, one leg with low and the other with normal muscle glycogen content. The purpose was to study the effect of low initial muscle glycogen content on the metabolic response during 1 h of exercise and 2 h of recovery. This model allows direct comparison of net fluxes of substrates and metabolites over the exercising legs receiving the same arterial inflow. 2. Muscle glycogen breakdown during exercise was 60% lower in the leg with a reduced pre-exercise glycogen concentration and the rate of glucose uptake during exercise was 30% higher. 3. The amount of pyruvate that was oxidized during exercise was calculated to be approximately 450 mmol in the low-glycogen leg and 750 mmol in the normal-glycogen leg, which suggests more fat and amino acid oxidation in the low-glycogen leg. 4. During exercise, there was a significant release of amino acids not metabolized in the muscle, e. g. tyrosine and phenylalanine, only from the low-glycogen leg, suggesting an increased rate of net protein degradation in this leg. 5. The release of tyrosine and phenylalanine from the low-glycogen leg during the exercise period and the change in their muscle concentrations yield a net tyrosine and phenylalanine production rate of 1.4 and 1.5 mmol h-1, respectively. The net rate of protein degradation was then calculated to be 7-12 g h-1. 6. The results suggest that the observed differences in metabolism between the low-glycogen and the normal-glycogen leg are induced by the glycogen level per se, since the legs received the same arterial supply of hormones and substrates.

  • 32.
    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)
  • 33.
    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.

  • 34.
    Borgenvik, Marcus
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Nordin, Marie
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Mattsson, C. Mikael
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Enqvist, Jonas K.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Alterations in amino acid concentrations in the plasma and muscle in human subjects during 24 h of simulated adventure racing2012In: European Journal of Applied Physiology, ISSN 1439-6319, E-ISSN 1439-6327, Vol. 112, p. 3679-3688Article in journal (Refereed)
    Abstract [en]

    This investigation was designed to evaluate changes in plasma and muscle levels of free amino acids during an ultra-endurance exercise and following recovery. Nine male ultra-endurance trained athletes participated in a 24-h standardized endurance trial with controlled energy intake. The participants performed 12 sessions of running, kayaking and cycling (4 x each discipline). Blood samples were collected before, during and after exercise, as well as after 28 h of recovery. Muscle biopsies were taken 1 week before the test and after exercise, as well as after 28 h of recovery. During the 24-h exercise, plasma levels of branched-chain (BCAA), essential amino acids (EAA) and glutamine fell 13%, 14% and 19% (P<0.05) respectively, whereas their concentrations in muscle were unaltered. Simultaneously, tyrosine and phenylalanine levels rose 38% and 50% (P<0.05) in the plasma and 66% and 46% (P<0.05) in muscle, respectively. After the 24-h exercise, plasma levels of BCAA were positively correlated with muscle levels of glycogen (r2=0.73, P<0.05), as was the combined concentrations of muscle tyrosine and phenylalanine with plasma creatine kinase (r2=0.55, P<0.05). Following 28-h of recovery, plasma and muscle levels of amino acids had either returned to their initial levels or were elevated. In conclusion, ultra-endurance exercise caused significant changes elevations in plasma and muscle levels of tyrosine and phenylalanine, which suggest an increase in net muscle protein breakdown during exercise. There was a reduction in plasma concentrations of EAA and glutamine during exercise, whereas no changes were detected in their muscle concentration after exercise.

  • 35. Burke, L M
    et al.
    Castell, L M
    Stear, S J
    Rogers, P J
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Gurr, S
    Mitchell, N
    Stephens, F B
    Greenhaff, P L
    BJSM reviews: A-Z of nutritional supplements2009In: British Journal of Sports Medicine, ISSN 0306-3674, E-ISSN 1473-0480, Vol. 43, no 14, p. 1088-90Article in journal (Other academic)
  • 36.
    Cardinale, Daniele A
    et al.
    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. Elite Performance Centre, Bosön.
    Gejl, Kasper D
    University of Southern Denmark.
    Ørtenblad, Niels
    University of Southern Denmark.
    Ekblom, Bjorn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom'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.
    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.
    Reliability of maximal mitochondrial oxidative phosphorylation in permeabilized fibers from the vastus lateralis employing high-resolution respirometry.2018In: Physiological Reports, E-ISSN 2051-817X, Vol. 6, no 4, article id e13611Article in journal (Refereed)
    Abstract [en]

    The purpose was to assess the impact of various factors on methodological errors associated with measurement of maximal oxidative phosphorylation (OXPHOS) in human skeletal muscle determined by high-resolution respirometry in saponin-permeabilized fibers. Biopsies were collected from 25 men to assess differences in OXPHOS between two muscle bundles and to assess the correlation between OXPHOS and the wet weight of the muscle bundle. Biopsies from left and right thighs of another five subjects were collected on two occasions to compare limbs and time-points. A single muscle specimen was used to assess effects of the anesthetic carbocaine and the influence of technician. The difference in OXPHOS between two fiber-bundles from the same biopsy exhibited a standard error of measurement (SEM) of 10.5 pmol · s-1  · mg-1 and a coefficient of variation (CV) of 15.2%. The differences between left and right thighs and between two different time-points had SEMs of 9.4 and 15.2 pmol · s-1  · mg-1 and CVs of 23.9% and 33.1%, respectively. The average (±SD) values obtained by two technicians monitoring different bundles of fibers from the same biopsy were 31.3 ± 7.1 and 26.3 ± 8.1 pmol · s-1  · mg-1 . The time that elapsed after collection of the biopsy (up to a least 5 h in preservation medium), wet weight of the bundle (from 0.5 to 4.5 mg) and presence of an anesthetic did not influence OXPHOS. The major source of variation in OXPHOS measurements is the sample preparation. The thigh involved, time-point of collection, size of fiber bundles, and time that elapsed after biopsy had minor or no effect.

  • 37.
    Edman, Sebastian
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology.
    Söderlund, Karin
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Björn Ekblom'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.
    Anabolic signalling in individual muscle fibres following resistance exercise in combination with amino acid intake: PO-2602018In: Exercise Biochemistry Review: Vol 1 No 5 (2018): Proceedings of IBEC 2018, Beijing, China (PO-201 -> PO-308), 2018Conference paper (Other academic)
    Abstract [en]

    Objective Human muscle consists of a mixture of fibres with different contractile and metabolic properties, type I (slow-twitch) and type II (fast-twitch) fibres. Little is known about the effect of anabolic stimuli, in particular nutrition, on the molecular response in the different fibre types. Here, we examine the effect of resistance exercise and essential amino acid (EAA) supplementation on mTOR signalling in individual type I and type II human muscle fibres.

    Methods Five strength-trained male subjects performed two sessions of leg press exercise (10 x 10 repetition at 62-85 % of 1RM). During exercise and recovery, the subjects ingested an aqueous solution with EAA (290 mg/kg) or flavoured water (placebo). Muscle biopsies were taken from the vastus lateralis before and 90 min after exercise. The biopsies were freeze-dried and single fibres dissected out and weighed (range 0.9 – 8 ug). The fibres were individually homogenized and analysed for proteins in the mTOR pathway using Western blot. Membranes were repeatedly stripped and fibres were identified as type I or type II following incubation with antibodies against the different myosin isoforms.

    Results Exercise led to a significant increase in mTOR and p70S6k1 phosphorylation and a fall in eEF2 phosphorylation, similar in both fibre types. There was a large variation between individual fibres; some fibres were highly activated whereas others were not activated at all despite the heavy exercise performed. Intake of EAA caused a 2- to 6-fold higher increase in mTOR and p70S6k1 phosphorylation in both type I and type II fibres as compared to intake of placebo, with no difference between the fibre types. The phosphorylation of eEF2 was not affected by intake of EAA. The total expression of p70S6k1 and eEF2 was 145% and 155% higher in type II than in type I fibres (P<0.05), respectively, whereas no difference between the fibre types was observed for mTOR protein.

    Conclusions The response to heavy resistance exercise regarding mTOR signalling was similar in type I and type II fibres in trained subjects, but with a large variation between single fibres of both types. Furthermore, ingestion of EAA enhanced the effect of resistance exercise on phosphorylation of mTOR and p70S6k1 in both fibre types.

  • 38.
    Eliasson, Jörgen
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Elfegoun, Thibault
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Nilsson, Johnny
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Köhnke, Rickard
    Ekblom, Björn
    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.
    Maximal lengthening contractions increase p70 S6 kinase phosphorylation in human skeletal muscle in the absence of nutritional supply.2006In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 291, no 6, p. 1197-1205Article in journal (Refereed)
    Abstract [en]

    The aim of this study was to compare the training stimuli of eccentric (lengthening) and concentric (shortening) contractions regarding the effect on signaling enzymes involved in protein synthesis. Ten male subjects performed 4 x 6 maximal eccentric contractions on one leg followed by 4 x 6 maximal concentric contractions on the other. Six additional subjects performed the same protocol, but with maximal concentric and submaximal eccentric exercise of equal force to that of the maximal concentric contractions. Muscle biopsy samples were taken from the vastus lateralis before, immediately after, and 1 and 2 h after exercise in both legs. The average peak force produced during the maximal eccentric exercise was 31% higher than during the maximal concentric exercise, 2,490 (+/-100) vs. 1,894 (+/-108) N (P < 0.05). The maximal eccentric contractions led to two- to eightfold increases in the phosphorylation of p70 S6 kinase (p70(S6k)) and the ribosomal protein S6 that persisted for 2 h into recovery but no significant changes in phosphorylation of Akt or mammalian target of rapamycin (mTOR). Maximal concentric and submaximal eccentric contractions did not induce any significant changes in Akt, mTOR, p70(S6k), or S6 phosphorylation up to 2 h after the exercise. The results indicate that one session of maximal eccentric contractions activates p70(S6k) in human muscle via an Akt-independent pathway and suggest that maximal eccentric contractions are more effective than maximal concentric contractions in stimulating protein synthesis in the absence of a nutritional intake, an effect that may be mediated through a combination of greater tension and stretching of the muscle.

  • 39.
    Esbjörnsson, M
    et al.
    Karolinska Institutet.
    Rundqvist, H C
    Karolinska Institutet.
    Mascher, H
    Karolinska Institutet.
    Österlund, T
    Karolinska Institutet.
    Rooyackers, O
    Karolinska Institutet.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Jansson, E
    Karolinska Institutet.
    Sprint exercise enhances skeletal muscle p70S6k phosphorylation and more so in women than in men.2012In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 205, no 3, p. 411-22Article in journal (Refereed)
    Abstract [en]

    AIM: Sprint exercise is characterized by repeated sessions of brief intermittent exercise at a high relative workload. However, little is known about the effect on mTOR pathway, an important link in the regulation of muscle protein synthesis. An earlier training study showed a greater increase in muscle fibre cross-sectional area in women than men. Therefore, we tested the hypothesis that the activation of mTOR signalling is more pronounced in women than in men. Healthy men (n=9) and women (n=8) performed three bouts of 30-s sprint exercise with 20-min rest in between.

    METHODS: Multiple blood samples were collected over time, and muscle biopsy specimens were obtained at rest and 140 min after the last sprint.

    RESULTS: Serum insulin increased by sprint exercise and more so in women than in men [gender (g) × time (t)]: P=0.04. In skeletal muscle, phosphorylation of Akt increased by 50% (t, P=0.001) and mTOR by 120% (t, P=0.002) independent of gender. The elevation in p70S6k phosphorylation was larger in women (g × t, P=0.03) and averaged 230% (P=0.006) as compared to 60% in men (P=0.04). Phosphorylation rpS6 increased by 660% over time independent of gender (t, P=0.003). Increase in the phosphorylation of p70S6k was directly related to increase in serum insulin (r=0.68, P=0.004).

    CONCLUSION: It is concluded that repeated 30-s all-out bouts of sprint exercise separated by 20 min of rest increases Akt/mTOR signalling in skeletal muscle. Secondly, signalling downstream of mTOR was stronger in women than in men after sprint exercise indicated by the increased phosphorylation of p70S6k.

  • 40. Essén-Gustavsson, Birgitta
    et al.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Effect of exercise on concentrations of free amino acids in pools of type I and type II fibres in human muscle with reduced glycogen stores.2002In: Acta Physiologica Scandinavica, ISSN 0001-6772, E-ISSN 1365-201X, Vol. 174, no 3, p. 275-81Article in journal (Refereed)
    Abstract [en]

    A few animal studies have shown that some amino acid concentrations vary between different muscle fibre types. In the present study, amino acid concentrations were measured in separate pools of different fibre types in human skeletal muscle, with reduced glycogen stores, before and after sustained exercise. Five subjects exercised at a submaximal work rate for 60 min and then at a maximal rate for 20 min. Biopsy samples were taken from the vastus lateralis muscle before and after exercise; they were freeze-dried and individual fibres were dissected out. Fragments of these fibres were stained for myosin-adenosine triphosphatase (ATPase) and identified as type I or type II fibres. The concentrations of free amino acids were measured by high performance liquid chromatography (HPLC) in perchloric acid (PCA) extracts containing pools of either type of fibre. After exercise, glycogen was decreased in type I fibres (53%) and in four subjects also in type II fibres. The concentrations of most amino acids were similar in the two fibre types before exercise, but the glutamate, aspartate and arginine levels were 10% higher in type II than in type I fibres. After exercise, the glutamate concentration was decreased by 45% in both fibre types and the branched-chain amino acids (BCAA) were decreased in type II fibres (14%). Exercise caused an increase by 25-30% in tyrosine concentration in both type I and type II fibres. The results show that amino acids can be measured in pools of fibre fragments and suggest that amino acid metabolism play an important role in both type I and type II fibres during exercise.

  • 41. Hassmén, Peter
    et al.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Mood change and marathon running: a pilot study using a Swedish version of the POMS test.1991In: Scandinavian Journal of Psychology, ISSN 0036-5564, E-ISSN 1467-9450, Vol. 32, no 3, p. 225-32Article in journal (Refereed)
    Abstract [en]

    Regular exercise is said to have positive effects on mood, especially if the exercise intensity is low to moderate. However, the acute effects resulting from participation in a strenuous competition, such as a marathon race, have been studied less. The present investigation used the Profile of Mood States (POMS) test to measure mood, before and after the 1989 Stockholm Marathon. A total of 106 male runners (mean age 40.0 years), with finishing times between 3h and 3h 45 min participated as subjects. Results showed great changes between pre- and post-marathon scores, most of them significant at the p less than 0.001 level. Furthermore, differences between a faster and a slower group of runners were demonstrated with regard to mood states, even though plasma glucose levels were comparable. It is concluded that participation in a marathon race greatly effects mood, mainly in a more negative way than low to moderately intense exercise does.

  • 42.
    Hassmén, Peter
    et al.
    Stockholms universitet.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Newsholme, E A
    Branched-chain amino acid supplementation during 30-km competitive run: mood and cognitive performance.1994In: Nutrition (Burbank, Los Angeles County, Calif.), ISSN 0899-9007, E-ISSN 1873-1244, Vol. 10, no 5, p. 405-10Article in journal (Refereed)
    Abstract [en]

    It has been suggested that an elevated concentration of the neurotransmitter serotonin (5-hydroxytryptamine, 5-HT) in specific areas of the brain may contribute to the development of central/mental fatigue during and after sustained exercise. Supplementation with branched-chain amino acids (BCAAs) should prevent the exercise-induced increase in the plasma concentration ratio of free tryptophan to other large neutral amino acids (including BCAAs) and thereby prevent an elevation in the level of 5-HT in the brain. In this study, subjects were given either a mixture of BCAAs in a carbohydrate solution or a placebo drink that contained only carbohydrates during a 30-km cross-country race. Several tasks to measure cognitive performance were performed before and after the race. When subjects were supplied with BCAAs, their performance in the different parts of the color-word test (words, colors and color words) was improved by an average of 3-7% (p < 0.05) after exercise, whereas there was no difference in performance before and after exercise in the subjects who were given the placebo. Furthermore, the experimental group, supplied with BCAAs, maintained their performance in the shape-rotation and figure-identification tasks, whereas an impairment in performance in these tests by 25% (p < 0.05) and 15% (p < 0.05), respectively, was found in the subjects who received the placebo. Thus, BCAA supplementation seemed to have an effect on the more complex tasks, whereas no effect could be detected on the less demanding tasks. However, an intake of BCAAs during exercise modified only slightly the exercise-induced changes in mood.

  • 43. Karlsson, Håkan K R
    et al.
    Nilsson, Per-Anders
    Nilsson, Johnny
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Laboratory for Biomechanics and Motor Control.
    Chibalin, Alexander V
    Zierath, Juleen R
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise.2004In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 287, no 1, p. E1-7Article in journal (Refereed)
    Abstract [en]

    The aim of the study was to investigate the effect of resistance exercise alone or in combination with oral intake of branched-chain amino acids (BCAA) on phosphorylation of the 70-kDa S6 protein kinase (p70(S6k)) and mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase (ERK1/2), and p38 MAPK in skeletal muscle. Seven male subjects performed one session of quadriceps muscle resistance training (4 x 10 repetitions at 80% of one repetition maximum) on two occasions. In a randomized order, double-blind, crossover test, subjects ingested a solution of BCAA or placebo during and after exercise. Ingestion of BCAA increased plasma concentrations of isoleucine, leucine, and valine during exercise and throughout recovery after exercise (2 h postexercise), whereas no change was noted after the placebo trial. Resistance exercise led to a robust increase in p70(S6k) phosphorylation at Ser(424) and/or Thr(421), which persisted 1 and 2 h after exercise. BCAA ingestion further enhanced p70(S6k) phosphorylation 3.5-fold during recovery. p70(S6k) phosphorylation at Thr(389) was unaltered directly after resistance exercise. However, during recovery, Thr(389) phosphorylation was profoundly increased, but only during the BCAA trial. Furthermore, phosphorylation of the ribosomal protein S6 was also increased in the recovery period only during the BCAA trial. Exercise led to a marked increase in ERK1/2 and p38 MAPK phosphorylation, which was completely suppressed upon recovery and unaltered by BCAA. In conclusion, BCAA, ingested during and after resistance exercise, mediate signal transduction through p70(S6k) in skeletal muscle.

  • 44. 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, ISSN 1932-6203, 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.

  • 45.
    Marcus, Moberg
    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.
    van Hall, Gerrit
    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.
    Lower body endurance exercise acutely affects resistance exercise induced transcriptional and translational signalling in the tricpes brachii muscleManuscript (preprint) (Other academic)
  • 46.
    Mascher, Henrik
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Andersson, H
    Nilsson, P-A
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Changes in signalling pathways regulating protein synthesis in human muscle in the recovery period after endurance exercise.2007In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 191, no 1, p. 67-75Article in journal (Refereed)
    Abstract [en]

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

  • 47.
    Mascher, Henrik
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Rooyackers, Olav
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Enhanced rates of muscle protein synthesis and elevated mTOR signalling following endurance exercise in human subjects.2011In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 202, no 2, p. 175-84Article in journal (Refereed)
    Abstract [en]

    AIM: The major aim of this study was to determine the fractional rate of protein synthesis (FSR) during the early period of recovery after intensive aerobic exercise in the absence of nutritional supplementation.

    METHODS: Sixteen male subjects performed one-legged cycling exercise for 1 h at approx. 65-70% of their one-legged maximal oxygen uptake. Using the stable isotope technique, the FSR in the vastus lateralis of both legs were determined during two periods, 0-90 min (n = 8) and 90-180 min (n = 8) after exercise. Biopsies were taken from both exercising and resting muscle before exercise, immediately after and following 90 or 180 min of recovery.

    RESULTS: During the initial 90 min of recovery, FSR in the exercising muscle tended to be higher than in the resting muscle (1.57 ± 0.12 vs. 1.44 ± 0.07% 24 h(-1); P = 0.1) and was significantly higher during the period 90-180 min after exercise (1.74 ± 0.14 vs. 1.43 ± 0.12% 24 h(-1) ; P < 0.05). Exercise induced a 60% increase (P < 0.05) in phosphorylation of mTOR and a fivefold increase (P < 0.05) in Thr(389) phosphorylation of p70S6 kinase as well as a 30% reduction (P < 0.05) in phosphorylation of eEF2. Phosphorylation of AMP-activated protein kinase was enhanced by 40% (P < 0.05) after exercise, but no significant effect on phosphorylation of Akt, or eIF2Bε was observed immediately after exercise.

    CONCLUSION: These findings indicate that during the first 3 h of recovery after intensive endurance exercise FSR gradually increases. Moreover, a stimulation of the mTOR-signalling pathway may be at least partially responsible for this elevated protein synthesis.

  • 48.
    Mascher, Henrik
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Tannerstedt, Jörgen
    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.
    Nya aspekter på aminosyrors roll i den muskulära anpassningen till träning2006In: Svensk Idrottsforskning: Organ för Centrum för Idrottsforskning, ISSN 1103-4629, Vol. 15, no 3, p. 56-60Article in journal (Other academic)
    Abstract [sv]

    Sammanfattningsvis kan sägas att tillgängligheten av protein/aminosyror är nödvändig för den muskulära anpassningen till träning vid både styrke- och uthållighetsträning. Betydligt fler studier har undersökt effekterna på styrketräning, men vid båda typer av träning är dock kunskaperna om de bakomliggande mekanismerna ännu så länge små. Genom den omfattande forskning som pågår inom området kommer med all säkerhet de molekylära och cellulära förändringar som sker i samband med träning att kartläggas inom en relativt snar framtid. Därmed öppnas nya möjligheter att förbättra och optimera träningen, t.ex. genom kombination av olika typer av aktiviteter (uthållighet och styrketräning). Denna kunskap är också avgörande för att förstå och eventuellt kunna påverka träningseffekten genom förändringar i nutritionens sammansättning.

  • 49.
    Mascher, Henrik
    et al.
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Tannerstedt, Jörgen
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Brink-Elfegoun, Thibault
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences.
    Ekblom, Björn
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Björn Ekblom's research group.
    Gustafsson, Thomas
    Blomstrand, Eva
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Eva Blomstrand's research group.
    Repeated resistance exercise training induces different changes in mRNA expression of MAFbx and MuRF-1 in human skeletal muscle.2008In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 294, no 1, p. E43-51Article in journal (Refereed)
    Abstract [en]

    The gain in muscle mass as a result of resistance training is dependent on changes in both anabolic and catabolic reactions. A frequency of two to three exercise sessions per week is considered optimal for muscle gain in untrained individuals. Our hypothesis was that a second exercise session would enlarge the anabolic response and/or decrease the catabolic response. Eight male subjects performed resistance exercise on two occasions separated by 2 days. Muscle biopsies were taken from the vastus lateralis before and 15 min, 1 h, and 2 h after exercise. Exercise led to severalfold increases in phosphorylation of mTOR at Ser2448, p70 S6 kinase (p70S6k) at Ser424/Thr421 and Thr389, and ribosomal protein S6, which persisted for up to 2 h of recovery on both occasions. There was a tendency toward a larger effect of the second exercise on p70S6k and S6, but the difference did not reach statistical significance. The mRNA expression of MuRF-1, which increased after exercise, was 30% lower after the second exercise session than after the first one. MAFbx expression was not altered after exercise but downregulated 30% 48 h later, whereas myostatin expression was reduced by 45% after the first exercise and remained low until after the second exercise session. The results indicate that 1) changes in expression of genes involved in protein degradation are attenuated as a response to repetitive resistance training with minor additional increases in enzymes regulating protein synthesis and 2) the two ubiquitin ligases, MuRF-1 and MAFbx, are differently affected by the exercise as well as by repeated exercise.

  • 50.
    Moberg, Marcus
    Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Åstrand Laboratory of Work Physiology, Eva Blomstrand's research group.
    Effects of exercise and amino acid intake on mechanisms regulating protein synthesis and breakdown in human muscle2016Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

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

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

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

     

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