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  • 1.
    Apro, William
    et al.
    Swedish School of Sport & Health Sciences, Stockholm, Sweden.
    Moberg, Marcus
    Swedish School of Sport & Health Sciences, Stockholm, Sweden.
    Hamilton, D. Lee
    University of Stirling, Scotland.
    Ekblom, Bjorn
    Swedish School of Sport & Health Sciences, Stockholm, Sweden.
    Rooyackers, Olav
    Karolinska Inst, Dept Clin Sci Intervent & Technol, Stockholm, Sweden .
    Holmberg, Hans-Christer
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Blomstrand, Eva
    Swedish Sch Sport & Hlth Sci, Astrand Lab, SE-11486 Stockholm, Sweden ; Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden.
    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 exercise2015In: 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 (EAAs). Nine male subjects performed resistance exercise on 4 occasions and were randomly supplied EAAs with leucine, EAAs 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 similar to 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 EAAs and does not appear to be caused by alterations inmTORC1 assembly.

  • 2.
    Apró, William
    et al.
    Swedish Sch Sport & Hlth Sci, Stockholm, Sweden.
    Holmberg, Hans-Christer
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Rooyackers, Olav
    Karolinska Univ Hosp, Huddinge, Sweden.
    Blomstrand, Eva
    Swedish Sch Sport & Hlth Sci, Stockholm, Sweden.
    Is leucine induced p70S6 kinase phosphorylation following resistance exercise dependent on elevated phenylalanine levels in human skeletal muscle?2010In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 24, p. lb273-Article in journal (Refereed)
    Abstract [en]

    The purpose of this study was to investigate the specific role of

    leucine in the stimulation of the mammalian target of rapamycin

    signalling pathway. Six male subjects performed four heavy

    resistance exercise sessions, each separated by approximately one

    week. Subjects were randomly supplemented with one of four

    drinks: placebo (flavored water), leucine or essential amino acids

    (EAA) with and without leucine. Immediately following each

    exercise session, four subjects were infused with a flooding dose of

    L-[2H5] phenylalanine (Inf) while two subjects served as controls

    (Ctrl). Muscle biopsies were taken before and one hour after

    exercise. In the Ctrl group, resistance exercise resulted in a

    substantial increase (45-fold) in p70 kinase phosphorylation

    when all EAA were ingested, whereas ingestion of leucine alone

    had no greater effect than that of placebo. In the Inf group,

    however, ingestion of leucine alone and EAA increased p70

    phosphorylation to a similar extent (35-fold). The divergent

    signalling response in the two groups suggests that leucine alone is

    insufficient to increase p70

    phosphorylation. Indeed, in the Inf

    group, there was a strong correlation (r=0.91) between

    p70 phosphorylation and the product of muscle leucine and

    phenylalanine levels. These results suggest that the stimulatory

    effect of leucine on p70 phosphorylation is dependent on

    elevated muscle phenylalanine levels. Supported by the Swedish

    National Centre for Research in Sports

     

  • 3.
    Cotter, Joshua Allan
    et al.
    Univ Calif Irvine, Irvine, CA USA .
    Haddad, Fadia
    Univ Calif Irvine, Irvine, CA USA .
    Yu, Alvin M.
    Univ Calif Irvine, Irvine, CA USA .
    Hoang, Theresa N.
    Univ Calif Irvine, Irvine, CA USA .
    Kreitenberg, Arthur
    Univ Calif Irvine, Irvine, CA USA .
    Baker, Michael J.
    Univ Calif Irvine, Irvine, CA USA .
    Tesch, Per A.
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Baldwin, Kenneth M.
    Univ Calif Irvine, Irvine, CA USA .
    Caiozzo, Vincent J.
    Univ Calif Irvine, Irvine, CA USA .
    Adams, Gregory R.
    Univ Calif Irvine, Irvine, CA USA .
    Influence of 10 days of unilateral lower limb suspension and combined exercise training on human vastus lateralis and soleus muscles2012In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 26Article in journal (Other academic)
  • 4.
    Larsen, Filip J.
    et al.
    Swedish Sch Sport & Hlth Sci, Stockholm, Sweden.
    Schiffer, Tomas A.
    Karolinska Inst, Dept Physiol & Pharmacol, SE-17177 Stockholm, Sweden.
    Örtenblad, Niels
    Univ Southern Denmark, Inst Sports Sci & Clin Biomech, Muscle Res Cluster, Odense, Denmark.
    Zinner, Christoph
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences. Univ Wurzburg, Dept Sport Sci, D-97070 Wurzburg, Germany.
    Morales-Alamo, David
    Res Inst Biomed & Hlth Sci IUIBS, Las Palmas Gran Canaria, Canary Islands, Spain.
    Willis, Sarah J.
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Calbet, Jose A.
    Res Inst Biomed & Hlth Sci IUIBS, Las Palmas Gran Canaria, Canary Islands, Spain.
    Holmberg, Hans-Christer
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Boushel, Robert
    Univ British Columbia, Sch Kinesiol, Vancouver, BC V5Z 1M9, Canada.
    High-intensity sprint training inhibits mitochondrial respiration through aconitase inactivation2016In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 30, no 1, p. 417-427Article in journal (Refereed)
    Abstract [en]

    Intense exercise training is a powerful stimulus that activates mitochondrial biogenesis pathways and thus increases mitochondrial density and oxidative capacity. Moderate levels of reactive oxygen species (ROS) during exercise are considered vital in the adaptive response, but high ROS production is a serious threat to cellular homeostasis. Although biochemical markers of the transition from adaptive to maladaptive ROS stress are lacking, it is likely mediated by redox sensitive enzymes involved in oxidative metabolism. One potential enzyme mediating such redox sensitivity is the citric acid cycle enzyme aconitase. In this study, we examined biopsy specimens of vastus lateralis and triceps brachii in healthy volunteers, together with primary human myotubes. An intense exercise regimen inactivated aconitase by 55-72%, resulting in inhibition of mitochondrial respiration by 50-65%. In the vastus, the mitochondrial dysfunction was compensated for by a 15-72% increase in mitochondrial proteins, whereas H2O2 emission was unchanged. In parallel with the inactivation of aconitase, the intermediary metabolite citrate accumulated and played an integral part in cellular protection against oxidative stress. In contrast, the triceps failed to increase mitochondrial density, and citrate did not accumulate. Instead, mitochondrial H2O2 emission was decreased to 40% of the pretraining levels, together with a 6-fold increase in protein abundance of catalase. In this study, a novel mitochondrial stress response was highlighted where accumulation of citrate acted to preserve the redox status of the cell during periods of intense exercise.

  • 5.
    Owerkowicz, T
    et al.
    Univ Calif Irvine, Irvine, CA USA.
    Cotter, J A
    Univ Calif Irvine, Irvine, CA USA.
    Tesch, Per A
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Caiozzo, V J
    Univ Calif Irvine, Irvine, CA USA.
    Adams, G R
    Univ Calif Irvine, Irvine, CA USA.
    Gravity-independent flywheel exercise training improves aerobic capacity and muscle strength in ambulatory subjects2011In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 25Article in journal (Refereed)
  • 6. Scheele, Camilla
    et al.
    Nielsen, Anders Rinnov
    Waldén, Tomas B.
    Sewell, Dean A.
    Fischer, Christian P
    Brogan, Robert J.
    Petrovic, Natasa
    Larsson, Ola
    Tesch, Per A
    Mid Sweden University, Faculty of Human Sciences, Department of Health Sciences.
    Wennmalm, Kristian
    Hutchinson, Dana S
    Cannon, Barbara
    Wahlestedt, Claes
    Pedersen, Bente K
    Timmons, James A
    Altered regulation of the PINK1 locus: a link between Type 2 diabetes and neurodegeneration?2007In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 21, no 13, p. 3653-3665Article in journal (Refereed)
    Abstract [en]

    Mutations in PINK1 cause the mitochondrial-related neurodegenerative disease Parkinson’s. Here we investigate whether obesity, type 2 diabetes, or inactivity alters transcription from the PINK1 locus. We utilized a cDNA-array and quantitative real-time PCR for gene expression analysis of muscle from healthy volunteers following physical inactivity, and muscle and adipose tissue from nonobese or obese subjects with normal glucose tolerance or type 2 diabetes. Functional studies of PINK1 were performed utilizing RNA interference in cell culture models. Following inactivity, the PINK1 locus had an opposing regulation pattern (PINK1 was down-regulated while natural antisense PINK1 was up-regulated). In type 2 diabetes skeletal muscle, all transcripts from the PINK1 locus were suppressed and gene expression correlated with diabetes status. RNA interference of PINK1 in human neuronal cell lines impaired basal glucose uptake. In adipose tissue, mitochondrial gene expression correlated with PINK1 expression although remained unaltered following siRNA knockdown of Pink1 in primary cultures of brown preadipocytes. In conclusion, regulation of the PINK1 locus, previously linked to neurodegenerative disease, is altered in obesity, type 2 diabetes and inactivity, while the combination of RNAi experiments and clinical data suggests a role for PINK1 in cell energetics rather than in mitochondrial biogenesis.

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