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Publications (10 of 25) Show all publications
Nilsson, L., Flockhart, M., Apro, W., Ekblom, B. & Larsen, F. J. (2019). Biphasic relationship between training load and glucose tolerance. In: : . Paper presented at Cell Symposia, Exercise Metabolism. May 5-7 2019, Sitges Spain.
Open this publication in new window or tab >>Biphasic relationship between training load and glucose tolerance
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2019 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [sv]

Biphasic relationship between training load and glucose tolerance

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

 

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

National Category
Cell Biology
Research subject
Medicine/Technology; Medicine/Technology; Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-5933 (URN)
Conference
Cell Symposia, Exercise Metabolism. May 5-7 2019, Sitges Spain
Funder
Swedish National Centre for Research in Sports
Available from: 2019-11-29 Created: 2019-11-29 Last updated: 2019-12-09Bibliographically approved
Flockhart, M., Nilsson, L., Apro, W., Ekblom, B. & Larsen, F. J. (2019). Dose-response relationship between exercise load and mitochondrial function. In: : . Paper presented at Cell Symposia: Exercise Metabolism, May 5-7 2019, Sitges Spain.
Open this publication in new window or tab >>Dose-response relationship between exercise load and mitochondrial function
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2019 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [en]

Dose-response relationship between exercise load and mitochondrial function

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

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

National Category
Cell Biology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-5932 (URN)
Conference
Cell Symposia: Exercise Metabolism, May 5-7 2019, Sitges Spain
Funder
Swedish National Centre for Research in Sports
Available from: 2019-11-29 Created: 2019-11-29 Last updated: 2019-12-09Bibliographically approved
Edman, S., Söderlund, K., Moberg, M., Apro, W. & Blomstrand, E. (2019). mTORC1 Signaling in Individual Human Muscle Fibers Following Resistance Exercise in Combination With Intake of Essential Amino Acids. Frontiers in nutrition, 6, Article ID 96.
Open this publication in new window or tab >>mTORC1 Signaling in Individual Human Muscle Fibers Following Resistance Exercise in Combination With Intake of Essential Amino Acids
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2019 (English)In: Frontiers in nutrition, ISSN 2296-861X, Vol. 6, article id 96Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
Frontiers Media S.A., 2019
Keywords
muscle fiber type, protein expression, S6K1, single muscle fiber, EAA
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-5807 (URN)10.3389/fnut.2019.00096 (DOI)000472610200002 ()31294029 (PubMedID)
Available from: 2019-08-14 Created: 2019-08-14 Last updated: 2019-12-05
Blomstrand, E. & Apro, W. (2018). Det viktigaste du behöver veta om protein och träning. Idrottsforskning.se, Article ID 30 maj.
Open this publication in new window or tab >>Det viktigaste du behöver veta om protein och träning
2018 (Swedish)In: Idrottsforskning.se, ISSN 2002-3944, article id 30 majArticle in journal (Other (popular science, discussion, etc.)) Published
Place, publisher, year, edition, pages
Stockholm: Centrum för idrottsforskning, CIF, 2018
National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-5443 (URN)
Available from: 2018-10-16 Created: 2018-10-16 Last updated: 2018-10-17Bibliographically approved
Rundqvist, H. C., Esbjörnsson, M., Rooyackers, O., Apro, W., Moberg, M., Österlund, T. & Jansson, E. (2016). Amino Acid Transport after Sprint Exercise and Oral Amino Acids: 90 Board #6 June 1, 9. In: Medicine & Science in Sports & Exercise: Volume 48(5S) Supplement 1, May 2016, p 5: . Paper presented at American College of Sports Medicine (ACSM) 63rd Annual Meeting, May 31-June 4 2016, Boston (pp. 5). , 48(5 Suppl 1)
Open this publication in new window or tab >>Amino Acid Transport after Sprint Exercise and Oral Amino Acids: 90 Board #6 June 1, 9
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2016 (English)In: Medicine & Science in Sports & Exercise: Volume 48(5S) Supplement 1, May 2016, p 5, 2016, Vol. 48, no 5 Suppl 1, p. 5-Conference paper, Published paper (Other academic)
Abstract [en]

PURPOSE: To study if oral ingestion of essential amino acids (oral EAA) increases the amino acid transporter SNAT2, Akt/mTOR signaling and muscle protein synthesis (MPS) after sprint exercise.

METHODS: 12 healthy subjects performed three 30-s sprints with 20 minutes rest in between. Subjects consumed EAA + maltodextrin solution or flavoured water (placebo) during the sprint exercise up to 15 min after the last sprint in a randomized order with one month interval. In vivo MPS rate was measured using a stable isotope technique. Subject received a stable isotope of phenylalanine (D5-phenylalanine) to label the precursor pool for protein synthesis. Continuous infusion started before the first sprint and was ended 200 min after the last sprint. Two post exercise biopsies (vastus lateralis) were obtained 80 min and 200 min after last sprint. The amount of labelled phenylalanine incorporated into muscle protein over these 2 hours represents the in vivo MPS rate and was expressed as fractional synthesis rate (FSR %) calculated by dividing amount of labelled phenylalanine incorporated during these 2 hours by the amount in the free amino acid (precursor) plasma pool. Biopsies were also analyzed for Akt/mTOR signaling and SNAT2 amino acid transporter by Western blot and for SNAT2 gene expression by real-time PCR. Blood samples were analyzed for amino acids, glucose, lactate, and insulin. Four subjects, involuntary vomiting after exercise during EAA condition, showed a minor increase in plasma leucine and were presented separately.

RESULTS: Non-vomiting subjects (n=8): The expression of the amino acid transporter SNAT2 was higher both at the protein (P<0.05) and the mRNA (P<0.001) level after EEA than after placebo. Fold increase for phosphorylated Akt, mTOR and p70 was 1.7-3.6 (P<0.01 - P<0.001) comparing EAA with placebo. FSR % after EEA was increased by 25 % (P=0.02) compared to placebo. None of these variables were significantly increased in the subjects who vomited.

CONCLUSION: Oral EAA increased MPS after sprint exercise. Enhanced capacity for amino acid transport and subsequent enhanced Akt/mTOR signaling are suggested to mediate the increased MPS.

National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-4566 (URN)10.1249/01.mss.0000485021.31770.d3 (DOI)27584180 (PubMedID)
Conference
American College of Sports Medicine (ACSM) 63rd Annual Meeting, May 31-June 4 2016, Boston
Available from: 2016-09-15 Created: 2016-09-15 Last updated: 2016-09-16Bibliographically approved
Apró, W., Moberg, M., Holmberg, H.-C. & Blomstrand, E. (2016). 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.. In: Medicine And Science In Sports And Exercise 2016 May; Vol. 48 (5S Suppl 1), pp. 17.: (pp. 17-17). , 48(5S Suppl 1)
Open this publication in new window or tab >>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.
2016 (English)In: 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, Published 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.

National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-4514 (URN)
Available from: 2016-08-05 Created: 2016-08-05 Last updated: 2016-08-08Bibliographically approved
Kazior, Z., Willis, S. J., Moberg, M., Apró, W., Calbet, J. A., Holmberg, H.-C. & Blomstrand, E. (2016). Endurance Exercise Enhances the Effect of Strength Training on Muscle Fiber Size and Protein Expression of Akt and mTOR.. PLoS ONE, 11(2), Article ID e0149082.
Open this publication in new window or tab >>Endurance Exercise Enhances the Effect of Strength Training on Muscle Fiber Size and Protein Expression of Akt and mTOR.
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2016 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 11, no 2, article id e0149082Article in journal (Refereed) Published
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.

National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-4363 (URN)10.1371/journal.pone.0149082 (DOI)000371218400061 ()26885978 (PubMedID)
Available from: 2016-02-24 Created: 2016-02-24 Last updated: 2017-11-30Bibliographically approved
Apro, W., Moberg, M., Ekblom, B., Holmberg, H.-C. & Blomstrand, E. (2016). High intensity interval cycling performed prior to resistance exercise stimulates autophagy signaling. In: Conference program & abstracts: . Paper presented at 2016 APS Intersociety Meeting. The Integrative Biology of Exercise VII. November 2-4 2016, Phoenix, Arizona. (pp. 84-84).
Open this publication in new window or tab >>High intensity interval cycling performed prior to resistance exercise stimulates autophagy signaling
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2016 (English)In: Conference program & abstracts, 2016, p. 84-84Conference paper, Oral presentation with published abstract (Other academic)
National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-4631 (URN)
Conference
2016 APS Intersociety Meeting. The Integrative Biology of Exercise VII. November 2-4 2016, Phoenix, Arizona.
Available from: 2016-11-08 Created: 2016-11-08 Last updated: 2017-03-31
Samuelsson, H., Moberg, M., Apró, W., Ekblom, B. & Blomstrand, E. (2016). Intake of branched-chain or essential amino acids attenuates the elevation in muscle levels of PGC-1α4 mRNA caused by resistance exercise.. American Journal of Physiology. Endocrinology and Metabolism, 311(1), E246-E251
Open this publication in new window or tab >>Intake of branched-chain or essential amino acids attenuates the elevation in muscle levels of PGC-1α4 mRNA caused by resistance exercise.
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2016 (English)In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 311, no 1, p. E246-E251Article in journal (Refereed) Published
Abstract [en]

The transcriptional co-activator PGC-1α is recognized as the master regulator of mitochondrial biogenesis. However, recently a novel isoform, PGC-1α4 that specifically regulates muscle hypertrophy was discovered. Since stimulation of mTORC1 activity is tightly coupled to hypertrophy, we hypothesized that activation of this pathway would upregulate PGC-1α4. Eight male subjects performed heavy resistance exercise (10 x 8-12 repetitions at ~75% of 1RM in leg press) on four different occasions, ingesting in random order a solution containing essential amino acids (EAA), branched-chain amino acids (BCAA), leucine or flavored water (placebo) during and after the exercise. Biopsies were taken from the vastus lateralis muscle before and immediately after exercise, as well as following 90 and 180 min of recovery. Signaling through mTORC1, as reflected in S6K1 phosphorylation, was stimulated to a greater extent by the EAA and BCAA than the leucine or placebo supplements. Unexpectedly, intake of EAA or BCAA attenuated the stimulatory effect of exercise on PGC-1α4 expression by ~50% (from a 10-fold to 5-fold increase with BCAA and EAA, P<0.05) 3 h after exercise, whereas intake of leucine alone did not reduce this response. The 60% increase (P<0.05) in the level of PGC-1α1 mRNA 90 min after exercise was uninfluenced by amino acid intake. Muscle glycogen levels were reduced and AMPKα2 activity and phosphorylation of p38 MAPK enhanced to the same extent with all four supplements. In conclusion, induction of PGC-1α4 does not appear to regulate the nutritional (BCAA or EAA) mediated activation of mTORC1 in human muscle.

National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-4460 (URN)10.1152/ajpendo.00154.2016 (DOI)000380372000020 ()27245337 (PubMedID)
External cooperation:
Available from: 2016-06-15 Created: 2016-06-15 Last updated: 2017-11-28Bibliographically approved
Apró, W., Moberg, M., Hamilton, D. L., Ekblom, B., Rooyackers, O., Holmberg, H.-C. & Blomstrand, E. (2015). 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.. The FASEB Journal, 29(10), 4358-4373
Open this publication in new window or tab >>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.
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2015 (English)In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 29, no 10, p. 4358-4373Article in journal (Refereed) Published
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.

National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-4132 (URN)10.1096/fj.15-273474 (DOI)000361367300024 ()26169935 (PubMedID)
Available from: 2015-09-14 Created: 2015-09-14 Last updated: 2019-12-05Bibliographically approved
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Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-1942-2919

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