Gymnastik- och idrottshögskolan, GIH

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Publications (10 of 20) Show all publications
Horwath, O., Nordström, F., von Walden, F., Apro, W. & Moberg, M. (2023). Acute hypoxia attenuates resistance exercise-induced ribosome signaling but does not impact satellite cell pool expansion in human skeletal muscle.. The FASEB Journal, 37(3), Article ID e22811.
Open this publication in new window or tab >>Acute hypoxia attenuates resistance exercise-induced ribosome signaling but does not impact satellite cell pool expansion in human skeletal muscle.
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2023 (English)In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 37, no 3, article id e22811Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
John Wiley & Sons, 2023
Keywords
Pax7, muscle fiber, myogenesis, resistance exercise, ribosome biogenesis
National Category
Physiology Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7523 (URN)10.1096/fj.202202065RR (DOI)000936598200001 ()36786723 (PubMedID)
Funder
Swedish National Centre for Research in Sports, D2017- 0012, D2019- 0050, D2019- 0035
Available from: 2023-03-06 Created: 2023-03-06 Last updated: 2023-03-23
Blackwood, S. J., Horwath, O., Moberg, M., Pontén, M., Apro, W., Ekblom, M., . . . Katz, A. (2023). Insulin resistance after a 3-day fast is associated with an increased capacity of skeletal muscle to oxidize lipids.. American Journal of Physiology. Endocrinology and Metabolism, 324(5), E390-E401
Open this publication in new window or tab >>Insulin resistance after a 3-day fast is associated with an increased capacity of skeletal muscle to oxidize lipids.
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2023 (English)In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 324, no 5, p. E390-E401Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
American Physiological Society, 2023
Keywords
glucose tolerance, insulin resistance, mitochondrial respiration, muscle fiber composition, starvation
National Category
Physiology Endocrinology and Diabetes
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7521 (URN)10.1152/ajpendo.00317.2022 (DOI)000974241700002 ()36791323 (PubMedID)
Available from: 2023-03-03 Created: 2023-03-03 Last updated: 2024-01-11
Edman, S., Horwath, O. & Apro, W. (2023). THRIFTY - A High-throughput Single Muscle Fiber Typing Method Based on Immunofluorescence Detection. Bio-protocol, 13(10), Article ID e4678.
Open this publication in new window or tab >>THRIFTY - A High-throughput Single Muscle Fiber Typing Method Based on Immunofluorescence Detection
2023 (English)In: Bio-protocol, E-ISSN 2331-8325, Vol. 13, no 10, article id e4678Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
Bio-protocol, 2023
Keywords
Muscle fiber type, Myosin heavy chain, Fiber type identification, Muscle
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7950 (URN)10.21769/BioProtoc.4678 (DOI)001089324100006 ()37251094 (PubMedID)
Available from: 2023-11-20 Created: 2023-11-20 Last updated: 2023-11-20
Moberg, M., Apro, W., Horwath, O., van Hall, G., Blackwood, S. J. & Katz, A. (2022). Acute normobaric hypoxia blunts contraction-mediated mTORC1- and JNK-signaling in human skeletal muscle.. Acta Physiologica, 234(2), Article ID e13771.
Open this publication in new window or tab >>Acute normobaric hypoxia blunts contraction-mediated mTORC1- and JNK-signaling in human skeletal muscle.
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2022 (English)In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 234, no 2, article id e13771Article in journal (Refereed) Published
Abstract [en]

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

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

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

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

Place, publisher, year, edition, pages
John Wiley & Sons, 2022
Keywords
FSR, Hippo-pathway, Muscle metabolites, deuterium oxide, oxygen
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-6900 (URN)10.1111/apha.13771 (DOI)000744361300001 ()34984845 (PubMedID)
Funder
Swedish National Centre for Research in Sports, D2017--0012
Available from: 2022-01-10 Created: 2022-01-10 Last updated: 2022-02-08
Jonsson, W. O., Ponette, J., Horwath, O., Rydenstam, T., Söderlund, K., Ekblom, B., . . . Blomstrand, E. (2022). Changes in plasma concentration of kynurenine following intake of branched-chain amino acids are not caused by alterations in muscle kynurenine metabolism.. American Journal of Physiology - Cell Physiology, 322, C49-C62
Open this publication in new window or tab >>Changes in plasma concentration of kynurenine following intake of branched-chain amino acids are not caused by alterations in muscle kynurenine metabolism.
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2022 (English)In: American Journal of Physiology - Cell Physiology, ISSN 0363-6143, E-ISSN 1522-1563, Vol. 322, p. C49-C62Article in journal (Refereed) Published
Abstract [en]

Administration of branched-chain amino acids (BCAA) has been suggested to enhance mitochondrial biogenesis, including levels of PGC-1α, which may, in turn, alter kynurenine metabolism. Ten healthy subjects performed 60 min of dynamic one-leg exercise at ~70% of Wmax on two occasions. They were in random order supplied either a mixture of BCAA or flavored water (placebo) during the experiment. Blood samples were collected during exercise and recovery, and muscle biopsies were taken from both legs before, after and 90 and 180 min following exercise. Ingestion of BCAA doubled their concentration in both plasma and muscle while causing a 30-40% reduction (P<0.05 vs. placebo) in levels of aromatic amino acids in both resting and exercising muscle during 3-h recovery. The muscle concentration of kynurenine decreased by 25% (P<0.05) during recovery, similar in both resting and exercising leg and with both supplements, although plasma concentration of kynurenine during recovery was 10% lower (P<0.05) when BCAA were ingested. Ingestion of BCAA reduced the plasma concentration of kynurenic acid by 60% (P<0.01) during exercise and recovery, while the level remained unchanged with placebo. Exercise induced a 3-4-fold increase (P<0.05) in muscle content of PGC-1a1 mRNA after 90 min of recovery under both conditions, whereas levels of KAT4 mRNA and protein were unaffected by exercise or supplement. In conclusion, the reduction of plasma levels of kynurenine and kynurenic acid caused by BCAA were not associated with any changes in the level of muscle kynurenine, suggesting that kynurenine metabolism was altered in tissues other than muscle.

Place, publisher, year, edition, pages
American Physiological Society, 2022
Keywords
PGC-1α, kynurenic acid, muscle, tryptophan
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-6862 (URN)10.1152/ajpcell.00285.2021 (DOI)000744029900005 ()34817270 (PubMedID)
Funder
Swedish National Centre for Research in SportsNovo Nordisk
Available from: 2021-12-02 Created: 2021-12-02 Last updated: 2022-02-23Bibliographically approved
Blackwood, S. J., Horwath, O., Moberg, M., Pontén, M., Apro, W., Ekblom, M., . . . Katz, A. (2022). Extreme Variations in Muscle Fiber Composition Enable Detection of Insulin Resistance and Excessive Insulin Secretion.. Journal of Clinical Endocrinology and Metabolism, 107(7), e2729-e2737, Article ID dgac221.
Open this publication in new window or tab >>Extreme Variations in Muscle Fiber Composition Enable Detection of Insulin Resistance and Excessive Insulin Secretion.
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2022 (English)In: Journal of Clinical Endocrinology and Metabolism, ISSN 0021-972X, E-ISSN 1945-7197, Vol. 107, no 7, p. e2729-e2737, article id dgac221Article in journal (Refereed) Published
Abstract [en]

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

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

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

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

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

Place, publisher, year, edition, pages
Oxford University Press, 2022
Keywords
insulin, insulin resistance, insulin secretion, intravenous glucose tolerance test, mitochondrial respiration, muscle fiber type
National Category
Endocrinology and Diabetes
Research subject
Medicine/Technology; Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7053 (URN)10.1210/clinem/dgac221 (DOI)000789019300001 ()35405014 (PubMedID)
Available from: 2022-05-18 Created: 2022-05-18 Last updated: 2022-12-06
Horwath, O., Moberg, M., Hirschberg, A. L., Ekblom, B. & Apro, W. (2022). Molecular Regulators of Muscle Mass and Mitochondrial Remodeling Are Not Influenced by Testosterone Administration in Young Women.. Frontiers in Endocrinology, 13, Article ID 874748.
Open this publication in new window or tab >>Molecular Regulators of Muscle Mass and Mitochondrial Remodeling Are Not Influenced by Testosterone Administration in Young Women.
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2022 (English)In: Frontiers in Endocrinology, E-ISSN 1664-2392, Vol. 13, article id 874748Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
Frontiers Media S.A., 2022
Keywords
androgen receptor, fission, fusion, mTORC1-signaling, ubiquitin-proteasome system
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7055 (URN)10.3389/fendo.2022.874748 (DOI)000795475000001 ()35498440 (PubMedID)
Available from: 2022-05-18 Created: 2022-05-18 Last updated: 2024-01-17
Horwath, O., Nordström, F., Apro, W. & Moberg, M. (2022). Satellite cell pool expansion induced by resistance exercise is not altered by acute normobaric hypoxia. In: Svensk idrottsmedicin 2022:2: . Paper presented at SFAIMs vårmöte 2022. Tillsammans för framtidens fysiska aktivitet och idrottsmedicin. Stockholm 19-20 maj 2022. (pp. 30). Svensk förening för fysisk aktivitet och idrottsmedicin, 41
Open this publication in new window or tab >>Satellite cell pool expansion induced by resistance exercise is not altered by acute normobaric hypoxia
2022 (English)In: Svensk idrottsmedicin 2022:2, Svensk förening för fysisk aktivitet och idrottsmedicin , 2022, Vol. 41, p. 30-Conference paper, Oral presentation with published abstract (Other academic)
Place, publisher, year, edition, pages
Svensk förening för fysisk aktivitet och idrottsmedicin, 2022
National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7430 (URN)
Conference
SFAIMs vårmöte 2022. Tillsammans för framtidens fysiska aktivitet och idrottsmedicin. Stockholm 19-20 maj 2022.
Available from: 2022-12-05 Created: 2022-12-05 Last updated: 2023-01-11
Horwath, O., Edman, S., Andersson, A., Larsen, F. J. & Apro, W. (2022). THRIFTY: a novel high-throughput method for rapid fibre type identification of isolated skeletal muscle fibres.. Journal of Physiology, 600(20), 4421-4438
Open this publication in new window or tab >>THRIFTY: a novel high-throughput method for rapid fibre type identification of isolated skeletal muscle fibres.
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2022 (English)In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 600, no 20, p. 4421-4438Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
The physiological society, 2022
Keywords
MyHC, SDS-PAGE, fibre typing, high-throughput, immunofluorescence
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7147 (URN)10.1113/JP282959 (DOI)000858344500001 ()36069036 (PubMedID)
Available from: 2022-10-10 Created: 2022-10-10 Last updated: 2022-12-06
Edman, S., Horwath, O., Andersson, A. & Apro, W. (2022). THRIFTY; A Novel Method For Rapid Fiber Type Identification Of Isolated Skeletal Muscle Fibers. In: Medicine & Science in Sports & Exercise 54(2022);Suppl. 2: . Paper presented at 2022 ACSM Annual Meeting & World Congresses, May 31 - June 4, San Diego, CA, USA (pp. 109-109). Lippincott Williams & Wilkins, 54(9), Article ID 457.
Open this publication in new window or tab >>THRIFTY; A Novel Method For Rapid Fiber Type Identification Of Isolated Skeletal Muscle Fibers
2022 (English)In: Medicine & Science in Sports & Exercise 54(2022);Suppl. 2, Lippincott Williams & Wilkins, 2022, Vol. 54, no 9, p. 109-109, article id 457Conference paper, Oral presentation with published abstract (Other academic)
Place, publisher, year, edition, pages
Lippincott Williams & Wilkins, 2022
National Category
Physiology
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7450 (URN)000888056600324 ()
Conference
2022 ACSM Annual Meeting & World Congresses, May 31 - June 4, San Diego, CA, USA
Available from: 2022-12-20 Created: 2022-12-20 Last updated: 2022-12-20
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-3500-2896

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