Gymnastik- och idrottshögskolan, GIH

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Publications (10 of 21) Show all publications
Blackwood, S. J., Tischer, D., van de Ven, M. P., Pontén, M., Edman, S., Horwath, O., . . . Katz, A. (2024). Elevated heart rate and decreased muscle endothelial nitric oxide synthase in early development of insulin resistance.. American Journal of Physiology. Endocrinology and Metabolism, 327(2), E172-E182
Open this publication in new window or tab >>Elevated heart rate and decreased muscle endothelial nitric oxide synthase in early development of insulin resistance.
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2024 (English)In: American Journal of Physiology. Endocrinology and Metabolism, ISSN 0193-1849, E-ISSN 1522-1555, Vol. 327, no 2, p. E172-E182Article in journal (Refereed) Published
Abstract [en]

Insulin resistance (IR) is a risk factor for the development of several major metabolic diseases. Muscle fiber composition is established early in life and is associated with insulin sensitivity. Hence, muscle fiber composition was used to identify early defects in the development of IR in healthy young individuals in the absence of clinical manifestations. Biopsies were obtained from the thigh muscle, followed by an intravenous glucose tolerance test. Indices of insulin action were calculated and cardiovascular measurements, analyses of blood and muscle were performed. Whole-body insulin sensitivity (SIgalvin) was positively related to expression of type I muscle fibers (r=0.49; P<0.001) and negatively related to resting heart rate (HR, r=-0.39; P<0.001), which was also negatively related to expression of type I muscle fibers (r=-0.41; P<0.001). Muscle protein expression of endothelial nitric oxide synthase (eNOS), whose activation results in vasodilation, was measured in two subsets of subjects expressing a high percentage of type I fibers (59±6%; HR = 57±9 beats/min; SIgalvin = 1.8±0.7 units) or low percentage of type I fibers (30±6%; HR = 71±11; SIgalvin = 0.8±0.3 units; P<0.001 for all variables vs. first group). eNOS expression was: 1. higher in subjects with high type I expression; 2. almost two-fold higher in pools of type I vs. II fibers; 3. only detected in capillaries surrounding muscle fibers; and 4. linearly associated with SIgalvin. These data demonstrate that an altered function of the autonomic nervous system and a compromised capacity for vasodilation in the microvasculature occur early in the development of IR.

Place, publisher, year, edition, pages
American Physiological Society, 2024
Keywords
Heart rate, Insulin resistance, Muscle fiber composition, Nitric oxide synthase, epabs, e-pabs, brain health, hjärnhälsa
National Category
Physiology and Anatomy Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-8276 (URN)10.1152/ajpendo.00148.2024 (DOI)001290185800002 ()38836779 (PubMedID)2-s2.0-85201861242 (Scopus ID)
Available from: 2024-06-07 Created: 2024-06-07 Last updated: 2025-02-11
Edman, S., Horwath, O., Van der Stede, T., Blackwood, S. J., Moberg, I., Strömlind, H., . . . Moberg, M. (2024). Pro-Brain-Derived Neurotrophic Factor (BDNF), but Not Mature BDNF, Is Expressed in Human Skeletal Muscle: Implications for Exercise-Induced Neuroplasticity.. Function, 5(3), Article ID zqae005.
Open this publication in new window or tab >>Pro-Brain-Derived Neurotrophic Factor (BDNF), but Not Mature BDNF, Is Expressed in Human Skeletal Muscle: Implications for Exercise-Induced Neuroplasticity.
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2024 (English)In: Function, E-ISSN 2633-8823, Vol. 5, no 3, article id zqae005Article in journal (Refereed) Published
Abstract [en]

Exercise promotes brain plasticity partly by stimulating increases in mature brain-derived neurotrophic factor (mBDNF), but the role of the pro-BDNF isoform in the regulation of BDNF metabolism in humans is unknown. We quantified the expression of pro-BDNF and mBDNF in human skeletal muscle and plasma at rest, after acute exercise (+/- lactate infusion), and after fasting. Pro-BDNF and mBDNF were analyzed with immunoblotting, enzyme-linked immunosorbent assay, immunohistochemistry, and quantitative polymerase chain reaction. Pro-BDNF was consistently and clearly detected in skeletal muscle (40-250 pg mg-1 dry muscle), whereas mBDNF was not. All methods showed a 4-fold greater pro-BDNF expression in type I muscle fibers compared to type II fibers. Exercise resulted in elevated plasma levels of mBDNF (55%) and pro-BDNF (20%), as well as muscle levels of pro-BDNF (∼10%, all P < 0.05). Lactate infusion during exercise induced a significantly greater increase in plasma mBDNF (115%, P < 0.05) compared to control (saline infusion), with no effect on pro-BDNF levels in plasma or muscle. A 3-day fast resulted in a small increase in plasma pro-BDNF (∼10%, P < 0.05), with no effect on mBDNF. Pro-BDNF is highly expressed in human skeletal muscle, particularly in type I fibers, and is increased after exercise. While exercising with higher lactate augmented levels of plasma mBDNF, exercise-mediated increases in circulating mBDNF likely derive partly from release and cleavage of pro-BDNF from skeletal muscle, and partly from neural and other tissues. These findings have implications for preclinical and clinical work related to a wide range of neurological disorders such as Alzheimer's, clinical depression, and amyotrophic lateral sclerosis.

Place, publisher, year, edition, pages
Oxford University Press, 2024
Keywords
exercise, fasting, lactate, muscle fiber type, neurotrophins, β-hydroxybutyrate
National Category
Physiology and Anatomy Sport and Fitness Sciences
Research subject
Medicine/Technology; Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-8240 (URN)10.1093/function/zqae005 (DOI)001225915100002 ()38706964 (PubMedID)
Available from: 2024-05-24 Created: 2024-05-24 Last updated: 2025-02-11
Goldberg, Y., Segal, S., Hamdi, L., Nabat, H., Fainstein, N., Mediouni, E., . . . Einstein, O. (2023). High-intensity interval training attenuates development of autoimmune encephalomyelitis solely by systemic immunomodulation.. Scientific Reports, 13(1), Article ID 16513.
Open this publication in new window or tab >>High-intensity interval training attenuates development of autoimmune encephalomyelitis solely by systemic immunomodulation.
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2023 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 13, no 1, article id 16513Article in journal (Refereed) Published
Abstract [en]

The impact of high-intensity interval training (HIIT) on the central nervous system (CNS) in autoimmune neuroinflammation is not known. The aim of this study was to determine the direct effects of HIIT on the CNS and development of experimental autoimmune encephalomyelitis (EAE). Healthy mice were subjected to HIIT by treadmill running and the proteolipid protein (PLP) transfer EAE model was utilized. To examine neuroprotection, PLP-reactive lymph-node cells (LNCs) were transferred to HIIT and sedentary (SED) mice. To examine immunomodulation, PLP-reactive LNCs from HIIT and SED donor mice were transferred to naïve recipients and analyzed in vitro. HIIT in recipient mice did not affect the development of EAE following exposure to PLP-reactive LNCs. HIIT mice exhibited enhanced migration of systemic autoimmune cells into the CNS and increased demyelination. In contrast, EAE severity in recipient mice injected with PLP-reactive LNCs from HIIT donor mice was significantly diminished. The latter positive effect was associated with decreased migration of autoimmune cells into the CNS and inhibition of very late antigen (VLA)-4 expression in LNCs. Thus, the beneficial effect of HIIT on EAE development is attributed solely to systemic immunomodulatory effects, likely because of systemic inhibition of autoreactive cell migration and reduced VLA-4 integrin expression.

Place, publisher, year, edition, pages
Nature Publishing Group, 2023
National Category
Immunology in the medical area
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7893 (URN)10.1038/s41598-023-43534-8 (DOI)001167376800004 ()37783693 (PubMedID)
Available from: 2023-10-06 Created: 2023-10-06 Last updated: 2024-03-21
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 and Anatomy 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: 2025-02-10
Flockhart, M., Tischer, D., Nilsson, L. C., Blackwood, S. J., Ekblom, B., Katz, A., . . . Larsen, F. J. (2023). Reduced glucose tolerance and insulin sensitivity after prolonged exercise in endurance athletes.. Acta Physiologica, 238(4), Article ID e13972.
Open this publication in new window or tab >>Reduced glucose tolerance and insulin sensitivity after prolonged exercise in endurance athletes.
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2023 (English)In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 238, no 4, article id e13972Article in journal (Refereed) Published
Abstract [en]

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

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

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

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

Place, publisher, year, edition, pages
John Wiley & Sons, 2023
Keywords
endurance athletes, endurance exercise, glucose tolerance, insulin sensitivity, mitochondria, reactive oxygen species
National Category
Sport and Fitness Sciences Endocrinology and Diabetes
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7627 (URN)10.1111/apha.13972 (DOI)000972308100001 ()37017615 (PubMedID)
Funder
Swedish National Centre for Research in Sports, P2017-0067, P2018-0083, P2019-0062, P2020-0061
Note

At the time of Mikael Flockhart's dissertation, this article was a submitted manuscript.

Available from: 2023-05-08 Created: 2023-05-08 Last updated: 2025-02-11
Nordström, F., Liegnell, R., Apro, W., Blackwood, S. J., Katz, A. & Moberg, M. (2023). The lactate receptor GPR81 is predominantly expressed in type II human skeletal muscle fibers: potential for lactate autocrine signaling.. Paper presented at 324(2):C477-C487. American Journal of Physiology - Cell Physiology, 324(2), C477-C487
Open this publication in new window or tab >>The lactate receptor GPR81 is predominantly expressed in type II human skeletal muscle fibers: potential for lactate autocrine signaling.
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2023 (English)In: American Journal of Physiology - Cell Physiology, ISSN 0363-6143, E-ISSN 1522-1563, Vol. 324, no 2, p. C477-C487Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
American Physiological Society, 2023
Keywords
CREB, HCAR1, PGC-1alpha, PKA, Resistance exercise
National Category
Sport and Fitness Sciences Physiology and Anatomy
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7464 (URN)10.1152/ajpcell.00443.2022 (DOI)000959663400012 ()36622074 (PubMedID)
Conference
324(2):C477-C487
Available from: 2023-01-11 Created: 2023-01-11 Last updated: 2025-02-11
Katz, A. (2023). The role of glycogen phosphorylase in glycogen biogenesis in skeletal muscle after exercise. Sports Medicine and Health Science, 5(1), 29-33
Open this publication in new window or tab >>The role of glycogen phosphorylase in glycogen biogenesis in skeletal muscle after exercise
2023 (English)In: Sports Medicine and Health Science, ISSN 2666-3376, Vol. 5, no 1, p. 29-33Article in journal (Refereed) Published
Abstract [en]

Initially it was believed that phosphorylase was responsible for both glycogen breakdown and synthesis in the living cell. The discovery of glycogen synthase and McArdle's disease (lack of phosphorylase activity), together with the high Pi/glucose 1-P ratio in skeletal muscle, demonstrated that glycogen synthesis could not be attributed to reversal of the phosphorylase reaction. Rather, glycogen synthesis was attributable solely to the activity of glycogen synthase, subsequent to the transport of glucose into the cell. However, the well-established observation that phosphorylase was inactivated (i.e., dephosphorylated) during the initial recovery period after prior exercise, when the rate of glycogen accumulation is highest and independent of insulin, suggested that phosphorylase could play an active role in glycogen accumulation. But the quantitative contribution of phosphorylase inactivation was not established until recently, when studying isolated murine muscle preparations during recovery from repeated contractions at temperatures ranging from 25 to 35 °C. Thus, in both slow-twitch, oxidative and fast-twitch, glycolytic muscles, inactivation of phosphorylase accounted for 45%–75% of glycogen accumulation during the initial hours of recovery following repeated contractions. Such data indicate that phosphorylase inactivation may be the most important mechanism for glycogen accumulation under defined conditions. These results support the initial belief that phosphorylase plays a quantitative role in glycogen formation in the living cell. However, the mechanism is not via activation of phosphorylase, but rather via inactivation of the enzyme.

Place, publisher, year, edition, pages
Elsevier, 2023
Keywords
Phosphorylase, Glycogen, Glycogen synthase, Muscle, Exercise
National Category
Physiology and Anatomy
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7426 (URN)10.1016/j.smhs.2022.11.001 (DOI)001107685800001 ()
Available from: 2022-12-02 Created: 2022-12-02 Last updated: 2025-02-10
Katz, A. (2022). A century of exercise physiology: key concepts in regulation of glycogen metabolism in skeletal muscle.. European Journal of Applied Physiology, 122(8), 1751-1772
Open this publication in new window or tab >>A century of exercise physiology: key concepts in regulation of glycogen metabolism in skeletal muscle.
2022 (English)In: European Journal of Applied Physiology, ISSN 1439-6319, E-ISSN 1439-6327, Vol. 122, no 8, p. 1751-1772Article in journal (Refereed) Published
Abstract [en]

Glycogen is a branched, glucose polymer and the storage form of glucose in cells. Glycogen has traditionally been viewed as a key substrate for muscle ATP production during conditions of high energy demand and considered to be limiting for work capacity and force generation under defined conditions. Glycogenolysis is catalyzed by phosphorylase, while glycogenesis is catalyzed by glycogen synthase. For many years, it was believed that a primer was required for de novo glycogen synthesis and the protein considered responsible for this process was ultimately discovered and named glycogenin. However, the subsequent observation of glycogen storage in the absence of functional glycogenin raises questions about the true role of the protein. In resting muscle, phosphorylase is generally considered to be present in two forms: non-phosphorylated and inactive (phosphorylase b) and phosphorylated and constitutively active (phosphorylase a). Initially, it was believed that activation of phosphorylase during intense muscle contraction was primarily accounted for by phosphorylation of phosphorylase b (activated by increases in AMP) to a, and that glycogen synthesis during recovery from exercise occurred solely through mechanisms controlled by glucose transport and glycogen synthase. However, it now appears that these views require modifications. Moreover, the traditional roles of glycogen in muscle function have been extended in recent years and in some instances, the original concepts have undergone revision. Thus, despite the extensive amount of knowledge accrued during the past 100 years, several critical questions remain regarding the regulation of glycogen metabolism and its role in living muscle.

Place, publisher, year, edition, pages
Springer, 2022
Keywords
Exercise, Glycogen, Glycogen synthase, Glycogenin, Muscle, Phosphorylase
National Category
Sport and Fitness Sciences
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7025 (URN)10.1007/s00421-022-04935-1 (DOI)000775865500001 ()35355125 (PubMedID)
Available from: 2022-04-26 Created: 2022-04-26 Last updated: 2025-02-11
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 and Anatomy
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: 2025-02-10
Hamdi, L., Nabat, H., Goldberg, Y., Fainstein, N., Segal, S., Mediouni, E., . . . Einstein, O. (2022). Exercise training alters autoimmune cell invasion into the brain in autoimmune encephalomyelitis.. Annals of Clinical and Translational Neurology, 9(11), 1792-1806
Open this publication in new window or tab >>Exercise training alters autoimmune cell invasion into the brain in autoimmune encephalomyelitis.
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2022 (English)In: Annals of Clinical and Translational Neurology, E-ISSN 2328-9503, Vol. 9, no 11, p. 1792-1806Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: The mechanisms by which exercise training (ET) elicits beneficial effects on the systemic immune system and the central nervous system (CNS) in autoimmune neuroinflammation are not fully understood.

OBJECTIVES: To investigate (1) the systemic effects of high-intensity continuous training (HICT) on the migratory potential of autoimmune cells; (2) the direct effects of HICT on blood-brain-barrier (BBB) properties.

METHODS: Healthy mice were subjected to high-intensity continuous training (HICT) by treadmill running. The proteolipid protein (PLP) transfer EAE model was utilized to examine the immunomodulatory effects of training, where PLP-reactive lymph-node cells (LNCs) from HICT and sedentary donor mice were analyzed in vitro and transferred to naïve recipients that developed EAE. To examine neuroprotection, encephalitogenic LNCs from donor mice were transferred into HICT or sedentary recipient mice and the BBB was analyzed.

RESULTS: Transfer of PLP-reactive LNCs obtained from HICT donor mice attenuated EAE severity and inflammation in recipient mice. HICT markedly inhibited very late antigen (VLA)-4 and lymphocyte function-associated antigen (LFA)-1 expression in LNCs. Transfer of encephalitogenic LNCs into HICT recipients resulted in milder EAE and attenuated CNS inflammation. HICT reduced BBB permeability and the expression of intercellular adhesion molecule (ICAM)-1 and vascular cell adhesion molecule (VCAM)-1 in CNS blood vessels.

INTERPRETATION: HICT attenuates EAE development by both immunomodulatory and neuroprotective effects. The reduction in destructive CNS inflammation in EAE is attributed to systemic inhibition of autoreactive cell migratory potential, as well as reduction in BBB permeability, which are associated with reduced VLA-4/VCAM-1 and LFA-1/ICAM-1 interactions.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2022
National Category
Immunology in the medical area
Research subject
Medicine/Technology
Identifiers
urn:nbn:se:gih:diva-7377 (URN)10.1002/acn3.51677 (DOI)000865642600001 ()36217574 (PubMedID)
Available from: 2022-11-10 Created: 2022-11-10 Last updated: 2022-12-16
Projects
E-PABS - a centre of Excellence in Physical Activity, healthy Brain functions and Sustainability [20210002 01 H]; Swedish School of Sport and Health Sciences, GIH; Publications
Heiland, E. G., Lindh, F., Regan, C., Ekblom, Ö., Kjellenberg, K., Larsen, F. J., . . . Helgadóttir, B. (2024). A randomised crossover trial of nitrate and breakfast on prefrontal cognitive and haemodynamic response functions.. NPJ science of food, 8(1), Article ID 64. Hoy, S., Norman, Å., Larsson, H. & de la Haye, K. (2024). Agents of change? Exploring relations among school staff connected to daily physical activity promotion in a Swedish secondary school from a social network perspective. In: : . Paper presented at AIESEP - The International Organization for Physical Education in Higher Education - International Conference, Jyväskylä, Finland, May 13-17th 2024. Wiklund, C. A., Ekblom, M. M., Wang, R. & Ekblom, Ö. (2024). Associations Between Physical Activity and Symptoms of Mental Health Disorders in Adolescence: Evidence From the Longitudinal Swedish Twin Register.. Journal of Adolescent Health, Article ID S1054-139X(24)00513-5. Projektet Fysisk aktivetet för hälsosamma hjärnfunktioner bland skolungdomar, ., Helgadóttir, B. & Kjellenberg, K. (2024). Balansen mellan skärmtid, rörelse och hjärnhälsa hos unga. Stockholm: Gymnastik- och idrottshögskolan, GIHFarias, L., Hellenius, M.-L., Nyberg, G. & Andermo, S. (2024). Building a healthy generation together: parents' experiences and perceived meanings of a family-based program delivered in ethnically diverse neighborhoods in Sweden.. International Journal for Equity in Health, 23(1), Article ID 180. Wiklund, C. A., Ekblom, Ö., Paulsson, S., Lindwall, M. & Ekblom Bak, E. (2024). Cardiorespiratory fitness in midlife and subsequent incident depression, long-term sickness absence, and disability pension due to depression in 330,247 men and women.. Preventive Medicine, 181, Article ID 107916. Wiklund, C., Lindwall, M., Ekblom, Ö., Nyberg, J., Åberg, M. I., Paulsson, S. & Ekblom Bak, E. (2024). Change in Cardiorespiratory Fitness and Risk of Depression, Anxiety, and Cerebrovascular Disease.. American Journal of Preventive Medicine, 67(6), 849-858Lönn, A., Ekblom, Ö., Kallings, L., Börjesson, M. & Ekström, M. (2024). Decrease in accelerometer assessed physical activity during the first-year post-myocardial infarction: a prospective cohort study.. Scandinavian Cardiovascular Journal, 58(1), Article ID 2397442. Blackwood, S. J., Tischer, D., van de Ven, M. P., Pontén, M., Edman, S., Horwath, O., . . . Katz, A. (2024). Elevated heart rate and decreased muscle endothelial nitric oxide synthase in early development of insulin resistance.. American Journal of Physiology. Endocrinology and Metabolism, 327(2), E172-E182Fridolfsson, J., Ekblom Bak, E., Ekblom, Ö., Bergström, G., Arvidsson, D. & Börjesson, M. (2024). Fitness-related physical activity intensity explains most of the association between accelerometer data and cardiometabolic health in persons 50-64 years old.. British Journal of Sports Medicine, 58(21), 1244-1250
Plasma markers of neurodegeneration, cognition and physical activity in healthy aging; Swedish School of Sport and Health Sciences, GIHMuscle to brain cross-talk in the molecular regulation of neuroplasticity [M21-0134_Åke Wiberg]; Swedish School of Sport and Health Sciences, GIHUse of xenotransfusion to elucidate how exercise training impacts neurofunction [CIF 2023-0083]; Swedish School of Sport and Health Sciences, GIH
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-3402-9891

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