Physical exercise increases autophagic signaling through ULK1 in human skeletal muscle
| Autor: | Niels Møller, Jens Otto Lunde Jørgensen, Niels Jessen, Berthil F. Clasen, Britt Christensen, Ann Mosegaard Bak, Mikkel H. Vendelbo, Andreas Buch Møller |
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| Rok vydání: | 2014 |
| Předmět: |
Sequestosome-1 Protein
Adult Blood Glucose Male medicine.medical_specialty Physiology Nutritional Status Physical exercise AMP-Activated Protein Kinases Fatty Acids Nonesterified Protein Serine-Threonine Kinases Random Allocation Young Adult AMP-activated protein kinase Physiology (medical) Internal medicine medicine Autophagy Autophagy-Related Protein-1 Homolog Humans Phosphorylation Protein kinase A Muscle Skeletal Exercise Adaptor Proteins Signal Transducing Cross-Over Studies biology Intracellular Signaling Peptides and Proteins Skeletal muscle Fasting Healthy Volunteers Endocrinology medicine.anatomical_structure biology.protein Microtubule-Associated Proteins |
| Zdroj: | Møller, A B, Vendelbo, M H, Christensen, B, Clasen, B F F, Bak, A M, Jørgensen, J O L, Møller, N & Jessen, N 2015, ' Physical exercise increases autophagic signaling through ULK1 in human skeletal muscle ', Journal of Applied Physiology, vol. 118, no. 8, pp. 971-9 . https://doi.org/10.1152/japplphysiol.01116.2014 |
| ISSN: | 1522-1601 |
| DOI: | 10.1152/japplphysiol.01116.2014 |
| Popis: | Data from transgenic animal models suggest that exercise-induced autophagy is critical for adaptation to physical training, and that Unc-51 like kinase-1 (ULK1) serves as an important regulator of autophagy. Phosphorylation of ULK1 at Ser555 stimulates autophagy, whereas phosphorylation at Ser757 is inhibitory. To determine whether exercise regulates ULK1 phosphorylation in humans in vivo in a nutrient-dependent manner, we examined skeletal muscle biopsies from healthy humans after 1-h cycling exercise at 50% maximal O2 uptake on two occasions: 1) during a 36-h fast, and 2) during continuous glucose infusion at 0.2 kg/h. Physical exercise increased ULK1 phosphorylation at Ser555 and decreased lipidation of light chain 3B. ULK1 phosphorylation at Ser555 correlated positively with AMP-activated protein kinase-α Thr172 phosphorylation and negatively with light chain 3B lipidation. ULK1 phosphorylation at Ser757 was not affected by exercise. Fasting increased ULK1 and p62 protein expression, but did not affect exercise-induced ULK1 phosphorylation. These data demonstrate that autophagy signaling is activated in human skeletal muscle after 60 min of exercise, independently of nutritional status, and suggest that initiation of autophagy constitutes an important physiological response to exercise in humans. |
| Databáze: | OpenAIRE |
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