Autophagy and protein turnover signaling in slow-twitch muscle during exercise
| العنوان: | Autophagy and protein turnover signaling in slow-twitch muscle during exercise |
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| المؤلفون: | Allan F. Pagano, Anthony Sanchez, Henri Bernardi, Guillaume Py, Robin Candau |
| المساهمون: | Dynamique Musculaire et Métabolisme (DMEM), Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Faculty of Sport Sciences of the University of Montpellier 1, Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM) |
| المصدر: | Medicine and Science in Sports and Exercise Medicine and Science in Sports and Exercise, American College of Sports Medicine (ACSM), 2014, 46 (7), pp.1314-1325. ⟨10.1249/MSS.0000000000000237⟩ |
| بيانات النشر: | HAL CCSD, 2014. |
| سنة النشر: | 2014 |
| مصطلحات موضوعية: | medicine.medical_specialty, autophagy, Ubiquitin-Protein Ligases, [SDV]Life Sciences [q-bio], amp protéine kinase, Muscle Proteins, Physical Therapy, Sports Therapy and Rehabilitation, autophagie, AMP-Activated Protein Kinases, 03 medical and health sciences, 0302 clinical medicine, Physical Conditioning, Animal, Internal medicine, medicine, Animals, Orthopedics and Sports Medicine, RNA, Messenger, Phosphorylation, Protein kinase B, 030304 developmental biology, exercice d'endurance, 0303 health sciences, Chemistry, Protein turnover, AMPK, Skeletal muscle, Mitochondria, Muscle, Mice, Inbred C57BL, mitochondria, Muscle Fibers, Slow-Twitch, Endocrinology, medicine.anatomical_structure, mitochondrial fusion, mitochondrie, Physical Endurance, MUL1, Mitochondrial fission, dégradation protéique, Biomarkers, Hepatocyte Nuclear Factor 3-gamma, 030217 neurology & neurosurgery, Signal Transduction |
| الوصف: | AB Purpose: The aim of this study was to characterize skeletal muscle protein breakdown and mitochondrial dynamics markers at different points of endurance exercise. Methods: Mice run at 10 m[middle dot]min-1 during 1 h, and running speed was increased by 0.5 m[middle dot]min-1 every minute during 40 min and then by 1 m[middle dot]min-1 until exhaustion. Animals were killed by cervical dislocation at 30, 60, 90, and 120 min; at time to exhaustion (Te); and at 3 and 24 h during recovery. The soleus and the deep red regions of the quadriceps muscles were pooled. Results: AMPK phosphorylation (Thr172) increased from 30 min to Te, and FoxO3a phosphorylation (Thr32 and Ser253) decreased from 120 min to 3 h after exercise. FoxO3a-dependent E3 ligases Mul1 and MuRF1 proteins increased from 30 min to Te and at Te and 3 h after exercise, respectively, whereas MAFbx/atrogin-1 protein expression did not change significantly. The autophagic markers LC3B-II increased at 120 min and Te, and p62 significantly decreased at Te. The AMPK-dependent phosphorylation of Ulk1 at Ser317 and Ser555 increased from 60 min to Te and at 30 and 60 min, respectively. Akt (Ser473), MTOR (Ser2448), and 4E-BP1 (Thr37/46) phosphorylation decreased from 90 min to Te, and the MTOR-dependent phosphorylation of Ulk1 (Ser757) decreased from 120 min to Te. Ser616 phosphorylation of the mitochondrial fission marker DRP1 increased from 60 min to Te, but protein expression of the fusion markers mitofusin-2, a substrate of Mul1, and OPA1 did not significantly change. Conclusions: These results fit with a regulation of protein breakdown triggered by FoxO3a and Ulk1 pathways after AMPK activation and Akt/MTOR inhibition. Furthermore, our data suggest that mitochondrial fission is quickly increased, and mitochondrial fusion is unchanged during exercise |
| اللغة: | English |
| تدمد: | 0195-9131 1530-0315 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0631e5e29ad4bd604dfa75ca59a85f18 https://hal.archives-ouvertes.fr/hal-01837569 |
| رقم الأكسشن: | edsair.doi.dedup.....0631e5e29ad4bd604dfa75ca59a85f18 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 01959131 15300315 |
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