دورية أكاديمية
Decrease in Akt/PKB signalling in human skeletal muscle by resistance exercise
| العنوان: | Decrease in Akt/PKB signalling in human skeletal muscle by resistance exercise |
|---|---|
| المؤلفون: | Deldicque, Louise, Atherton, Philip, Patel, Rekha, Theisen, Daniel, Nielens, Henri, Rennie, Michael J., Francaux, Marc |
| المساهمون: | UCL - (SLuc) Service de médecine physique et de réadaptation motrice, UCL - MD/IEPR - Institut d'éducation physique et de réadaptation, UCL - (SLuc) Service d'orthopédie et de traumatologie de l'appareil locomoteur |
| المصدر: | European Journal of Applied Physiology, Vol. 104, no. 1, p. 57-65 (2008) |
| بيانات النشر: | Springer |
| سنة النشر: | 2008 |
| المجموعة: | DIAL@UCL (Université catholique de Louvain) |
| مصطلحات موضوعية: | p38 Mitogen-Activated Protein Kinases, Signal Transduction, Ribosomal Protein S6 Kinases, 70-kDa, Quadriceps Muscle, Proto-Oncogene Proteins c-akt, Protein Kinase Inhibitors, Phosphorylation, Phosphoproteins, Myoblasts, Skeletal, Muscle Contraction, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinase 1, Mice, Male, Humans, Fasting, Exercise, Cell Line, Animals, Adult, Adaptor Proteins, Signal Transducing |
| الوصف: | We analysed the effects of resistance exercise upon the phosphorylation state of proteins associated with adaptive processes from the Akt/PKB (protein kinase B) and the mitogen-activated protein kinase (MAPK) pathways. Nine healthy young men (21.7 +/- 0.55 year) performed 10 sets of 10 leg extensions at 80% of their 1-RM (repetition maximum). Muscle biopsies were taken from the vastus lateralis at rest, within the first 30 s after exercise and at 24 h post-exercise. Immediately post exercise, the phosphorylation states of Akt/PKB on Thr308 and Ser473 and 4E-BP1 on Thr37/46 (eukaryotic initiation factor 4E-binding protein 1) were decreased (-60 to -90%, P < 0.05). Conversely, the phosphorylation of p70(s6k) (p70 ribosomal S6 kinase) on Thr421/Ser424 was increased more than 20-fold (P < 0.05), and this was associated with a 10- to 50-fold increase in the phosphorylation of p38 and ERK1/2 (extracellular signal-regulated kinase) (P < 0.05). Twenty-four hours post-exercise the phosphorylation state of Akt/PKB on Thr308 was depressed, whereas the phosphorylation of p70(s6k) on Thr421/Ser424 and sarcoplasmic ERK1/2 were elevated. The present results indicate that high-intensity resistance exercise in the fasted state inhibits Akt/PKB and 4E-BP1 whilst concomitantly augmenting MAPK signalling and p70(s6k) on Thr421/Ser424. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1439-6319 1439-6327 |
| العلاقة: | boreal:12638; http://hdl.handle.net/2078.1/12638Test; info:pmid/18535836; urn:ISSN:1439-6319; urn:EISSN:1439-6327 |
| DOI: | 10.1007/s00421-008-0786-7 |
| الإتاحة: | https://doi.org/10.1007/s00421-008-0786-7Test http://hdl.handle.net/2078.1/12638Test |
| حقوق: | info:eu-repo/semantics/restrictedAccess |
| رقم الانضمام: | edsbas.D2EFEABE |
| قاعدة البيانات: | BASE |
| تدمد: | 14396319 14396327 |
|---|---|
| DOI: | 10.1007/s00421-008-0786-7 |