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Changes in signalling pathways regulating protein synthesis in human muscle in the recovery period after endurance exercise.
Acta Physiol (Oxf). 2007 Sep; 191(1):67-75.AP

Abstract

AIM

Exercise induced alterations in the rate of muscle protein synthesis may be related to activity changes in signalling pathways involved in protein synthesis. The aim of the present study was to investigate whether such changes in enzyme phosphorylation occur after endurance exercise.

METHODS

Six male subjects performed ergometer cycling exercise for 1 h at 75% of the maximal oxygen uptake. Muscle biopsy samples from the vastus lateralis were taken before, immediately after, 30 min, 1 h, 2 h and 3 h after exercise for the determination of protein kinase B (PKB/Akt), mammalian target of rapamycin (mTOR), glycogen synthase 3 kinase (GSK-3), p70S6 kinase (p70(S6k)) and eukaryotic elongation factor 2 (eEF2) phosphorylation.

RESULTS

The phosphorylation of Akt was unchanged directly after exercise, but two- to fourfold increased 1 and 2 h after the exercise, whereas GSK-3alpha and beta phosphorylation were two- to fourfold elevated throughout most of the 3-h recovery period. Phosphorylation of mTOR was elevated threefold directly after, 30 min and 2 h after exercise and eEF2 phosphorylation was decreased by 35-75% from 30 min to 3 h-recovery. Exercise led to a five- to eightfold increase in Ser(424)/Thr(421) phosphorylation of p70(S6k) up to 30 min after exercise, but no change in Thr(389) phosphorylation.

CONCLUSIONS

The marked decrease in eEF2 phosphorylation suggests an activation of translation elongation and possibly protein synthesis in the recovery period after sustained endurance exercise. The lack of p70(S6k) activation suggests that translation initiation is activated via alternative pathways, possibly via the activation of eukaryotic initiating factor 2B.

Authors+Show Affiliations

Astrand Laboratory, Swedish School of Health and Sport Sciences, Stockholm, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Clinical Trial
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17488244

Citation

Mascher, H, et al. "Changes in Signalling Pathways Regulating Protein Synthesis in Human Muscle in the Recovery Period After Endurance Exercise." Acta Physiologica (Oxford, England), vol. 191, no. 1, 2007, pp. 67-75.
Mascher H, Andersson H, Nilsson PA, et al. Changes in signalling pathways regulating protein synthesis in human muscle in the recovery period after endurance exercise. Acta Physiol (Oxf). 2007;191(1):67-75.
Mascher, H., Andersson, H., Nilsson, P. A., Ekblom, B., & Blomstrand, E. (2007). Changes in signalling pathways regulating protein synthesis in human muscle in the recovery period after endurance exercise. Acta Physiologica (Oxford, England), 191(1), 67-75.
Mascher H, et al. Changes in Signalling Pathways Regulating Protein Synthesis in Human Muscle in the Recovery Period After Endurance Exercise. Acta Physiol (Oxf). 2007;191(1):67-75. PubMed PMID: 17488244.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Changes in signalling pathways regulating protein synthesis in human muscle in the recovery period after endurance exercise. AU - Mascher,H, AU - Andersson,H, AU - Nilsson,P-A, AU - Ekblom,B, AU - Blomstrand,E, Y1 - 2007/05/03/ PY - 2007/5/10/pubmed PY - 2007/12/11/medline PY - 2007/5/10/entrez SP - 67 EP - 75 JF - Acta physiologica (Oxford, England) JO - Acta Physiol (Oxf) VL - 191 IS - 1 N2 - AIM: Exercise induced alterations in the rate of muscle protein synthesis may be related to activity changes in signalling pathways involved in protein synthesis. The aim of the present study was to investigate whether such changes in enzyme phosphorylation occur after endurance exercise. METHODS: Six male subjects performed ergometer cycling exercise for 1 h at 75% of the maximal oxygen uptake. Muscle biopsy samples from the vastus lateralis were taken before, immediately after, 30 min, 1 h, 2 h and 3 h after exercise for the determination of protein kinase B (PKB/Akt), mammalian target of rapamycin (mTOR), glycogen synthase 3 kinase (GSK-3), p70S6 kinase (p70(S6k)) and eukaryotic elongation factor 2 (eEF2) phosphorylation. RESULTS: The phosphorylation of Akt was unchanged directly after exercise, but two- to fourfold increased 1 and 2 h after the exercise, whereas GSK-3alpha and beta phosphorylation were two- to fourfold elevated throughout most of the 3-h recovery period. Phosphorylation of mTOR was elevated threefold directly after, 30 min and 2 h after exercise and eEF2 phosphorylation was decreased by 35-75% from 30 min to 3 h-recovery. Exercise led to a five- to eightfold increase in Ser(424)/Thr(421) phosphorylation of p70(S6k) up to 30 min after exercise, but no change in Thr(389) phosphorylation. CONCLUSIONS: The marked decrease in eEF2 phosphorylation suggests an activation of translation elongation and possibly protein synthesis in the recovery period after sustained endurance exercise. The lack of p70(S6k) activation suggests that translation initiation is activated via alternative pathways, possibly via the activation of eukaryotic initiating factor 2B. SN - 1748-1708 UR - https://www.unboundmedicine.com/medline/citation/17488244/Changes_in_signalling_pathways_regulating_protein_synthesis_in_human_muscle_in_the_recovery_period_after_endurance_exercise_ L2 - https://doi.org/10.1111/j.1748-1716.2007.01712.x DB - PRIME DP - Unbound Medicine ER -