*Contributed equally to the present work.
Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise
Article first published online: 25 OCT 2010
© 2010 John Wiley & Sons A/S
Scandinavian Journal of Medicine & Science in Sports
Volume 22, Issue 2, pages 207–216, April 2012
How to Cite
Gandra, P. G., Valente, R. H., Perales, J., Pacheco, A. G. and Macedo, D. V. (2012), Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise. Scandinavian Journal of Medicine & Science in Sports, 22: 207–216. doi: 10.1111/j.1600-0838.2010.01235.x
- Issue published online: 9 MAR 2012
- Article first published online: 25 OCT 2010
- Accepted for publication 16 August 2010
- skeletal muscle;
- two-dimensional electrophoresis;
- mass spectrometry
Exercise can alter gene transcriptional and protein translational rates leading to changes in protein abundance toward adaptation to exercise. We investigated the alterations in protein abundance in skeletal muscle after one bout of an exhaustive exercise through proteomic analysis. Gastrocnemius muscles were sampled from non-exercised control rats and from rats exercised on a treadmill with incremental increases in speed until exhaustion (approximately 30 min). Rats were sacrificed 3 and 24 h after exercise cessation. Two-dimensional gel electrophoresis was performed and spots with a significant alteration in relative volume were identified by mass spectrometry. Six spots presented statistically significant altered abundances after exercise. The spots identified as the metabolic related proteins triosephosphate isomerase 1, glyceraldehyde-3-phosphate dehydrogenase, the β subunit of pyruvate dehydrogenase E1 and carnitine palmitoyltransferase 2 were all more abundant after exercise. One spot identified as heat shock cognate 70 was also more abundant after exercise. One spot demonstrated a decreased abundance after exercise and was identified as α-actin. These results suggest that a single session of exhaustive incremental exercise in untrained muscle can alter thin filaments synthesis/degradation rate and enhance cytosolic and mitochondrial proteins synthesis. The identified proteins may be important to a general preconditioning of skeletal muscle for subsequent exercise sessions.