Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise

Gandra, PG; Valente, RH; Perales, J; Pacheco, AG; Macedo, DV; ,

HERO ID

7169828

Reference Type

Journal Article

Year

2012

Language

English

PMID

20973830

HERO ID 7169828
In Press No
Year 2012
Title Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise
Authors Gandra, PG; Valente, RH; Perales, J; Pacheco, AG; Macedo, DV; ,
Journal Scandinavian Journal of Medicine and Science
Page Numbers 207-216
Abstract 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 E(1) 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.
Doi 10.1111/j.1600-0838.2010.01235.x
Pmid 20973830
Wosid WOS:000301288100011
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English