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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Gandra, P. G. [1] ; Valente, R. H. [2] ; Perales, J. [2] ; Pacheco, A. G. [3] ; Macedo, D. V. [1]
Total Authors: 5
Affiliation:
[1] Univ Estadual Campinas, Inst Biol, Lab Bioquim Exercicio LABEX, Campinas, SP - Brazil
[2] Inst Oswaldo Cruz, Lab Toxinol, BR-20001 Rio De Janeiro - Brazil
[3] Programa Comp Cient, Rio De Janeiro - Brazil
Total Affiliations: 3
Document type: Journal article
Source: SCANDINAVIAN JOURNAL OF MEDICINE & SCIENCE IN SPORTS; v. 22, n. 2, p. 207-216, APR 2012.
Web of Science Citations: 11
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 beta 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 a-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. (AU)