Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle.

Details

Serval ID
serval:BIB_3441334BFC73
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle.
Journal
Journal of Physiology
Author(s)
Féasson L., Stockholm D., Freyssenet D., Richard I., Duguez S., Beckmann J.S., Denis C.
ISSN
0022-3751
Publication state
Published
Issued date
08/2002
Peer-reviewed
Oui
Volume
543
Number
Pt 1
Pages
297-306
Language
english
Abstract
The molecular events by which eccentric muscle contractions induce muscle damage and remodelling remain largely unknown. We assessed whether eccentric exercise modulates the expression of proteinases (calpains 1, 2 and 3, proteasome, cathepsin B+L), muscle structural proteins (alpha-sarcoglycan and desmin), and the expression of the heat shock proteins Hsp27 and alphaB-crystallin. Vastus lateralis muscle biopsies from twelve healthy male volunteers were obtained before, immediately after, and 1 and 14 days after a 30 min downhill treadmill running exercise. Eccentric exercise induced muscle damage as evidenced by the analysis of muscle pain and weakness, creatine kinase serum activity, myoglobinaemia and ultrastructural analysis of muscle biopsies. The calpain 3 mRNA level was decreased immediately after exercise whereas calpain 2 mRNA level was increased at day 1. Both mRNA levels returned to control values by day 14. By contrast, cathepsin B+L and proteasome enzyme activities were increased at day 14. The alpha-sarcoglycan protein level was decreased immediately after exercise and at day 1, whereas the desmin level peaked at day 14. alphaB-crystallin and Hsp27 protein levels were increased at days 1 and 14. Our results suggest that the differential expression of calpain 2 and 3 mRNA levels may be important in the process of exercise-induced muscle damage, whereas expression of alpha-sarcoglycan, desmin, alphaB-crystallin and Hsp27 may be essentially involved in the subsequent remodelling of myofibrillar structure. This remodelling response may limit the extent of muscle damage upon a subsequent mechanical stress.
Keywords
Actins/analysis, Adaptation, Physiological/physiology, Adult, Calpain/genetics, Cysteine Endopeptidases/metabolism, Cytoskeletal Proteins/analysis, Desmin/analysis, Exercise/physiology, Gene Expression/physiology, HSP27 Heat-Shock Proteins, Heat-Shock Proteins, Humans, Lysosomes/enzymology, Male, Membrane Glycoproteins/analysis, Multienzyme Complexes/metabolism, Muscle Contraction/physiology, Muscle Proteins/genetics, Muscle, Skeletal/chemistry, Muscle, Skeletal/injuries, Neoplasm Proteins/analysis, Neuromuscular Diseases/physiopathology, Proteasome Endopeptidase Complex, RNA, Messenger/analysis, Running/physiology, Sarcoglycans, Stress, Mechanical, alpha-Crystallins/analysis, beta-Crystallins/analysis
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 16:17
Last modification date
20/08/2019 13:20
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