Document Detail

Temperature- and exercise-induced gene expression and metabolic enzyme changes in skeletal muscle of adult zebrafish (Danio rerio).
MedLine Citation:
PMID:  16990399     Owner:  NLM     Status:  MEDLINE    
Both exercise training and cold acclimatization induce muscle remodelling in vertebrates, producing a more aerobic phenotype. In ectothermic species exercise training and cold-acclimatization represent distinct stimuli. It is currently unclear if these stimuli act through a common mechanism or if different mechanisms lead to a common phenotype. The goal of this study was to survey responses that represent potential mechanisms responsible for contraction- and temperature-induced muscle remodelling, using an ectothermic vertebrate. Separate groups of adult zebrafish (Danio rerio) were either swim trained or cold acclimatized for 4 weeks. We found that the mitochondrial marker enzyme citrate synthase (CS) was increased by 1.5x in cold and by 1.3x with exercise (P<0.05). Cytochrome c oxidase (COx) was increased by 1.2x following exercise training (P<0.05) and 1.2x (P=0.07) with cold acclimatization. However, only cold acclimatization increased beta-hydroxyacyl-CoA dehydrogenase (HOAD) compared to exercise-trained (by 1.3x) and pyruvate kinase (PK) relative to control zebrafish. We assessed the whole-animal performance outcomes of these treatments. Maximum absolute sustained swimming speed (Ucrit) was increased in the exercise trained group but not in the cold acclimatized group. Real-time PCR analysis indicated that increases in CS are primarily transcriptionally regulated with exercise but not with cold treatments. Both treatments showed increases in nuclear respiratory factor (NRF)-1 mRNA which was increased by 2.3x in cold-acclimatized and 4x in exercise-trained zebrafish above controls. In contrast, peroxisome proliferator-activated receptor (PPAR)-alpha mRNA levels were decreased in both experimental groups while PPAR-beta1 declined in exercise training only. Moreover, PPAR-gamma coactivator (PGC)-1alpha mRNA was not changed by either treatment. In zebrafish, both temperature and exercise produce a more aerobic phenotype, but there are stimulus-dependent responses (i.e. HOAD and PK activities). While similar changes in NRF-1 mRNA suggest that common responses might underlie aerobic muscle remodelling there are distinct changes (i.e. CS and PPAR-beta1 mRNA) that contribute to specific temperature- and exercise-induced phenotypes.
Grant B McClelland; Paul M Craig; Kalindi Dhekney; Shawn Dipardo
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-09-21
Journal Detail:
Title:  The Journal of physiology     Volume:  577     ISSN:  0022-3751     ISO Abbreviation:  J. Physiol. (Lond.)     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2006-12-01     Completed Date:  2007-01-26     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  0266262     Medline TA:  J Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  739-51     Citation Subset:  IM    
Department of Biology, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4K1, Canada.
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MeSH Terms
3-Hydroxyacyl CoA Dehydrogenases / metabolism
Acclimatization / physiology*
Citrate (si)-Synthase / metabolism
Cold Temperature*
Electron Transport Complex IV / metabolism
Eye Proteins / metabolism
Gene Expression Regulation, Enzymologic*
Muscle Fatigue
Muscle, Skeletal / enzymology*,  metabolism
Nuclear Respiratory Factor 1 / metabolism
Peroxisome Proliferator-Activated Receptors / metabolism
Physical Conditioning, Animal / physiology*
Polymerase Chain Reaction
Pyruvate Kinase / metabolism
RNA, Messenger / metabolism
Time Factors
Zebrafish / metabolism*
Zebrafish Proteins / metabolism*
Reg. No./Substance:
0/Eye Proteins; 0/NRF1 protein, zebrafish; 0/Nuclear Respiratory Factor 1; 0/Peroxisome Proliferator-Activated Receptors; 0/RNA, Messenger; 0/Zebrafish Proteins; EC CoA Dehydrogenases; EC Transport Complex IV; EC (si)-Synthase; EC Kinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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